Dr. Saad Tayyab
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Dr. Saad Tayyab

Professor
Faculty of Science, Institute of Biological Sciences, Universiti Malaya, Kuala Lumpur, Malaysia


Highest Degree
Ph.D. in Biochemistry from Aligarh Muslim University, Aligarh, India

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Biography

Dr. Saad Tayyab received his degree in 1987 in Biochemistry at Aligarh Muslim University, India. Currently, he is working as Professor of Biochemistry, Institute of Biological Sciences, University of Malaysia, Malaysia. His prior working experience includes Lecturer of Biochemistry at University of Kashmir, India and Aligarh Muslim University, India and Associate Professor at Alemaya University, Ethiopia. His research interest includes Protein denaturation/ folding, Protein/Enzyme stabilization, Ligand-protein interaction, Protein-Structure & Function and Bilirubin transport. He supervised 8 PhD, 5 Mphil, 1 M.D., 6 M.Sc. scholars and 11 M.Sc., 22 B.Sc. projects and presently supervising 5 PhD, 2 M.Sc. scholars and 2 B.Sc. projects. Publications to his credit includes 91 research papers, 15 popular articles, 1 learning aid, 1 book and 3 book reviews (h-index = 17). He is life member of Society of Biological Chemists, Indian Biophysical Society, Indian Science Congress Association and member of Association of Clinical Biochemists of India, Malaysian Society for Biochemistry & Molecular Biology. He has 28 years teaching experience and 33 years research experience. He is serving as editorial board member of International Journal of Biological Chemistry and Asian Journal of Biochemistry. He is also serving as referee to Biomacromolecules, Journal of Agricultural & Food Chemistry, Journal of Luminescence, Journal of Physical Chemistry, Colloids & Surfaces, Journal of Molecular Catalysis, Journal of Pharmaceutical & Biomedical Analysis, Biochimie, Pesticide Biochemistry & Physiology, Journal of Photochemistry & Photobiology, Applied Biochemistry & Biotechnology, Molecular Biology Reports and Protein & Peptide Letters etc.

Area of Interest:

Chemistry
100%
Protein Biochemistry
62%
Molecular Biology
90%
Phytochemistry
75%
Chemical Biology
55%

Research Publications in Numbers

Books
1
Chapters
1
Articles
153
Abstracts
0

Selected Publications

  1. Kandandapani, S., M.Z. Kabir, N.F.W. Ridzwan, S.B. Mohamad and S. Tayyab, 2022. Biomolecular interaction mechanism of an anticancer drug, pazopanib with human serum albumin: A multi-spectroscopic and computational approach. J. Biomol. Struct. Dyn., 40: 8312-8323.
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  2. Tayyab, S., M.K.A. Magesvaran, M.Z. Kabir, N.F.W. Ridzwan and S.B. Mohamad, 2021. Biophysical and computational view on the in vitro combination between an anticancer drug, saracatinib and human serum albumin. J. Biomol. Struct. Dyn., 39: 3565-3575.
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  3. Tayyab, S. and S.R. Feroz, 2021. Serum albumin: Clinical significance of drug binding and development as drug delivery vehicle. Adv. Protein Chem. Struct. Biol., 123: 193-218.
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  4. Tan, C.Y., C.S. Lim, S.M. Liew, A.A. Abd Halim and S. Tayyab, 2021. Lysine modification of human serum albumin and its effect on protein conformation and nalidixic acid binding. J. Indian Chem. Soc., Vol. 98. 10.1016/j.jics.2021.100031.
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  5. Roslan, A.A., S.B. Mohamad and S. Tayyab, 2021. Docking evaluation of the interaction between green tea active ingredient, l-theanine and human serum albumin. Nat. Acad. Sci. Lett., 44: 17-19.
