Avadhesha Surolia

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Avadhesha Surolia
Born (1947-12-03) 3 December 1947 (age 76)
Kishangarh, Rajasthan
Alma mater University of Jodhpur (B.Sc.), Maharaja Sayajirao University of Baroda (M.Sc.), Madras University (Ph.D., D.Sc.)
Known forLectin structure and interactions, protein folding, diabetes research, antimalarials, anti-cancer agents
AwardsBhatnagar Fellowship, Honorary D.Sc. from Queen's University, Belfast
Scientific career
Fields Glycobiology, Biochemistry
InstitutionsIndian Institute of Science, Bangalore
Doctoral advisor Bimal Kumar Bachhawat

Avadhesha Surolia (born 3 December 1947) [1] is a glycobiologist at the Indian Institute of Science (IISc), Bangalore. He was born in Kishangarh, Rajasthan, India. Presently, he is an honorary professor at the Molecular Biophysics Unit, IISc [2] and holds the Bhatnagar fellowship of the Council of Scientific and Industrial Research (CSIR). [2] He is known for his work on lectin structure and interactions, orientation and dynamics of cell surface carbohydrate receptors and protein folding, diabetes, antimalarials and anti-cancer agents based on curcumin, flavonoids, etc. In addition, neuropathic pain, neurodegenerative disorders and the link between immunity and obsessive–compulsive disorder are areas of his current[ when? ] interest

Contents

Education and career

Surolia obtained his bachelor's degree in chemistry and biology from the University of Jodhpur in 1970. He earned his master's degree in biochemistry from Maharaja Sayajirao University of Baroda in 1972. He completed his Ph.D. under the guidance of B. K. Bachhawat from Madras University in 1976. In 1978, he was awarded a Doctor of Science degree by Madras University. After his doctoral studies he joined Indian Institute of Chemical Biology (IICB), Calcutta, as a scientist in 1977 until 1981. He further held the position of assistant professor at IICB until 1986, after which he joined Molecular Biophysics Unit (MBU) at IISc as an associate professor (1986–1991). He was a professor at MBU, IISc from 1991 to 2013 and served as its chairman from 2000 to 2006. From 2006 to 2011 he held the directorship of India's prestigious research institute, National Institute of Immunology (NII), New Delhi. [3] [4] During his tenure NII was recognized by Thomson Reuters Innovation Award in 2010 as the most innovative research institute nationally. [5] [6] He holds honorary professorship at Jawaharlal Nehru Centre for Advanced Scientific Research, Bangalore. [7] In recognition of his contributions to medicine and science, he was conferred an Honorary D.Sc. degree in 2013 by Queen's University, Belfast, UK. [8] [9] [10] [11]

