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{{short description|Indian biophysicist (born 1944)}}
{{Use dmy dates|date=January 2019}}
{{Use Indian English|date=January 2019}}
{{Infobox scientist
{{Infobox scientist
|name = Tej P. Singh
| name = Tej Pal Singh
| image = TPSingh.jpg
|color=slate
|image = TPSingh.jpg
| image_size = 200px
| birth_date = {{birth year|1944}} (age {{age|df=y|1944|01|01}})
|image_size = 200px
|residence = [[New Delhi]]
| citizenship =
|citizenship = India
| nationality = [[Indian people|Indian]]
| field = Rational structure based Drug Design
|nationality = [[India]]n
| work_institutions = [[All India Institute of Medical Sciences]]
|field = Rational structure based Drug Design
|work_institutions = [[All India Institute of Medical Sciences]]
| alma_mater = [[Indian Institute of Science, Bangalore]]
| known_for = Protein Structure Determination, Peptide Design<br>Drug Design
|alma_mater = [[Indian Institute of Science, Bangalore]]
| prizes = Goyal Prize 2010 for Life Sciences <br /> Distinguished Biotechnology Research Professor (DBT) (2009)<br /> Distinguished Biotechnologist (DBT) (2006) <br /> GN Ramachandran Gold Medal CSIR)
|known_for = Protein Structure Determination, Peptide Design, Drug Design
| children = [[Vineeta Singh]] (daughter)
|prizes = Goyal Prize 2010 for Life Sciences <br /> Distinguished Biotechnology Research Professor (DBT) (2009)<br /> Distinguished Biotechnologist (DBT) (2006) <br /> GN Ramachandran Gold Medal CSIR)
}}
}}
'''Tej Pal Singh''' (born 1944) is an Indian [[biophysicist]] known for his work in the fields of rational structure-based drug design, structural biology of proteins and X-ray crystallography.<ref name="On ResearchGate">{{Cite web |url=https://www.researchgate.net/profile/Tej_Singh |title=On ResearchGate |date=2018-01-29 |access-date=2018-01-29}}</ref> He has played an active role in the development of drug design in the fields of antibacterial therapeutics,<ref>{{Cite journal|last1=Sharma|first1=Pradeep|last2=Dube|first2=Divya|last3=Sinha|first3=Mau|last4=Yadav|first4=Savita|last5=Kaur|first5=Punit|last6=Sharma|first6=Sujata|last7=Singh|first7=Tej P.|date=2013-01-01|title=Structural insights into the dual strategy of recognition by peptidoglycan recognition protein, PGRP-S: structure of the ternary complex of PGRP-S with lipopolysaccharide and stearic acid|journal=PLOS ONE|volume=8|issue=1|pages=e53756|doi=10.1371/journal.pone.0053756|issn=1932-6203|pmc=3541179|pmid=23326499|bibcode=2013PLoSO...853756S|doi-access=free}}</ref><ref>{{Cite journal|last1=Singh|first1=Amit Kumar|last2=Singh|first2=Nagendra|last3=Sharma|first3=Sujata|last4=Singh|first4=S. Baskar|last5=Kaur|first5=Punit|last6=Bhushan|first6=A.|last7=Srinivasan|first7=A.|last8=Singh|first8=Tej P.|date=2008-02-29|title=Crystal structure of lactoperoxidase at 2.4 A resolution|journal=Journal of Molecular Biology|volume=376|issue=4|pages=1060–1075|doi=10.1016/j.jmb.2007.12.012|issn=1089-8638|pmid=18191143}}</ref><ref>{{Cite journal|last1=Rastogi|first1=Nilisha|last2=Nagpal|first2=Nitish|last3=Alam|first3=Hammad|last4=Pandey|first4=Sadanand|last5=Gautam|first5=Lovely|last6=Sinha|first6=Mau|last7=Shin|first7=Kouichirou|last8=Manzoor|first8=Nikhat|last9=Virdi|first9=Jugsharan S.|date=2014-01-01|title=Preparation and antimicrobial action of three tryptic digested functional molecules of bovine lactoferrin|journal=PLOS ONE|volume=9|issue=3|pages=e90011|doi=10.1371/journal.pone.0090011|issn=1932-6203|pmc=3940724|pmid=24595088|bibcode=2014PLoSO...990011R|doi-access=free}}</ref><ref>{{Cite journal|last1=Rastogi|first1=Nilisha|last2=Singh|first2=Avinash|last3=Pandey|first3=Sada Nand|last4=Sinha|first4=Mau|last5=Bhushan|first5=Asha|last6=Kaur|first6=Punit|last7=Sharma|first7=Sujata|last8=Singh|first8=Tej P.|date=2014-06-01|title=Structure of the iron-free true C-terminal half of bovine lactoferrin produced by tryptic digestion and its functional significance in the gut|journal=The FEBS Journal|volume=281|issue=12|pages=2871–2882|doi=10.1111/febs.12827|issn=1742-4658|pmid=24798798|s2cid=24534041|doi-access=free}}</ref><ref name="auto1">{{Cite journal|last1=Singh|first1=Avinash|last2=Gautam|first2=Lovely|last3=Sinha|first3=Mau|last4=Bhushan|first4=Asha|last5=Kaur|first5=Punit|last6=Sharma|first6=Sujata|last7=Singh|first7=T. P.|date=2014-01-01|title=Crystal structure of peptidyl-tRNA hydrolase from a Gram-positive bacterium, Streptococcus pyogenes at 2.19 Å resolution shows the closed structure of the substrate-binding cleft|journal=FEBS Open Bio|volume=4|pages=915–922|doi=10.1016/j.fob.2014.10.010|issn=2211-5463|pmc=4226762|pmid=25389518}}</ref> [[tuberculosis]],<ref>{{Cite journal|last1=Sharma|first1=Pradeep|last2=Yamini|first2=Shavait|last3=Dube|first3=Divya|last4=Singh|first4=Amar|last5=Mal|first5=Gorakh|last6=Pandey|first6=Nisha|last7=Sinha|first7=Mau|last8=Singh|first8=Abhay Kumar|last9=Dey|first9=Sharmistha|date=2013-01-01|title=Structural basis of the binding of fatty acids to peptidoglycan recognition protein, PGRP-S through second binding site|journal=Archives of Biochemistry and Biophysics|volume=529|issue=1|pages=1–10|doi=10.1016/j.abb.2012.11.001|issn=1096-0384|pmid=23149273}}</ref><ref name="auto1"/><ref>{{Cite journal|last1=Singh|first1=Avinash|last2=Kumar|first2=Ashok|last3=Gautam|first3=Lovely|last4=Sharma|first4=Pradeep|last5=Sinha|first5=Mau|last6=Bhushan|first6=Asha|last7=Kaur|first7=Punit|last8=Sharma|first8=Sujata|last9=Arora|first9=Ashish|date=2014-11-01|title=Structural and binding studies of peptidyl-tRNA hydrolase from Pseudomonas aeruginosa provide a platform for the structure-based inhibitor design against peptidyl-tRNA hydrolase|journal=The Biochemical Journal|volume=463|issue=3|pages=329–337|doi=10.1042/BJ20140631|issn=1470-8728|pmid=25101795}}</ref> [[inflammation]],<ref>{{Cite journal|last1=Shukla|first1=Prakash Kumar|last2=Gautam|first2=Lovely|last3=Sinha|first3=Mau|last4=Kaur|first4=Punit|last5=Sharma|first5=Sujata|last6=Singh|first6=Tej P.|date=2015-04-01|title=Structures and binding studies of the complexes of phospholipase A2 with five inhibitors|journal=Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics|volume=1854|issue=4|pages=269–277|doi=10.1016/j.bbapap.2014.12.017|issn=0006-3002|pmid=25541253}}</ref><ref name="auto">{{Cite journal|last1=Sharma|first1=Pradeep|last2=Dube|first2=Divya|last3=Singh|first3=Amar|last4=Mishra|first4=Biswajit|last5=Singh|first5=Nagendra|last6=Sinha|first6=Mau|last7=Dey|first7=Sharmistha|last8=Kaur|first8=Punit|last9=Mitra|first9=Dipendra K.|date=2011-05-06|title=Structural basis of recognition of pathogen-associated molecular patterns and inhibition of proinflammatory cytokines by camel peptidoglycan recognition protein|journal=The Journal of Biological Chemistry|volume=286|issue=18|pages=16208–16217|doi=10.1074/jbc.M111.228163|issn=1083-351X|pmc=3091228|pmid=21454594|doi-access=free}}</ref> [[cancer]]<ref>{{Cite journal|last1=Bilgrami|first1=Sameeta|last2=Yadav|first2=Savita|last3=Kaur|first3=Punit|last4=Sharma|first4=Sujata|last5=Perbandt|first5=Markus|last6=Betzel|first6=Christian|last7=Singh|first7=Tej P.|date=2005-08-23|title=Crystal structure of the disintegrin heterodimer from saw-scaled viper (Echis carinatus) at 1.9 A resolution|journal=Biochemistry|volume=44|issue=33|pages=11058–11066|doi=10.1021/bi050849y|issn=0006-2960|pmid=16101289}}</ref><ref>{{Cite journal|last1=Mohanty|first1=Ashok K.|last2=Singh|first2=Garima|last3=Paramasivam|first3=Murugan|last4=Saravanan|first4=Kolandaivelu|last5=Jabeen|first5=Talat|last6=Sharma|first6=Sujata|last7=Yadav|first7=Savita|last8=Kaur|first8=Punit|last9=Kumar|first9=Pravindra|date=2003-04-18|title=Crystal structure of a novel regulatory 40-kDa mammary gland protein (MGP-40) secreted during involution|journal=The Journal of Biological Chemistry|volume=278|issue=16|pages=14451–14460|doi=10.1074/jbc.M208967200|issn=0021-9258|pmid=12529329|doi-access=free}}</ref> and [[Stomach disease|gastropathy]].<ref name="auto"/><ref>{{Cite journal|last1=Mir|first1=Rafia|last2=Singh|first2=Nagendra|last3=Vikram|first3=Gopalakrishnapillai|last4=Sinha|first4=Mau|last5=Bhushan|first5=Asha|last6=Kaur|first6=Punit|last7=Srinivasan|first7=Alagiri|last8=Sharma|first8=Sujata|last9=Singh|first9=Tej P.|date=2010-08-15|title=Structural and binding studies of C-terminal half (C-lobe) of lactoferrin protein with COX-2-specific non-steroidal anti-inflammatory drugs (NSAIDs)|journal=Archives of Biochemistry and Biophysics|volume=500|issue=2|pages=196–202|doi=10.1016/j.abb.2010.05.026|issn=1096-0384|pmid=20515646}}</ref>
'''Tej P. Singh''' (तेज प सिंह) is an eminent [[India]]n [[biophysicist]] and a scientific leader who has made original and novel contributions in the fields of Rational Structure based drug design, Protein Structure biology and X-ray crystallography. He has played an active role in the development of research programmes on drug design in the fields of Tuberculosis, Inflammation, Cancer, Epilepsy, Gastropathy and Arthritis in India. He has published more than 350 research papers in leading international journals. Since he has been implementing an extensive programme on structure determinations of new proteins and structure - based rational drug design, he has submitted the highest number of protein structures in India in the Protein Data Bank (PDB). He has also mentored more than 70 MSc, PhD, MD and Post-Doc students who are currently independent group leaders in leading scientific institutions in various parts of the country. He has made significant collaborations with other academic institutions as well as industry partners all over the country. He has been nominated as a fellow of six national and international academies, namely, the Third World Academy of Sciences, Indian National Science Academy, National Academy of Sciences, Indian Academy of Sciences, Alexander von Humboldt Foundation and Biotech Research Society of India. He has been awarded various national and international awards over the years, for instance, the Jawaharlal Nehru Birth Centenary Lecture Award of INSA (2011), Annual Award of the Instrumentation Society of India (2011), CSIR Foundation Day Lecture award (2010), Goyal Prize in Life Sciences (2007), Professor G.N. Ramachandran CSIR Gold Medal for the Excellence in Biological Sciences and Technology (2006), Professor G.N. Ramachandran 60th Birthday Commemoration INSA Medal (2006) etc.