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  6. Musa, K.A., N.F.W. Ridzwan, S.B. Mohamad and S. Tayyab, 2021. Exploring the combination characteristics of lumefantrine, an antimalarial drug and human serum albumin through spectroscopic and molecular docking studies. J. Biomol. Struct. Dyn., 39: 691-702.
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  7. Tayyab, S., L.H. Min, M.Z. Kabir, S. Kandandapani, N.F.W. Ridzwan and S.B. Mohamad, 2020. Exploring the interaction mechanism of a dicarboxamide fungicide, iprodione with bovine serum albumin. Chem. Pap., 74: 1633-1646.
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  8. Musa, K.A., T. Ning, S.B. Mohamad and S. Tayyab, 2020. Intermolecular recognition between pyrimethamine, an antimalarial drug and human serum albumin: Spectroscopic and docking study. J. Mol. Liq., Vol. 311. 10.1016/j.molliq.2020.113270.
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  9. Musa, K.A., N.F.W. Ridzwan, S.B. Mohamad and S. Tayyab, 2020. Combination mode of antimalarial drug mefloquine and human serum albumin: Insights from spectroscopic and docking approaches. Biopolymers, Vol. 111. 10.1002/bip.23337.
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  10. Kandandapani, S., N.F.W. Ridzwan, S.B. Mohamad and S. Tayyab, 2020. Exploring the interaction between tyrphostin 9 and human serum albumin using biophysical and computational methods. J. Biomol. Struct. Dyn., 38: 4134-4142.
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  11. Kabir, M.Z., Z. Benbekhti, N.F.W. Ridzwan, R. Merrouche, N. Bouras, S.B. Mohamad and S. Tayyab, 2020. Biophysical and in silico investigations of the molecular association between a potent RNA polymerase inhibitor, thiolutin and human serum albumin. J. Mol. Liq., Vol. 303. 10.1016/j.molliq.2020.112648.
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  12. Kabir, M.Z., A.A. Roslan, N.F.W. Ridzwan, S.B. Mohamad and S. Tayyab, 2020. Biomolecular interaction of a platelet aggregation inhibitor, 3,4-methylenedioxy-β-nitrostyrene with human serum albumin: Multi-spectral and computational characterization. J. Biomol. Struct. Dyn., 38: 2693-2703.
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  13. Francis, J.A., M. Shalauddin, N.F.W. Ridzwan, S.B. Mohamad, W.J. Basirun and S. Tayyab, 2020. Interaction mechanism of an antimalarial drug, sulfadoxine with human serum albumin. Spectros. Lett., 53: 391-405.
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  14. Tayyab, S., S.E. Sam, M.Z. Kabir, N.F.W. Ridzwan and S.B. Mohamad, 2019. Molecular interaction study of an anticancer drug, ponatinib with human serum albumin using spectroscopic and molecular docking methods. Spectrochim. Acta Part A: Mol. Biomol. Spectros., 214: 199-206.
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  15. Tayyab, S., J.A. Francis, M.Z. Kabir, H. Ghani and S.B. Mohamad, 2019. Probing the interaction of 2,4-dichlorophenoxyacetic acid with human serum albumin as studied by experimental and computational approaches. Spectrochim. Acta Part A: Mol. Biomol. Spectrosc., 207: 284-293.
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  16. Saufi, A.N.M., N.F.W. Ridzwan, S.B. Mohamad, S. Tayyab and A.A. Abd Halim, 2019. Fluorometric and docking analysis of the complex formation between an anti-cancer drug, chlorambucil and bovine serum albumin. Indian J. Pharm. Educ. Res., 53: 682-687.
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  17. Roslan, A.A., S. Kandandapani, N.F.W. Ridzwan, S.B. Mohamad and S. Tayyab, 2019. Biophysical and computational approaches to unravel the molecular interaction mechanism of bromodeoxyuridine, a proliferative marker with human serum albumin. Monatshefte für Chemie-Chem. Mon., 150: 2061-2070.
