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		<summary type="html">&lt;p&gt;Reformat 1 archive link. &lt;a href=&quot;/w/index.php?title=User:GreenC/WaybackMedic_2.5&amp;amp;action=edit&amp;amp;redlink=1&quot; class=&quot;new&quot; title=&quot;User:GreenC/WaybackMedic 2.5 (page does not exist)&quot;&gt;Wayback Medic 2.5&lt;/a&gt;&lt;/p&gt;
&lt;p&gt;&lt;b&gt;New page&lt;/b&gt;&lt;/p&gt;&lt;div&gt;{{Short description|Indian glycobiologist}}&lt;br /&gt;
{{Context|date=May 2020}}&lt;br /&gt;
{{Use dmy dates|date=May 2018}}&lt;br /&gt;
{{Use Indian English|date=May 2018}}&lt;br /&gt;
&lt;br /&gt;
&amp;#039;&amp;#039;&amp;#039;Avadhesha Surolia&amp;#039;&amp;#039;&amp;#039; (born 3 December 1947, [[Kishangarh]], Rajasthan)&amp;lt;ref name=&amp;quot;Indian Fellow-Avadhesha Surolia&amp;quot;&amp;gt;{{Cite web |url=http://insaindia.res.in/detail/N90-1070 |title=Indian Fellow-Avadhesha Surolia |website=insaindia.org |publisher=INSA |access-date=2017-10-22 |archive-date=27 February 2020 |archive-url=https://web.archive.org/web/20200227094726/http://insaindia.res.in/detail/N90-1070 |url-status=dead }}&amp;lt;/ref&amp;gt; is a Glycobiologist at Indian Institute of Science (IISc), Bangalore. Presently, he is an Honorary Professor at the Molecular Biophysics Unit (MBU), IISc&amp;lt;ref name=ics&amp;gt;{{cite web|title=Avadhesha Surolia|url=http://ics2014bangalore.in/ics-resume/Avadhesha%20Surolia.pdf|website=ics2014bangalore.in|access-date=25 March 2014}}{{Dead link|date=October 2018 |bot=InternetArchiveBot |fix-attempted=yes }}&amp;lt;/ref&amp;gt;  and holds the Bhatnagar fellowship of the [[Council of Scientific and Industrial Research]] (CSIR), India.&amp;lt;ref name=ics&amp;gt;{{cite web|title=Avadhesha Surolia|url=http://ics2014bangalore.in/ics-resume/Avadhesha%20Surolia.pdf|website=ics2014bangalore.in|access-date=25 March 2014}}{{Dead link|date=October 2018 |bot=InternetArchiveBot |fix-attempted=yes }}&amp;lt;/ref&amp;gt;  He is known for his work on lectin structure and interactions, orientation and dynamics of cell surface carbohydrate receptors and protein folding, diabetes, anti-malarials 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 interest&lt;br /&gt;
&lt;br /&gt;
==Education and career==&lt;br /&gt;
&lt;br /&gt;
Surolia obtained his bachelor&amp;#039;s degree in chemistry and biology from University of Jodhpur, in 1970. He earned his master&amp;#039;s degree in biochemistry from [[Maharaja Sayajirao University of Baroda|Maharaja Sayajirao University]], 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 D.Sc. degree by Madras University.&lt;br /&gt;
After his doctoral studies he joined [[Indian Institute of Chemical Biology]] (IICB), Calcutta, India 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 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&amp;#039;s prestigious research institute, National Institute of Immunology, New Delhi.&amp;lt;ref name=insa&amp;gt;{{cite web|title=Indian Fellow|url=http://insaindia.org/detail.php?id=N90-1070|website=insaindia.org|publisher=INSA|access-date=25 March 2014|archive-url=https://web.archive.org/web/20160304054624/http://insaindia.org/detail.php?id=N90-1070|archive-date=4 March 2016|url-status=dead|df=dmy-all}}&amp;lt;/ref&amp;gt;&amp;lt;ref name=mbulab&amp;gt;{{cite web|title=Prof. Surolia&amp;#039;s Lab|url=http://mbu.iisc.ernet.in/~aslab/|website=mbu.iisc.ernet.in|publisher=MBU|access-date=25 March 2014}}&amp;lt;/ref&amp;gt;  During his tenure NII was recognized by Thomson Reuters Innovation Award in 2010 as the most innovative research institute nationally.