• Venkatachalam, S., Murlidharan, N., Krishnan, S. R., Ramakrishnan, C., Setshedi, M., Pandian, R., Barh, D., Tiwari, S., Azevedo, V. & Sayed, Y. (2023). Genes (Basel). 14, 533.
• Dean Sherry, Ramesh Pandian, and Yasien Sayed. (2022). Non-active site mutations in the HIV protease: Diminished drug binding affinity is achieved through modulating the hydrophobic sliding mechanism. International Journal of Biological Macromolecules 217, 27-41.
• Ramesh, P.,* Sundaresan, S. S., Shobana, N., Vinuchakkaravarthy, T., Sivakumar, K., Yasien, S., and Ponnuswamy, M.N. (2021). Structural studies of hemoglobin from two flightless birds, ostrich and turkey: insights into their differing oxygen-binding properties. Acta Cryst. D77, 690–702. (* Corresponding author)
• Sundaresan, S. S. Ramesh, P.,* Shobana, N., Vinuchakkaravarthy, T., Yasien, S., and Ponnuswamy, M.N. (2021). Crystal structure of hemoglobin from mouse (Mus musculus) compared with those from other small animals and humans. Acta Cryst. F77, 113–120. (* Corresponding author)
• Blessing O. Akumadu, Ramesh Pandian, Jessica Olfsen, Roland Worth, Monare Thulo, Tshireletso Mentor, Sylvia Fanucchi, Yasien Sayed, Heini W. Dirr , Ikechukwu Achilonu (2020). Molecular basis of inhibition of Schistosoma japonicum glutathione transferase by ellagic acid: Insights into biophysical and structural studies. Molecular & Biochemical Parasitology, 240:111319.
• Nandhini, D., Subashchandrabose, S., Ramesh, P., Mohan Radheep, D. & Sakthipandi, K. (2019).  Synthesis, Characterization and computation of potassium doped calcium hydroxide nanoparticles and nanotubes. International Journal of Mechanical and Production Engineering Research and Development, 9(1), 441-448.
• Ambrosio Camuenho, A. Jorge Parola, Alfonso Alejo-Armijo, Ramesh Pandian, Clara S. B. Gomes, Cesar A. T. Laia and Fernando Pina (2019). A model compound for pyridinechalcone-based multistate systems. Ring opening-closure as the slowest kinetic step of the multistate. New Journal of Chemistry 43, 18229-18239.
• Eththilu Babu, Paulpandian Muthu Mareeswaran, Pandian Ramesh & Seenivasan Rajagopal. (2016). Label free luminescence strategy for sensitive detection of ATP using aptamer-Ru(II) complexes, Journal of Luminescence 175, 267-273.
• Ryu, B.H., Duc, D.N., Ngo, T.D., Oh, C., Pandian, R., Kim, K.K. & Kim, T.D. (2014). Crystallization and preliminary X-ray analysis of a highly stable novel SGNH hydrolase (Est24) from Sinorhizobium meliloti. Acta Cryst. F70, 193-195.
• Kyungmin Kim, Bum Han Ryu, Sung Soo Kim, Deu Rae An, Tri Duc Ngo, Ramesh Pandian, Kyeong Kyu Kim, T Doohun Kim 2015. Structural and biochemical characterization of a carbohydrate acetylesterase from Sinorhizobium meliloti 1021. FEBS letters, Volume 589, Issue 1, 117–122.
• Pandian Ramesh,S. Sundaresan, Pon. Sathya Moorthy, M. Balasubramanian and M.N. Ponnuswamy. (2014). “Response to comments on Structural studies of hemoglobin from pisces species Shortfin mako shark (Isurus oxyrinchus) at 1.9Å resolution, P. Ramesh et al., 2013. Journal of Synchrotron Radiation, 20, 843-847”. Journal of Synchrotron Radiation, 21, 834. (Corresponding author)
• Ramesh, P. Edayadulla, N. Vinodhkumar, V. Peters, Günther H. &  Ponnuswamy, M. N. (2014). Chemistry Central Journal 8, 34:1-7.
• Duy Duc Nguyen, Ramesh Pandian, Doyoun Kim, Sung Chul Ha, Hye-Jin Yoon, Kap Sun Kim, Kyung Hee Yun, Jin-Hahn Kim & Kyeong Kyu Kim. (2014). Structural and kinetic bases for the metal preference of the M18 aminopeptidase from Pseudomonas aeruginosa. Biochem. and Biophy. Res. Comm. 447, 101-107.
• Ju, H., Pandian, R., Kim, K., Kim, K.K. & Kim, T.D. (2014). Crystallization and preliminary X-ray analysis of a novel type of lipolytic hydrolase from Bacillus licheniformis Acta Cryst. F70, 473-475. (First two authors are equally contributed).
• Pandian Ramesh,S. Sundaresan, Pon. Sathya Moorthy, M. Balasubramanian and M.N. Ponnuswamy. (2013). Structural studies of hemoglobin from pisces species Shortfin mako shark (Isurus oxyrinchus) at 1.9Å resolution, Journal of Synchrotron Radiation, 20, 843-847. (Corresponding author)
• Nandakumar, Prakasam Thirumurugan, Paramasivan T. Perumal, P. Vembu, M. N. Ponnuswamy and P. Ramesh (2010). Bioorganic & Medicinal Chemistry Letters 20, 4252–4258.
• N. Gunasekaran, P. Ramesh, M.N. Ponnuswamy and R. Karvembu (2011).  Dalton Trans. 40, 12519-12526.
• S. Sundaresan, P. Ramesh, K. Sivakumar & M. N. Ponnuswamy (2009). Purification, crystallization and preliminary X-ray analysis of haemoglobin from ostrich (Struthio camelus). Acta Cryst. F65, 681-683.
• Loganayaki, V. Siva Shankar, P. Ramesh, M.N Ponnuswamy, P Murugakoothan. (2011). Growth and Characterization of Guanidinium Trifluoroacetate–Second Harmonic Generation from a Centrosymmetric Crystal. Journal of Minerals & Materials Characterization & Engineering 10 (9), 843-853.
• Ravichandran, R. Manikannan, S. Muthusubramanian, P. Ramesh & M. N. Ponnuswamy (2013). 4-(2-Hydroxyphenyl)-3,5-dithiaheptanedioic acid. Acta Cryst. E69, o893.
• Ravichandran, P. Sakthivel, P. Ramesh, S. Ponnuswamy & M. N. Ponnuswamy (2012). 1-Formyl-c-3,t-3-dimethyl-r-2,c-6-diphenylpiperidin-4-one. Acta Cryst. E68, o870.
• R. Velmurugan, M. Sekar, A. V. Vijayasankar, P. Ramesh & M. N. Ponnuswamy (2011). 6-Bromo-2-[(E)-thiophen-2-ylmethylidene]-2,3,4,9-tetrahydro-1H-carbazol-1-one. Acta Cryst. E67, o3271.
• M. Sekar, R. Velmurugan, A. Chandramohan, P. Ramesh & M. N. Ponnuswamy (2011). 2-(6-Methyl-2,3,4,9-tetrahydro-1H-carbazol-1-ylidene)propanedinitrile. Acta Cryst. E67, o3270. 
• R. Velmurugan, M. Sekar, A. V. Vijayasankar, P. Ramesh & M. N. Ponnuswamy (2011). 6-Bromo-2-(3-phenylallylidene)-2,3,4,9-tetrahydro-1H-carbazol-1-one. Acta Cryst. E67, o3269.
• Sekar, R. Velmurugan, A. V. Vijayasankar, P. Ramesh & M. N. Ponnuswamy (2011). 2-(6-Chloro-2,3,4,9-tetrahydro-1H-carbazol-1-ylidene)propanedinitrile. Acta Cryst. E67, o3268.
• S. Mohan, S. Ananthan, P. Ramesh, D. Saravanan & M. N. Ponnuswamy (2011). N'-[(E)-2-Chlorobenzylidene]-2-[(1,3,4-thiadiazol-2-yl)sulfanyl]acetohydrazide. Acta Cryst. E67, o2612. 
• Sugumar, N. Edayadulla, P. Ramesh, P. Ramesh & M. N. Ponnuswamy (2011). Diethyl 1,1-dioxo-3,5-bis(pyridin-2-yl)-16,4-thiomorpholine-2,6-dicarboxylate. Acta Cryst. E67, o305. 
• Velmurugan, M. Sekar, A. Chandramohan, P. Ramesh & M. N. Ponnuswamy (2010). 2-(1,2,3,4-Tetrahydro-9H-carbazol-1-ylidene)propanedinitrile. Acta Cryst. E66, o2965. 
• Chandraprakash, P. Ramesh, K. Ravichandran, P. S. Mohan & M. N. Ponnuswamy (2010). 2-Methoxyquinoline-3-carbaldehyde. Acta Cryst. E66, o2510. 
• Uvarani, P. Ramesh, K. Ravichandran, P. S. Mohan & M. N. Ponnuswamy (2010). 8-Methoxy-3,3,5-trimethyl-3,11-dihydropyrano[3,2-a]carbazole. Acta Cryst. E66, o1581. 
• S. Sivaramkumar, R. Velmurugan, M. Sekar, P. Ramesh & M. N. Ponnuswamy (2010). Benzamide-picric acid (1/1). Acta Cryst. E66, o1820. 
• S. Sivaramkumar, R. Velmurugan, M. Sekar, P. Ramesh & M. N. Ponnuswamy (2010). 2-Aminopyridinium picrate. Acta Cryst. E66, o1821.
• Ravichandran, P. Ramesh, P. Sakthivel, S. Ponnuswamy & M. N. Ponnuswamy (2010). 1-Formyl-t-3,t-5-dimethyl-r-2,c-6-diphenylpiperidin-4-one. Acta Cryst. E66, o1505. 
• Ravichandran, P. Ramesh, M. Rani, S. Kabilan & M. N. Ponnuswamy (2010). 1-Chloroacetyl-2,6-bis(2-chlorophenyl)-3,5-dimethylpiperidin-4-one oxime. Acta Cryst. E66, o1506. 
• Mohan, P. Ramesh, D. Saravanan & M. N. Ponnuswamy (2010). 1-{[(Cyclo hexyloxy)carbonyl]oxy}ethyl 3-{[2'-(2-ethyl-2H-tetrazol-5-yl)biphenyl-4-yl]methyl}-2-oxo-2,3-dihydro-1H-benzimidazole-4-carboxylate. Acta Cryst. E66, o998. 
• Ramesh, R. Akalya, A. Chandramohan & M. N. Ponnuswamy (2010). 4-tert-Butylpyridinium picrate. Acta Cryst. E66, o999. 
• Ramesh, R. Akalya, A. Chandramohan & M. N. Ponnuswamy (2010). 4-Aminopyridinium picrate. Acta Cryst. E66, o1000. 
• Revathi, M. Sankaran, P. Ramesh, P. S. Mohan & M. N. Ponnuswamy (2010). 4-Hydroxy-3-(1'-methyl-2-oxo-4'-phenylspiro[indoline-3,2'-pyrrolidine]-3'-ylcarbonyl)quinolin-2(1H)-one. Acta Cryst. E66, o952. 
• S. Sundaresan, P. Ramesh, N. Arumugam, R. Raghunathan & M. N. Ponnuswamy (2010). Ethyl 3-[1-(4-methoxyphenyl)-4-oxo-3-phenylazetidin-2-yl]-2-nitro-1-phenyl-2,3,10,10a-tetrahydro-1H,5H-pyrrolo[1,2-b]isoquinoline-10a-carboxylate. Acta Cryst. E66, o646. 
• Ravichandran, P. Ramesh, P. Sakthivel, S. Ponnuswamy & M. N. Ponnuswamy (2010). 1-Dichloroacetyl-r-2,c-6-bis(4-methoxyphenyl)-t-3-methylpiperidin-4-one. Acta Cryst. E66, o262. 
• Ravichandran, P. Ramesh, C. Neeladevi, S. Ponnuswamy & M. N. Ponnuswamy (2010). 1-Dichloroacetyl-r-2,c-6-bis(4-methoxyphenyl)-t-3,t-5-dimethylpiperidin-4-one. Acta Cryst. E66, o263. 
• Ravichandran, P. Ramesh, P. Jeganathan, S. Ponnuswamy & M. N. Ponnuswamy (2010). 1-Chloroacetyl-3-isopropyl-r-2,c-6-diphenylpiperidin-4-one. Acta Cryst. E66, o276-o277. 
• Ramesh, R. Manikannan, S. Muthusubramanian, K. Ravichandran & M. N. Ponnuswamy (2010). (E)-3-(4-Bromophenyl)-3-[3-(4-bromophenyl)-1H-pyrazol-1-yl]prop-2-enal. Acta Cryst. E66, o279.
• Ravichandran, P. Ramesh, C. M. Mahalakshmi, K. Anbalagan & M. N. Ponnuswamy (2009). Chloridobis(ethane-1,2-diamine)(4-methylaniline)cobalt(III) dichloride monohydrate. Acta Cryst. E65, m1458-m1459. 
• Ramesh, R. Manikannan, S. Muthusubramanian, S. S. Sundaresan & M. N. Ponnuswamy (2009). 3-(4-Chlorophenyl)-1-[(E)-1-(4-chlorophenyl)-2-(4-methylphenylsulfanyl)ethenyl]-4-(4-methylphenylsulfanyl)-1H-pyrazole. Acta Cryst. E65, o2881-o2882. 
• Ravichandran, P. Ramesh, P. Sakthivel, S. Ponnuswamy & M. N. Ponnuswamy (2009). 1-Chloroacetyl-r-2,c-6-bis(4-methoxyphenyl)-t-3-methylpiperidin-4-one. Acta Cryst. E65, o2883. 
• Ravichandran, P. Ramesh, S. Sethuvasan, S. Ponnuswamy & M. N. Ponnuswamy (2009). c-3,t-3-Dimethyl-r-2,c-7-diphenyl-1,4-diazepan-5-one. Acta Cryst. E65, o2884. 
• Ravichandran, P. Ramesh, S. Sethuvasan, S. Ponnuswamy & M. N. Ponnuswamy (2009). t-3-Ethyl-r-2,c-7-bis(4-methoxyphenyl)-1,4-diazepan-5-one. Acta Cryst. E65, o2885-o2886. 
• Ravichandran, P. Ramesh, M. Tamilselvan, K. Anbalagan & M. N. Ponnuswamy (2009). (Benzylamine)chloridobis(ethane-1,2-diamine)cobalt(III) dichloride hemihydrate. Acta Cryst. E65, m1174-m1175. 
• Ravichandran, P. Sakthivel, S. Ponnuswamy, P. Ramesh & M. N. Ponnuswamy (2009). 5-Chloroacetyl-4-methyl-2,3,4,5-tetrahydro-1H-1,5-benzodiazepin-2-one. Acta Cryst. E65, o2361.
• Ravichandran, P. Sakthivel, S. Ponnuswamy, P. Ramesh & M. N. Ponnuswamy (2009). 4-Methyl-2-oxo-2,3,4,5-tetrahydro-1H-1,5-benzodiazepine-5-carbaldehyde. Acta Cryst. E65, o2362. 
• Ramesh, S. S. Sundaresan, N. V. Lakshmi, P. T. Perumal & M. N. Ponnuswamy (2009). 1'-Methyl-2,2''-dioxoindoline-3-spiro-2'-pyrrolidine-3'-spiro-3''-indoline-4',4'-dicarbonitrile. Acta Cryst. E65, o1945. 
• Aravindhan, S. Ponnuswamy, M. Jamesh, P. Ramesh & M. N. Ponnuswamy (2009). 1-Acetyl-c-3,t-3-dimethyl-r-2,c-6-diphenylpiperidin-4-one. Acta Cryst. E65, o1974.
• Aravindhan, S. Ponnuswamy, J. Umamaheswari, P. Ramesh & M. N. Ponnuswamy (2009). 1-Benzoyl-c-3,t-3-dimethyl-r-2,c-6-diphenylpiperidin-4-one. Acta Cryst. E65, o1975.
• Ramesh, S. S. Sundaresan, N. V. Lakshmi, P. T. Perumal & M. N. Ponnuswamy (2009). 3'-Benzyloxy-3-hydroxy-3,3'-bi-1H-indole-2,2'(3H,3'H)-dione monohydrate. Acta Cryst. E65, o994.
• Ramesh, S. S. Sundaresan, P. Thirumurugan, P. T. Perumal & M. N. Ponnuswamy (2009). 4-(4-Chlorophenyl)-6-methoxy-2,2'-bipyridine-5-carbonitrile. Acta Cryst. E65, o995.
• Ramesh, S. S. Sundaresan, P. Thirumurugan, P. T. Perumal & M. N. Ponnuswamy (2009). 4-(2,4-Dichlorophenyl)-6-(1H-indol-3-yl)-2,2'-bipyridine-5-carbonitrile. Acta Cryst. E65, o996-o997.
• Ramesh, A. Subbiahpandi, P. Thirumurugan, P. T. Perumal & M. N. Ponnuswamy (2009). 2-(1H-indol-3-ylcarbonyl)acetonitrile. Acta Cryst. E65, o447.
• Ramesh, A. Subbiahpandi, P. Thirumurugan, P. T. Perumal & M. N. Ponnuswamy (2009). 4-(4-Bromophenyl)-6-(1H-indol-3-yl)-2,2'-bipyridine-5-carbonitrile. Acta Cryst. E65, o450. 
• Sathyanarayanan, P. Ramesh, R. Murugan, S. S. Narayanan & M. N. Ponnuswamy (2008). Ethyl 4'-ethenyl-2'-oxo-4-phenyl-2-(3,4,5-trimethoxyphenyl)spiro[pyrrolidine-3,3'-indoline]-5-carboxylate monohydrate. Acta Cryst. E64, o2052-o2053. 
• Ramesh, A. Subbiahpandi, R. Manikannan, S. Muthusubramanian & M. N. Ponnuswamy (2008). 4-(4-Chlorophenylsulfanyl)-1-[(E)-2-(4-chlorophenylsulfanyl)-1-phenylethenyl]-3-phenyl-1H-pyrazole. Acta Cryst. E64, o2054-o2055. 
• Ramesh, R. Venkatesan, R. Manikannan, S. Muthusubramanian & M. N. Ponnuswamy (2008). 1-(2,4-Dinitrophenyl)-3-(4-methylphenyl)-4-phenylsulfanyl-1H-pyrazole. Acta Cryst. E64, o2093. 
• Ramesh, A. Subbiahpandi, R. Manikannan, S. Muthusubramanian & M. N. Ponnuswamy (2008). 4-(Cyclohexylsulfanyl)-1-[(E)-2-(cyclohexylsulfanyl)-1-phenylethenyl]-3-phenyl-1H-pyrazole. Acta Cryst. E64, o2132-o2133. 
• Ramesh, A. Subbiahpandi, R. Manikannan, S. Muthusubramanian & M. N. Ponnuswamy (2008). (E)-3-(4-Methylphenyl)-3-[3-(4-methylphenyl)-1H-pyrazol-1-yl]-2-propenal. Acta Cryst. E64, o2243. 
• Ramesh, A. Subbiahpandi, P. Thirumurugan, P. T. Perumal & M. N. Ponnuswamy (2008). 4-(2,4-Dichlorophenyl)-2-(1H-indol-3-yl)-6-(2-pyridyl)-1,4-dihydropyridine-4-carbonitrile. Acta Cryst. E64, o1891. 
• Ramesh, A. Subbiahpandi, R. Manikannan, S. Muthusubramanian & M. N. Ponnuswamy (2008). 1-[(E)-2-Formyl-1-(4-methylphenyl)ethenyl]-3-(4-methylphenyl)pyrazole-4-carbaldehyde. Acta Cryst. E64, o1889. 
• Ramesh, A. Subbiahpandi, R. Manikannan, S. Muthusubramanian & M. N. Ponnuswamy (2008). 3-Cyclohexylsulfanyl-2-(4-methylphenyl)-5,7-dinitro-1H-indole. Acta Cryst. E64, o1890. 
• Ramesh, A. Subbiahpandi, P. Thirumurugan, P. T. Perumal & M. N. Ponnuswamy (2008). 4-(2,4-Dichlorophenyl)-2-(1H-indol-3-yl)-6-methoxypyridine-3,5-dicarbonitrile. Acta Cryst. E64, o1892. 
• Sundaresan, P. Ramesh, N. Arumugam, R. Raghunathan & M. N. Ponnuswamy (2008). Methyl 2-benzyl-5-[1-(4-methoxyphenyl)-4-oxo-3-phenylazetidin-2-yl]-4-nitro-3-phenylpyrrolidine-2-carboxylate. Acta Cryst. E64, o1993. 
• Sundaresan, P. Ramesh, N. Arumugam, R. Raghunathan & M. N. Ponnuswamy (2008). Ethyl 1-(4-chlorophenyl)-3-[1-(4-methoxyphenyl)-4-oxo-3-phenylazetidin-2-yl]-2-nitro-2,3,10,10a-tetrahydro-1H,5H-pyrrolo[1,2-b]isoquinoline-10a-carboxylate. Acta Cryst. E64, o2042. 
• Ramesh, A. SubbiahPandi, P. Jothi, C. Revathi & A. Dayalan (2008). Dichlorido(dimethylglyoximato-2N,N')(dimethylglyoxime-2N,N')cobalt(III). Acta Cryst. E64, m300-m301. 
• Ramesh, S. Murugavel, A. S. Pandi, R. Murugan & S. S. Narayanan (2007). (2E)-3-(2-Chlorophenyl)-1-[1'-(2-chlorophenyl)indoline-3-spiro-3'-perhydropyrrolo[1,2-a]indol-2'-yl]prop-2-en-1-one. Acta Cryst. E63, o4851. 
• Ramesh, S. Murugavel, A. S. Pandi, R. Murugan & S. S. Narayanan (2007). Ethyl 3-phenyl-4-[(Z)-3-phenylacryloyl] 5-(3,4,5-trimethoxyphenyl)pyrrolidine-2-carboxylate. Acta Cryst. E63, o4873. 
• Ramesh, S. Murugavel, A. SubbiahPandi, R. Murugan & S. S. Narayanan (2007). 3-(4-Methyl-1,3-thiazol-5-yl)-1-[1'-(4-methyl-1,3-thiazol-5-yl)-2-oxo-2,3,2',3',5',6',7',7a'-octahydro-1H-indole-3-spiro-3'-1H-pyrrolizin-2'-yl]prop-2-en-1-one. Acta Cryst. E63, o4106-o4107. 
• Murugavel, P. Ramesh, A. SubbiahPandi, E. Ramesh & R. Raghunathan (2007). 6-[(4-Bromophenyl)iminomethyl]-1,3-dimethyl-7-(2-methylpropenyl)-1,2,3,4-tetrahydro-7H-pyrrolo[2,3-d]pyrimidine-2,4-dione. Acta Cryst. E63, o4108. 
• Murugavel, P. Ramesh, A. SubbiahPandi, E. Ramesh & R. Raghunathan (2007). Methyl 1'-(2-hydroxy-1,3-dioxoindan-2-yl)-1,3-dioxoindane-2-spiro-3'-pyrrolizidine-1'-carboxylate. Acta Cryst. E63, o3610. 
• Ramesh, S. Murugavel, A. SubbiahPandi, E. Ramesh & R. Raghunathan (2007). Methyl 1'-(3-hydroxy-2-oxo-2,3-dihydro-1H-indol-3-yl)-2-oxo-2,3-dihydro-1H-indole-3-spiro-3'-pyrrolizidine-1'-carboxylate. Acta Cryst. E63, o3625-o3626.    