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  18. Roslan, A.A. and S. Tayyab, 2019. Exploring ligand-protein interaction: A laboratory exercise on herbicide binding to plasma transport protein. Biochem. Mol. Biol. Educ., 47: 156-160.
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  19. Lee, W.Q., N.I.A. Kameel, S. Mohamad and S. Tayyab, 2019. Comparison of pendimethalin binding properties of serum albumins from various mammalian species. Turk. J. Biochem., 44: 363-369.
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  20. Lee, S.T., R. Rahman, K. Muthoosamy, N.A.H. Mohamed, X. Su, S. Tayyab and S.Y. New, 2019. Amplification-free and direct fluorometric determination of telomerase activity in cell lysates using chimeric DNA-templated silver nanoclusters. Microchim. Acta, Vol. 186. 10.1007/s00604-018-3194-7.
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  21. Foo, Y.Y., W.S. Saw, V. Periasamy, W.Y. Chong, S.N. Abd Malek and S. Tayyab, 2019. Green synthesised-gold nanoparticles in photothermal therapy of breast cancer. Micro Nano Lett., 14: 470-474.
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  22. Kabir, M.Z., N.A.B. Hamzah, H. Ghani, S.B. Mohamad, Z. Alias and S. Tayyab, 2018. Biophysical and computational characterization of vandetanib-lysozyme interaction. Spectrochim. Acta Part A: Mol. Biomol. Spectrosc., 189: 485-494.
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  23. Kabir, M.Z., H. Ghani, S.B. Mohamad, Z. Alias and S. Tayyab, 2018. Interactive association between RhoA transcriptional signaling inhibitor, CCG1423 and human serum albumin: Biophysical and in silico studies. J. Biomol. Struct. Dyn., 36: 2495-2507.
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  24. Foo, Y.Y., M.Z. Kabir, V. Periasamy, S.N. Abd Malek and S. Tayyab, 2018. Spectroscopic studies on the interaction of green synthesized-gold nanoparticles with human serum albumin. J. Mol. Liq., 265: 105-113.
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  25. Lee, W.Q., I.S.M. Affandi, S.R. Feroz, S.B. Mohamad and S. Tayyab, 2017. Evaluation of pendimethalin binding to human serum albumin: Insights from spectroscopic and molecular modeling approach. J. Biochem. Mol. Toxicol., Vol. 31. 10.1002/jbt.21839.
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  26. Kabir, M.Z., W.V. Tee, S.B. Mohamad, Z. Alias and S. Tayyab, 2017. Comprehensive insight into the binding of sunitinib, a multi-targeted anticancer drug to human serum albumin. Spectrochim. Acta Part A: Mol. Biomol. Spectrosc., 181: 254-263.
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  27. Halim, A.A.A., M.S. Zaroog, H.A. Kadir and S. Tayyab, 2017. Alcohol-induced structural transitions in the acid-denatured Bacillus licheniformis α-amylase. J. Saudi Chem. Soc., 21: S349-S358.
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  28. Halim, A.A.A., H.A. Kadir and S. Tayyab, 2017. Increased chemical stability of Bacillus licheniformis α-amylase upon acetylation. Studia UBB Chemia, 2: 319-332.
  29. Affandi, I.S.M., W.Q. Lee, S.R. Feroz, S.B. Mohamad and S. Tayyab, 2017. Interaction of stattic, a STAT3 inhibitor with human serum albumin: Spectroscopic and computational study. J. Biomol. Struct. Dynamics, 35: 3581-3590.
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  30. Wong, Y.H., H.A. Kadir and S. Tayyab, 2016. A comparative analysis of protein stabilizing potential of honey and simulated honey sugar cocktail. Protein Peptide Lett., 23: 898-904.
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  31. Tayyab, S., M.M. Izzudin, M.Z. Kabir, S.R. Feroz, W.V. Tee, S.B. Mohamad and Z. Alias, 2016. Binding of an anticancer drug, axitinib to human serum albumin: Fluorescence quenching and molecular docking study. J. Photochem. Photobiol. B Biol., 162: 386-394.