He is first Indian to receive all the six Ramachandran awards of the country.<ref>{{Cite web |date=19 March 2020 |title=Prof T P Singh became the first Indian to receive all Ramachandran Awards |url=https://www.biotechexpressmag.com/prof-t-p-singh-became-the-first-indian-to-receive-all-g-n-ramachandran-awards-of-our-country/ |url-status=live |archive-url=https://web.archive.org/web/20220506111515/https://www.biotechexpressmag.com/prof-t-p-singh-became-the-first-indian-to-receive-all-g-n-ramachandran-awards-of-our-country/ |archive-date=6 May 2022 |access-date=6 May 2022 |website=biotechexpressmag.com}}</ref> He is a fellow of six academies, namely, the [[Third World Academy of Sciences]], [[Indian National Science Academy]], [[National Academy of Sciences]], [[Indian Academy of Sciences]], [[Alexander von Humboldt Foundation]] and Biotech Research Society of India.<ref>{{Cite web|url=https://www.brsi.in/|title=BRSI|website=www.brsi.in}}</ref>
==Work==
The three-dimensional structures of various proteins including [[lactoperoxidase]] and [[lactoferrin]] from several species, [[ribosome]] inactivating protein and its complex with a natural ligand from [[mistletoe]], bifunctional inhibitor proteins from plant seeds and various [[serine proteases]] and their inhibitors have been determined by his group.