Protein Data Bank (PDB) entries:

•  PDB ID:  8CI7

 Apo-crystal structure of a wild-type South African HIV-1 subtype C protease at 2.4 angstrom

Authors: Dlamini, N.P., Pandian, R., Onisuru, O., Achilonu, I.A., Sayed, Y.

• PDB ID:  8BHZ

The apo-crystal structure of a variant form of the 28-kDa Schistosoma haematobium glutathione transferase in orthorhombic form

Authors: Pandian, R., Mfeka, S.M., Onisuru, O., Sayed, Y., Achilonu, I.A.

• PDB ID:  8ALS

The apo-crystal structure of a variant form of the 28-kDa Schistosoma haematobium glutathione transferase

Authors: Pandian, R., Makumbe, H.H., Sayed, Y., Achilonu, I.A.

• PDB ID: 8AII

High-Resolution Crystal Structure of Enterococcus faecium Nicotinate Nucleotide Adenylyltransferase Complexed with Adenine

Authors: Pandian, R., Jeje, O.A., Sayed, Y., Achilonu, I.A.

• PDB ID: 8AIH

Crystal Structure of Enterococcus faecium Nicotinate Nucleotide Adenylyltransferase at 1.9 Angstroms Resolution

Authors: Pandian, R., Jeje, O.A., Sayed, Y., Achilonu, I.A.

• PDB ID: 6ZMY

Crystal structure of hemoglobin from turkey (Meleagiris gallopova) crystallized in monoclinic form at 1.66 Angstrom resolution

Authors:  Pandian, R., Shobana, N., Sundaresan, S.S., Thangaraj, V., Sayed, Y., Ponnuswamy, M.N.

• PDB ID: 6ZMX

Crystal structure of hemoglobin from turkey (Meleagiris gallopova) crystallized in orthorhombic form at 1.4 Angstrom resolution

Authors: Pandian, R., Shobana, N., Sundaresan, S.S., Sayed, Y., Ponnuswamy, M.N.