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  32. Nasruddin, A.N., S.R. Feroz, A.K. Mukarram, S.B. Mohamad and S. Tayyab, 2016. Fluorometric and molecular docking investigation on the binding characteristics of SB202190 to human serum albumin. J. Lumin., 174: 77-84.
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  33. Kandandapani, S., C.Y. Tan, A.S. Shuib and S. Tayyab, 2016. Influence of buffer composition and calcium chloride on GdnHCl denaturation of bacillus licheniformis α-amylase. Protein Pept. Lett., 23: 537-543.
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  34. Kameel, N.I.A., Y.H. Wong, A.S. Shuib and S. Tayyab, 2016. Conformational analysis of champedak galactose-binding lectin under different urea concentrations. Plant Physiol. Biochem., 98: 57-63.
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  35. Kameel, N.I.A., A.S. Shuib and S. Tayyab, 2016. Acid-induced unfolding of champedak galactose-binding lectin. Protein Peptide Lett., 23: 1111-1117.
  36. Kabir, M.Z., W.V. Tee, S.B. Mohamad, Z. Alias and S. Tayyab, 2016. Interaction of an anticancer drug, gefitinib with human serum albumin: Insights from fluorescence spectroscopy and computational modeling analysis. RSC Adv., 6: 91756-91767.
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  37. Kabir, M.Z., S.R. Feroz, A.K. Mukarram, Z. Alias, S.B. Mohamad and S. Tayyab, 2016. Interaction of a tyrosine kinase inhibitor, vandetanib with human serum albumin as studied by fluorescence quenching and molecular docking. J. Biomol. Struct. Dyn., 34: 1693-1704.
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  38. Kabir, M.Z., A.K. Mukarram, S.B. Mohamad, Z. Alias and S. Tayyab, 2016. Characterization of the binding of an anticancer drug, lapatinib to human serum albumin. J. Photochem. Photobiol. B Biol., 160: 229-239.
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  39. Feroz, S.R., S.N.A. Malek and S. Tayyab, 2016. Characteristics and thermodynamics of the interaction of 6-shogaol with human serum albumin as studied by isothermal titration calorimetry. Braz. J. Pharm. Sci., 52: 443-446.
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  40. Bortolotti, A., Y.H. Wong, S.S. Korsholm, N.H.B. Bahring and S. Bobone et al., 2016. On the purported “backbone fluorescence” in protein three-dimensional fluorescence spectra. RSC Adv., 6: 112870-112876.
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  41. Wong, Y.H., H.A. Kadir and S. Tayyab, 2015. Targeting chemical and thermal stability of ovalbumin by simulated honey sugar cocktail. Int. J. Biol. Macromol., 73: 207-214.
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  42. Wong, Y.H., H.A. Kadir and S. Tayyab, 2015. Intrinsic fluorescence as a spectral probe for protein denaturation studies in the presence of honey. J. Appl. Spectrosc., 82: 845-848.
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  43. Tayyab, S., M.S. Zaroog, S.R. Feroz, S.B. Mohamad and S.N.A. Malek, 2015. Exploring the interaction between the antiallergic drug, tranilast and human serum albumin: Insights from calorimetric, spectroscopic and modeling studies. Int. J. Pharm., 491: 352-358.
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  44. Sakhaei, N., A.A.A. Halim and S. Tayyab, 2015. Warfarin binding to native and structurally-altered human serum albumins. Indian J. Pharm. Educ. Res., 49: 225-230.
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  45. Manoharan, P., Y.H. Wong and S. Tayyab, 2015. Stabilization of human serum albumin against urea denaturation by diazepam and ketoprofen. Protein Pept. Lett., 22: 611-617.