The elaborate structural studies of proteins from several important systems as potential drug targets such as [[phospholipase]] A2, [[cyclooxygenase]], [[lipoxygenase]], [[endothelin]] receptor, endothelin converting enzyme, [[breast cancer]] regression proteins and matrix metanosomal proteins as well as their complexes with natural and designed synthetic ligands have been carried out.

His laboratory has submitted more than 301 sets of proteins structure coordinates in the [[protein data bank]] (PDB) which makes it the highest number in India. Initially, he had contributed significantly on the structure - function studies of a number of [[antipyretic]], [[analgesic]] and anti-inflammatory agents and then on [[antibactrial]] sufonamides and their derivatives. He had developed the rules of peptide design with alpha, beta – dehydro - amino acids through extensive studies using syntheses, and X-ray and NMR structure determinations. These design rules are being exploited for making specific peptides to act as tight inhibitors of target enzymes and potent antagonists of target receptors for eventually leading to useful therapeutic agents.

As part of his protein structural studies, a large number of structures of [[lactoferrin]] proteins from various species in iron-saturated and apo-forms as well as those of its proteolytically generated monoferric functional N- and C-lobes have been determined in his laboratory through which it was demonstrated that large scale conformational changes occur in the structures of lactoferrins upon iron-binding and iron-release, cations other than ferric ion also bind to the iron-binding cleft but with lower affinity, similarly anions other than carbonate/bicarbonate can also bind with reduced potency, and bilobal [[lactoferrin]] can be converted into two functional N-terminal and C-terminal lobes with [[proteinase]] K. It was only his group in the whole world that successfully demonstrated the proteolytic production of N- and C-terminal molecular halves of lactoferrin and determined their three-dimensional structures. These studies have provided valuable insights into the structural basis of iron-binding and iron-release in lactoferrins and their roles as antibacterial agents and in other therapeutic applications.

While carrying out enzymatic cleavage of lactoferrin proteins, a novel [[Antifungal protein|antifungal]] decapeptide was discovered whose excellent potency against bacterial infections has been established.

His group has carried out extensive structural studies of [[phospholipase]] A2 enzymes and their complexes with various natural compounds, substrate analogues, non-steroidal anti-inflammatory agents and designed peptides. The new molecules have also been designed against cyclooxygenase and lypoxygenase. The enzymes phospholipase A2, cyclooxygenase and lypoxygenase are involved in the production of pro-inflammatory compounds collectively called as eicosanoids. He has already developed several highly potent inhibitors that are under consideration for further evaluation as anti-inflammatory agents. His group has been practicing the rational approach of structure-based drug design for developing therapeutic agents against various inflammatory disorders such as rheumatism and arthritis using PLA2, COX-2 and LOX enzymes as macromolecular targets.

In yet another area of current interest, his group has determined the crystal structures of several secretory glycoproteins isolated from dry secretions of various mammalian species including humans. This is a new class of proteins, first time detected whose functions and structures were unknown. These proteins are implicated as protective signaling factors in the large scale tissue remodeling processes. Their role in the breast cancers as protective factors for the breast cancer cells makes them important targets for structure - based drug design and offers opportunities for developing new therapeutic agents against breast cancer. He has been able to design several peptides that bind to these proteins with potencies ranging up to 10-7 M. The crystal structures of the complexes of these proteins with designed peptides have helped in identifying the site of binding in this protein. The structures of the complexes with various oligosachharides have provided information about the potencies of sugar binding. It also indicated the type and nature of sugars that will bind to this class of proteins specifically. Furthermore, several crystal structures of the ternary complexes of these proteins with peptides and sugars have helped in understanding the mode of binding of these proteins to cell surface receptors.