• PDB ID: 6Y1E

Crystal structure of human glutathione transferase P1-1 (hGSTP1-1) that was co-crystallised in the presence of indanyloxyacetic acid-94 (IAA-94)

Authors: Pandian, R., Worth, R., Thangaraj, V., Sayed, Y., Dirr, H.W.

• PDB ID: 6RWD

Crystal structure of SjGST in complex with GSH and ellagic acid at 1.53 Angstrom resolution

Authors:  Olfsen, J., Pandian, R., Sayed, Y., Dirr, H.W., Achilonu, I.A.

• PDB ID: 6I45

Crystal structure of I13V/I62V/V77I South African HIV-1 subtype C protease containing a D25A mutation

Authors:  Sherry, D., Pandian, R., Achilonu, I.A., Dirr, H.W., Sayed, Y.

• PDB ID: 4TX1

The crystal structure of carbohydrate acetylesterase family member from Sinorhizobium meliloti

Authors: Kim, K., Kim, S.S., Pandian, R., Ngo, T.D.

• PDB ID: 4OIW

Structural and kinetic bases for the metal preference of the M18 aminopeptidase from Pseudomonas aeruginosa.

Authors: Nguyen, D.D., Pandian, R., Kim, D.Y., Ha, S.C., Yoon, H.J., Kim, K.S., Yun, K.H., Kim, J.H., Kim, K.K.

• PDB ID: 4OID

Structural and kinetic bases for the metal preference of the M18 aminopeptidase from Pseudomonas aeruginosa.

Authors: Nguyen, D.D., Pandian, R., Kim, D.Y., Ha, S.C., Yoon, H.J., Kim, K.S., Yun, K.H., Kim, J.H., Kim, K.K.

• PDB ID: 4NJR

Structural and kinetic bases for the metal preference of the M18 aminopeptidase from Pseudomonas aeruginosa.

Authors: Nguyen, D.D., Pandian, R., Kim, D.Y., Ha, S.C., Yoon, H.J., Kim, K.S., Yun, K.H., Kim, J.H., Kim, K.K.

• PDB ID: 3WT4

Structural and kinetic bases for the metal preference of the M18 aminopeptidase from Pseudomonas aeruginosa.

Authors: Nguyen, D.D., Pandian, R., Kim, D.Y., Ha, S.C.,  Yoon, H.J.,  Kim, K.S.,  Yun, K.H.,  Kim, J.H.,  Kim, K.K.

• PDB ID: 4NJQ

Structural and kinetic bases for the metal preference of the M18 aminopeptidase from Pseudomonas aeruginosa.

Authors: Nguyen, D.D., Pandian, R.,  Kim, D.Y.,  Ha, S.C.,  Yoon, H.J.,  Kim, K.S.,  Yun, K.H.,  Kim, J.H.,  Kim, K.K.

• PDB ID: 3HRW

         Crystal structure of hemoglobin from mouse (Mus musculus)at 2.8 Å.

         Authors: Sundaresan, S.S., Ramesh, P. and Ponnuswamy, M.N.

• PDB ID: 3GOU

         Crystal structure of dog (Canis familiaris) hemoglobin.                   

         Authors: Sundaresan, S.S.,   Ramesh, P.,   Thenmozhi, M. and Ponnuswamy, M.N.

• PDB ID: 3FS4

Crystal structure determination of Ostrich hemoglobin at 2.2 Å resolution.

Authors: Sundaresan, S.S.,   Ramesh, P.,   Sivakumar, K. and Ponnuswamy, M.N.

•  PDB ID: 3MKB

Crystal structure of shortfin mako shark (Isurus  oxyrinchus) hemoglobin at 1.9Å resolution.

Authors: Ramesh, P., Sundaresan, S.S., Sathya Moorthy, Pon., Balasubramanian,  M. and Ponnuswamy, M.N. 

•  PDB ID: 3K8B

X ray crystal structure of turkey (Meleagiris gallopova) hemoglobin at 2.3 Å resolution.

 Authors: Ramesh, P.,  Sundaresan, S. and Ponnuswamy, M.N.

 

• Valli, A., Achilonu, I., 2022. Comparative structural analysis of the human and Schistosoma glutathione transferase dimer interface using selective binding of bromosulfophthalein. Proteins: Structure, Function and Bioinformatics.
• Otun, S., Escrich, A., Achilonu, I., Rauwane, M., Alexis, J., Lerma-Escalera, Morones-Ramírez, J.R., Rios-Solis, L., 2022. The future of cassava in the era of biotechnology in Southern Africa. Critical Reviews in Biotechnology, 1-19.
• Daya, T., Jeje, O., Maake, R., Aloke, C., Khoza, T., Achilonu, I., 2022. Expression, Purification, and Biophysical Characterization of Klebsiella Pneumoniae Nicotinate Nucleotide Adenylyltransferase. The Protein Journal, 1-16.
• Othman, H., Messaoud, H.B., Khamessi, O., Ben-Mabrouk, H., Ghedira, K., Bharuthram, A., Treurnicht, F., Achilonu, I., Sayed, Y., Srairi-Abid, N., 2022. SARS-CoV-2 spike protein unlikely to bind to integrins via the Arg-Gly-Asp (RGD) motif of the receptor binding domain: evidence from structural analysis and microscale accelerated molecular dynamics. Frontiers in Molecular Biosciences, 9.
• Padi, N., Akumadu, B.O., Faerch, O., Aloke, C., Meyer, V., Achilonu, I., 2021. Engineering a Pseudo-26-kDa Schistosoma Glutathione Transferase from bovis/haematobium for Structure, Kinetics, and Ligandin Studies. Biomolecules, 11, 1844.
• Pooe, K., Worth, R., Iwuchukwu, E.A., Dirr, H.W., Achilonu, I., 2021. An empirical and theoretical description of Schistosoma japonicum glutathione transferase inhibition by bromosulfophthalein and indanyloxyacetic acid 94. Journal of Molecular Structure 1223, 128892.
• Jeje, O., Maake, R., van Deventer, R., Esau, V., Iwuchukwu, E.A., Meyer, V., Khoza, T., Achilonu, I., 2021. Effect of Divalent Metal Ion on the Structure, Stability and Function of Klebsiella pneumoniae Nicotinate-Nucleotide Adenylyltransferase: Empirical and Computational Studies. International Journal of Molecular Sciences 23, 116.
• Motiwala, T., Akumadu, B.O., Zuma, S., Mfeka, M.S., Chen, W., Achilonu, I., Syed, K., Khoza, T., 2021. Caseinolytic Proteins (Clp) in the Genus Klebsiella: Special Focus on ClpK. Molecules 27, 200.
• Achilonu, I., Iwuchukwu, E.A., Achilonu, O.J., Fernandes, M.A., Sayed, Y., 2020. Targeting the SARS-CoV-2 main protease using FDA-approved Isavuconazonium, a P2–P3 α-ketoamide derivative and Pentagastrin: An in-silico drug discovery approach. Journal of Molecular Graphics and Modelling, 101, 107730.
• Akumadu, B.O., Pandian, R., Olfsen, J., Worth, R., Thulo, M., Mentor, T., Fanucchi, S., Sayed, Y., Dirr, H.W., Achilonu, I., 2020. Molecular basis of inhibition of Schistosoma japonicum glutathione transferase by ellagic acid: Insights into biophysical and structural studies. Molecular and Biochemical Parasitology, 240, 111319.
• Mfeka, M.S., Martínez-Oyanedel, J., Chen, W., Achilonu, I., Syed, K., Khoza, T., 2020. Comparative analyses and structural insights of new class glutathione transferases in Cryptosporidium species. Scientific Reports 10, 1-12.
• Keshav, V., Achilonu, I., Dirr, H., Kondiah, K., 2019. Recombinant expression and purification of a functional bacterial metallo-chaperone PbrD-fusion construct as a potential biosorbent for Pb (II). Protein Expression and Purification 158, 27-35.
• Williams, A., Basson, A., Achilonu, I., Dirr, H.W., Morris, L., Sayed, Y., 2019. Double trouble? Gag in conjunction with double insert in HIV protease contributes to reduced DRV susceptibility. Biochemical Journal 476, 375-384.
• Zondagh, J., Basson, A.E., Achilonu, I., Morris, L., Dirr, H.W., Sayed, Y., 2019. Drug susceptibility and replication capacity of a rare HIV-1 subtype C protease hinge region Antiviral Therapy 24, 333-342.

• Thulo M., Rabie, M.A., Pahad, N., Donald, H.L., Blane A.A., Perumal, C.M., Penedo, J.C. and Fanucchi, S. (2020) The influence of various regions of the FOXP2 sequence on its structure and DNA-binding function. Bioscience Reports (2020) 00 1-13
• Akumadu, B.O., Pandian, R., Olfsen, J., Worth, R., Thulo, M., Mentor, T., Fanucchi, S., Sayed, Y., Dirr, H.W., Achilonu, I (2020) Molecular basis of inhibition of Schistosoma japonicum glutathione
• Schnetler, R., Fanucchi, S., Moldoveanu, T. and Koorsen, G. (2020) Linker Histone H1.3 Directly activates BAK through the K/RVVKP Motif on the C-Terminal domain. Biochemistry, 2020, 59(36), pp. 3332–3346
• Morris, G., Pahad, N., Dirr, H. and Fanucchi, S. (2018) A conserved cation binding site in the DNA binding domain of forkhead box transcription factors regulates DNA binding by FOXP2. Archives of Biochemistry and Biophysics, August 2018 (657) 56-64
• Blane, A., Dirr, H. and Fanucchi, S. (2018) A phosphomimetic study implicates Ser557 in regulation of FOXP2 DNA binding. Protein Journal (37) 311-323
• Morris, G., Stoychev, S., Naicker, P., Dirr, H. and Fanucchi, S. (2018) The forkhead domain hinge -loop plays a pivotal role in DNA binding and transcriptional activity of FOXP2. Biological chemistry (399) 881-893 

• Webb, H., Steeb, O., Blane, A., Rotherham, L., Aron, S., Machanick, P., Dirr, H. and Fanucchi, S.The FOXP2 forkhead domain binds to a variety of DNA sequences with different rates and affinities. Journal of Biochemistry162, 45-54 
• Morris, G. and Fanucchi, S.A key evolutionary mutation enhances DNA binding of the FOXP2 forkhead domain. Biochemistry 55(13), 1959-1967 
• Blane, A. and Fanucchi, S.The effect of pH on the DNA binding affinity of the FOXP2 forkhead domain. Biochemistry 54(25), 4001-4007 
• Perumal, K., Dirr, H.W. and Fanucchi, S. Replacement of Tyr540 at the dimer interface with a phenylalanine increases the dimerisation potential of the FOXP2 forkhead domain. The protein journal 34, 111-121 
• Cross, M.O., Fernandes, M.A., Dirr, H. W. and Fanucchi, S.Glutamate 85 and Glutamate 228 Contribute to the pH-Response of the Soluble Form of Chloride Intracellular Channel 1 Molecular and Cellular Biochemistry 398,83-93 
• Peter, B., Fanucchi, S. and Dirr, H.W.A conserved cationic motif enhances membrane binding and insertion of the chloride intracellular channel protein 1 transmembrane domain European Biophysics Journal 43, 405-414 
• Peter, B., Polyansky, A., Fanucchi, S. and Dirr, H.W. (2014) A Lys−Trp Cation−π Interaction Mediates the Dimerization and Function of the Chloride Intracellular Channel Protein 1 Transmembrane Domain. Biochemistry 53: 57-67
• Naicker, P. Achilonu, I., Fanucchi, , Fernandes, M., Ibrahim, MA., Dirr, HW., Soliman, M.E. and Sayed, Y. (2013) Structural insights into the South African HIV-1 subtype C protease: impact of hinge region dynamics and flap flexibility in drug resistance. J Biomol Struct Dyn. 31(12): 1370-1380
• Peter, B., Ngubane, N.C., Fanucchi, S. and Dirr, H.W. (2013) Membrane mimetics induce helix formation and oligomerization of the chloride intracellular channel protein 1 transmembrane domain. Biochemistry 52(16):2739-49
• Derryn Legg-E'Silva, Ikechukwu Achilonu, Sylvia Fanucchi, Stoyan H. Stoychev, Manuel Antonio Fernandes, and Heini W Dirr (2012) Role of Arginine 29 and Glutamic acid 81 Interactions in the Conformational Stability of Human Chloride Intracellular Channel 1. Biochemistry 51(40): 7854-62.
• Achilonu I, Fanucchi S, Cross M, Fernandes M, Dirr HW (2012) Role of individual histidines in the pH-dependent global stability of human chloride intracellular channel 1. Biochemistry 51, 995-1004
• Parbhoo N, Stoychev SH, Fanucchi S, Achilonu I, Adamson RJ, Fernandes M, Gildenhuys S, Dirr HW. (2011) A Conserved Domain Interaction is a Determinant of Folding Cooperativity in the GST Fold. Biochemistry 50: 7067-7075.
• Balchin, D., Fanucchi, S., Achilonu, I., Adamson, R.J., Burke, J., Fernandes, M., Gildenhuys, S. and Dirr, H.W. (2010) Stability of the Domain Interface Contributes Towards the Catalytic Function at the H-site of Class Alpha Glutathione Transferase A1-1. Biophys. Acta 1804, 2228-2233 
• Achilonou, I., Gildenhuys, S., Fisher, L., Burke, J., Fanucchi, S., Sewell, B.T., Fernandes, M. and Dirr, H.W. (2010) The role of a topologically conserved isoleucine in glutathione transferase structure, stability and function. Acta Cryst, F66, 776-780
• Stoychev, S.H., Nathaniel, C., Fanucchi, S., Brock, M., Li, S., Asmus, K., Woods, V.L. Jr. and Dirr, H.W. (2009) Structural Dynamics of Soluble Chloride Intracellular Channel Protein CLIC1 Examined by Amide Hydrogen-Deuterium Exchange Mass Spectrometry. Biochemistry 48, 8413 – 8421 
• Fanucchi, S., Adamson, R.J. and Dirr, H.W. (2008) Formation of an Unfolding Intermediate State of Soluble Chloride Intracellular Channel Protein CLIC1 at Acidic pH. Biochemistry 47, 11674 – 11681 