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  46. Hamdi, O.A.A., S.R. Feroz, J.A. Shilpi, E.H. Anouar and A.K. Mukarram et al., 2015. Spectrofluorometric and molecular docking studies on the binding of curcumenol and curcumenone to human serum albumin. Int. J. Mol. Sci., 16: 5180-5193.
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  47. Feroz, S.R., Y.J. Teoh, S.B. Mohamad, S.L. Hong, S.N. Malek and S. Tayyab, 2015. Interaction of flavokawain B with lysozyme: A photophysical and molecular simulation study. J. Lumin., 160: 101-109.
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  48. Feroz, S.R., S.B. Mohamad, G.S. Lee, S.N.A. Malek and S. Tayyab, 2015. Supramolecular interaction of 6-shogaol, a therapeutic agent of Zingiber officinale with human serum albumin as elucidated by spectroscopic, calorimetric and molecular docking methods. Phytomed., 22: 621-630.
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  49. Feroz, S.R., A. Rumana, S.N. Malek and S. Tayyab, 2015. A comparative analysis on the binding characteristics of various mammalian albumins towards a multitherapeutic agent, pinostrobin. Exp. Anim., 64: 101-108.
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  50. Zaroog, M.S., H.A. Kadir and S. Tayyab, 2014. Structural transitions in the acid-denatured ficin induced by halogenols and alkanols. Bulgarian Chem. Commun., 46: 602-610.
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  51. Wong, Y.H., C.H. Lim, H.A. Kadir and S. Tayyab, 2014. Towards increasing chemical and thermal stability of lysozyme with a simulated honey sugar cocktail. RSC Adv., 4: 53891-53898.
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  52. Tayyab, S. and A.N. Boyce, 2014. Outsourcing in scientific research: A boon or a curse. Curr. Sci., 106: 789-789.
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  53. Rahim, N.A., P. Hassandarvish, S. Golbabapour, S. Ismail, S. Tayyab and M.A. Abdulla, 2014. Gastroprotective effect of ethanolic extract of Curcuma xanthorrhiza leaf against Ethanol-induced gastric mucosal lesions in Sprague-dawley rats. BioMed Res. Int., 10.1155/2014/416409.
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  54. Abd Halim, A.A., M.S. Zaroog, H. Abdul Kadir and S. Tayyab, 2014. Molten globule-like partially folded state of Bacillus licheniformis α-Amylase at low ph induced by 1, 1, 1, 3, 3, 3-Hexafluoroisopropanol. Scient. World J., 10.1155/2014/824768.
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  55. Zaroog, M.S., H. Abdul Kadir and S. Tayyab, 2013. Stabilizing effect of various polyols on the native and the denatured states of glucoamylase. Scient. World J., 10.1155/2013/570859.
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  56. Zaroog, M.S. and S. Tayyab, 2013. Halogenol-versus alkanol-induced structural transitions of acid-denatured glucoamylase: Characterization of alcohol-induced states. Process Bioch., 48: 853-862.
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  57. Wong, Y.H., H. Abdul Kadir and S. Tayyab, 2013. Honey-induced protein stabilization as studied by fluorescein isothiocyanate fluorescence. Scient. World J., 10.1155/2013/981902.
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  58. Toosi, A.F., B.B. Bakar and S. Tayyab, 2013. Chemical analysis of Brassica juncea (L.) Czern var. Ensabi. Vegetos, 26: 93-97.
  59. Tayyab, S. and A.N. Boyce, 2013. Open access: Good or bad. Curr. Sci., 104: 810-810.
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  60. Tayyab, S. and A.N. Boyce, 2013. Impactor factor versus Q1 class of journals in world university rankings. Curr. Sci., 104: 417-419.
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  61. Sidek, N.A.A., Z. Alias and S. Tayyab, 2013. Gel chromatographic analysis of ficin under native and under denaturing conditions. Bulgarian Chem. Commun., 45: 93-99.
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  62. Sidek, N.A.A., A.A.A. Halim, H.A. Kadir and S. Tayyab, 2013. Structural stability of commercial ficin under different denaturing conditions. Turk. J. Biochem., 38: 319-328.