Scientific contributions

Surolia has elucidated the role of glycosphingolipids as biological receptors through studies on lectin-glycolipid interactions using liposomes. [12] He discovered novel blood group and tumor antigen specific lectins [13] and made original contribution towards elucidation of the energetics and mechanism of protein-sugar recognition. He genetically re-engineered carbohydrate specificities of lectins imparting T-antigen tumor recognizing ability to peanut agglutinin. [14] He delineated the molecular basis of carbohydrate recognition by legume lectins [15] [16] [17] [18] [19] and demonstrated the novel C-H...O/N hydrogen bond in protein-sugar interactions. [20] He studied thermal unfolding of lectins that led to the discovery of novel modes of oligomerization in them. [21] [22] He found a molten globule monomeric intermediate during the folding of peanut agglutinin that retained its carbohydrate binding ability - establishing 'wet' molten globule as an "on pathway" folding intermediate and characterized other early intermediates. [22] [23] [24] His studies showed that the monomers of legume lectins have the necessary structural features for carbohydrate recognition and that oligomerization imparts them with topology necessary for their biologic activities such as agglutination, mitogenesis, etc. He elucidated the molecular features of substrate recognition by endoplasmic reticulum chaperones calreticulin and calnexin. [25] [26] He discovered the unusual quaternary structure of peanut agglutinin [27] and a novel lectin fold in Jacalin [28] as well as the structural basis of inactivation of ribosomes by gelonin. [29] He enunciated that solvent reorganization in protein-ligand interactions modulates their specificities. [30] [31] He showed the existence of co-operativity in lectin-multimeric sugar interactions. Surolia explained the enigmatic endotoxin neutralizing activity of polymyxin B to its specific ability to remove endotoxin from its assembly and attributed it to its unique amphiphilicity. [32] [33] [34] [35] He popularized Protein A as a tool in immunology. [36] [37] He discovered the broad substrate specificity of a key enzyme of biotin biosynthesis from M. tuberculosis [38] and reported novel inhibitors for it. He has demonstrated the potential of common dietary components - curcumin and green tea catechins as anti-cancer and antimalarial agents. [39] [40] [41] He has developed a rhodanine, BCFMT, as a potential therapeutic for cancer. [42] Surolia co-discovered the existence of the fatty acid synthesis pathway in Plasmodium and demonstrated its remarkable distinction from that of its human host. [43] He co-identified triclosan, a widely used biocide, to compromise the growth of the parasite by inhibiting its enoyl-ACP reductase (FabI). [43] Recently, Surolia and colleagues have identified pranlukast (a US Food and Drug Administration approved drug for asthma) as novel inhibitor of Mtb ArgJ, an enzyme of the arginine biosynthesis pathway, essential for pathogenicity and survival in host cells. [44] Pranlukast demonstrated remarkable efficiency in pre-clinical models of Mycobacterium Tuberculosis. [44] These apart, Surolia has also ventured into the field of chronic disease biology where he has developed a novel form of insulin, Supramolecular Insulin Assembly-II (SIA-II), for long-lasting treatment of type I diabetes mellitus. [45] [46] [47] In addition to protein–sugar interactions his research is also focused on neuropathic pain, neurodegenerative disorders and the link between immunity and obsessive–compulsive disorder. Curcumin and its designed analogs are being developed as experimental therapeutics for these diseases and cancer. His findings have been commercially exploited by a number of international companies such as Amersham-Pharmacia, Sigma Chemical Co., Pierce Corporation, Bangalore Genei, Datascope Corp., and Shantha Biotechniques Pvt. Ltd. He has about 19 national and international patents. [48] Surolia has published about 360 scientific papers in peer-reviewed journals of high impact factor. He has an h-index of 41 and his publications have been cited over 5000 times.

Fellowships and memberships

Surolia is a member of: Third World Academy of Sciences (TWAS), Trieste, Italy [49] and International Molecular Biologists Network. [50] He is a fellow of all the science academies in the country- National Science Academy, Indian National Science Academy and Indian Academy of Sciences. [1] [51] He was a member of the Board of Trustees, Human Frontier Scientific Programme (HFSP, Strasbourg). [2] [52] [53] He is the only Indian member of the International Glycoconjugate Organization since 1998 and served as its president from 2001 to 2004. [4] [54] He has been a visiting scientist at Massachusetts Institute of Technology, University of Maryland and University of Michigan, USA. [4] He has chaired a number of Study sections of Department of Biotechnology, Department of Science and Technology and CSIR (India) and continues to advise a number of Institutions and Academic bodies in India and abroad. He is currently Bhatnagar Fellow of CSIR (India), was a JC Bose Fellow of DST (India), Honorary Professor, Indian Institute of Science, and member executive committee of the International Union of Biochemistry and Molecular Biology (IUBMB). [2] [55] He is in the editorial advisory board of IUBMB-Life and PLoS ONE. He has served as an editor of the Proceedings of the Indian National Science Academy from 1998 to 2001. He is an editorial board member of the Proceedings of the National Academy of Sciences (India) and the Indian Journal of Biotechnology.