• Othman, H., Messaoud, H.B., Khamessi, H.B., Ben-Mabrouk, H., Ghedira, K., Bharuthram, A., Treurnicht, F., Achilonu, I., Sayed, Y, and Srairi-Abid, N. (2022). SARS-CoV-2 Spike Protein Unlikely to Bind to Integrins via the Arg-Gly-Asp (RGD) Motif of the Receptor Binding Domain: Evidence From Structural Analysis and Microscale Accelerated Molecular Dynamics. Frontiers in Molecular Biosciences, Volume 9, 1-11, Article 834857, 14 February 2022 https://doi.org/10.3389/fmolb.2022.834857. IF=5,246 
• Sherry, D., Worth, R, and Sayed, Y. (2021). Elasticity-associated functionality and inhibition of the HIV protease. Protein Reviews. Advances in Experimental Medicine and Biology, vol 1371.  Springer, Cham. https://doi.org/10.1007/5584_2021_655.
• Sherry, D., Worth, R., Sheik Ismail, Z and Sayed, Y. (2021). Cantilever-centric mechanism of cooperative non-active site mutations in HIV protease: Implications for flap dynamic. Journal of Molecular Graphics and Modelling, 106, 107931, 1-19. DOI: https://doi.org/10.1016/j.jmgm.2021.107931. IF=2,079
• Pandian, R., Selvarajan, S. S., Nagaraj, S., Thangaraj, V., Kandasamy, S., Sayed, Y, and Mondikalipudur, N.G.P. (2021). Structural studies of hemoglobin from two flightless birds, ostrich and turkey: insights into their differing oxygen-binding properties. Acta Cryst. D77, 690–702 DOI: https://doi.org/10.1107/S2059798321003417. IF=5,266
• Selvarajan, S.S., Pandian, R., Nagaraj, S., Thangaraj, V., Sayed, Y, and Mondikalipudur, N.G.P. (2021). Crystal structure of hemoglobin from mouse (Mus musculus) compared with those from other small animals and humans. Acta Cryst. F77, 113–120. DOI: https://doi.org/10.1107/S2053230X2100306X. IF=1,9
• Odame, F., Hosten, E., Krause, J., Isaacs, M., Hoppe, H., Khanye, S.D., Sayed, Y., Frost, F., Lobb, K and Tshentu, Z. (2020). Synthesis, Characterization and Biological Activity of Some Dithiourea Derivatives. Acta Chim. Slov. 67, 764–777. DOI: 10.17344/acsi.2019.5689. IF = 1,104
• Akumadu, B. O., Pandian, R., Olfsen, J., Worth, R., Thulo, M., Mentor, T., Fanucchi, S., Sayed, Y., Dirr, H. W., and Achilonu, I. (2020). Molecular basis of inhibition of Schistosoma japonicum glutathione transferase by ellagic acid: insights into biophysical and structural studies. Molecular and Biochemical Parasitology.org/10.1016/j.molbiopara.2020.111319. IF = 1,571
• Achilonu, I., Iwuchukwu, E. A., Achilonu, O. J., Fernandes, M. A., and Sayed, Y. (2020). Targeting the SARS-CoV-2 main protease using FDA-approved Isavuconazonium, a P2-P3 α-ketoamide derivative and Pentagastrin: An in-silico drug discovery approach. Journal of Molecular Graphics and Modelling. https://doi.org/10.1016/j.jmgm.2020.107730. IF = 2,079
• Sherry, D., Worth, R., and Sayed, Y. (2020). Two-step preparation of highly pure, soluble HIV protease from inclusion bodies recombinantly expressed in Escherichia coli. Current Protocols in Protein Science, 100, doi: 10.1002/cpps.106. IF = 1,92
• Rashamuse, T. J., Njengele, Z., Coyanis, E. M., Sayed, Y., Mosebi, S., and Bode, L, M. (2020) Design, synthesis and biological evaluation of novel 2-(5-aryl-1Himidazol-1-yl) derivatives as potential inhibitors of the HIV-1 Vpu and host BST-2 protein interaction, European Journal of Medicinal Chemistry. 190, 112111. IF = 4,833
• Ismail, N. O., Odendaal, C., Serem, J. C., Strӧmstedt, A. A., Bester, M. J., Sayed, Y., Neitz, A. W. H., and Gaspar, A. R. M. (2019) Antimicrobial function of short amidated peptide fragments from the tick-derived OsDef2 defensin, J Pept Sci. Nov 12:e3223. doi: 10.1002/psc.3223. [Epub ahead of print] PMID: 31713951. IF = 2,081
• Maseko, S., Padayachee, E., Maphumulo, S., Govender, T., Sayed, Y., Maguire, G., Lin, J., Naicker., and Gerhardus, K. H. (2019) Kinetic and thermodynamic characterisation of HIV-protease inhibitors against E35D↑G↑S mutant in the South African HIV-1 subtype C protease, J Enzyme Inhib Med Chem. Dec;34(1):1451-1456. doi: 10.1080/14756366.2019.1636234. IF = 4,027
• Zondagh, J., Basson, A. E., Achilonu, I., Morris, L., Dirr, H. W., and Sayed, Y. (2019) Drug susceptibility and replication capacity of a rare HIV-1 subtype C protease hinge region variant, Antivir Ther. 24(5):333-342. doi: 10.3851/IMP3308. IF = 3,04
• Ledwaba, J., Sayed, Y., Pillay, V., Morris, L., and Hunt, G. (2019 ) Low Frequency of Protease Inhibitor Resistance Mutations and Insertions in HIV-1 Subtype C Protease Inhibitor-Naïve Sequences, AIDS Res Hum Retroviruses. Jul;35(7):673-678. doi: 10.1089/AID.2019.0012. Epub 2019 Apr 4. IF = 1,805
• Williams, A., Basson, A., Achilonu, I., Dirr, H. W., Morris, L., and Sayed, Y. (2019) Double trouble? Gag in conjunction with double insert in HIV protease contributes to reduced DRV susceptibility, Biochem J. Jan 31;476(2):375-384. doi: 10.1042/BCJ20180692. IF = 4,331
• Zondagh, J., Williams, A., Achilonu, I., Dirr, H. W., and Sayed, Y. (2018) Overexpression, Purification and Functional Characterisation of Wild-Type HIV-1 Subtype C Protease and Two Variants Using a Thioredoxin and His-Tag Protein Fusion System, Protein Journal, 1-11. IF = 1,133
• Zondagh, J., Balakrishnan, V., Achilonu, I., Dirr, H. W., and Sayed, Y. (2018) Molecular dynamics and ligand docking of a hinge region variant of South African HIV-1 subtype C protease, Journal of Molecular Graphics and Modelling 82, 1-11. IF = 1,885
• Odame, F., Betz, R., Hosten, E. C., Krause, J., Isaacs, M., Hoppe, H. C., Khanye, S. D., Sayed, Y., Frost, C., Lobb, K. A., & Tshentu, Z. R (2018). A New Synthetic Method for Tetraazatricyclic Derivatives and Evaluation of Their Biological Properties. Chemistry Select, 3, 13613– 13618. DOI: 10.1002/slct.201802930. IF = 1,70
• van Eeden, C., Wibmer, C. K., Scheepers, C., Richardson, S. I., Nonyane, M., Lambson, B., Mkhize, N. N., Vijayakumar, B., Sheng, Z., Stanfield-Oakley, S., Bhiman, J. N., Bekker, V., Hermanus, T., Mabvakure, B., Ismail, A., Moody, M. A., Wiehe, K., Garrett, N., Karim, S. A., Dirr, H., Fernandes, M. A., Sayed, Y., Shapiro, L., Ferrari, G., Haynes, B. F., Moore, P. L., and Morris, L. (2018) V2-Directed Vaccine-like Antibodies from HIV-1 Infection Identify an Additional K169-Binding Light Chain Motif with Broad ADCC Activity, Cell Reports 25, 3123-3135 e3126. IF = 8,032
• Robertson, G. J., Stoychev, S. H., Sayed, Y., Achilonu, I., and Dirr, H. W. (2017) The effects of mutating Tyr9 and Arg15 on the structure, stability, conformational dynamics and mechanism of GSTA3-3, Biophys Chemistry 224, 40-48. IF = 1,870
• Maseko, S. B., Padayachee, E., Govender, T., Sayed, Y., Kruger, G., Maguire, G. E., and Lin, J. (2017) I36T↑ T mutation in South African subtype C (C-SA) HIV-1 protease significantly alters protease-drug interactions, Biological Chemistry 398, 1109-1117. IF = 3,022
• Tshabalala, T. N., Tomescu, M.-S., Prior, A., Balakrishnan, V., Sayed, Y., Dirr, H. W., and Achilonu, I. (2016) Energetics of glutathione binding to human eukaryotic elongation factor 1 gamma: isothermal titration calorimetry and molecular dynamics studies, Protein Journal 35, 448-458. IF = 1,133
• Njengele, Z., Kleynhans, R., Sayed, Y., and Mosebi, S. (2016) Expression, purification and characterization of a full-length recombinant HIV-1 Vpu from inclusion bodies, Protein Expression and Purification 128, 109-114. IF = 1,338
• Maseko, S. B., Natarajan, S., Sharma, V., Bhattacharyya, N., Govender, T., Sayed, Y., Maguire, G. E., Lin, J., and Kruger, H. G. (2016) Purification and characterization of naturally occurring HIV-1 (South African subtype C) protease mutants from inclusion bodies, Protein Expression and Purification 122, 90-96. IF = 1,338
• Lockhat, H. A., Silva, J. R., Alves, C. N., Govender, T., Lameira, J., Maguire, G. E., Sayed, Y., and Kruger, H. G. (2016) Binding free energy calculations of nine FDA‐approved protease inhibitors against HIV‐1 subtype C I36T↑ T containing 100 amino acids per monomer, Chemical Biology & Drug Design 87, 487-498. IF = 2,328
• Naicker, P., Stoychev, S., Dirr, H. W., and Sayed, Y. (2014) Amide hydrogen exchange in HIV–1 subtype B and C proteases–insights into reduced drug susceptibility and dimer stability, The FEBS Journal 281, 5395-5410. IF = 4,53
• Naicker, P., and Sayed, Y. (2014) Non-B HIV-1 subtypes in sub-Saharan Africa: impact of subtype on protease inhibitor efficacy, Biological Chemistry 395, 1151-1161. IF = 3,022
• Prinsloo, L., Naidoo, A., Serem, J., Taute, H., Sayed, Y., Bester, M., Neitz, A., and Gaspar, A. (2013) Structural and functional characterization of peptides derived from the carboxy‐terminal region of a defensin from the tick Ornithodoros savignyi, Journal of Peptide Science 19, 325-332. IF = 1,969
• Pawar, S. A., Jabgunde, A. M., Maguire, G. E., Kruger, H. G., Sayed, Y., Soliman, M. E., Dhavale, D. D., and Govender, T. (2013) Linear and cyclic glycopeptide as HIV protease inhibitors, European Journal of Medicinal Chemistry 60, 144-154. IF = 4,816
• Olomola, T. O., Klein, R., Mautsa, N., Sayed, Y., and Kaye, P. T. (2013) Synthesis and evaluation of coumarin derivatives as potential dual-action HIV-1 protease and reverse transcriptase inhibitors, Bioorganic & Medicinal Chemistry 21, 1964-1971. IF = 2,881
• Naicker, P., Seele, P., Dirr, H. W., and Sayed, Y. (2013b) F99 is critical for dimerization and activation of South African HIV-1 subtype C protease, Protein Journal 32, 560-567. IF = 1,133
• Naicker, P., Achilonu, I., Fanucchi, S., Fernandes, M., Ibrahim, M. A., Dirr, H. W., Soliman, M. E., and Sayed, Y. (2013a) Structural insights into the South African HIV-1 subtype C protease: impact of hinge region dynamics and flap flexibility in drug resistance, Journal of Biomolecular Structure and Dynamics 31, 1370-1380. IF = 3,107
• Makatini, M. M., Petzold, K., Alves, C. N., Arvidsson, P. I., Honarparvar, B., Govender, P., Govender, T., Kruger, H. G., Sayed, Y., and JerônimoLameira. (2013) Synthesis, 2D-NMR and molecular modelling studies of pentacycloundecane lactam-peptides and peptoids as potential HIV-1 wild type C-SA protease inhibitors, Journal of Enzyme Inhibition and Medicinal Chemistry 28, 78-88. IF = 3,638
• Karpoormath, R., Sayed, Y., Govender, T., Kruger, H. G., Soliman, M. E., and Maguire, G. E. (2013) Novel PCU cage diol peptides as potential targets against wild-type CSA HIV-1 protease: synthesis, biological screening and molecular modelling studies, Medicinal Chemistry Research 22, 3918-3933. IF = 1,607
• Ahmed, S. M., Kruger, H. G., Govender, T., Maguire, G. E., Sayed, Y., Ibrahim, M. A., Naicker, P., and Soliman, M. E. (2013) Comparison of the molecular dynamics and calculated binding free energies for nine FDA-approved HIV-1 PR drugs against subtype B and C-SA HIV PR, Chemical Biology & Drug Design 81, 208-218. IF = 2,328
• Thafeni, M. A., Sayed, Y., and Motadi, L. R. (2012) Euphorbia mauritanica and Kedrostis hirtella extracts can induce anti-proliferative activities in lung cancer cells, Molecular Biology Reports 39, 10785-10794. IF = 1,889
• Pawar, S. A., Jabgunde, A. M., Govender, P., Maguire, G. E., Kruger, H. G., Parboosing, R., Soliman, M. E., Sayed, Y., Dhavale, D. D., and Govender, T. (2012) Synthesis and molecular modelling studies of novel carbapeptide analogs for inhibition of HIV-1 protease, European Journal of Medicinal Chemistry 53, 13-21. IF = 4,816
• Makatini, M. M., Petzold, K., Arvidsson, P. I., Honarparvar, B., Govender, T., Maguire, G. E., Parboosing, R., Sayed, Y., Soliman, M. E., and Kruger, H. G. (2012) Synthesis, screening and computational investigation of pentacycloundecane-peptoids as potent CSA-HIV PR inhibitors, European Journal of Medicinal Chemistry 57, 459-467. IF = 4,816
• Karpoormath, R., Sayed, Y., Govender, P., Govender, T., Kruger, H. G., Soliman, M. E., and Maguire, G. E. (2012) Pentacycloundecane derived hydroxy acid peptides: a new class of irreversible non-scissile ether bridged type isoster as potential HIV-1 wild type C-SA protease inhibitors, Bioorganic Chemistry 40, 19-29. IF =3,929
• Honarparvar, B., Makatini, M. M., Pawar, S. A., Petzold, K., Soliman, M. E., Arvidsson, P. I., Sayed, Y., Govender, T., Maguire, G. E., and Kruger, H. G. (2012) Pentacycloundecane‐diol‐based HIV‐1 protease inhibitors: biological screening, 2D NMR, and molecular simulation studies, ChemMedChem 7, 1009-1019. IF = 3,009
• Makatini, M. M., Petzold, K., Sriharsha, S. N., Soliman, M. E., Honarparvar, B., Arvidsson, P. I., Sayed, Y., Govender, P., Maguire, G. E., and Kruger, H. G. (2011) Pentacycloundecane-based inhibitors of wild-type C-South African HIV-protease, Bioorganic & Medicinal Chemistry Letters 21, 2274-2277. IF = 2,442
• Makatini, M. M., Petzold, K., Sriharsha, S. N., Ndlovu, N., Soliman, M. E., Honarparvar, B., Parboosing, R., Naidoo, A., Arvidsson, P. I., and Sayed, Y. (2011) Synthesis and structural studies of pentacycloundecane-based HIV-1 PR inhibitors: A hybrid 2D NMR and docking/QM/MM/MD approach, European Journal of Medicinal Chemistry 46, 3976-3985. IF = 4,816
• Balchin, D., Dirr, H. W., and Sayed, Y. (2011) Energetics of ligand binding to human glutathione transferase A1-1: Tyr-9 associated localisation of the C-terminal helix is ligand-dependent, Biophysical Chemistry 156, 153-158. IF = 1,870
• Olomola, T. O., Klein, R., Lobb, K. A., Sayed, Y., and Kaye, P. T. (2010) Towards the synthesis of coumarin derivatives as potential dual-action HIV-1 protease and reverse transcriptase inhibitors, Tetrahedron Letters 51, 6325-6328. IF = 2,125
• Gildenhuys, S., Wallace, L. A., Burke, J. P., Balchin, D., Sayed, Y., and Dirr, H. W. (2010) Class Pi glutathione transferase unfolds via a dimeric and not monomeric intermediate: functional implications for an unstable monomer, Biochemistry 49, 5074-5081. IF = 2,997
• Gildenhuys, S., Dobreva, M., Kinsley, N., Sayed, Y., Burke, J., Pelly, S., Gordon, G. P., Sayed, M., Sewell, T., and Dirr, H. W. (2010) Arginine 15 stabilizes an SNAr reaction transition state and the binding of anionic ligands at the active site of human glutathione transferase A1-1, Biophysical Chemistry 146, 118-125. IF = 1,870
• Mosebi, S., Morris, L., Dirr, H. W., and Sayed, Y. (2008) Active-site mutations in the South African human immunodeficiency virus type 1 subtype C protease have a significant impact on clinical inhibitor binding: kinetic and thermodynamic study, Journal of Virology 82, 11476-11479. IF = 4,368
• Kinsley, N., Sayed, Y., Mosebi, S., Armstrong, R. N., and Dirr, H. W. (2008) Characterization of the binding of 8-anilinonaphthalene sulfonate to rat class Mu GST M1-1, Biophysical Chemistry 137, 100-104. IF = 1,879
• Alves, C. S., Kuhnert, D. C., Sayed, Y., and Dirr, H. W. (2006) The intersubunit lock-and-key motif in human glutathione transferase A1-1: role of the key residues Met51 and Phe52 in function and dimer stability, Biochemical Journal 393, 523-528. IF = 3,857
• Kuhnert, D. C., Sayed, Y., Mosebi, S., Sayed, M., Sewell, T., and Dirr, H. W. (2005) Tertiary interactions stabilise the C-terminal region of human glutathione transferase A1-1: a crystallographic and calorimetric study, Journal of Molecular Miology 349, 825-838. IF = 4,894
• Dirr, H. W., Little, T., Kuhnert, D. C., and Sayed, Y. (2005) A conserved N-capping motif contributes significantly to the stabilization and dynamics of the C-terminal region of class Alpha glutathione S-transferases, Journal of Biological Chemistry 280, 19480-19487. IF = 4,010
• Kolobe, D., and Sayed, Y. (2004) Characterization of bromosulphophthalein binding to human glutathione S-transferase A1-1: thermodynamics and inhibition kinetics, Biochemical Journal 382, 703-709. IF = 3,857
• Velázquez-Campoy, A., Vega, S., Fleming, E., Bacha, U., Sayed, Y., Dirr, H. W., and Freire, E. (2003) Protease inhibition in African subtypes of HIV-1, Aids Rev 5, 165-171. IF = 2,775
• Mosebi, S., Sayed, Y., Burke, J., and Dirr, H. W. (2003) Residue 219 impacts on the dynamics of the C-terminal region in glutathione transferase A1-1: implications for stability and catalytic and ligandin functions, Biochemistry 42, 15326-15332. IF = 2,997
• Sayed, Y., Hornby, J. A., Lopez, M., and Heini, D. (2002) Thermodynamics of the ligandin function of human class Alpha glutathione transferase A1-1: energetics of organic anion ligand binding, Biochemical Journal 363, 341-346. IF = 3,857
• Sayed, Y., Wallace, L. A., and Dirr, H. W. (2000) The hydrophobic lock‐and‐key intersubunit motif of glutathione transferase A1‐1: implications for catalysis, ligandin function and stability, FEBS Letters 465, 169-172. IF = 2,999