&amp;lt;ref&amp;gt;{{cite web|title=Intellectual Property and Science|url=http://ip-science.thomsonreuters.com/ssr/india-innovation-awards-2010/#awardees|website=ip-science.thomsonreuters.com|publisher=Thomson Reuters|access-date=25 March 2014}}&amp;lt;/ref&amp;gt;&amp;lt;ref&amp;gt;{{cite web|title=THOMSON REUTERS AND CONFEDERATION OF INDIAN INDUSTRY (CII) RECOGNISE INDIA&amp;#039;S MOST INNOVATIVE ACADEMIC INSTITUTIONS AND ENTERPRISES|url=http://www.iii.gov.in/index.php?option=com_content&amp;amp;view=article&amp;amp;id=163:thomson-reuters-and-confederation-of-indian-industry-cii-recognise-indias-most-innovative-academic-institutions-and-enterprises&amp;amp;catid=69:archive-news|website=www.iii.gov.in|access-date=25 March 2014}}{{Dead link|date=November 2018 |bot=InternetArchiveBot |fix-attempted=yes }}&amp;lt;/ref&amp;gt;&lt;br /&gt;
He holds Honorary Professorship at [[Jawaharlal Nehru Centre for Advanced Scientific Research]] (JNCASR), Bangalore, India.&amp;lt;ref&amp;gt;{{cite web|title=Honorary Faculty|url=http://www.jncasr.ac.in/main_page.php/Honorary-Faculty/27/1/21/|website=www.jncasr.ac.in|publisher=JNCASR|access-date=25 March 2014}}&amp;lt;/ref&amp;gt;&lt;br /&gt;
In recognition of his contributions to medicine and science, he was conferred an Honorary D.Sc. degree in 2013 by [[Queen&amp;#039;s University Belfast|Queen&amp;#039;s University, Belfast]], UK.&amp;lt;ref&amp;gt;{{cite web|title=Winter Graduation|url=https://www.qub.ac.uk/home/Graduation/Summer2013HonoraryGraduates/ProfessorAvadheshaSurolia/|website=www.qub.ac.uk|publisher=QUB|access-date=25 March 2014|archive-url=https://web.archive.org/web/20131012215252/http://www.qub.ac.uk/home/Graduation/Summer2013HonoraryGraduates/ProfessorAvadheshaSurolia/|archive-date=12 October 2013|url-status=dead|df=dmy-all}}&amp;lt;/ref&amp;gt;&amp;lt;ref&amp;gt;{{cite web|url=http://www.mediator.qub.ac.uk/ms/graduations/summer2013/Hongrad13SH.wmv|website=www.mediator.qub.ac.uk|publisher=QUB|access-date=25 March 2014|title=Archived copy|archive-url=https://web.archive.org/web/20131011014029/http://www.mediator.qub.ac.uk/ms/graduations/summer2013/Hongrad13SH.wmv|archive-date=11 October 2013|url-status=dead|df=dmy-all}}&amp;lt;/ref&amp;gt;&amp;lt;ref&amp;gt;{{cite web|title=Team GB mastermind and international leading scientists honoured at Queen&amp;#039;s|url=http://qub.co.uk/home/ceao/News/Title,397826,en.html|archive-url=https://archive.today/20140901014818/http://qub.co.uk/home/ceao/News/Title,397826,en.html|url-status=dead|archive-date=1 September 2014|website=www.qub.co.uk|publisher=QUB|access-date=25 March 2014}}&amp;lt;/ref&amp;gt;&amp;lt;ref&amp;gt;{{cite web|title=Recent News from Queen&amp;#039;s|url=http://media.wix.com/ugd/896ed7_7e8d0bff8351cc0fbc9372e04576113a.pdf|website=media.wix.com|publisher=QUB|access-date=25 March 2014}}&amp;lt;/ref&amp;gt;&lt;br /&gt;
&lt;br /&gt;
==Scientific contributions==&lt;br /&gt;
&lt;br /&gt;
Surolia  has elucidated the role of [[glycosphingolipid]]s as biological receptors through studies on lectin-glycolipid interactions using liposomes.&amp;lt;ref&amp;gt;{{Cite book|first=Surolia A.|last=Satish P.R.|title=Liposome Methods and Protocols|chapter=Preparation and characterization of glycolipid-bearing multilamellar and unilamellar liposomes|series=Methods in Molecular Biology|date=2002|volume=199|pages=193–202|pmid=12094570|doi=10.1385/1-59259-175-2:193|isbn=978-1-59259-175-6}}&amp;lt;/ref&amp;gt;  He discovered novel blood group and tumor antigen specific lectins&amp;lt;ref&amp;gt;{{cite journal|last=Patanjali S.R.|author2=Surolia A.|first=Sajjan S. U.|title=Erythrocyte-binding studies on an acidic lectin from winged bean (Psophocarpus tetragonolobus)|journal=Biochemical Journal|date=1988|volume=252|issue=3|pages=625–631|pmid=2458714|doi=10.1042/bj2520625|pmc=1149194}}&amp;lt;/ref&amp;gt;  and made original contribution towards elucidation of the energetics and mechanism of protein-sugar recognition. He genetically re-engineered carbohydrate specificities of lectins imparting exquisite T-antigen tumor recognizing ability to peanut agglutinin.