Awards

Jawaharlal Nehru Birth Centenary Lecture (2008)., [56] B.K. Bachhawat Memorial Award 2007, J.C.Bose Fellowship (2006), [57] Dr. B.R. Ambedkar Centenary Award for Excellence in Biomedical Research (2003), [58] Goyal Prize in the area of Life Sciences (2002), [1] TWAS Prize in Biology (2001), [59] Professor GN Ramachandran 60th Birthday Commemoration Medal (2000), [56] Alumni Award (IISc, 1999), [1] Ranbaxy Science Foundation Award in Basic Medical Sciences (1995), [1] Shri Om Prakhash Bhasin Award for Biotechnology (1993), [60] FICCI award for outstanding research in Biological Sciences (1993), W.H. Stillmark Prize (Honorary) for outstanding research contributions on lectins (1990), [1] S.S. Bhatnagar Award for Outstanding Research in Biological Sciences (1987), [1] INSA Young Scientist Medal (1976) [1]

Related Research Articles

<span class="mw-page-title-main">Lectin</span> Carbohydrate-binding protein

Lectins are carbohydrate-binding proteins that are highly specific for sugar groups that are part of other molecules, so cause agglutination of particular cells or precipitation of glycoconjugates and polysaccharides. Lectins have a role in recognition at the cellular and molecular level and play numerous roles in biological recognition phenomena involving cells, carbohydrates, and proteins. Lectins also mediate attachment and binding of bacteria, viruses, and fungi to their intended targets.

<span class="mw-page-title-main">Concanavalin A</span> Lectin (carbohydrate-binding protein) originally extracted from the jack-bean

Concanavalin A (ConA) is a lectin originally extracted from the jack-bean. It is a member of the legume lectin family. It binds specifically to certain structures found in various sugars, glycoproteins, and glycolipids, mainly internal and nonreducing terminal α-D-mannosyl and α-D-glucosyl groups. Its physiological function in plants, however, is still unknown. ConA is a plant mitogen, and is known for its ability to stimulate mouse T-cell subsets giving rise to four functionally distinct T cell populations, including precursors to regulatory T cells; a subset of human suppressor T-cells is also sensitive to ConA. ConA was the first lectin to be available on a commercial basis, and is widely used in biology and biochemistry to characterize glycoproteins and other sugar-containing entities on the surface of various cells. It is also used to purify glycosylated macromolecules in lectin affinity chromatography, as well as to study immune regulation by various immune cells.

<span class="mw-page-title-main">Glucosepane</span> Chemical compound

Glucosepane is a lysine-arginine protein cross-linking product and advanced glycation end product (AGE) derived from D-glucose. It is an irreversible, covalent cross-link product that has been found to make intermolecular and intramolecular cross-links in the collagen of the extracellular matrix (ECM) and crystallin of the eyes. Covalent protein cross-links irreversibly link proteins together in the ECM of tissues. Glucosepane is present in human tissues at levels 10 to 1000 times higher than any other cross-linking AGE, and is currently considered to be the most important cross-linking AGE.

Collectins (collagen-containing C-type lectins) are a part of the innate immune system. They form a family of collagenous Ca2+-dependent defense lectins, which are found in animals. Collectins are soluble pattern recognition receptors (PRRs). Their function is to bind to oligosaccharide structure or lipids that are on the surface of microorganisms. Like other PRRs they bind pathogen-associated molecular patterns (PAMPs) and damage-associated molecular patterns (DAMPs) of oligosaccharide origin. Binding of collectins to microorganisms may trigger elimination of microorganisms by aggregation, complement activation, opsonization, activation of phagocytosis, or inhibition of microbial growth. Other functions of collectins are modulation of inflammatory, allergic responses, adaptive immune system and clearance of apoptotic cells.

Neutralite Avidin protein is a deglycosylated version of chicken avidin, with a mass of approximately 60,000 daltons. As a result of carbohydrate removal, lectin binding is reduced to undetectable levels, yet biotin binding affinity is retained because the carbohydrate is not necessary for this activity. Avidin has a high pI but NeutrAvidin has a near-neutral pI, minimizing non-specific interactions with the negatively-charged cell surface or with DNA/RNA. Neutravidin still has lysine residues that remain available for derivatization or conjugation.

<span class="mw-page-title-main">Peanut agglutinin</span>

Peanut agglutinin (PNA) is plant lectin protein derived from the fruits of Arachis hypogaea. Peanut agglutinin may also be referred to as Arachis hypogaea lectin. Lectins recognise and bind particular sugar sequences in carbohydrates; peanut agglutinin binds the carbohydrate sequence Gal-β(1-3)-GalNAc. The name "peanut agglutinin" originates from its ability to stick together (agglutinate) cells, such as neuraminidase-treated erythrocytes, which have glycoproteins or glycolipids on their surface which include the Gal-β(1-3)-GalNAc carbohydrate sequence.