 

Othman,H., Messaoud, H.B.,  Khamessi, O., Ben-Mabrouk, H., Ghedira, K., Bharuthram, A., Treurnicht, F., Achilonu, I., Sayed, Y and Srairi-Abid, N. (2022). SARS-CoV-2 Spike Protein Unlikely to Bind to Integrins via the Arg-Gly-Asp (RGD) Motif of the Receptor Binding Domain: Evidence From Structural Analysis and Microscale Accelerated Molecular Dynamics. Frontiers in Molecular Biosciences, Volume 9, 1-11, Article 834857, 14 February 2022 https://doi.org/10.3389/fmolb.2022.834857. IF=5,246 

Valli, A., Achilonu, I., 2022. Comparative structural analysis of the human and Schistosoma glutathione transferase dimer interface using selective binding of bromosulfophthalein. Proteins: Structure, Function and Bioinformatics.

Otun, S., Escrich, A., Achilonu, I., Rauwane, M., Alexis, J., Lerma-Escalera, Morones-Ramírez, J.R., Rios-Solis, L., 2022. The future of cassava in the era of biotechnology in Southern Africa. Critical Reviews in Biotechnology, 1-19.

Daya, T., Jeje, O., Maake, R., Aloke, C., Khoza, T., Achilonu, I., 2022. Expression, Purification, and Biophysical Characterization of Klebsiella Pneumoniae Nicotinate Nucleotide Adenylyltransferase. The Protein Journal, 1-16.

Othman, H., Messaoud, H.B., Khamessi, O., Ben-Mabrouk, H., Ghedira, K., Bharuthram, A., Treurnicht, F., Achilonu, I., Sayed, Y., Srairi-Abid, N., 2022. SARS-CoV-2 spike protein unlikely to bind to integrins via the Arg-Gly-Asp (RGD) motif of the receptor binding domain: evidence from structural analysis and microscale accelerated molecular dynamics. Frontiers in Molecular Biosciences, 9.

Sherry, D., Worth, R, and Sayed, Y. (2021). Elasticity-associated functionality and inhibition of the HIV protease. Protein Reviews.  Advances in Experimental Medicine and Biolo, vol 1371.  springer, Cham. https://doi.org/101007/5584_2021_655

Sherry, D., Worth, R., Sheik Ismail, Z and Sayed, Y. (2021). Cantilever-centric mechanism of cooperative non-active site mutations in HIV protease: Implications for flap dynamic. Journal of Molecular Graphics and Modelling, 106, 107931, 1-19. DOI: https://doi.org/10.1016/j.jmgm.2021.107931. IF=2,079

Pandian, R., Selvarajan, S. S., Nagaraj, S., Thangaraj, V., Kandasamy, S., Sayed, Y, and Mondikalipudur, N.G.P. (2021). Structural studies of hemoglobin from two flightless birds, ostrich and turkey: insights into their differing oxygen-binding properties. Acta Cryst. D77, 690–702 DOI: https://doi.org/10.1107/S2059798321003417. IF=5,266

Selvarajan, S.S., Pandian, R., Nagaraj, S., Thangaraj, V., Sayed, Y, and Mondikalipudur, N.G.P. (2021). Crystal structure of hemoglobin from mouse (Mus musculus) compared with those from other small animals and humans. Acta Cryst. F77, 113–120. DOI: https://doi.org/10.1107/S2053230X2100306X. IF=1,9

Padi, N., Akumadu, B.O., Faerch, O., Aloke, C., Meyer, V., Achilonu, I., 2021. Engineering a Pseudo-26-kDa Schistosoma Glutathione Transferase from bovis/haematobium for Structure, Kinetics, and Ligandin Studies. Biomolecules, 11, 1844.

Pooe, K., Worth, R., Iwuchukwu, E.A., Dirr, H.W., Achilonu, I., 2021. An empirical and theoretical description of Schistosoma japonicum glutathione transferase inhibition by bromosulfophthalein and indanyloxyacetic acid 94. Journal of Molecular Structure 1223, 128892.

Jeje, O., Maake, R., van Deventer, R., Esau, V., Iwuchukwu, E.A., Meyer, V., Khoza, T., Achilonu, I., 2021. Effect of Divalent Metal Ion on the Structure, Stability and Function of Klebsiella pneumoniae Nicotinate-Nucleotide Adenylyltransferase: Empirical and Computational Studies. International Journal of Molecular Sciences 23, 116.