    Direct Link  |  
  63. Halim, A.A.A., S.R. Feroz and S. Tayyab, 2013. Does recovery in the spectral characteristics of GdnHCl-denatured Bacillus licheniformis α-amylase due to added calcium point towards protein stabilization? Biosci. Biotechnol. Biochem., 77: 87-96.
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  64. Feroz, S.R., S.B. Mohamad, Z.S. Bakri, S.N. Malek and S. Tayyab, 2013. Probing the interaction of a therapeutic flavonoid, pinostrobin with human serum albumin: Multiple spectroscopic and molecular modeling investigations. PLOS ONE, Vol. 8. 10.1371/journal.pone.0076067.
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  65. Zaroog, M.S. and S. Tayyab, 2012. Formation of molten globule-like state during acid denaturation of Aspergillus niger glucoamylase. Process Biochem., 47: 775-784.
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  66. Wong, Y.H. and S. Tayyab, 2012. Protein stabilizing potential of simulated honey sugar cocktail under various denaturation conditions. Process Biochem., 47: 1933-1943.
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  67. Tan, C.Y. and S. Tayyab, 2012. Demonstration of size-based separation of molecules by gel chromatography: An exercise for biology beginners. Life Sci. J., 9: 1560-1563.
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  68. Sing, K.W., M. Sofian-Azirun and S. Tayyab, 2012. Protein analysis of Chrysomya megacephala maggot meal. Anim. Nutr. Feed Technol., 12: 35-46.
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  69. Feroz, S.R., S.B. Mohamad, N. Bujang, S.N. Malek and S. Tayyab, 2012. Multispectroscopic and molecular modeling approach to investigate the interaction of flavokawain B with human serum albumin. J. Agric. Food Chem., 60: 5899-5908.
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  70. Faizul, F.M., H.A. Kadir and S. Tayyab, 2012. Bilirubin clearance in temporarily hyperbilirubinemic rats treated with aqueous extract of Sida rhombifolia. Life Sci. J., 9: 2254-2256.
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  71. Toosi, A.F., B. Arumugam, B.B. Baki and S. Tayyab, 2011. Protein profiling of Brassica juncea (L.) czern var. ensabi at different developmental stages. J. Biol. Sci., 11: 165-172.
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  72. Tan, C.Y., R.Z.B.R. Rahman, H.A. Kadir and S. Tayyab, 2011. Conformational destabilization of Bacillus licheniformis α-amylase induced by lysine modification and calcium depletion. Acta Biochim. Pol., 58: 405-412.
    Direct Link  |  
  73. Tan, C.Y., H.A. Kadir and S. Tayyab, 2010. Calcium-induced stabilization of-amylase against guanidine hydrochloride denaturation. Afr. J. Biotechnol., 9: 7934-7941.
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  74. Sidek, N.A.A., A.A.A. Halim and S. Tayyab, 2010. Denatured states of ficin induced by urea and guanidine hydrochloride. Turk. J. Biochem., 35: 45-49.
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  75. Arumugam, B., H.A. Kadir and S. Tayyab, 2010. Effect of charge neutralization at lysine residues on the free energy of stabilization of hen egg white lysozyme. Rom. J. Biochem., 47: 115-133.
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  76. Ong, H.N., B. Arumugam and S. Tayyab, 2009. Succinylation-induced conformational destabilization of lysozyme as studied by guanidine hydrochloride denaturation. J. Biochem., 146: 895-904.
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  77. Mathavan, V.M., B.K. Boh and S. Tayyab, 2009. Characterization of erythrosine B binding to bovine serum albumin and bilirubin displacement. Indian J. Biochem. Biophys., 46: 325-331.
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  78. Faizul, F.M., N. Aminudin, H.A. Kadir and S. Tayyab, 2009. Bilirubin lowering potential of Orthosiphon stamineus in temporarily jaundiced adult rats. Afr. J. Pharmacy Pharmacol., 3: 359-361.