<span class="mw-page-title-main">Legume lectin</span>

The legume lectins are a family of sugar-binding proteins or lectins found in the seeds and, in smaller amounts, in the roots, stems, leaves and bark of plants of the family Fabaceae. The exact function of the legume lectins in vivo is unknown but they are probably involved in the defense of plants against predators. Related proteins in other plant families and in animals have also been found. They have been used for decades as a model system for the study of protein-carbohydrate interactions, because they show a wide variety of binding specificities and are easy to obtain, purify, and characterize the structure of. Well-studied members of this protein family include phytohemagglutinin, soybean agglutinins, and concanavalin A.

<span class="mw-page-title-main">Hemagglutinin</span> Substance that causes red blood cells to agglutinate

In molecular biology, hemagglutinins are receptor-binding membrane fusion glycoproteins produced by viruses in the Paramyxoviridae and Orthomyxoviridae families. Hemagglutinins are responsible for binding to receptors on host cells to initiate viral attachment and infection.

BanLec is a lectin from the jacalin-related lectin family isolated from the fruit of the bananas Musa acuminata and Musa balbisiana. BanLec is one of the predominant proteins in the pulp of ripe bananas and has binding specificity for mannose and mannose-containing oligosaccharides. A 2010 study reported that BanLec was a potent inhibitor of HIV replication.

<span class="mw-page-title-main">M. Vijayan</span> Indian structural biologist (1941–2022)

Mamannamana Vijayan was an Indian structural biologist.

<span class="mw-page-title-main">Jacalin-like lectin domain</span>

In molecular biology, the jacalin-like lectin domain is a mannose-binding lectin domain with a beta-prism fold consisting of three 4-stranded beta-sheets, with an internal pseudo 3-fold symmetry. Some lectins in this group stimulate distinct T- and B-cell functions, such as Jacalin, which binds to the T-antigen and acts as an agglutinin. This domain is found in 1 to 6 copies in lectins. The domain is also found in the salt-stress induced protein from rice and an animal prostatic spermine-binding protein.

Macrophage inducible Ca2+-dependent lectin receptor, (abbreviated to Mincle), is a member of the C-type lectin superfamily encoded by the gene CLEC4E. It is a pattern recognition receptor that can recognize glycolipids including mycobacterial cord factor, trehalose-6,6'-dimycolate (TDM). The mincle receptor binds a range of carbohydrate structures, predominantly containing glucose or mannose, and play an important role in recognition of bacterial glycolipids by the immune system. Upon activation by cord factor, Mincle binds the Fc receptor FcRγ and Syk. Cord factor also binds and activates the related C-type lectin MCL. Upon receptor stimulation is PKC-δ activated, which subsequently phosphorylates CARD9 that triggers recruitment of BCL10 and MALT1, leading to a CARD-CC/BCL10/MALT1 (CBM) signaling complex. This signaling complex in turn triggers downstream recruitment of TRAF6 and NF-κB activation.

<span class="mw-page-title-main">Soybean agglutinin</span>

Soybean agglutinins (SBA) also known as soy bean lectins (SBL) are lectins found in soybeans. It is a family of similar legume lectins. As a lectin, it is an antinutrient that chelates minerals. In human foodstuffs, less than half of this lectin is deactivated even with extensive cooking.

Sunil Kumar Podder was an Indian molecular biologist and biophysicist, known for his biophysical studies on Ligand. Focusing his researches on the recognition processes in biological systems and their chemical specificity, he proposed a model for measuring the specificity using free energy of association of amino acids of proteins with nucleic acid bases.