Motiwala, T., Akumadu, B.O., Zuma, S., Mfeka, M.S., Chen, W., Achilonu, I., Syed, K., Khoza, T., 2021. Caseinolytic Proteins (Clp) in the Genus Klebsiella: Special Focus on ClpK. Molecules 27, 200.

Thulo M., Rabie, M.A., Pahad, N., Donald, H.L., Blane A.A., Perumal, C.M., Penedo, J.C. and Fanucchi, S. (2020) The influence of various regions of the FOXP2 sequence on its structure and DNA-binding function. Bioscience Reports (2020) 00 1-13

Akumadu, B.O., Pandian, R., Olfsen, J., Worth, R., Thulo, M., Mentor, T., Fanucchi, S., Sayed, Y., Dirr, H.W., Achilonu, I (2020) Molecular basis of inhibition of Schistosoma japonicum glutathione

Schnetler, R., Fanucchi, S., Moldoveanu, T. and Koorsen, G. (2020) Linker Histone H1.3 Directly activates BAK through the K/RVVKP Motif on the C-Terminal domain. Biochemistry, 2020, 59(36), pp. 3332–3346

Odame, F., Hosten, E., Krause, J., Isaacs, M., Hoppe, H., Khanye, S.D., Sayed, Y., Frost, F., Lobb, K and Tshentu, Z. (2020). Synthesis, Characterization and Biological Activity of Some Dithiourea Derivatives. Acta Chim. Slov. 67, 764–777. DOI: 10.17344/acsi.2019.5689. IF = 1,104

Akumadu, B. O., Pandian, R., Olfsen, J., Worth, R., Thulo, M., Mentor, T., Fanucchi, S., Sayed, Y., Dirr, H. W., and Achilonu, I. (2020). Molecular basis of inhibition of Schistosoma japonicum glutathione transferase by ellagic acid: insights into biophysical and structural studies. Molecular and Biochemical Parasitology.org/10.1016/j.molbiopara.2020.111319. IF = 1,571

Achilonu, I., Iwuchukwu, E. A., Achilonu, O. J., Fernandes, M. A., and Sayed, Y. (2020). Targeting the SARS-CoV-2 main protease using FDA-approved Isavuconazonium, a P2-P3 α-ketoamide derivative and Pentagastrin: An in-silico drug discovery approach. Journal of Molecular Graphics and Modelling. https://doi.org/10.1016/j.jmgm.2020.107730. IF = 2,079

Sherry, D., Worth, R., and Sayed, Y. (2020). Two-step preparation of highly pure, soluble HIV protease from inclusion bodies recombinantly expressed in Escherichia coli. Current Protocols in Protein Science, 100, doi: 10.1002/cpps.106. IF = 1,92

Rashamuse, T. J., Njengele, Z., Coyanis, E. M., Sayed, Y., Mosebi, S., and Bode, L, M. (2020) Design, synthesis and biological evaluation of novel 2-(5-aryl-1Himidazol-1-yl) derivatives as potential inhibitors of the HIV-1 Vpu and host BST-2 protein interaction, European Journal of Medicinal Chemistry. 190, 112111. IF = 4,833

Achilonu, I., Iwuchukwu, E.A., Achilonu, O.J., Fernandes, M.A., Sayed, Y., 2020. Targeting the SARS-CoV-2 main protease using FDA-approved Isavuconazonium, a P2–P3 α-ketoamide derivative and Pentagastrin: An in-silico drug discovery approach. Journal of Molecular Graphics and Modelling, 101, 107730.

Akumadu, B.O., Pandian, R., Olfsen, J., Worth, R., Thulo, M., Mentor, T., Fanucchi, S., Sayed, Y., Dirr, H.W., Achilonu, I., 2020. Molecular basis of inhibition of Schistosoma japonicum glutathione transferase by ellagic acid: Insights into biophysical and structural studies. Molecular and Biochemical Parasitology, 240, 111319.

Mfeka, M.S., Martínez-Oyanedel, J., Chen, W., Achilonu, I., Syed, K., Khoza, T., 2020. Comparative analyses and structural insights of new class glutathione transferases in Cryptosporidium species. Scientific Reports 10, 1-12.

Keshav, V., Achilonu, I., Dirr, H., Kondiah, K., 2019. Recombinant expression and purification of a functional bacterial metallo-chaperone PbrD-fusion construct as a potential biosorbent for Pb (II). Protein Expression and Purification 158, 27-35.

Williams, A., Basson, A., Achilonu, I., Dirr, H.W., Morris, L., Sayed, Y., 2019. Double trouble? Gag in conjunction with double insert in HIV protease contributes to reduced DRV susceptibility. Biochemical Journal 476, 375-384.

Zondagh, J., Basson, A.E., Achilonu, I., Morris, L., Dirr, H.W., Sayed, Y., 2019. Drug susceptibility and replication capacity of a rare HIV-1 subtype C protease hinge region Antiviral Therapy 24, 333-342.

Ismail, N. O., Odendaal, C., Serem, J. C., Strӧmstedt, A. A., Bester, M. J., Sayed, Y., Neitz, A. W. H., and Gaspar, A. R. M. (2019) Antimicrobial function of short amidated peptide fragments from the tick-derived OsDef2 defensin, J Pept Sci. Nov 12:e3223. doi: 10.1002/psc.3223. [Epub ahead of print] PMID: 31713951. IF = 2,081

Maseko, S., Padayachee, E., Maphumulo, S., Govender, T., Sayed, Y., Maguire, G., Lin, J., Naicker., and Gerhardus, K. H. (2019) Kinetic and thermodynamic characterisation of HIV-protease inhibitors against E35D↑G↑S mutant in the South African HIV-1 subtype C protease, J Enzyme Inhib Med Chem. Dec;34(1):1451-1456. doi: 10.1080/14756366.2019.1636234. IF = 4,027

Zondagh, J., Basson, A. E., Achilonu, I., Morris, L., Dirr, H. W., and Sayed, Y. (2019) Drug susceptibility and replication capacity of a rare HIV-1 subtype C protease hinge region variant, Antivir Ther. 24(5):333-342. doi: 10.3851/IMP3308. IF = 3,04

Ledwaba, J., Sayed, Y., Pillay, V., Morris, L., and Hunt, G. (2019 ) Low Frequency of Protease Inhibitor Resistance Mutations and Insertions in HIV-1 Subtype C Protease Inhibitor-Naïve Sequences, AIDS Res Hum Retroviruses. Jul;35(7):673-678. doi: 10.1089/AID.2019.0012. Epub 2019 Apr 4. IF = 1,805

Williams, A., Basson, A., Achilonu, I., Dirr, H. W., Morris, L., and Sayed, Y. (2019) Double trouble? Gag in conjunction with double insert in HIV protease contributes to reduced DRV susceptibility, Biochem J. Jan 31;476(2):375-384. doi: 10.1042/BCJ20180692. IF = 4,331

Morris, G., Pahad, N., Dirr, H. and Fanucchi, S. (2018) A conserved cation binding site in the DNA binding domain of forkhead box transcription factors regulates DNA binding by FOXP2. Archives of Biochemistry and Biophysics, August 2018 (657) 56-64

Blane, A., Dirr, H. and Fanucchi, S. (2018) A phosphomimetic study implicates Ser557 in regulation of FOXP2 DNA binding. Protein Journal (37) 311-323

Morris, G., Stoychev, S., Naicker, P., Dirr, H. and Fanucchi, S. (2018) The forkhead domain hinge -loop plays a pivotal role in DNA binding and transcriptional activity of FOXP2. Biological chemistry (399) 881-893 

Zondagh, J., Williams, A., Achilonu, I., Dirr, H. W., and Sayed, Y. (2018) Overexpression, Purification and Functional Characterisation of Wild-Type HIV-1 Subtype C Protease and Two Variants Using a Thioredoxin and His-Tag Protein Fusion System, Protein Journal, 1-11. IF = 1,133

Zondagh, J., Balakrishnan, V., Achilonu, I., Dirr, H. W., and Sayed, Y. (2018) Molecular dynamics and ligand docking of a hinge region variant of South African HIV-1 subtype C protease, Journal of Molecular Graphics and Modelling 82, 1-11. IF = 1,885

Odame, F., Betz, R., Hosten, E. C., Krause, J., Isaacs, M., Hoppe, H. C., Khanye, S. D., Sayed, Y., Frost, C., Lobb, K. A., & Tshentu, Z. R (2018). A New Synthetic Method for Tetraazatricyclic Derivatives and Evaluation of Their Biological Properties. Chemistry Select, 3, 13613– 13618. DOI: 10.1002/slct.201802930. IF = 1,70

van Eeden, C., Wibmer, C. K., Scheepers, C., Richardson, S. I., Nonyane, M., Lambson, B., Mkhize, N. N., Vijayakumar, B., Sheng, Z., Stanfield-Oakley, S., Bhiman, J. N., Bekker, V., Hermanus, T., Mabvakure, B., Ismail, A., Moody, M. A., Wiehe, K., Garrett, N., Karim, S. A., Dirr, H., Fernandes, M. A., Sayed, Y., Shapiro, L., Ferrari, G., Haynes, B. F., Moore, P. L., and Morris, L. (2018) V2-Directed Vaccine-like Antibodies from HIV-1 Infection Identify an Additional K169-Binding Light Chain Motif with Broad ADCC Activity, Cell Reports 25, 3123-3135 e3126. IF = 8,032

Webb, H., Steeb, O., Blane, A., Rotherham, L., Aron, S., Machanick, P., Dirr, H. and Fanucchi, S.The FOXP2 forkhead domain binds to a variety of DNA sequences with different rates and affinities. Journal of Biochemistry162, 45-54 

Morris, G. and Fanucchi, S.A key evolutionary mutation enhances DNA binding of the FOXP2 forkhead domain. Biochemistry 55(13), 1959-1967 

Blane, A. and Fanucchi, S. The effect of pH on the DNA binding affinity of the FOXP2 forkhead domain. Biochemistry 54(25), 4001-4007 

Perumal, K., Dirr, H.W. and Fanucchi, S. Replacement of Tyr540 at the dimer interface with a phenylalanine increases the dimerisation potential of the FOXP2 forkhead domain. The protein journal 34, 111-121 

Cross, M.O., Fernandes, M.A., Dirr, H. W. and Fanucchi, S.Glutamate 85 and Glutamate 228 Contribute to the pH-Response of the Soluble Form of Chloride Intracellular Channel 1 Molecular and Cellular Biochemistry 398,83-93 

Peter, B., Fanucchi, S. and Dirr, H.W.  A conserved cationic motif enhances membrane binding and insertion of the chloride intracellular channel protein 1 transmembrane domain European Biophysics Journal 43, 405-414 

Peter, B., Polyansky, A., Fanucchi, S. and Dirr, H,W.  (2014)  A Lys-Trp Cation- interaction Mediates the Dimerization and Function of the Chloride Intracellular Channel Protein 1 Transmembrane Domain.  Biochemistry 53: 57-67

Robertson, G. J., Stoychev, S. H., Sayed, Y., Achilonu, I., and Dirr, H. W. (2017) The effects of mutating Tyr9 and Arg15 on the structure, stability, conformational dynamics and mechanism of GSTA3-3, Biophys Chemistry 224, 40-48. IF = 1,870

Maseko, S. B., Padayachee, E., Govender, T., Sayed, Y., Kruger, G., Maguire, G. E., and Lin, J. (2017) I36T↑ T mutation in South African subtype C (C-SA) HIV-1 protease significantly alters protease-drug interactions, Biological Chemistry 398, 1109-1117. IF = 3,022

Tshabalala, T.N., Tomescu, M.S, Prior, A., Balakrishnan, V., Sayed, Y., Dirr, H.W., and Achilonou, I (2016).  Energetics of gluthathione binding to human eukaryotic elongation factor 1 gamma: isothermal tritration calorimetry and molecular dynamic studies, Protein Journal 35, 448-458. 