&amp;lt;ref&amp;gt;{{cite journal|last=Sharma V|first=Vijayan M|author2=Surolia A|title=Imparting exquisite specificity to peanut agglutinin for the tumor-associated Thomsen-Friedenreich antigen by redesign of its combining site|journal=Journal of Biological Chemistry|date=1996|volume=271|issue=35|pages=21209–21213|pmid=8702892|doi=10.1074/jbc.271.35.21209|doi-access=free}}&amp;lt;/ref&amp;gt;  He delineated the molecular basis of carbohydrate recognition by legume lectins&amp;lt;ref&amp;gt;{{cite journal|last=Banerjee R|first=Das K, Ravishankar R, Suguna K, Surolia A|author2=Vijayan M|title=Conformation, protein-carbohydrate interactions and a novel subunit association in the refined structure of peanut lectin-lactose complex|journal=Journal of Molecular Biology|date=1996|volume=259|issue=2|pages=281–296|pmid=8656429|doi=10.1006/jmbi.1996.0319|citeseerx=10.1.1.335.6342}}&amp;lt;/ref&amp;gt;&amp;lt;ref&amp;gt;{{cite journal|last=Sharma V|first=Surolia A|title=Analyses of carbohydrate recognition by legume lectins: size of the combining site loops and their primary specificity|journal=Journal of Molecular Biology|date=1997|volume=267|issue=2|pages=433–445|pmid=9096236|doi=10.1006/jmbi.1996.0863}}&amp;lt;/ref&amp;gt;&amp;lt;ref&amp;gt;{{cite journal|last=Sharma V|first=Srinivas VR, Adhikari P, Vijayan M|author2=Surolia A|title=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|journal=Glycobiology|date=1998|volume=8|issue=10|pages=1007–1012|pmid=9719681|doi=10.1093/glycob/8.10.1007|doi-access=free}}&amp;lt;/ref&amp;gt;&amp;lt;ref&amp;gt;{{cite journal|last=Thomas CJ|first=Surolia A|title=Mode of molecular recognition of L-fucose by fucose-binding legume lectins|journal=Biochemical and Biophysical Research Communications|date=2000|volume=268|issue=2|pages=262–267|pmid=10679191|doi=10.1006/bbrc.2000.2110}}&amp;lt;/ref&amp;gt;&amp;lt;ref&amp;gt;{{cite journal|last=Srinivas VR|first=Acharya S, Rawat S, Sharma V|author2=Surolia A|title=The primary structure of the acidic lectin from winged bean (Psophocarpus tetragonolobus): insights in carbohydrate recognition, adenine binding and quaternary association|journal=FEBS Letters|date=2000|volume=474|issue=1|pages=76–82|pmid=10828455|doi=10.1016/s0014-5793(00)01580-5|doi-access=free}}&amp;lt;/ref&amp;gt;  and demonstrated the novel C-H...O/N hydrogen bond in protein-sugar interactions.&amp;lt;ref&amp;gt;{{cite journal|last=Ravishankar R|first=Ravindran M, Suguna K, Surolia A|author2=Vijayan M|title=Crystal structure of the peanut lectin – T-antigen complex. Carbohydrate specificity generated by water bridges|journal=Current Science|date=1997|volume=72|pages=855–861}}&amp;lt;/ref&amp;gt;  He studied thermal unfolding of lectins that led to the discovery of novel modes of oligomerization in them.&amp;lt;ref&amp;gt;{{cite journal|last=Reddy GB|first=Bharadwaj S|author2=Surolia A|title=Thermal stability and mode of oligomerization of the tetrameric peanut agglutinin: a differential scanning calorimetry study|journal=Biochemistry|date=1999|volume=38|issue=14|pages=4464–4470|pmid=10194368|doi=10.1021/bi982828s}}&amp;lt;/ref&amp;gt;&amp;lt;ref name=&amp;quot;Reddy GB 1999 4500–4503&amp;quot;&amp;gt;{{cite journal|last=Reddy GB|first=Srinivas VR, Ahmad N|author2=Surolia A|title=Molten globule-like state of peanut lectin monomer retains its carbohydrate specificity. Implications in protein folding and legume lectin oligomerization|journal=Journal of Biological Chemistry|date=1999|volume=274|issue=8|pages=4500–4503|pmid=9988681|doi=10.1074/jbc.274.8.4500|doi-access=free}}&amp;lt;/ref&amp;gt;  He found a molten globule monomeric intermediate during the folding of peanut agglutinin that retained its carbohydrate binding ability - establishing &amp;#039;wet&amp;#039; molten globule as an &amp;quot;on pathway&amp;quot; folding intermediate and characterized other early intermediates.