Umesh Varshney is an Indian molecular biologist, academician and the head of a laboratory at the Indian Institute of Science, Bengaluru. He is a J. C. Bose National Fellow of the Department of Science and Technology and is known for his studies on protein synthesis and DNA repair in Escherichia coli and Mycobacterium tuberculosis. An elected fellow of the Indian Academy of Sciences, Indian National Science Academy and the National Academy of Sciences (India), he is also a recipient of the National Bioscience Award for Career Development of the Government of India. The Council of Scientific and Industrial Research, awarded him the Shanti Swarup Bhatnagar Prize for Science and Technology, one of the highest Indian science awards, in 2001, and then in 2014 with the G. N. Ramachandran Gold Medal for Excellence in Biological Sciences & Technology for his contributions to biological sciences.

Raghavan Varadarajan is an Indian biophysicist and a professor at the Indian Institute of Science. He is known for his researches in the fields of protein structure and protein folding and his contributions in developing vaccines and drugs for treating a type of fatal influenza and HIV-1. He is a former J. C. Bose National Fellow of the Department of Science and Technology and an elected fellow of the Indian Academy of Sciences and the Indian National Science Academy. The Council of Scientific and Industrial Research, the apex agency of the Government of India for scientific research, awarded him the Shanti Swarup Bhatnagar Prize for Science and Technology, one of the highest Indian science awards, in 2002, for his contributions to biological sciences.

Narayanaswamy Srinivasan was an Indian molecular biophysicist and a professor and the head of Proteins: Structure, Function and Evolutionary Group at the Molecular Biophysics Unit of the Indian Institute of Science. He is known for his researches in the fields of computational genomics and protein structure analysis. An elected fellow of the Indian Academy of Sciences and the National Academy of Sciences, India, he is a J. C. Bose National fellow of the Department of Biotechnology and a recipient of the National Bioscience Award for Career Development of the Department of Science and Technology. The Council of Scientific and Industrial Research, the apex agency of the Government of India for scientific research, awarded him the Shanti Swarup Bhatnagar Prize for Science and Technology, one of the highest Indian science awards, in 2007, for his contributions to biological sciences.

Balasubramanian Gopal is an Indian structural biologist, molecular biophysicist and a professor at the Molecular Biophysics Unit of the Indian Institute of Science. He is known for his studies on cell wall synthesis in Staphylococcus aureus and is an elected fellow of the National Academy of Sciences, India, Indian National Science Academy and the Indian Academy of Sciences. He received the National Bioscience Award for Career Development of the Department of Biotechnology in 2010. The Council of Scientific and Industrial Research, the apex agency of the Government of India for scientific research, awarded him the Shanti Swarup Bhatnagar Prize for Science and Technology, one of the highest Indian science awards, in 2015, for his contributions to biological sciences.

Kanakaraj Sekar is an Indian bioinformatician and a professor at the Department of Computational and Data Sciences of the Indian Institute of Science (IISc). Known for his studies in the field of bioinformatics, Sekar heads the Laboratory for Structural Biology and Bio-computing at IISc. The Department of Biotechnology of the Government of India awarded him the National Bioscience Award for Career Development, one of the highest Indian science awards, for his contributions to biosciences in 2004.

<span class="mw-page-title-main">Glycan-protein interactions</span> Class of biological intermolecular interactions

Glycan-Protein interactions represent a class of biomolecular interactions that occur between free or protein-bound glycans and their cognate binding partners. Intramolecular glycan-protein (protein-glycan) interactions occur between glycans and proteins that they are covalently attached to. Together with protein-protein interactions, they form a mechanistic basis for many essential cell processes, especially for cell-cell interactions and host-cell interactions. For instance, SARS-CoV-2, the causative agent of COVID-19, employs its extensively glycosylated spike (S) protein to bind to the ACE2 receptor, allowing it to enter host cells. The spike protein is a trimeric structure, with each subunit containing 22 N-glycosylation sites, making it an attractive target for vaccine search.