Njengele, Z., Kleynhans, R., Sayed, Y., and Mosebi, S. (2016) Expression, purification and characterization of a full-length recombinant HIV-1 Vpu from inclusion bodies, Protein Expression and Purification 128, 109-114. IF = 1,338

Maseko, S. B., Natarajan, S., Sharma, V., Bhattacharyya, N., Govender, T., Sayed, Y., Maguire, G. E., Lin, J., and Kruger, H. G. (2016) Purification and characterization of naturally occurring HIV-1 (South African subtype C) protease mutants from inclusion bodies, Protein Expression and Purification 122, 90-96. IF = 1,338

Lockhat, H. A., Silva, J. R., Alves, C. N., Govender, T., Lameira, J., Maguire, G. E., Sayed, Y., and Kruger, H. G. (2016) Binding free energy calculations of nine FDA‐approved protease inhibitors against HIV‐1 subtype C I36T↑ T containing 100 amino acids per monomer, Chemical Biology & Drug Design 87, 487-498. IF = 2,328

Naicker, P., Stoychev, S., Dirr, H. W., and Sayed, Y. (2014) Amide hydrogen exchange in HIV–1 subtype B and C proteases–insights into reduced drug susceptibility and dimer stability, The FEBS Journal 281, 5395-5410. IF = 4,53

Naicker, P., and Sayed, Y. (2014) Non-B HIV-1 subtypes in sub-Saharan Africa: impact of subtype on protease inhibitor efficacy, Biological Chemistry 395, 1151-1161. IF = 3,022

Peter, B., Polyansky, A., Fanucchi, S. and Dirr, H.W. (2014) A Lys−Trp Cation−π Interaction Mediates the Dimerization and Function of the Chloride Intracellular Channel Protein 1 Transmembrane Domain. Biochemistry 53: 57-67

Legg-E'Silva, D., Achilonou, I., Fanucchi, S., Stoychev, S.H., Fernandes, M.A., and Dirr, H.W. (2012)  Role of the Arginine 29 and Glutamic acid 81 interactions in the Conformational Stability of Human Chloride Intracellular Channel 1.  Biochemistry 51(40): 7854-62

Prinsloo, L., Naidoo, A., Serem, J., Taute, H., Sayed, Y., Bester, M., Neitz, A., and Gaspar, A. (2013) Structural and functional characterization of peptides derived from the carboxy‐terminal region of a defensin from the tick Ornithodoros savignyi, Journal of Peptide Science 19, 325-332. IF = 1,969

Pawar, S. A., Jabgunde, A. M., Maguire, G. E., Kruger, H. G., Sayed, Y., Soliman, M. E., Dhavale, D. D., and Govender, T. (2013) Linear and cyclic glycopeptide as HIV protease inhibitors, European Journal of Medicinal Chemistry 60, 144-154. IF = 4,816

Olomola, T. O., Klein, R., Mautsa, N., Sayed, Y., and Kaye, P. T. (2013) Synthesis and evaluation of coumarin derivatives as potential dual-action HIV-1 protease and reverse transcriptase inhibitors, Bioorganic & Medicinal Chemistry 21, 1964-1971. IF = 2,881

Naicker, P., Seele, P., Dirr, H. W., and Sayed, Y. (2013b) F99 is critical for dimerization and activation of South African HIV-1 subtype C protease, Protein Journal 32, 560-567. IF = 1,133

Naicker, P., Achilonu, I., Fanucchi, S., Fernandes, M., Ibrahim, M. A., Dirr, H. W., Soliman, M. E., and Sayed, Y. (2013a) Structural insights into the South African HIV-1 subtype C protease: impact of hinge region dynamics and flap flexibility in drug resistance, Journal of Biomolecular Structure and Dynamics 31, 1370-1380. IF = 3,107

Makatini, M. M., Petzold, K., Alves, C. N., Arvidsson, P. I., Honarparvar, B., Govender, P., Govender, T., Kruger, H. G., Sayed, Y., and JerônimoLameira. (2013) Synthesis, 2D-NMR and molecular modelling studies of pentacycloundecane lactam-peptides and peptoids as potential HIV-1 wild type C-SA protease inhibitors, Journal of Enzyme Inhibition and Medicinal Chemistry 28, 78-88. IF = 3,638

Karpoormath, R., Sayed, Y., Govender, T., Kruger, H. G., Soliman, M. E., and Maguire, G. E. (2013) Novel PCU cage diol peptides as potential targets against wild-type CSA HIV-1 protease: synthesis, biological screening and molecular modelling studies, Medicinal Chemistry Research 22, 3918-3933. IF = 1,607

Ahmed, S. M., Kruger, H. G., Govender, T., Maguire, G. E., Sayed, Y., Ibrahim, M. A., Naicker, P., and Soliman, M. E. (2013) Comparison of the molecular dynamics and calculated binding free energies for nine FDA-approved HIV-1 PR drugs against subtype B and C-SA HIV PR, Chemical Biology & Drug Design 81, 208-218. IF = 2,328

Naicker, P., Achilonu, I., Fanucchi, S., Fernandes, M., Ibrahim, MA., Dirr, HW., Soliman, M.E. and Sayed, Y. (2013) Structural insights into the South African HIV-1 subtype C protease: impact of hinge region dynamics and flap flexibility in drug resistance. J Biomol Struct Dyn. 31(12): 1370-1380

Peter, B., Ngubane, N.C., Fanucchi, S. and Dirr, H.W. (2013) Membrane mimetics induce helix formation and oligomerization of the chloride intracellular channel protein 1 transmembrane domain. Biochemistry 52(16): 2739-49

Achilonu, I., Fanucchi, S., Cross, M., Fernandes, M., Dirr, H.W., 2012.  Role of individual histidines in the pH-dependant stability of human chloride intracellular channel 1.  Biochemistry 51, 995-1004.

Thafeni, M.A., Sayed, Y., and Motadi, L.R. (2012)  Euphorbia mauritanica and Kedrostis hirtella extracts can induce anti-proliferative activities in lung cancer cells, Molecular Biology Reports 39, 10785-10794.

Pawar, S. A., Jabgunde, A. M, Govender, P., Maguire, G. E., Kruge, H. G., Parboosing, R., Solman, M.E., Sayed, Y., Dhavale, D.D., and Govender, T. (2012)  Synthesis and molecular modeling studies of novel carbapeptide analogs for inhibition of HOV-1 protease, European Journal of Medicinal Chemistry 53, 13-21. 

Makatini, M. M., Petzold, K., Arvidsson, P. I., Honarparvar, B., Govender, T., Maguire, G. E., Parboosing, R., Sayed, Y., Soliman, M. E., and Kruger, H. G. (2012) Synthesis, screening and computational investigation of pentacycloundecane-peptoids as potent CSA-HIV PR inhibitors, European Journal of Medicinal Chemistry 57, 459-467. IF = 4,816

Karpoormath, R., Sayed, Y., Govender, P., Govender, T., Kruger, H. G., Soliman, M. E., and Maguire, G. E. (2012) Pentacycloundecane derived hydroxy acid peptides: a new class of irreversible non-scissile ether bridged type isoster as potential HIV-1 wild type C-SA protease inhibitors, Bioorganic Chemistry 40, 19-29. IF =3,929

Honarparvar, B., Makatini, M. M., Pawar, S. A., Petzold, K., Soliman, M. E., Arvidsson, P. I., Sayed, Y., Govender, T., Maguire, G. E., and Kruger, H. G. (2012) Pentacycloundecane‐diol‐based HIV‐1 protease inhibitors: biological screening, 2D NMR, and molecular simulation studies, ChemMedChem 7, 1009-1019. IF = 3,009

Makatini, M. M., Petzold, K., Sriharsha, S.N., Soliman, M.E., Honarparavar, B., Arvidsson, P.I., Sayed, Y., Govender, P., Maguire, G.E., and Kruger, H.G. (2011)  Pentacycloundecane-based inhibitors of wild-type C-South African HIV-protease, Bioorganic & Medical Chemistry Letters 21, 2274-2277. 

Derryn Legg-E'Silva, Ikechukwu Achilonu, Sylvia Fanucchi, Stoyan H. Stoychev, Manuel Antonio Fernandes, and Heini W Dirr (2012) Role of Arginine 29 and Glutamic acid 81 Interactions in the Conformational Stability of Human Chloride Intracellular Channel 1. Biochemistry 51(40): 7854-62.

Achilonu I, Fanucchi S, Cross M, Fernandes M, Dirr HW (2012) Role of individual histidines in the pH-dependent global stability of human chloride intracellular channel 1. Biochemistry 51, 995-1004

Makatini, M. M., Petzold, K., Sriharsha, S. N., Soliman, M. E., Honarparvar, B., Arvidsson, P. I., Sayed, Y., Govender, P., Maguire, G. E., and Kruger, H. G. (2011) Pentacycloundecane-based inhibitors of wild-type C-South African HIV-protease, Bioorganic & Medicinal Chemistry Letters 21, 2274-2277. IF = 2,442

Makatini, M. M., Petzold, K., Sriharsha, S. N., Ndlovu, N., Soliman, M. E., Honarparvar, B., Parboosing, R., Naidoo, A., Arvidsson, P. I., and Sayed, Y. (2011) Synthesis and structural studies of pentacycloundecane-based HIV-1 PR inhibitors: A hybrid 2D NMR and docking/QM/MM/MD approach, European Journal of Medicinal Chemistry 46, 3976-3985. IF = 4,816

Balchin, D., Dirr, H. W., and Sayed, Y. (2011) Energetics of ligand binding to human glutathione transferase A1-1: Tyr-9 associated localisation of the C-terminal helix is ligand-dependent, Biophysical Chemistry 156, 153-158. IF = 1,870

Parbhoo N, Stoychev SH, Fanucchi S, Achilonu I, Adamson RJ, Fernandes M, Gildenhuys S, Dirr HW. (2011) A Conserved Domain Interaction is a Determinant of Folding Cooperativity in the GST Fold. Biochemistry 50: 7067-7075.

Olomola, T. O., Klein, R., Lobb, K. A., Sayed, Y., and Kaye, P. T. (2010) Towards the synthesis of coumarin derivatives as potential dual-action HIV-1 protease and reverse transcriptase inhibitors, Tetrahedron Letters 51, 6325-6328. IF = 2,125

Gildenhuys, S., Wallace, L. A., Burke, J. P., Balchin, D., Sayed, Y., and Dirr, H. W. (2010) Class Pi glutathione transferase unfolds via a dimeric and not monomeric intermediate: functional implications for an unstable monomer, Biochemistry 49, 5074-5081. IF = 2,997

Gildenhuys, S., Dobreva, M., Kinsley, N., Sayed, Y., Burke, J., Pelly, S., Gordon, G. P., Sayed, M., Sewell, T., and Dirr, H. W. (2010) Arginine 15 stabilizes an SNAr reaction transition state and the binding of anionic ligands at the active site of human glutathione transferase A1-1, Biophysical Chemistry 146, 118-125. IF = 1,870

Balchin, D., Fanucchi, S., Achilonu, I., Adamson, R.J., Burke, J., Fernandes, M., Gildenhuys, S. and Dirr, H.W. (2010) Stability of the Domain Interface Contributes Towards the Catalytic Function at the H-site of Class Alpha Glutathione Transferase A1-1. Biophys. Acta 1804, 2228-2233 

Achilonou, I., Gildenhuys, S., Fisher, L., Burke, J., Fanucchi, S., Sewell, B.T., Fernandes, M. and Dirr, H.W. (2010) The role of a topologically conserved isoleucine in glutathione transferase structure, stability and function. Acta Cryst, F66, 776-780

Stoychev, S.H., Nathaniel, C., Fanucchi, S., Brock, M., Li, S., Asmus, K., Woods, V.L. Jr. and Dirr, H.W. (2009) Structural Dynamics of Soluble Chloride Intracellular Channel Protein CLIC1 Examined by Amide Hydrogen-Deuterium Exchange Mass Spectrometry. Biochemistry 48, 8413 – 8421 

Mosebi, S., Morris, L., Dirr, H. W., and Sayed, Y. (2008) Active-site mutations in the South African human immunodeficiency virus type 1 subtype C protease have a significant impact on clinical inhibitor binding: kinetic and thermodynamic study, Journal of Virology 82, 11476-11479. IF = 4,368

Kinsley, N., Sayed, Y., Mosebi, S., Armstrong, R. N., and Dirr, H. W. (2008) Characterization of the binding of 8-anilinonaphthalene sulfonate to rat class Mu GST M1-1, Biophysical Chemistry 137, 100-104. IF = 1,879

Fanucchi, S., Adamson, R.J. and Dirr, H.W. (2008) Formation of an Unfolding Intermediate State of Soluble Chloride Intracellular Channel Protein CLIC1 at Acidic pH. Biochemistry 47, 11674 – 11681 

Zondagh, J., Williams, A., Achilonu, I., Dirr, H. W., and Sayed, Y. (2018) Overexpression, Purification and Functional Characterisation of Wild-Type HIV-1 Subtype C Protease and Two Variants Using a Thioredoxin and His-Tag Protein Fusion System, Protein Journal, 1-11. IF = 1,133

Zondagh, J., Balakrishnan, V., Achilonu, I., Dirr, H. W., and Sayed, Y. (2018) Molecular dynamics and ligand docking of a hinge region variant of South African HIV-1 subtype C protease, Journal of Molecular Graphics and Modelling 82, 1-11. IF = 1,885