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  79. Kim, B.B. and S. Tayyab, 2008. Resistance towards calcium induced bilirubin dependent hemolysis in porcine erythrocytes. Indian J. Clin. Biochem., 23: 17-23.
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  80. Halim, A.A.A., H.A. Kadir and S. Tayyab, 2008. Guanidine hydrochloride-induced denaturation of bovine serum albumin: A comparative study and analysis using different probes. Malaysian J. Sci., 27: 9-17.
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  81. Halim, A.A.A., H.A. Kadir and S. Tayyab, 2008. Bromophenol blue binding as a probe to study urea and guanidine hydrochloride denaturation of bovine serum albumin. J. Biochem., 144: 33-38.
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  82. Faizul, F.M., H.A. Kadir and S. Tayyab, 2008. Spectroscopic studies on the binding of bromocresol purple to different serum albumins and its bilirubin displacing action. J. Photochem. Photobiol. B., 90: 1-7.
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  83. Boon Kim, B., H. Abdul Kadir and S. Tayyab, 2008. Bromophenol blue binding to mammalian albumins and displacement of albumin-bound bilirubin. Pak. J. Biol. Sci., 11: 2418-2422.
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  84. Tayyab, S., 2007. Educational Playing Cards (Amino Acids). Stratum Publishers, New Delhi, India.
  85. Tayyab, S. and A.N. Boyce, 2006. A journey from amino acids to proteins. University Malaya Press, Kuala Lumpur, Malaysia., ISBN: 983-100-368-3, Pages: 156..
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  86. Ahmad, N., K. Arif, S.M. Faisal, M.K. Neyaz, S. Tayyab and M. Owais, 2006. PLGA-microsphere mediated clearance of bilirubin in temporarily hyperbiliru-binemic rats: An alternate strategy for the treatment of experimental jaundice. Biochim. Biophys. Acta, 1760: 227-232.
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  87. Rashid, H., M.M. Khan and S. Tayyab, 2005. Interaction of bilirubin with sealed and human serum albumin-entrapped sealed membranes. Mol. Cell. Biochem., 277: 101-107.
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  88. Kumar, Y., S. Muzammil and S. Tayyab, 2005. Influence of fluoro, chloro and alkyl alcohols on the folding pathway of human serum albumin. J. Biochem., 138: 335-341.
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  89. Masood, A.K., S. Moin, S. Tayyab, F.F. Abul, M. Siddiqui and M. Owais, 2004. Liposome-bilirubin interaction: A novel strategy to eliminate bilirubin from systemic circulation. J. Liposome Res., 14: 111-122.
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  90. Kumar, Y., S. Tayyab and S. Muzammil, 2004. Molten-globule like partially folded states of human serum albumin induced by fluoro and alkyl alcohols at low pH. Arch. Biochem. Biophys., 426: 3-10.
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  91. Tayyab, S., N.J. Khan, M.A. Khan and Y. Kumar, 2003. Behavior of various mammalian albumins towards bilirubin binding and photochemical properties of different bilirubin-albumin complexes. Int. J. Biol. Macromol., 31: 187-193.
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  92. Tayyab, S., 2003. Examinations and evaluation: A fear or a challenge. Alemaya Univ. Newsl., 2: 18-20.
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  93. Rashid, H. and S. Tayyab, 2003. Interaction of bilirubin with native and protein depleted human erythrocyte membranes. Mol. Cell. Biochem., 246: 171-177.
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  94. Tayyab, S., B. Ahmad, Y. Kumar and M.M. Khan, 2002. Salt-induced refolding in different domains of partially folded bovine serum albumin. Int. J. Biol. Macromol., 30: 17-22.
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  95. Tayyab, S., 2002. Class room teaching: An affair with students. Alemaya Univ. Newsl., 2: 28-29.