Recently he initiated a new programme on [[Clinical Proteomics]] in which it is intended to characterize all the proteins that are expressed during various patho/physiological conditions. The newly identified proteins will either be useful as biomarkers or they may be associated with the progression of diseases making them important targets for drug design.

He has published more than 307 research papers in the leading journals.

{| class="wikitable" border="1"
|-
|<!--column1-->[[File:PGRP.png|200px]]
|<!--column2-->[[File:LP.png|200px]]
|<!--column3-->[[File:Lf.png|200px]]
|<!--column4-->[[File:SPX.png|200px]]

|-
|- style="background: black; color: white"
|<!--column1-->Structure of Peptidoglycan Recognition Protein
|<!--column2-->Structure of Lactoperoxidase
|<!--column3-->Structure of Lactoferrin
|<!--column3-->Structure of SPX-40
|-
|<!--column1-->[[File:Phyco.png|200px]]
|<!--column2-->[[File:Nt.png|200px]]
|<!--column3-->[[File:Viscumin.png|200px]]
|<!--column4-->[[File:ZAG.png|200px]]
|-
|- style="background: black; color: white"
|<!--column1-->Structure of Phycoerythrin
|<!--column2-->Structure of Neurotoxin
|<!--column3-->Structure of Viscumin
|<!--column3-->Structure of Complex of ZAG and PIP

|}<!--end wikitable-->


==Education==
==Education==


Professor Tej Singh obtained his Masters in Science in first rank from the University of [[Allahabad]]. He started his research career in 1971 as a graduate student at the [[Indian Institute of Science]], [[Bangalore]]. He obtained his Ph. D degree in the mid 70's working on the crystal structure determinations and design of anti-inflammatory analgesics for new drug discovery.
Tej obtained his master's degree in science from the [[University of Allahabad]]. He started his research career in 1971 as a graduate student at the [[Indian Institute of Science]], [[Bangalore]]. He obtained his Ph.D. degree in the mid-1970s working on the crystal structure determinations and design of anti-inflammatory analgesics for new drug discovery. [http://www.insaindia.res.in/detail/P01-1304]. Before going for his bachelor's degree in Science in Allahabad University, Tej Pal Singh has studied in his neighbourhood village school i.e. Kisan Intermediate College Deorhi-Wajidpur (District-Amroha UP) and later Government Intermediate College (GIC) in Amroha (UP).


==Professional career==
==Area of Specialization==


Soon after obtaining his Ph.D. degree, Tej worked for a year as a lecturer at the University of Indore. He then spent more than two years (1978–1980) as an Alexander von Humboldt / Max-Planck, post doctoral fellow in the German laboratory of Professor [[Robert Huber]], who later received the [[Nobel Prize]]. After his return to India he worked as a reader at Sardar Patel University (1980–83) and an additional professor (1984–85) in the Department of Biophysics at the All India Institute of Medical Sciences, New Delhi. He was appointed professor and head of the department in 1986 [http://www.insaindia.res.in/detail/P01-1304] [http://www.biotechexpressmag.com/prof-t-p-singh-became-the-first-indian-to-receive-all-g-n-ramachandran-awards-of-our-country]
Structural Biology ; Protein Crystallography ; Rational Structure based Drug Design and Drug Discovery


==Contributions in protein structural biology==
==Professional career==
The three-dimensional structures of various proteins including [[lactoperoxidase]],<ref>{{Cite journal|title=Crystal structures of lactoperoxidase at 2.4 A resolution |last1=Singh |first1=A..|last2=Singh |first2=N.|last3=Sharma |first3=S.|last4=Singh |first4=S.B.|last5=Kaur |first5=P. |last6=Bhushan|first6=A.|last7=Srinivasan |first7=A. |last8=Singh |first8=T.P.|date=14 December 2007 |volume=376|issue=4 |pages=1060–1075| pmid = 18191143|journal=Journal of Molecular Biology |doi=10.1016/j.jmb.2007.12.012}}</ref> [[peptidoglycan recognition protein]], [[lactoferrin]]<ref>{{Cite journal|title= Crystal structure of a proteolytically generated functional monoferric C-lobe of bovine lactoferrin at 1.9A resolution.|last1=Sharma|first1=S.|last2=Jasti |first2=J.| last3=Kumar|first3=J. | last4=Mohanty |first4=A.K. |last5=Singh|first5=T.P. |date=8 August 2003 |volume=331|issue=2 |pages=485–96| pmid = 12888354|journal=Journal of Molecular Biology | doi=10.1016/s0022-2836(03)00717-4}}</ref><ref>{{Cite journal|title= Camel lactoferrin, a transferrin-cum-lactoferrin: crystal structure of camel apolactoferrin at 2.6 A resolution and structural basis of its dual role.|last1=Khan|first1=J.A.|last2=Kumar|first2=P.| last3=Paramasivam|first3=M. | last4=Yadav |first4=R.S. |last5=Sahani|first5=M.S.| last6=Sharma|first6=S. |last7=Srinivasan|first7=A. |last8=Singh|first8=T.P. |date=8 June 2001 |volume=309|issue=3 |pages=751–761| pmid = 11397094|journal=Journal of Molecular Biology | doi=10.1006/jmbi.2001.4692|doi-access=free}}</ref><ref>{{Cite journal|title= The structural basis for the prevention of nonsteroidal antiinflammatory drug-induced gastrointestinal tract damage by the C-lobe of bovine colostrum lactoferrin.|last1=Mir|first1=R.|last2=Singh|first2=N.| last3=Vikram|first3=G. | last4=Kumar |first4=R.P. |last5=Sinha|first5=M.| last6=Bhushan|first6=A. |last7=Kaur|first7=P. |last8=Srinivasan|first8=A. |last9=Sharma|first9=S. |last10=Singh|first10=T.P. |date=16 December 2009 |volume=97|issue=12 |pages=3178–3186| pmid = 20006955|journal=Biophysical Journal | doi=10.1016/j.bpj.2009.09.030 | pmc=2793366|bibcode=2009BpJ....97.3178M}}</ref> from several species, [[ribosome]] inactivating proteins,<ref>{{Cite journal|title= Crystal structures of a type-1 ribosome inactivating protein from Momordica balsamina in the bound and unbound states.|last1=Kushwaha|first1=G.S.|last2=Pandey|first2=N.| last3=Sinha|first3=M. | last4=Singh |first4=S.B. |last5=Kaur|first5=P.| last6=Sharma|first6=S. |last7=Singh|first7=T.P. |journal=Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics|date= April 2012 |volume=1824|issue=4 |pages=679–91| pmid = 22361570| doi=10.1016/j.bbapap.2012.02.005}}</ref> bifunctional inhibitor proteins from plant seeds and various [[serine proteases]] and their inhibitors have been determined by his group. The elaborate structural studies of proteins from several important systems as potential drug targets such as [[phospholipase]] A2, [[cyclooxygenase]], [[lipoxygenase]], [[endothelin]] receptor, endothelin converting enzyme, [[breast cancer]] regression proteins and matrix metanosomal proteins as well as their complexes with natural and designed synthetic ligands have been carried out. He had developed the rules of peptide design with alpha, beta – dehydro – amino acids through extensive studies using syntheses, and X-ray and NMR structure determinations. These design rules are being exploited for making specific peptides to act as tight inhibitors of target enzymes and potent antagonists of target receptors for eventually leading to useful therapeutic agents.