&amp;lt;ref name=&amp;quot;Reddy GB 1999 4500–4503&amp;quot;/&amp;gt;&amp;lt;ref&amp;gt;{{cite journal|last=Mitra N|first=Sinha S, Kini RM|author2=Surolia A|title=Analysis of the peanut agglutinin molten globule-like intermediate by limited proteolysis|journal=Biochimica et Biophysica Acta (BBA) - General Subjects|date=2005|volume=1725|issue=3|pages=283–289|pmid=16051441|doi=10.1016/j.bbagen.2005.04.031}}&amp;lt;/ref&amp;gt;&amp;lt;ref&amp;gt;{{cite journal|last=Hansia P|first=Dev S, Surolia A|author2=Vishveshwara S|title=Insight into the early stages of thermal unfolding of peanut agglutinin by molecular dynamics simulations|journal=Proteins|date=2007|volume=69|issue=1|pages=32–42|pmid=17596827|doi=10.1002/prot.21512}}&amp;lt;/ref&amp;gt;  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.&amp;lt;ref&amp;gt;{{cite journal|last=Kapoor M|first=Srinivas H, Kandiah E, Gemma E, Ellgaard L, Oscarson S, Helenius A|author2=Surolia A|title=Interactions of substrate with calreticulin, an endoplasmic reticulum chaperone|journal=Journal of Biological Chemistry|date=2003|volume=278|issue=8|pages=6194–6200|pmid=12464625|doi=10.1074/jbc.m209132200|doi-access=free}}&amp;lt;/ref&amp;gt;&amp;lt;ref&amp;gt;{{cite journal|last=Gopalakrishnapai J|first=Gupta G, Karthikeyan T, Sinha S, Kandiah E, Gemma E, Oscarson S|author2=Surolia A|title=Isothermal titration calorimetric study defines the substrate binding residues of calreticulin|journal=Biochemical and Biophysical Research Communications|date=2006|volume=351|issue=1|pages=14–20|pmid=17049488|doi=10.1016/j.bbrc.2006.09.164}}&amp;lt;/ref&amp;gt;  He discovered the unusual quaternary structure of peanut agglutinin&amp;lt;ref&amp;gt;{{cite journal|last=Banerjee R|first=Mande SC, Ganesh V, Das K, Dhanaraj V, Mahanta SK, Suguna K, Surolia A|author2=Vijayan M|title=Crystal structure of peanut lectin, a protein with an unusual quaternary structure|journal=Proceedings of the National Academy of Sciences of the United States of America|date=1994|volume=91|issue=1|pages=227–231|pmid=8278370|doi=10.1073/pnas.91.1.227|pmc=42920|bibcode=1994PNAS...91..227B}}&amp;lt;/ref&amp;gt;  and a novel lectin fold in Jacalin&amp;lt;ref&amp;gt;{{cite journal|last=Sankaranarayanan R|first=Sekar K, Banerjee R, Sharma V, Surolia A|author2=Vijayan M|title=A novel mode of carbohydrate recognition in jacalin, a Moraceae plant lectin with a beta-prism fold|journal=Nature Structural Biology|date=1998|volume=3|issue=7|pages=596–603|pmid=8673603|doi=10.1038/nsb0796-596}}&amp;lt;/ref&amp;gt;  as well as the structural basis of inactivation of ribosomes by gelonin.&amp;lt;ref&amp;gt;{{cite journal|last=Hosur MV|first=Nair B, Satyamurthy P, Misquith S, Surolia A|author2=Kannan KK|title=X-ray structure of gelonin at 1.8 A resolution|journal=Journal of Molecular Biology|date=1995|volume=250|issue=3|pages=368–380|pmid=7608981|doi=10.1006/jmbi.1995.0383}}&amp;lt;/ref&amp;gt; He enunciated that solvent reorganization in protein-ligand interactions modulates their specificities.&amp;lt;ref&amp;gt;{{cite journal|last=Singha NC|first=Surolia N|author2=Surolia A|title=On the relationship of thermodynamic parameters with the buried surface area in protein-ligand complex formation|journal=Bioscience Reports|date=1996|volume=16|issue=1|pages=1–10|pmid=8861535|doi=10.1007/bf01200996}}&amp;lt;/ref&amp;gt;&amp;lt;ref&amp;gt;{{cite journal|last=Swaminathan CP|first=Nandi A, Visweswariah SS|author2=Surolia A|title=Thermodynamic analyses reveal role of water release in epitope recognition by a monoclonal antibody against the human guanylyl cyclase C receptor|journal=Journal of Biological Chemistry|date=1999|volume=274|issue=44|pages=31272–31278|pmid=10531324|doi=10.1074/jbc.274.44.31272|doi-access=free}}&amp;lt;/ref&amp;gt;  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.