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  96. Khan, M.A., Y. Kumar and S. Tayyab, 2002. Bilirubin binding properties of pigeon serum albumin and its comparison with human serum albumin. Int. J. Biol. Macromol., 30: 171-178.
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  97. Tayyab, S., P. Paliwal and M.M. Khan, 2001. Modulation in the photosensitivity of albumin-bound bilirubin. Int. J. Biol. Macromol., 29: 267-271.
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  98. Rashid, H., M. Owais and S. Tayyab, 2001. Bilirubin binding to normal and modified human erythrocyte membranes: Effect of phospholipases, neuraminidase, trypsin and CaCl2. Mol. Cell. Biochem., 228: 15-23.
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  99. Khan, M.M. and S. Tayyab, 2001. Understanding the role of internal lysine residues of serum albumins in conformational stability and bilirubin binding. Biochim. Biophys. Acta, 1545: 263-277.
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  100. Ali, M.K., M.U. Siddiqui and S. Tayyab, 2001. Enhanced bilirubin binding to different mammalian erythrocytes in the presence of magnesium ions. Indian J. Clin. Biochem., 16: 31-36.
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  101. Ali, M.K. and S. Tayyab, 2001. Effect of phospholipase C, trypsin and neuraminidase on binding of bilirubin to mammalian erythrocyte membranes. Comparative Biochem. Physiol. Part A Mol. Integr. Physiol., 129: 355-362.
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  102. Ali, M.K. and S. Tayyab, 2001. Effect of metal ions on binding of bilirubin to erythrocyte membranes. Indian J. Biochem. Biophys., 38: 230-234.
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  103. Tayyab, S., N. Sharma and M.M. Khan, 2000. Use of domain specific ligands to study urea induced unfolding of bovine serum albumin. Biochem. Biophys. Res. Commun., 277: 83-88.
  104. Tayal, D., M.M. Khan and S. Tayyab, 2000. Stabilization of wheat germ acid phosphatase with glutaraldehyde. Res. J. Chem. Environ., 4: 13-17.
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  105. Rashid, H., M.K. Ali and S. Tayyab, 2000. Effect of pH and temperature on the binding of bilirubin to human erythrocyte membranes. J. Biosci., 25: 157-161.
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  106. Rashid, H., M.K. Ali and S. Tayyab, 2000. Differential accessibility of bilirubin to erythrocyte membrane vesicles bearing different spectral features. Comparative Biochem. Physiol., 127: 345-350.
  107. Muzammil, S., Y. Kumar and S. Tayyab, 2000. Anion-induced stabilization of human serum albumin prevents the formation of intermediate during urea denaturation. Proteins: Struct. Function Genet., 40: 29-38.
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  108. Muzammil, S., Y. Kumar and S. Tayyab, 2000. Anion-induced refolding of human serum albumin under low pH conditions. Biochim. Biophys. Acta, 1476: 139-148.
    CrossRef  |  
  109. Khan, M.M., S. Muzammil and S. Tayyab, 2000. Role of salt-bridge(s) in the binding and photoconversion of bilirubin bound to high affinity site on human serum albumin. Biochim. Biophys. Acta Protein Struct. Mol. Enzymol., 1479: 103-113.
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  110. Khan, M.M., S. Muzammil and S. Tayyab, 2000. Chloroform-induced conformational changes in the bound pigment in bilirubin-albumin complexes. Biochimie, 82: 203-209.
    PubMed  |  
  111. Khan, M.M. and S. Tayyab, 2000. On the modulation of photoinduced fluorescence enhancenment and conformational stability of albumin-bound bilirubin: Effect of ε-NH2 groups blocking and chloroform binding. Biochim. Biophys. Acta, 1523: 147-153.
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  112. Muzammil, S., Y. Kumar and S. Tayyab, 1999. Molten globule-like state of human serum albumin at low pH. Eur. J. Biochem., 266: 26-32.
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