He initiated a new programme on [[Clinical Proteomics]] at the All India Institute of Medical Sciences in which it is intended to characterize all the proteins that are expressed during various patho/physiological conditions. The newly identified proteins will either be useful as biomarkers or they may be associated with the progression of diseases making them important targets for drug design.
Soon after obtaining his Ph. D degree, he worked about a year (1977) as a lecturer at the University of Indore. He then spent more than two years (1978–1980) as an Alexander von Humboldt / Max-Planck, post doctoral fellow in the German laboratory of Professor [[Robert Huber]], who later received the [[Nobel Prize]]. After his return to India he worked as a reader at Sardar Patel University (1980–83) and an Additional Professor (1984–85) in the Department of Biophysics at the All India Institute of Medical Sciences, New Delhi. He was appointed Professor and Head of the Department in 1986, where he established a flourishing school of structural biology and new drug discovery.


==Awards and honors==
==Awards and honors==
Tej is a fellow of the [[Third World Academy of Sciences]], [[Indian National Science Academy]], [[National Academy of Sciences]] [[Indian Academy of Sciences]], [[Alexander von Humboldt Foundation]] and [[Biotech Research Society of India]]. He has won the Goyal Prize for Life [http://www.tribuneindia.com/2010/20100423/harplus.htm#7 Sciences], Distinguished Biotechnology Research Professor (DBT) (2009), GN Ramachandran Gold Medal for excellence in Science and Technology (CSIR) ([http://www.csirhrdg.res.in/list_gnr_2010.htm 2006)], Distinguished Biotechnologist (DBT), [http://www.biospectrumindia.com/biospecindia/news/156339/awards-galore-dbt-foundation-day 2006], JC Bose Memorial Award (2005), Alexander von Humboldt Fellow (1977), Canadian development Agency Award (1999)


==References==
Goyal Prize for Life Sciences, 2010
{{reflist}}


==External links==
Distinguished Biotechnology Research Professor (DBT), 2009
* https://scholar.google.com/citations?hl=en&authuser=1&user=K0sRm3QAAAAJ
* https://www.aiims.edu/en/faculty-staff.html?id=715
* https://www.researchgate.net/profile/Tej-Singh-16


{{authority control}}
GN Ramachandran Gold Medal for excellence in Science and Technology (CSIR), 2006


Distinguished Biotechnologist (DBT), 2006

Vice President, Indian National Science Academy, 2007–2009

JC Bose Memorial Award, 2005

Alexander von Humboldt Fellow, 1977

Canadian Development Agency Award, 1999

Fellow of the Indian Academy of Sciences, 1994

Fellow of the National Academy of Sciences, 1998

Fellow of the Indian National Science Academy, 2000 -

Fellow of the Third World Academy of Sciences : F.T.W.A.S. 2003 -

Member of the Commission on Biological Macromolecules of the International Union of Crystallography (IUCr) (2005–2008)

Executive member of the International Union of Pure and Applied Biophysics (IUPAB) (2002–2005)

Member Secretary of the INSA National Committee for IUPAB (1988–91)

Member of the INSA National Committee for International Union of Pure and Applied Biophysics (IUPAB) (1985–88)

Member of the INSA National Committee for International Union of Crystallography (IUCr) (2000–2003)

Ex-officio member of the Joint National Committee of INSA for IUPAB and IUCr (2002–2005) , (2005–2008)

Member of a committee to select fellows for Indian National Science Academy (2001–2003)

Member of the Committee to select fellows for the Indian Academy of Sciences, 2005

Member of the Indian Biophysical Society since 1977

Member of the Society of Biological Chemists of India , 1982

Vice President of the Indian Biophysical society (1994–1996)

Member of the American Society for Biochemistry and Molecular Biology (ASBMB), since 2000

Member Technology Development Board on Pharmaceutical Industry (2002)