References

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  15. ↑ Banerjee R, Das K, Ravishankar R, Suguna K, Surolia A; Vijayan M (1996). "Conformation, protein-carbohydrate interactions and a novel subunit association in the refined structure of peanut lectin-lactose complex". Journal of Molecular Biology. 259 (2): 281–296. CiteSeerX   10.1.1.335.6342 . doi:10.1006/jmbi.1996.0319. PMID   8656429.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  16. ↑ Sharma V, Surolia A (1997). "Analyses of carbohydrate recognition by legume lectins: size of the combining site loops and their primary specificity". Journal of Molecular Biology. 267 (2): 433–445. doi:10.1006/jmbi.1996.0863. PMID   9096236.
  17. ↑ Sharma V, Srinivas VR, Adhikari P, Vijayan M; Surolia A (1998). "Molecular basis of recognition by Gal/GalNAc specific legume lectins: influence of Glu 129 on the specificity of peanut agglutinin (PNA) towards C2-substituents of galactose". Glycobiology. 8 (10): 1007–1012. doi: 10.1093/glycob/8.10.1007 . PMID   9719681.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  18. ↑ Thomas CJ, Surolia A (2000). "Mode of molecular recognition of L-fucose by fucose-binding legume lectins". Biochemical and Biophysical Research Communications. 268 (2): 262–267. doi:10.1006/bbrc.2000.2110. PMID   10679191.
  19. ↑ Srinivas VR, Acharya S, Rawat S, Sharma V; Surolia A (2000). "The primary structure of the acidic lectin from winged bean (Psophocarpus tetragonolobus): insights in carbohydrate recognition, adenine binding and quaternary association". FEBS Letters. 474 (1): 76–82. doi:10.1016/s0014-5793(00)01580-5. PMID   10828455.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  20. ↑ Ravishankar R, Ravindran M, Suguna K, Surolia A; Vijayan M (1997). "Crystal structure of the peanut lectin – T-antigen complex. Carbohydrate specificity generated by water bridges". Current Science. 72: 855–861.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  21. ↑ Reddy GB, Bharadwaj S; Surolia A (1999). "Thermal stability and mode of oligomerization of the tetrameric peanut agglutinin: a differential scanning calorimetry study". Biochemistry. 38 (14): 4464–4470. doi:10.1021/bi982828s. PMID   10194368.
  22. 1 2 Reddy GB, Srinivas VR, Ahmad N; Surolia A (1999). "Molten globule-like state of peanut lectin monomer retains its carbohydrate specificity. Implications in protein folding and legume lectin oligomerization". Journal of Biological Chemistry. 274 (8): 4500–4503. doi: 10.1074/jbc.274.8.4500 . PMID   9988681.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  23. ↑ Mitra N, Sinha S, Kini RM; Surolia A (2005). "Analysis of the peanut agglutinin molten globule-like intermediate by limited proteolysis". Biochimica et Biophysica Acta (BBA) - General Subjects. 1725 (3): 283–289. doi:10.1016/j.bbagen.2005.04.031. PMID   16051441.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  24. ↑ Hansia P, Dev S, Surolia A; Vishveshwara S (2007). "Insight into the early stages of thermal unfolding of peanut agglutinin by molecular dynamics simulations". Proteins. 69 (1): 32–42. doi:10.1002/prot.21512. PMID   17596827. S2CID   21088531.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  25. ↑ Kapoor M, Srinivas H, Kandiah E, Gemma E, Ellgaard L, Oscarson S, Helenius A; Surolia A (2003). "Interactions of substrate with calreticulin, an endoplasmic reticulum chaperone". Journal of Biological Chemistry. 278 (8): 6194–6200. doi: 10.1074/jbc.m209132200 . PMID   12464625.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  26. ↑ Gopalakrishnapai J, Gupta G, Karthikeyan T, Sinha S, Kandiah E, Gemma E, Oscarson S; Surolia A (2006). "Isothermal titration calorimetric study defines the substrate binding residues of calreticulin". Biochemical and Biophysical Research Communications. 