&amp;lt;ref&amp;gt;{{cite journal|last=Srimal S|first=Surolia N, Balasubramanian S|author2=Surolia A|title=Titration calorimetric studies to elucidate the specificity of the interactions of polymyxin B with lipopolysaccharides and lipid A|journal=Biochemical Journal|date=1996|volume=315|issue=Pt2|pages=679–686|pmid=8615847|doi=10.1042/bj3150679|pmc=1217250}}&amp;lt;/ref&amp;gt;&amp;lt;ref&amp;gt;{{cite journal|last=Thomas CJ|first=Surolia N|author2=Surolia A|title=Surface plasmon resonance studies resolve the enigmatic endotoxin neutralizing activity of polymyxin B|journal=Journal of Biological Chemistry|date=1999|volume=274|issue=42|pages=29624–29627|pmid=10514430|doi=10.1074/jbc.274.42.29624|doi-access=free}}&amp;lt;/ref&amp;gt;&amp;lt;ref&amp;gt;{{cite journal|last=Thomas CJ|first=Surolia A|title=Kinetics of the interaction of endotoxin with polymyxin B and its analogs: a surface plasmon resonance analysis|journal=FEBS Letters|date=1999|volume=445|issue=2–3|pages=420–424|pmid=10094500|doi=10.1016/s0014-5793(99)00150-7|doi-access=free}}&amp;lt;/ref&amp;gt;&amp;lt;ref&amp;gt;{{cite journal|last=Bhor VM|first=Thomas CJ, Surolia N|author2=Surolia A|title=Polymyxin B: an ode to an old antidote for endotoxic shock|journal=Molecular BioSystems|date=2005|volume=1|issue=3|pages=213–222|pmid=16880985|doi=10.1039/b500756a|url=http://eprints.iisc.ac.in/4950/1/Polymyxin_B.pdf}}&amp;lt;/ref&amp;gt;  He popularized Protein A as a tool in immunology.&amp;lt;ref&amp;gt;{{cite journal|last=Pain D|first=Surolia A|title=Preparation of protein A-peroxidase monoconjugate using a heterobifunctional reagent, and its use in enzyme immunoassays|journal=Journal of Immunological Methods|date=1981|volume=40|issue=2|pages=219–230|pmid=6265559|doi=10.1016/0022-1759(81)90068-5}}&amp;lt;/ref&amp;gt;&amp;lt;ref&amp;gt;{{cite journal|last=Pain D|first=Surolia A|title=Protein A-enzyme monoconjugate as a versatile tool for enzyme immunoassays|journal=FEBS Letters|date=1979|volume=107|issue=1|pages=73–76|pmid=387451|doi=10.1016/0014-5793(79)80466-4|doi-access=free}}&amp;lt;/ref&amp;gt;  He discovered the broad substrate specificity of a key enzyme of biotin biosysnthesis from M. tuberculosis&amp;lt;ref&amp;gt;{{cite journal|last=Bhor VM|first=Dev S, Vasanthakumar GR, Kumar P, Sinha S|author2=Surolia A|title=Broad substrate stereospecificity of the Mycobacterium tuberculosis 7-keto-8-aminopelargonic acid synthase: Spectroscopic and kinetic studies|journal=Journal of Biological Chemistry|date=2006|volume=281|issue=35|pages=25076–25088|pmid=16769720|doi=10.1074/jbc.m604477200|doi-access=free}}&amp;lt;/ref&amp;gt;  and reported novel inhibitors for it. He has demonstrated the potential of common dietary components- curcumin and green tea catechins as anti-cancer and anti-malarial agents.&amp;lt;ref&amp;gt;{{cite journal|last=Sharma SK|first=Parasuraman P, Kumar G, Surolia N|author2=Surolia A|title=Green tea catechins potentiate triclosan binding to enoyl-ACP reductase from Plasmodium falciparum (PfENR)|journal=Journal of Medicinal Chemistry|date=2007|volume=50|issue=4|pages=765–775|pmid=17263522|doi=10.1021/jm061154d}}&amp;lt;/ref&amp;gt;&amp;lt;ref&amp;gt;{{cite journal|last=Mishra S|first=Karmodiya K, Surolia N|author2=Surolia A|title=Synthesis and exploration of novel curcumin analogues as anti-malarial agents|journal=Bioorganic and Medicinal Chemistry|date=2008|volume=16|issue=6|pages=2894–2902|pmid=18194869|doi=10.1016/j.bmc.2007.12.054}}&amp;lt;/ref&amp;gt;&amp;lt;ref&amp;gt;{{cite journal|last=Chakraborti S|first=Das L, Kapoor N, Das A, Dwivedi V, Poddar A, Chakraborti G, Janik M, Basu G, Panda D, Chakrabarti P, Surolia A|author2=Bhattacharyya B|title=Curcumin recognizes a unique binding site of tubulin|journal=Journal of Medicinal Chemistry|date=2011|volume=54|issue=18|pages=6183–6196|pmid=21830815|doi=10.1021/jm2004046}}&amp;lt;/ref&amp;gt;  He has developed a rhodanine, BCFMT, as a potential therapeutic for cancer.