Member of the Senate of Indian Institute of Technology Delhi, (2001–2002)

Chairman of the DST Committee for the Fast Track Programme in life Sciences (2002–2004) , (2005–2007)

Member of the Apex Committee of the DBT for the programme support at I.I.Sc. Bangalore (1998–2001), (2002–2004) , (2005–2008)

Member of the Programme Advisory Committee of DST on Biochemistry, Biophysics, Molecular Biology including Microbiology (1996–1998) , (1999–2001)

Member of the DBT task force on Basic Biology / Modern Biology (1996–1998) , (1999–2001)

Member of the DBT task force on Infrastructure (2001–2003) , (2004–2006) , (2006–2008)

Member of the DBT task force on Bioinformatics (1994–1996)

Member of the Advisory Committee of Biotechnology Teaching Programme of the Biotechnology Centre, JNU (2002)

Member of the Executive Committee of the Bioinformatics Centre at Madurai Kamraj University (2002–2003)

Member of the Academic Committee of the Biotechnology Unit of AMU, Aligarh (2004–2006)

Member of the Research Area Panel of the National Institute of Immunology (1994–1996)

Member of the Special Committee of the School of Life Sciences, JNU (1988–1990) , (1991–1993)

Member of the Special Committee of the Centre for Biotechnology, JNU (1991–1993) , (1994–1996) , (1997–1999) , (2000–2002) , (2003–2005)

Member of the Special Committee of the Special Centre of Molecular Medicine, JNU (2001–2003) , (2004–2006)

Member of the Special Committee of the School of Environmental Sciences, JNU (2001–2003) , (2004–2006)

Member of the Academic Committee of the Nuclear Science Centre, New Delhi, (2002–2004), (2004–2006)

Member of the Academic Committee of Central Drug Research Institute, Lucknow, (2005–2006)

Member of the Academic Committee of the Institute of Microbial Technology, Chandigarh, (2005–2006)

Member of the Executive Council of the Centre of Bioinformatics, Institute of Microbial Technology, Chandigarh, 2005

Member of the Academic Council of the Central Unversityof Hyderabad, 2006–2007

Executive member of the Council of the International Union of Pure and Applied Biophysics (IUPAB) (2005–2008)

K.K.Foundation National Award for Science and Technology, 2001

Chairman of the Fast-Track Programme of DST in Life Sciences, 2001–2003

Member of the Technology Development Board on Pharmaceutical Industry, 2002–2003

Executive member of the Council of International Union of Pure and Applied Biophysics, 2002–2005

Max-Planck - Humbodt Award - 1999

Canadian Development Agency Award - 1991

Danish International Development Agency Award - 1978

First Rank in M.Sc. in the University of Allahabad - 1971

==External links==
* http://dst.gov.in/whats_new/press-release07/biotech-award.htm
* http://www.jbc.org/cgi/reprint/M208967200v1.pdf
* http://timesofindia.indiatimes.com/articleshow/753224.cms
* http://www.bio-medicine.org/medicine-news/Five-New-Anti-Inflammatory-Compounds-Produced-By-Indian-Scientists-6838-1/
* http://pib.nic.in/release/release.asp?relid=25773

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{{DEFAULTSORT:Singh, Tej P.}}
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[[Category:Crystallography]]
[[Category:Indian chemists]]
[[Category:Indian biologists]]
[[Category:Living people]]
[[Category:Living people]]
[[Category:1944 births]]
[[Category:Indian crystallographers]]
[[Category:20th-century Indian biologists]]
[[Category:Indian biophysicists]]
[[Category:Members of the United States National Academy of Sciences]]
[[Category:Academic staff of the All India Institute of Medical Sciences, New Delhi]]
[[Category:Fellows of the Indian National Science Academy]]
[[Category:Fellows of the Indian Academy of Sciences]]
[[Category:Fellows of the National Academy of Sciences, India]]
[[Category:People from New Delhi]]
[[Category:Scientists from Delhi]]
[[Category:20th-century Indian physicists]]

Latest revision as of 08:02, 12 May 2024

Tej Pal Singh
Born1944 (1944) (age 80)
NationalityIndian
Alma materIndian Institute of Science, Bangalore
Known forProtein Structure Determination, Peptide Design
Drug Design
ChildrenVineeta Singh (daughter)
AwardsGoyal Prize 2010 for Life Sciences
Distinguished Biotechnology Research Professor (DBT) (2009)
Distinguished Biotechnologist (DBT) (2006)
GN Ramachandran Gold Medal CSIR)
Scientific career
FieldsRational structure based Drug Design
InstitutionsAll India Institute of Medical Sciences

Tej Pal Singh (born 1944) is an Indian biophysicist known for his work in the fields of rational structure-based drug design, structural biology of proteins and X-ray crystallography.[1] He has played an active role in the development of drug design in the fields of antibacterial therapeutics,[2][3][4][5][6] tuberculosis,[7][6][8] inflammation,[9][10] cancer[11][12] and gastropathy.[10][13]

He is first Indian to receive all the six Ramachandran awards of the country.[14] He is a fellow of six academies, namely, the Third World Academy of Sciences, Indian National Science Academy, National Academy of Sciences, Indian Academy of Sciences, Alexander von Humboldt Foundation and Biotech Research Society of India.[15]

Education

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Tej obtained his master's degree in science from the University of Allahabad. He started his research career in 1971 as a graduate student at the Indian Institute of Science, Bangalore. He obtained his Ph.D. degree in the mid-1970s working on the crystal structure determinations and design of anti-inflammatory analgesics for new drug discovery. [1]. Before going for his bachelor's degree in Science in Allahabad University, Tej Pal Singh has studied in his neighbourhood village school i.e. Kisan Intermediate College Deorhi-Wajidpur (District-Amroha UP) and later Government Intermediate College (GIC) in Amroha (UP).