351 (1): 14–20. doi:10.1016/j.bbrc.2006.09.164. PMID   17049488.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  27. ↑ Banerjee R, Mande SC, Ganesh V, Das K, Dhanaraj V, Mahanta SK, Suguna K, Surolia A; Vijayan M (1994). "Crystal structure of peanut lectin, a protein with an unusual quaternary structure". Proceedings of the National Academy of Sciences of the United States of America. 91 (1): 227–231. Bibcode:1994PNAS...91..227B. doi: 10.1073/pnas.91.1.227 . PMC   42920 . PMID   8278370.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  28. ↑ Sankaranarayanan R, Sekar K, Banerjee R, Sharma V, Surolia A; Vijayan M (1998). "A novel mode of carbohydrate recognition in jacalin, a Moraceae plant lectin with a beta-prism fold". Nature Structural Biology. 3 (7): 596–603. doi:10.1038/nsb0796-596. PMID   8673603. S2CID   23593928.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  29. ↑ Hosur MV, Nair B, Satyamurthy P, Misquith S, Surolia A; Kannan KK (1995). "X-ray structure of gelonin at 1.8 A resolution". Journal of Molecular Biology. 250 (3): 368–380. doi:10.1006/jmbi.1995.0383. PMID   7608981.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  30. ↑ Singha NC, Surolia N; Surolia A (1996). "On the relationship of thermodynamic parameters with the buried surface area in protein-ligand complex formation". Bioscience Reports. 16 (1): 1–10. doi:10.1007/bf01200996. PMID   8861535. S2CID   2509797.
  31. ↑ Swaminathan CP, Nandi A, Visweswariah SS; Surolia A (1999). "Thermodynamic analyses reveal role of water release in epitope recognition by a monoclonal antibody against the human guanylyl cyclase C receptor". Journal of Biological Chemistry. 274 (44): 31272–31278. doi: 10.1074/jbc.274.44.31272 . PMID   10531324.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  32. ↑ Srimal S, Surolia N, Balasubramanian S; Surolia A (1996). "Titration calorimetric studies to elucidate the specificity of the interactions of polymyxin B with lipopolysaccharides and lipid A". Biochemical Journal. 315 (Pt2): 679–686. doi:10.1042/bj3150679. PMC   1217250 . PMID   8615847.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  33. ↑ Thomas CJ, Surolia N; Surolia A (1999). "Surface plasmon resonance studies resolve the enigmatic endotoxin neutralizing activity of polymyxin B". Journal of Biological Chemistry. 274 (42): 29624–29627. doi: 10.1074/jbc.274.42.29624 . PMID   10514430.
  34. ↑ Thomas CJ, Surolia A (1999). "Kinetics of the interaction of endotoxin with polymyxin B and its analogs: a surface plasmon resonance analysis". FEBS Letters. 445 (2–3): 420–424. doi: 10.1016/s0014-5793(99)00150-7 . PMID   10094500.
  35. ↑ Bhor VM, Thomas CJ, Surolia N; Surolia A (2005). "Polymyxin B: an ode to an old antidote for endotoxic shock" (PDF). Molecular BioSystems. 1 (3): 213–222. doi:10.1039/b500756a. PMID   16880985.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  36. ↑ Pain D, Surolia A (1981). "Preparation of protein A-peroxidase monoconjugate using a heterobifunctional reagent, and its use in enzyme immunoassays". Journal of Immunological Methods. 40 (2): 219–230. doi:10.1016/0022-1759(81)90068-5. PMID   6265559.
  37. ↑ Pain D, Surolia A (1979). "Protein A-enzyme monoconjugate as a versatile tool for enzyme immunoassays". FEBS Letters. 107 (1): 73–76. doi:10.1016/0014-5793(79)80466-4. PMID   387451.