&amp;lt;ref&amp;gt;{{cite journal|last=Rai A|first=Surolia A|author2=Panda D|title=An antitubulin agent BCFMT inhibits proliferation of cancer cells and induces cell death by inhibiting microtubule dynamics|journal=PLOS ONE|date=2012|volume=7|issue=8|pmid=22952952|doi=10.1371/journal.pone.0044311|pmc=3432122|pages=e44311|bibcode=2012PLoSO...744311R}}&amp;lt;/ref&amp;gt;&lt;br /&gt;
Surolia co-discovered the existence of the fatty acid synthesis (FAS) pathway in Plasmodium and demonstrated its remarkable distinction from that of its human host.&amp;lt;ref name=&amp;quot;Surolia N 2001 167–173&amp;quot;&amp;gt;{{cite journal|last=Surolia N|first=Surolia A|title=Triclosan offers protection against blood stages of malaria by inhibiting enoyl-ACP reductase of Plasmodium falciparum|journal=Nature Medicine|date=2001|volume=7|issue=2|pages=167–173|pmid=11175846|doi=10.1038/84612}}&amp;lt;/ref&amp;gt;  He co-identified [[triclosan]], a widely used biocide, to compromise the growth of the parasite by inhibiting its enoyl-ACP reductase (FabI).&amp;lt;ref name=&amp;quot;Surolia N 2001 167–173&amp;quot;/&amp;gt; Recently, Surolia and colleagues have identified Pranlukast (an FDA 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.&amp;lt;ref name=&amp;quot;Mishra A 2018&amp;quot;&amp;gt;{{cite journal|last= Mishra A|title=An allosteric inhibitor of Mycobacterium tuberculosis ArgJ: Implications to a novel combinatorial therapy|journal=EMBO Molecular Medicine|volume=10|issue=4|pages=e8038|date=2018|doi=10.15252/emmm.201708038|pmid=29483133|pmc=5887547}}&amp;lt;/ref&amp;gt; Pranlukast demonstrated remarkable efficiency in pre‐clinical models of [[Mycobacterium tuberculosis|Mycobacterium Tuberculosis]].&amp;lt;ref name=&amp;quot;Mishra A 2018&amp;quot;&amp;gt;{{cite journal|last= Mishra A|title=An allosteric inhibitor of Mycobacterium tuberculosis ArgJ: Implications to a novel combinatorial therapy|journal=EMBO Molecular Medicine|volume=10|issue=4|pages=e8038|date=2018|doi=10.15252/emmm.201708038|pmid=29483133|pmc=5887547}}&amp;lt;/ref&amp;gt; &lt;br /&gt;
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.&amp;lt;ref&amp;gt;{{cite journal|last=Gupta S|first=Chattopadhyay T, Pal Singh M|author2=Surolia A|title=Supramolecular insulin assembly II for a sustained treatment of type 1 diabetes mellitus|journal=Proceedings of the National Academy of Sciences of the United States of America|date=2010|volume=107|issue=30|pages=13246–13251|pmid=20628017|doi=10.1073/pnas.1005704107|pmc=2922159|bibcode=2010PNAS..10713246G}}&amp;lt;/ref&amp;gt;&amp;lt;ref&amp;gt;{{cite news|title=Good tidings for diabetes patients|url=http://www.thehindu.com/sci-tech/health/medicine-and-research/good-tidings-for-diabetes-patients/article512681.ece|access-date=27 March 2014|newspaper=The Hindu|date=13 July 2010}}&amp;lt;/ref&amp;gt;&amp;lt;ref&amp;gt;{{cite news|title=Alternative solution to fight diabetes proposed|url=http://www.thehindu.com/todays-paper/tp-national/tp-kerala/alternative-solution-to-fight-diabetes-proposed/article2846537.ece|access-date=27 March 2014|newspaper=The Hindu|date=31 January 2012}}&amp;lt;/ref&amp;gt;  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.&lt;br /&gt;
