Jingshan Ren mainly investigates Virology, Reverse transcriptase, Stereochemistry, Drug resistance and Virus. As part of his studies on Virology, he frequently links adjacent subjects like Plasma protein binding. His Reverse transcriptase study integrates concerns from other disciplines, such as Hydrogen bond, Nucleotidyltransferase, Binding site and Nucleoside.
As a member of one scientific family, Jingshan Ren mostly works in the field of Binding site, focusing on Protein subunit and, on occasion, Mutant, Molecular biology and DNA polymerase. His work deals with themes such as Crystallography, Polymerase, Protein structure and Active site, which intersect with Stereochemistry. His study looks at the intersection of Virus and topics like Epitope with Peptide library, Viral entry, Neutralization, Peptide sequence and Allosteric regulation.
His main research concerns Virology, Stereochemistry, Biochemistry, Reverse transcriptase and Virus. His Virology research includes elements of Epitope, Antibody and Mutant. His Stereochemistry study combines topics in areas such as Crystal structure, Active site, Substrate, Enzyme and Aspergillus nidulans.
His Reverse transcriptase research is multidisciplinary, relying on both Molecular biology, Nucleotidyltransferase, Drug resistance and Nucleoside. His Virus study combines topics from a wide range of disciplines, such as RNA, Picornavirus and Recombinant DNA. His study in Binding site is interdisciplinary in nature, drawing from both Plasma protein binding and Protein subunit.
Jingshan Ren focuses on Virology, Antibody, Virus, Epitope and Neutralization. In the subject of general Virology, his work in Viral replication is often linked to Severe acute respiratory syndrome coronavirus 2, thereby combining diverse domains of study. The study incorporates disciplines such as Immune system and Binding site in addition to Antibody.
In his study, Recombinant DNA is strongly linked to Antigen, which falls under the umbrella field of Binding site. Jingshan Ren has researched Neutralization in several fields, including Serum samples, Cell entry, Immunity and Vaccination. He interconnects Protein structure, Protein domain and Ebolavirus in the investigation of issues within Glycoprotein.
Jingshan Ren mainly focuses on Virology, Antibody, Epitope, Virus and Neutralization. Virology and Glycoprotein are frequently intertwined in his study. His biological study spans a wide range of topics, including Protein structure and Binding site.
The Protein structure study combines topics in areas such as Peptide library and Plasma protein binding. The concepts of his Binding site study are interwoven with issues in Protein domain, Neutralizing antibody and Antigen. All of his Virus and Viral entry and Viral protein investigations are sub-components of the entire Virus study.
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High resolution structures of HIV-1 RT from four RT-inhibitor complexes.
J Ren;R Esnouf;E Garman;D Somers.
Nature Structural & Molecular Biology (1996)
Mechanism of inhibition of HIV-1 reverse transcriptase by non-nucleoside inhibitors.
Robert Esnouf;Jingshan Ren;Carl Ross;Yvonne Jones.
Nature Structural & Molecular Biology (1995)
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.
Journal of Medicinal Chemistry (1996)
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..
Nature Structural & Molecular Biology (2020)
A sensor-adaptor mechanism for enterovirus uncoating from structures of EV71
Xiangxi Wang;Wei Peng;Jingshan Ren;Zhongyu Hu.
Nature Structural & Molecular Biology (2012)
Structure and functionality in flavivirus NS-proteins: Perspectives for drug design
Michela Bollati;Karin Alvarez;René Assenberg;Cécile Baronti.
Antiviral Research (2010)
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.
Nature Structural & Molecular Biology (2000)
Neutralization of SARS-CoV-2 by Destruction of the Prefusion Spike.
Jiandong Huo;Jiandong Huo;Yuguang Zhao;Jingshan Ren;Daming Zhou.
Cell Host & Microbe (2020)
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