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Biology and Biochemistry

D-Index
70
Citations
19905
World Ranking
6935
National Ranking
528

Overview

Jingshan Ren is affiliated with the University of Oxford in the United Kingdom. Their research primarily focuses on medicine and biochemistry, genetics, and molecular biology. Within these broad fields, their work emphasizes infectious diseases and molecular biology, with additional attention to cardiology and cardiovascular medicine, animal science and zoology, and radiology, nuclear medicine, and imaging.

The scientist's research topics cover a range of areas related to viral infections and immunology. More specifically, their main topics of investigation include SARS-CoV-2 and COVID-19 research, COVID-19 clinical research studies, animal virus infections studies, monoclonal and polyclonal antibodies research, vaccines and immunoinformatics approaches, and viral gastroenteritis research and epidemiology.

Jingshan Ren has authored numerous publications, with frequent appearances in several scientific venues. Significant numbers of their papers have been published in:

  • bioRxiv (Cold Spring Harbor Laboratory)
  • Cell
  • Nature Communications
  • SSRN Electronic Journal
  • Nature Structural & Molecular Biology

Their recent papers include:

  • Evidence of escape of SARS-CoV-2 variant B.1.351 from natural and vaccine-induced sera (2021, Cell)
  • SARS-CoV-2 Omicron-B.1.1.529 leads to widespread escape from neutralizing antibody responses (2022, Cell)
  • Antibody escape of SARS-CoV-2 Omicron BA.4 and BA.5 from vaccine and BA.1 serum (2022, Cell)
  • Reduced neutralization of SARS-CoV-2 B.1.617 by vaccine and convalescent serum (2021, Cell)
  • Antibody evasion by the P.1 strain of SARS-CoV-2 (2021, Cell)

Collaboration appears to be an important aspect of their work, with frequent coauthors including:

  • David I. Stuart
  • Elizabeth E. Fry
  • Daming Zhou
  • Helen M. E. Duyvesteyn
  • Gavin Screaton

Best Publications

  • Evidence of escape of SARS-CoV-2 variant B.1.351 from natural and vaccine-induced sera.

    D Zhou;W Dejnirattisai;P Supasa;C Liu

  • High resolution structures of HIV-1 RT from four RT-inhibitor complexes.

    J Ren;R Esnouf;E Garman;D Somers

  • Reduced neutralization of SARS-CoV-2 B.1.617 by vaccine and convalescent serum.

    C Liu;H M Ginn;W Dejnirattisai;P Supasa

  • Mechanism of inhibition of HIV-1 reverse transcriptase by non-nucleoside inhibitors.

    Robert Esnouf;Jingshan Ren;Carl Ross;Yvonne Jones

  • Antibody evasion by the P.1 strain of SARS-CoV-2.

    W Dejnirattisai;D Zhou;P Supasa;C Liu

  • Neutralizing nanobodies bind SARS-CoV-2 spike RBD and block interaction with ACE2.

    J Huo;J Huo;A Le Bas;A Le Bas;R R Ruza;Duyvesteyn Hme.

  • Reduced neutralization of SARS-CoV-2 B.1.1.7 variant by convalescent and vaccine sera.

    P Supasa;D Zhou;W Dejnirattisai;C Liu

  • A sensor-adaptor mechanism for enterovirus uncoating from structures of EV71

    Xiangxi Wang;Wei Peng;Jingshan Ren;Zhongyu Hu

  • Complexes of HIV-1 reverse transcriptase with inhibitors of the HEPT series reveal conformational changes relevant to the design of potent non-nucleoside inhibitors

    A. L. Hopkins;Jingshan Ren;R. M. Esnouf;B. E. Willcox

  • Structure and functionality in flavivirus NS-proteins: Perspectives for drug design

    Michela Bollati;Karin Alvarez;René Assenberg;Cécile Baronti

  • The antigenic anatomy of SARS-CoV-2 receptor binding domain.

    Wanwisa Dejnirattisai;Daming Zhou;Helen M. Ginn;Helen M.E. Duyvesteyn

  • Neutralization of SARS-CoV-2 by Destruction of the Prefusion Spike.

    Jiandong Huo;Jiandong Huo;Yuguang Zhao;Jingshan Ren;Daming Zhou

  • Structural basis for the resilience of efavirenz (DMP-266) to drug resistance mutations in HIV-1 reverse transcriptase.

    Jingshan Ren;John Milton;Kurt L. Weaver;Steven A. Short

  • Lysine methylation as a routine rescue strategy for protein crystallization.

    Thomas S. Walter;Christoph Meier;Rene Assenberg;Kin Fai Au

  • Structural origins of the selectivity of the trifunctional oxygenase clavaminic acid synthase.

    Zhihong Zhang;Jingshan Ren;David K. Stammers;Jack E. Baldwin

  • Structural basis for the neutralization of SARS-CoV-2 by an antibody from a convalescent patient.

    D Zhou;Duyvesteyn Hme.;Chen C-P.;Huang C-G.;Huang C-G.

  • Crystal structure of human α-lactalbumin at 1·7 Å resolution

    K. Ravi Acharya;Jingshan Ren;David I. Stuart;David C. Phillips

  • Structure of HIV-2 reverse transcriptase at 2.35-Å resolution and the mechanism of resistance to non-nucleoside inhibitors

    J. Ren;L. E. Bird;P. P. Chamberlain;G. B. Stewart-Jones

  • The structure of HIV-1 reverse transcriptase complexed with 9-chloro-TIBO: lessons for inhibitor design.

    Jingshan Ren;Robert Esnouf;Andrew Hopkins;Carl Ross

  • Structural mechanisms of drug resistance for mutations at codons 181 and 188 in HIV-1 reverse transcriptase and the improved resilience of second generation non-nucleoside inhibitors.

    J. Ren;C. Nichols;L. Bird;P. Chamberlain

Frequent Co-Authors

David I. Stuart
David I. Stuart University of Oxford
David K. Stammers
David K. Stammers University of Oxford
Elizabeth E. Fry
Elizabeth E. Fry University of Oxford
Raymond J. Owens
Raymond J. Owens University of Oxford
Zihe Rao
Zihe Rao Tsinghua University
Miles W. Carroll
Miles W. Carroll University of Oxford
Juthathip Mongkolsapaya
Juthathip Mongkolsapaya University of Oxford
Alain Townsend
Alain Townsend University of Oxford
E Y Jones
E Y Jones University of Oxford
Jonathan M. Grimes
Jonathan M. Grimes University of Oxford

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