  38. ↑ Bhor VM, Dev S, Vasanthakumar GR, Kumar P, Sinha S; Surolia A (2006). "Broad substrate stereospecificity of the Mycobacterium tuberculosis 7-keto-8-aminopelargonic acid synthase: Spectroscopic and kinetic studies". Journal of Biological Chemistry. 281 (35): 25076–25088. doi: 10.1074/jbc.m604477200 . PMID   16769720.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  39. ↑ Sharma SK, Parasuraman P, Kumar G, Surolia N; Surolia A (2007). "Green tea catechins potentiate triclosan binding to enoyl-ACP reductase from Plasmodium falciparum (PfENR)". Journal of Medicinal Chemistry. 50 (4): 765–775. doi:10.1021/jm061154d. PMID   17263522.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  40. ↑ Mishra S, Karmodiya K, Surolia N; Surolia A (2008). "Synthesis and exploration of novel curcumin analogues as anti-malarial agents". Bioorganic and Medicinal Chemistry. 16 (6): 2894–2902. doi:10.1016/j.bmc.2007.12.054. PMID   18194869.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  41. ↑ Chakraborti S, Das L, Kapoor N, Das A, Dwivedi V, Poddar A, Chakraborti G, Janik M, Basu G, Panda D, Chakrabarti P, Surolia A; Bhattacharyya B (2011). "Curcumin recognizes a unique binding site of tubulin". Journal of Medicinal Chemistry. 54 (18): 6183–6196. doi:10.1021/jm2004046. PMID   21830815.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  42. ↑ Rai A, Surolia A; Panda D (2012). "An antitubulin agent BCFMT inhibits proliferation of cancer cells and induces cell death by inhibiting microtubule dynamics". PLOS ONE. 7 (8): e44311. Bibcode:2012PLoSO...744311R. doi: 10.1371/journal.pone.0044311 . PMC   3432122 . PMID   22952952.
  43. 1 2 Surolia N, Surolia A (2001). "Triclosan offers protection against blood stages of malaria by inhibiting enoyl-ACP reductase of Plasmodium falciparum". Nature Medicine. 7 (2): 167–173. doi:10.1038/84612. PMID   11175846. S2CID   44570829.
  44. 1 2 Mishra A (2018). "An allosteric inhibitor of Mycobacterium tuberculosis ArgJ: Implications to a novel combinatorial therapy". EMBO Molecular Medicine. 10 (4): e8038. doi:10.15252/emmm.201708038. PMC   5887547 . PMID   29483133.
  45. ↑ Gupta S, Chattopadhyay T, Pal Singh M; Surolia A (2010). "Supramolecular insulin assembly II for a sustained treatment of type 1 diabetes mellitus". Proceedings of the National Academy of Sciences of the United States of America. 107 (30): 13246–13251. Bibcode:2010PNAS..10713246G. doi: 10.1073/pnas.1005704107 . PMC   2922159 . PMID   20628017.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  46. ↑ "Good tidings for diabetes patients". The Hindu. 13 July 2010. Retrieved 27 March 2014.
  47. ↑ "Alternative solution to fight diabetes proposed". The Hindu. 31 January 2012. Retrieved 27 March 2014.
  48. ↑ "Biodata of Prof. A. Surolia". mbu.iisc.ernet.in. MBU. Archived from the original on 27 July 2012. Retrieved 27 March 2014.
  49. ↑ "Avadhesha Surolia". www.twas.org. TWAS. Retrieved 27 March 2014.
  50. ↑ "Member List". www.a-imbn.org. IMBN. Retrieved 27 March 2014.
  51. ↑ "Zone wise list of fellows and honorary fellows" (PDF). www.nasi.org.in. NASI. Retrieved 27 March 2014.
  52. ↑ "India joins elite life sciences group". Deccan Herald. 28 December 2006. Archived from the original on 5 March 2016. Retrieved 27 March 2014.
  53. ↑ "India joins Human Frontier Science Program Organisation". www.docstoc.com. DOCSTOC. Retrieved 27 March 2014.
  54. ↑ "National Representatives". www.intl-glyco.org. Retrieved 27 March 2014.
  55. ↑ "The Members of the IUBMB Executive Committee". www.iubmb.org. IUBMB. Retrieved 27 March 2014.
  56. 1 2 "Awards Recipients". insaindia.org. INSA. Archived from the original on 4 April 2014. Retrieved 27 March 2014.
  57. ↑ "JC Bose Fellows" (PDF). www.serb.gov.in. SERB. Retrieved 27 March 2014.
  58. ↑ "ICMR Awards and Prizes" (PDF). www.icmr.nic.in. ICMR. Archived from the original (PDF) on 4 March 2016. Retrieved 27 March 2014.
  59. ↑ "Recipients of TWAS Awards/Prizes". twas-old.ictp.it. TWAS. Retrieved 27 March 2014.
  60. ↑ "Shri Om Prakash Bhasin Awards". www.opbfawards.com. Retrieved 27 March 2014.
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