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., Shantha Biotechniques Pvt. Ltd. He has about 19 national and international patents.&amp;lt;ref&amp;gt;{{cite web|title=Biodata of Prof. A. Surolia|url=http://mbu.iisc.ernet.in/~aslab/bio.html|website=mbu.iisc.ernet.in|publisher=MBU|access-date=27 March 2014|archive-url=https://web.archive.org/web/20120727013657/http://mbu.iisc.ernet.in/~aslab/bio.html|archive-date=27 July 2012|url-status=dead|df=dmy-all}}&amp;lt;/ref&amp;gt;&lt;br /&gt;
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.&lt;br /&gt;
&lt;br /&gt;
==Fellowships and memberships==&lt;br /&gt;
Surolia is a member of: [[The World Academy of Sciences|Third World Academy of Sciences]] (TWAS), Trieste, Italy&amp;lt;ref&amp;gt;{{cite web|title=Avadhesha Surolia|url=http://www.twas.org/member/surolia-avadhesha|website=www.twas.org|publisher=TWAS|access-date=27 March 2014}}&amp;lt;/ref&amp;gt;  and International Molecular Biologists Network.&amp;lt;ref&amp;gt;{{cite web|title=Member List|url=http://www.a-imbn.org/memb/memb_list.php?member_level=Member&amp;amp;search_keyfield=&amp;amp;search_keyword=&amp;amp;page=2|website=www.a-imbn.org|publisher=IMBN|access-date=27 March 2014}}&amp;lt;/ref&amp;gt; He is a fellow of all the science academies in the country- National Science Academy, [[Indian National Science Academy]] and Indian Academy of Sciences.&amp;lt;ref name=&amp;quot;Indian Fellow-Avadhesha Surolia&amp;quot; /&amp;gt;&amp;lt;ref&amp;gt;{{cite web|title=Zone wise list of fellows and honorary fellows|url=http://www.nasi.org.in/ZONE%20_2013_%20FINAL%20-%20IDS.pdf|website=www.nasi.org.in|publisher=NASI|access-date=27 March 2014}}&amp;lt;/ref&amp;gt; He was a member of the   Board of Trustees, Human Frontier Scientific Programme (HFSP, Strasbourg).&amp;lt;ref name=ics /&amp;gt;&amp;lt;ref&amp;gt;{{cite news|title=India joins elite life sciences group|url=http://archive.deccanherald.com/deccanherald/dec282006/national22402520061227.asp|access-date=27 March 2014|newspaper=Deccan Herald|date=28 December 2006|archive-url=https://web.archive.org/web/20160305023256/http://archive.deccanherald.com/deccanherald/dec282006/national22402520061227.asp|archive-date=5 March 2016|url-status=dead|df=dmy-all}}&amp;lt;/ref&amp;gt;&amp;lt;ref&amp;gt;{{cite web|title=India joins Human Frontier Science Program Organisation|url=http://www.docstoc.com/docs/5445349/HFSPO-Press-Release-Strasbourg-December-India-joins-Human-Frontier|website=www.docstoc.com|publisher=DOCSTOC|access-date=27 March 2014}}&amp;lt;/ref&amp;gt;  He is the only Indian member of the International Glycoconjugate Organization since 1998 and served as its president from 2001-2004.&amp;lt;ref name=mbulab /&amp;gt;&amp;lt;ref&amp;gt;{{cite web|title=National Representatives|url=http://www.intl-glyco.org/national_representatives.html|website=www.intl-glyco.org|access-date=27 March 2014}}&amp;lt;/ref&amp;gt;  &lt;br /&gt;
He has been a visiting scientist at Massachusetts Institute of Technology, University of Maryland and University of Michigan, USA.&amp;lt;ref name=mbulab /&amp;gt; &lt;br /&gt;
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).&amp;lt;ref name=ics /&amp;gt;&amp;lt;ref&amp;gt;{{cite web|title=The Members of the IUBMB Executive Committee|url=http://www.iubmb.org/index.php?id=17|website=www.iubmb.org|publisher=IUBMB|access-date=27 March 2014}}&amp;lt;/ref&amp;gt;&lt;br /&gt;
He is in the editorial advisory board of&amp;#039;&amp;#039; IUBMB-Life&amp;#039;&amp;#039; and&amp;#039;&amp;#039; PLoS ONE.&amp;#039;&amp;#039; He has served as an editor of the &amp;#039;&amp;#039;Proceedings of the Indian National Science Academy&amp;#039;&amp;#039; from 1998 to 2001. He is an editorial board member of the &amp;#039;&amp;#039;Proceedings of the National Academy of Sciences (India)&amp;#039;&amp;#039; and the&amp;#039;&amp;#039; Indian Journal of Biotechnology.&amp;#039;&amp;#039;&lt;br /&gt;
&lt;br /&gt;
==Awards==&lt;br /&gt;
&lt;br /&gt;