Professional career

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Soon after obtaining his Ph.D. degree, Tej worked for a year as a lecturer at the University of Indore. He then spent more than two years (1978–1980) as an Alexander von Humboldt / Max-Planck, post doctoral fellow in the German laboratory of Professor Robert Huber, who later received the Nobel Prize. After his return to India he worked as a reader at Sardar Patel University (1980–83) and an additional professor (1984–85) in the Department of Biophysics at the All India Institute of Medical Sciences, New Delhi. He was appointed professor and head of the department in 1986 [2] [3]

Contributions in protein structural biology

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The three-dimensional structures of various proteins including lactoperoxidase,[16] peptidoglycan recognition protein, lactoferrin[17][18][19] from several species, ribosome inactivating proteins,[20] bifunctional inhibitor proteins from plant seeds and various serine proteases and their inhibitors have been determined by his group. The elaborate structural studies of proteins from several important systems as potential drug targets such as phospholipase A2, cyclooxygenase, lipoxygenase, endothelin receptor, endothelin converting enzyme, breast cancer regression proteins and matrix metanosomal proteins as well as their complexes with natural and designed synthetic ligands have been carried out. He had developed the rules of peptide design with alpha, beta – dehydro – amino acids through extensive studies using syntheses, and X-ray and NMR structure determinations. These design rules are being exploited for making specific peptides to act as tight inhibitors of target enzymes and potent antagonists of target receptors for eventually leading to useful therapeutic agents.

He initiated a new programme on Clinical Proteomics at the All India Institute of Medical Sciences in which it is intended to characterize all the proteins that are expressed during various patho/physiological conditions. The newly identified proteins will either be useful as biomarkers or they may be associated with the progression of diseases making them important targets for drug design.

Awards and honors

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Tej is a fellow of the Third World Academy of Sciences, Indian National Science Academy, National Academy of Sciences Indian Academy of Sciences, Alexander von Humboldt Foundation and Biotech Research Society of India. He has won the Goyal Prize for Life Sciences, Distinguished Biotechnology Research Professor (DBT) (2009), GN Ramachandran Gold Medal for excellence in Science and Technology (CSIR) (2006), Distinguished Biotechnologist (DBT), 2006, JC Bose Memorial Award (2005), Alexander von Humboldt Fellow (1977), Canadian development Agency Award (1999)