Odame, F., Betz, R., Hosten, E. C., Krause, J., Isaacs, M., Hoppe, H. C., Khanye, S. D., Sayed, Y., Frost, C., Lobb, K. A., & Tshentu, Z. R (2018). A New Synthetic Method for Tetraazatricyclic Derivatives and Evaluation of Their Biological Properties. Chemistry Select, 3, 13613– 13618. DOI: 10.1002/slct.201802930. IF = 1,70

van Eeden, C., Wibmer, C. K., Scheepers, C., Richardson, S. I., Nonyane, M., Lambson, B., Mkhize, N. N., Vijayakumar, B., Sheng, Z., Stanfield-Oakley, S., Bhiman, J. N., Bekker, V., Hermanus, T., Mabvakure, B., Ismail, A., Moody, M. A., Wiehe, K., Garrett, N., Karim, S. A., Dirr, H., Fernandes, M. A., Sayed, Y., Shapiro, L., Ferrari, G., Haynes, B. F., Moore, P. L., and Morris, L. (2018) V2-Directed Vaccine-like Antibodies from HIV-1 Infection Identify an Additional K169-Binding Light Chain Motif with Broad ADCC Activity, Cell Reports 25, 3123-3135 e3126. IF = 8,032

Robertson, G. J., Stoychev, S. H., Sayed, Y., Achilonu, I., and Dirr, H. W. (2017) The effects of mutating Tyr9 and Arg15 on the structure, stability, conformational dynamics and mechanism of GSTA3-3, Biophys Chemistry 224, 40-48. IF = 1,870

Maseko, S. B., Padayachee, E., Govender, T., Sayed, Y., Kruger, G., Maguire, G. E., and Lin, J. (2017) I36T↑ T mutation in South African subtype C (C-SA) HIV-1 protease significantly alters protease-drug interactions, Biological Chemistry 398, 1109-1117. IF = 3,022

Tshabalala, T. N., Tomescu, M.-S., Prior, A., Balakrishnan, V., Sayed, Y., Dirr, H. W., and Achilonu, I. (2016) Energetics of glutathione binding to human eukaryotic elongation factor 1 gamma: isothermal titration calorimetry and molecular dynamics studies, Protein Journal 35, 448-458. IF = 1,133

Njengele, Z., Kleynhans, R., Sayed, Y., and Mosebi, S. (2016) Expression, purification and characterization of a full-length recombinant HIV-1 Vpu from inclusion bodies, Protein Expression and Purification 128, 109-114. IF = 1,338

Maseko, S. B., Natarajan, S., Sharma, V., Bhattacharyya, N., Govender, T., Sayed, Y., Maguire, G. E., Lin, J., and Kruger, H. G. (2016) Purification and characterization of naturally occurring HIV-1 (South African subtype C) protease mutants from inclusion bodies, Protein Expression and Purification 122, 90-96. IF = 1,338

Lockhat, H. A., Silva, J. R., Alves, C. N., Govender, T., Lameira, J., Maguire, G. E., Sayed, Y., and Kruger, H. G. (2016) Binding free energy calculations of nine FDA‐approved protease inhibitors against HIV‐1 subtype C I36T↑ T containing 100 amino acids per monomer, Chemical Biology & Drug Design 87, 487-498. IF = 2,328

Naicker, P., Stoychev, S., Dirr, H. W., and Sayed, Y. (2014) Amide hydrogen exchange in HIV–1 subtype B and C proteases–insights into reduced drug susceptibility and dimer stability, The FEBS Journal 281, 5395-5410. IF = 4,53

Naicker, P., and Sayed, Y. (2014) Non-B HIV-1 subtypes in sub-Saharan Africa: impact of subtype on protease inhibitor efficacy, Biological Chemistry 395, 1151-1161. IF = 3,022

Prinsloo, L., Naidoo, A., Serem, J., Taute, H., Sayed, Y., Bester, M., Neitz, A., and Gaspar, A. (2013) Structural and functional characterization of peptides derived from the carboxy‐terminal region of a defensin from the tick Ornithodoros savignyi, Journal of Peptide Science 19, 325-332. IF = 1,969

Pawar, S. A., Jabgunde, A. M., Maguire, G. E., Kruger, H. G., Sayed, Y., Soliman, M. E., Dhavale, D. D., and Govender, T. (2013) Linear and cyclic glycopeptide as HIV protease inhibitors, European Journal of Medicinal Chemistry 60, 144-154. IF = 4,816

Olomola, T. O., Klein, R., Mautsa, N., Sayed, Y., and Kaye, P. T. (2013) Synthesis and evaluation of coumarin derivatives as potential dual-action HIV-1 protease and reverse transcriptase inhibitors, Bioorganic & Medicinal Chemistry 21, 1964-1971. IF = 2,881

Naicker, P., Seele, P., Dirr, H. W., and Sayed, Y. (2013b) F99 is critical for dimerization and activation of South African HIV-1 subtype C protease, Protein Journal 32, 560-567. IF = 1,133

Naicker, P., Achilonu, I., Fanucchi, S., Fernandes, M., Ibrahim, M. A., Dirr, H. W., Soliman, M. E., and Sayed, Y. (2013a) Structural insights into the South African HIV-1 subtype C protease: impact of hinge region dynamics and flap flexibility in drug resistance, Journal of Biomolecular Structure and Dynamics 31, 1370-1380. IF = 3,107

Makatini, M. M., Petzold, K., Alves, C. N., Arvidsson, P. I., Honarparvar, B., Govender, P., Govender, T., Kruger, H. G., Sayed, Y., and JerônimoLameira. (2013) Synthesis, 2D-NMR and molecular modelling studies of pentacycloundecane lactam-peptides and peptoids as potential HIV-1 wild type C-SA protease inhibitors, Journal of Enzyme Inhibition and Medicinal Chemistry 28, 78-88. IF = 3,638

Karpoormath, R., Sayed, Y., Govender, T., Kruger, H. G., Soliman, M. E., and Maguire, G. E. (2013) Novel PCU cage diol peptides as potential targets against wild-type CSA HIV-1 protease: synthesis, biological screening and molecular modelling studies, Medicinal Chemistry Research 22, 3918-3933. IF = 1,607

Ahmed, S. M., Kruger, H. G., Govender, T., Maguire, G. E., Sayed, Y., Ibrahim, M. A., Naicker, P., and Soliman, M. E. (2013) Comparison of the molecular dynamics and calculated binding free energies for nine FDA-approved HIV-1 PR drugs against subtype B and C-SA HIV PR, Chemical Biology & Drug Design 81, 208-218. IF = 2,328

Thafeni, M. A., Sayed, Y., and Motadi, L. R. (2012) Euphorbia mauritanica and Kedrostis hirtella extracts can induce anti-proliferative activities in lung cancer cells, Molecular Biology Reports 39, 10785-10794. IF = 1,889

Pawar, S. A., Jabgunde, A. M., Govender, P., Maguire, G. E., Kruger, H. G., Parboosing, R., Soliman, M. E., Sayed, Y., Dhavale, D. D., and Govender, T. (2012) Synthesis and molecular modelling studies of novel carbapeptide analogs for inhibition of HIV-1 protease, European Journal of Medicinal Chemistry 53, 13-21. IF = 4,816

Makatini, M. M., Petzold, K., Arvidsson, P. I., Honarparvar, B., Govender, T., Maguire, G. E., Parboosing, R., Sayed, Y., Soliman, M. E., and Kruger, H. G. (2012) Synthesis, screening and computational investigation of pentacycloundecane-peptoids as potent CSA-HIV PR inhibitors, European Journal of Medicinal Chemistry 57, 459-467. IF = 4,816

Karpoormath, R., Sayed, Y., Govender, P., Govender, T., Kruger, H. G., Soliman, M. E., and Maguire, G. E. (2012) Pentacycloundecane derived hydroxy acid peptides: a new class of irreversible non-scissile ether bridged type isoster as potential HIV-1 wild type C-SA protease inhibitors, Bioorganic Chemistry 40, 19-29. IF =3,929

Honarparvar, B., Makatini, M. M., Pawar, S. A., Petzold, K., Soliman, M. E., Arvidsson, P. I., Sayed, Y., Govender, T., Maguire, G. E., and Kruger, H. G. (2012) Pentacycloundecane‐diol‐based HIV‐1 protease inhibitors: biological screening, 2D NMR, and molecular simulation studies, ChemMedChem 7, 1009-1019. IF = 3,009

Makatini, M. M., Petzold, K., Sriharsha, S. N., Soliman, M. E., Honarparvar, B., Arvidsson, P. I., Sayed, Y., Govender, P., Maguire, G. E., and Kruger, H. G. (2011) Pentacycloundecane-based inhibitors of wild-type C-South African HIV-protease, Bioorganic & Medicinal Chemistry Letters 21, 2274-2277. IF = 2,442

Makatini, M. M., Petzold, K., Sriharsha, S. N., Ndlovu, N., Soliman, M. E., Honarparvar, B., Parboosing, R., Naidoo, A., Arvidsson, P. I., and Sayed, Y. (2011) Synthesis and structural studies of pentacycloundecane-based HIV-1 PR inhibitors: A hybrid 2D NMR and docking/QM/MM/MD approach, European Journal of Medicinal Chemistry 46, 3976-3985. IF = 4,816

Balchin, D., Dirr, H. W., and Sayed, Y. (2011) Energetics of ligand binding to human glutathione transferase A1-1: Tyr-9 associated localisation of the C-terminal helix is ligand-dependent, Biophysical Chemistry 156, 153-158. IF = 1,870

Olomola, T. O., Klein, R., Lobb, K. A., Sayed, Y., and Kaye, P. T. (2010) Towards the synthesis of coumarin derivatives as potential dual-action HIV-1 protease and reverse transcriptase inhibitors, Tetrahedron Letters 51, 6325-6328. IF = 2,125

Gildenhuys, S., Wallace, L. A., Burke, J. P., Balchin, D., Sayed, Y., and Dirr, H. W. (2010) Class Pi glutathione transferase unfolds via a dimeric and not monomeric intermediate: functional implications for an unstable monomer, Biochemistry 49, 5074-5081. IF = 2,997

Gildenhuys, S., Dobreva, M., Kinsley, N., Sayed, Y., Burke, J., Pelly, S., Gordon, G. P., Sayed, M., Sewell, T., and Dirr, H. W. (2010) Arginine 15 stabilizes an SNAr reaction transition state and the binding of anionic ligands at the active site of human glutathione transferase A1-1, Biophysical Chemistry 146, 118-125. IF = 1,870

Mosebi, S., Morris, L., Dirr, H. W., and Sayed, Y. (2008) Active-site mutations in the South African human immunodeficiency virus type 1 subtype C protease have a significant impact on clinical inhibitor binding: kinetic and thermodynamic study, Journal of Virology 82, 11476-11479. IF = 4,368

Kinsley, N., Sayed, Y., Mosebi, S., Armstrong, R. N., and Dirr, H. W. (2008) Characterization of the binding of 8-anilinonaphthalene sulfonate to rat class Mu GST M1-1, Biophysical Chemistry 137, 100-104. IF = 1,879

Alves, C. S., Kuhnert, D. C., Sayed, Y., and Dirr, H. W. (2006) The intersubunit lock-and-key motif in human glutathione transferase A1-1: role of the key residues Met51 and Phe52 in function and dimer stability, Biochemical Journal 393, 523-528. IF = 3,857

Kuhnert, D. C., Sayed, Y., Mosebi, S., Sayed, M., Sewell, T., and Dirr, H. W. (2005) Tertiary interactions stabilise the C-terminal region of human glutathione transferase A1-1: a crystallographic and calorimetric study, Journal of Molecular Miology 349, 825-838. IF = 4,894

Dirr, H. W., Little, T., Kuhnert, D. C., and Sayed, Y. (2005) A conserved N-capping motif contributes significantly to the stabilization and dynamics of the C-terminal region of class Alpha glutathione S-transferases, Journal of Biological Chemistry 280, 19480-19487. IF = 4,010

Kolobe, D., and Sayed, Y. (2004) Characterization of bromosulphophthalein binding to human glutathione S-transferase A1-1: thermodynamics and inhibition kinetics, Biochemical Journal 382, 703-709. IF = 3,857

Velázquez-Campoy, A., Vega, S., Fleming, E., Bacha, U., Sayed, Y., Dirr, H. W., and Freire, E. (2003) Protease inhibition in African subtypes of HIV-1, Aids Rev 5, 165-171. IF = 2,775

Mosebi, S., Sayed, Y., Burke, J., and Dirr, H. W. (2003) Residue 219 impacts on the dynamics of the C-terminal region in glutathione transferase A1-1: implications for stability and catalytic and ligandin functions, Biochemistry 42, 15326-15332. IF = 2,997

Sayed, Y., Hornby, J. A., Lopez, M., and Heini, D. (2002) Thermodynamics of the ligandin function of human class Alpha glutathione transferase A1-1: energetics of organic anion ligand binding, Biochemical Journal 363, 341-346. IF = 3,857

Sayed, Y., Wallace, L. A., and Dirr, H. W. (2000) The hydrophobic lock‐and‐key intersubunit motif of glutathione transferase A1‐1: implications for catalysis, ligandin function and stability, FEBS Letters 465, 169-172. IF = 2,999