Jawaharlal Nehru Birth Centenary Lecture (2008).,&amp;lt;ref name=insaaward&amp;gt;{{cite web|title=Awards Recipients |url=http://www.insaindia.org/recipients.php |archive-url=https://archive.today/20140404115326/http://www.insaindia.org/recipients.php |url-status=dead |archive-date=4 April 2014 |website=insaindia.org |publisher=INSA |access-date=27 March 2014 }}&amp;lt;/ref&amp;gt; B.K. Bachhawat Memorial Award 2007, J.C.Bose Fellowship (2006),&amp;lt;ref&amp;gt;{{cite web|title=JC Bose Fellows|url=http://www.serb.gov.in/pdfs/research/Contents.pdf|website=www.serb.gov.in|publisher=SERB|access-date=27 March 2014}}&amp;lt;/ref&amp;gt; Dr. B.R. Ambedkar Centenary Award for Excellence in Biomedical Research	(2003),&amp;lt;ref&amp;gt;{{cite web|title=ICMR Awards and Prizes|url=http://www.icmr.nic.in/annual/icmrhq2004-05/awards%20&amp;amp;%20prizes.pdf|website=www.icmr.nic.in|publisher=ICMR|access-date=27 March 2014|archive-url=https://web.archive.org/web/20160304212316/http://icmr.nic.in/annual/icmrhq2004-05/Awards%20%26%20Prizes.pdf|archive-date=4 March 2016|url-status=dead|df=dmy-all}}&amp;lt;/ref&amp;gt; Goyal Prize in the area of Life Sciences (2002),&amp;lt;ref name=&amp;quot;Indian Fellow-Avadhesha Surolia&amp;quot; /&amp;gt; [[TWAS Prize]] in Biology (2001),&amp;lt;ref&amp;gt;{{cite web|title=Recipients of TWAS Awards/Prizes|url=http://twas-old.ictp.it/prog/prizes/recipients-of-twas-awards-prizes#2001|website=twas-old.ictp.it|publisher=TWAS|access-date=27 March 2014}}&amp;lt;/ref&amp;gt; Professor GN Ramachandran  60th  Birthday  Commemoration  Medal (2000),&amp;lt;ref name=insaaward /&amp;gt; Alumni  Award (IISc, 1999),&amp;lt;ref name=&amp;quot;Indian Fellow-Avadhesha Surolia&amp;quot; /&amp;gt; Ranbaxy  Science Foundation  Award  in  Basic  Medical Sciences (1995),&amp;lt;ref name=&amp;quot;Indian Fellow-Avadhesha Surolia&amp;quot; /&amp;gt; Shri Om Prakhash  Bhasin  Award for  Biotechnology (1993),&amp;lt;ref&amp;gt;{{cite web|title=Shri Om Prakash Bhasin Awards|url=http://www.opbfawards.com/biotechnology.html|website=www.opbfawards.com|access-date=27 March 2014}}&amp;lt;/ref&amp;gt; FICCI award  for outstanding research in Biological Sciences (1993), W.H.  Stillmark Prize (Honorary) for outstanding research contributions on lectins (1990),&amp;lt;ref name=&amp;quot;Indian Fellow-Avadhesha Surolia&amp;quot; /&amp;gt; S.S.  Bhatnagar Award for Outstanding Research in Biological Sciences (1987),&amp;lt;ref name=&amp;quot;Indian Fellow-Avadhesha Surolia&amp;quot; /&amp;gt; INSA Young Scientist Medal (1976)&amp;lt;ref name=&amp;quot;Indian Fellow-Avadhesha Surolia&amp;quot; /&amp;gt;&lt;br /&gt;
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== References ==&lt;br /&gt;
{{Reflist}}&lt;br /&gt;
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== External links ==&lt;br /&gt;
* {{Cite web |url=https://www.indiatoday.in/india/photo/profile-of-top-25-scientists-in-india-366262-2011-09-11 |title=Profile of Top 25 scientists in India |date=2011-09-11 |website=India Today |language=en-US |access-date=2018-01-17}}&lt;br /&gt;
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{{Authority control}}&lt;br /&gt;
&lt;br /&gt;
{{SSBPST recipients in Biological Science}}&lt;br /&gt;
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{{DEFAULTSORT:Surolia, Avadhesha}}&lt;br /&gt;
[[Category:1947 births]]&lt;br /&gt;
[[Category:20th-century Indian biologists]]&lt;br /&gt;
[[Category:People from Ajmer district]]&lt;br /&gt;
[[Category:University of Madras alumni]]&lt;br /&gt;
[[Category:Living people]]&lt;br /&gt;
[[Category:Scientists from Rajasthan]]&lt;br /&gt;
[[Category:TWAS laureates]]&lt;br /&gt;
[[Category:Recipients of the Shanti Swarup Bhatnagar Award in Biological Science]]&lt;/div&gt;</summary>
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