References

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  1. ^ "On ResearchGate". 29 January 2018. Retrieved 29 January 2018.
  2. ^ Sharma, Pradeep; Dube, Divya; Sinha, Mau; Yadav, Savita; Kaur, Punit; Sharma, Sujata; Singh, Tej P. (1 January 2013). "Structural insights into the dual strategy of recognition by peptidoglycan recognition protein, PGRP-S: structure of the ternary complex of PGRP-S with lipopolysaccharide and stearic acid". PLOS ONE. 8 (1): e53756. Bibcode:2013PLoSO...853756S. doi:10.1371/journal.pone.0053756. ISSN 1932-6203. PMC 3541179. PMID 23326499.
  3. ^ Singh, Amit Kumar; Singh, Nagendra; Sharma, Sujata; Singh, S. Baskar; Kaur, Punit; Bhushan, A.; Srinivasan, A.; Singh, Tej P. (29 February 2008). "Crystal structure of lactoperoxidase at 2.4 A resolution". Journal of Molecular Biology. 376 (4): 1060–1075. doi:10.1016/j.jmb.2007.12.012. ISSN 1089-8638. PMID 18191143.
  4. ^ Rastogi, Nilisha; Nagpal, Nitish; Alam, Hammad; Pandey, Sadanand; Gautam, Lovely; Sinha, Mau; Shin, Kouichirou; Manzoor, Nikhat; Virdi, Jugsharan S. (1 January 2014). "Preparation and antimicrobial action of three tryptic digested functional molecules of bovine lactoferrin". PLOS ONE. 9 (3): e90011. Bibcode:2014PLoSO...990011R. doi:10.1371/journal.pone.0090011. ISSN 1932-6203. PMC 3940724. PMID 24595088.
  5. ^ Rastogi, Nilisha; Singh, Avinash; Pandey, Sada Nand; Sinha, Mau; Bhushan, Asha; Kaur, Punit; Sharma, Sujata; Singh, Tej P. (1 June 2014). "Structure of the iron-free true C-terminal half of bovine lactoferrin produced by tryptic digestion and its functional significance in the gut". The FEBS Journal. 281 (12): 2871–2882. doi:10.1111/febs.12827. ISSN 1742-4658. PMID 24798798. S2CID 24534041.
  6. ^ a b Singh, Avinash; Gautam, Lovely; Sinha, Mau; Bhushan, Asha; Kaur, Punit; Sharma, Sujata; Singh, T. P. (1 January 2014). "Crystal structure of peptidyl-tRNA hydrolase from a Gram-positive bacterium, Streptococcus pyogenes at 2.19 Å resolution shows the closed structure of the substrate-binding cleft". FEBS Open Bio. 4: 915–922. doi:10.1016/j.fob.2014.10.010. ISSN 2211-5463. PMC 4226762. PMID 25389518.
  7. ^ Sharma, Pradeep; Yamini, Shavait; Dube, Divya; Singh, Amar; Mal, Gorakh; Pandey, Nisha; Sinha, Mau; Singh, Abhay Kumar; Dey, Sharmistha (1 January 2013). "Structural basis of the binding of fatty acids to peptidoglycan recognition protein, PGRP-S through second binding site". Archives of Biochemistry and Biophysics. 529 (1): 1–10. doi:10.1016/j.abb.2012.11.001. ISSN 1096-0384. PMID 23149273.
  8. ^ Singh, Avinash; Kumar, Ashok; Gautam, Lovely; Sharma, Pradeep; Sinha, Mau; Bhushan, Asha; Kaur, Punit; Sharma, Sujata; Arora, Ashish (1 November 2014). "Structural and binding studies of peptidyl-tRNA hydrolase from Pseudomonas aeruginosa provide a platform for the structure-based inhibitor design against peptidyl-tRNA hydrolase". The Biochemical Journal. 463 (3): 329–337. doi:10.1042/BJ20140631. ISSN 1470-8728. PMID 25101795.
  9. ^ Shukla, Prakash Kumar; Gautam, Lovely; Sinha, Mau; Kaur, Punit; Sharma, Sujata; Singh, Tej P. (1 April 2015). "Structures and binding studies of the complexes of phospholipase A2 with five inhibitors". Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1854 (4): 269–277. doi:10.1016/j.bbapap.2014.12.017. ISSN 0006-3002. PMID 25541253.
  10. ^ a b Sharma, Pradeep; Dube, Divya; Singh, Amar; Mishra, Biswajit; Singh, Nagendra; Sinha, Mau; Dey, Sharmistha; Kaur, Punit; Mitra, Dipendra K. (6 May 2011). "Structural basis of recognition of pathogen-associated molecular patterns and inhibition of proinflammatory cytokines by camel peptidoglycan recognition protein". The Journal of Biological Chemistry. 286 (18): 16208–16217. doi:10.1074/jbc.M111.228163. ISSN 1083-351X. PMC 3091228. PMID 21454594.
  11. ^ Bilgrami, Sameeta; Yadav, Savita; Kaur, Punit; Sharma, Sujata; Perbandt, Markus; Betzel, Christian; Singh, Tej P. (23 August 2005). "Crystal structure of the disintegrin heterodimer from saw-scaled viper (Echis carinatus) at 1.9 A resolution". Biochemistry. 44 (33): 11058–11066. doi:10.1021/bi050849y. ISSN 0006-2960. PMID 16101289.
  12. ^ Mohanty, Ashok K.; Singh, Garima; Paramasivam, Murugan; Saravanan, Kolandaivelu; Jabeen, Talat; Sharma, Sujata; Yadav, Savita; Kaur, Punit; Kumar, Pravindra (18 April 2003). "Crystal structure of a novel regulatory 40-kDa mammary gland protein (MGP-40) secreted during involution". The Journal of Biological Chemistry. 278 (16): 14451–14460. doi:10.1074/jbc.M208967200. ISSN 0021-9258. PMID 12529329.
  13. ^ Mir, Rafia; Singh, Nagendra; Vikram, Gopalakrishnapillai; Sinha, Mau; Bhushan, Asha; Kaur, Punit; Srinivasan, Alagiri; Sharma, Sujata; Singh, Tej P. (15 August 2010). "Structural and binding studies of C-terminal half (C-lobe) of lactoferrin protein with COX-2-specific non-steroidal anti-inflammatory drugs (NSAIDs)". Archives of Biochemistry and Biophysics. 500 (2): 196–202. doi:10.1016/j.abb.2010.05.026. ISSN 1096-0384. PMID 20515646.
  14. ^ "Prof T P Singh became the first Indian to receive all Ramachandran Awards". biotechexpressmag.com. 19 March 2020. Archived from the original on 6 May 2022. Retrieved 6 May 2022.
  15. ^ "BRSI". www.brsi.in.
  16. ^ Singh, A..; Singh, N.; Sharma, S.; Singh, S.B.; Kaur, P.; Bhushan, A.; Srinivasan, A.; Singh, T.P. (14 December 2007). "Crystal structures of lactoperoxidase at 2.4 A resolution". Journal of Molecular Biology. 376 (4): 1060–1075. doi:10.1016/j.jmb.2007.12.012. PMID 18191143.
  17. ^ Sharma, S.; Jasti, J.; Kumar, J.; Mohanty, A.K.; Singh, T.P. (8 August 2003). "Crystal structure of a proteolytically generated functional monoferric C-lobe of bovine lactoferrin at 1.9A resolution". Journal of Molecular Biology. 331 (2): 485–96. doi:10.1016/s0022-2836(03)00717-4. PMID 12888354.
  18. ^ Khan, J.A.; Kumar, P.; Paramasivam, M.; Yadav, R.S.; Sahani, M.S.; Sharma, S.; Srinivasan, A.; Singh, T.P. (8 June 2001). "Camel lactoferrin, a transferrin-cum-lactoferrin: crystal structure of camel apolactoferrin at 2.6 A resolution and structural basis of its dual role". Journal of Molecular Biology. 309 (3): 751–761. doi:10.1006/jmbi.2001.4692. PMID 11397094.
  19. ^ Mir, R.; Singh, N.; Vikram, G.; Kumar, R.P.; Sinha, M.; Bhushan, A.; Kaur, P.; Srinivasan, A.; Sharma, S.; Singh, T.P. (16 December 2009). "The structural basis for the prevention of nonsteroidal antiinflammatory drug-induced gastrointestinal tract damage by the C-lobe of bovine colostrum lactoferrin". Biophysical Journal. 97 (12): 3178–3186. Bibcode:2009BpJ....97.3178M. doi:10.1016/j.bpj.2009.09.030. PMC 2793366. PMID 20006955.
  20. ^ Kushwaha, G.S.; Pandey, N.; Sinha, M.; Singh, S.B.; Kaur, P.; Sharma, S.; Singh, T.P. (April 2012). "Crystal structures of a type-1 ribosome inactivating protein from Momordica balsamina in the bound and unbound states". Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1824 (4): 679–91. doi:10.1016/j.bbapap.2012.02.005. PMID 22361570.
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