World's Best Scientists 2026 revealed!

D-Index & Metrics

Biology and Biochemistry

D-Index
79
Citations
19752
World Ranking
4376
National Ranking
2132

Overview

Jun Qin is affiliated with the Cleveland Clinic Lerner College of Medicine in the United States. Their research primarily spans the fields of Medicine and Biochemistry, Genetics and Molecular Biology, with a significant focus on Molecular Biology and Cell Biology among other subfields.

Their scientific output includes work in Surgery, Immunology and Allergy, and Cancer Research. Key areas of study encompass Cell Adhesion Molecules Research, Cellular Mechanics and Interactions, RNA modifications and cancer, as well as Caveolin-1 and cellular processes. They have also contributed to studies related to COVID-19 Clinical Research, Birth, Development, and Health, and Bone Metabolism and Diseases.

Jun Qin's recent publications include:

  • Mechanism of integrin activation by talin and its cooperation with kindlin, 2022, Nature Communications
  • Integrin mediates cell entry of the SARS-CoV-2 virus independent of cellular receptor ACE2, 2022, Journal of Biological Chemistry
  • Rhoifolin ameliorates osteoarthritis via the Nrf2/NF-κB axis: in vitro and in vivo experiments, 2022, Osteoarthritis and Cartilage
  • Initiation of focal adhesion assembly by talin and kindlin: A dynamic view, 2020, Protein Science
  • Small Extracellular Vesicle Regulation of Mitochondrial Dynamics Reprograms a Hypoxic Tumor Microenvironment, 2020, Developmental Cell

The scientist frequently publishes in venues such as SSRN Electronic Journal, arXiv (Cornell University), Journal of Biological Chemistry, Circulation Research, and Cells.

Collaborative efforts involve regular coauthorship with researchers including Liaobin Chen, Edward F. Plow, Kai Tie, Hui Wang, and Fan Lü.

Best Publications

  • INVOLVEMENT OF THE TIP60 HISTONE ACETYLASE COMPLEX IN DNA REPAIR AND APOPTOSIS

    Tsuyoshi Ikura;Vasily V Ogryzko;Mikhail Grigoriev;Regina Groisman

  • A Structural Mechanism of Integrin αIIbβ3 “Inside-Out” Activation as Regulated by Its Cytoplasmic Face

    Olga Vinogradova;Algirdas Velyvis;Asta Velyviene;Bin Hu

  • Histone-like TAFs within the PCAF Histone Acetylase Complex

    Vasily V Ogryzko;Tomohiro Kotani;Xiaolong Zhang;R.Louis Schiltz

  • Identity between TRAP and SMCC complexes indicates novel pathways for the function of nuclear receptors and diverse mammalian activators.

    Mitsuhiro Ito;Chao-Xing Yuan;Sohail Malik;Wei Gu

  • Structure of the double-stranded RNA-binding domain of the protein kinase PKR reveals the molecular basis of its dsRNA-mediated activation.

    Sambasivarao Nanduri;Bruce W. Carpick;Yanwu Yang;Bryan R.G. Williams

  • A Novel Human SRB/MED-Containing Cofactor Complex, SMCC, Involved in Transcription Regulation

    Wei Gu;Sohail Malik;Mitsuhiro Ito;Chao-Xing Yuan

  • Kindlin-2 (Mig-2): a co-activator of β3 integrins

    Yan Qing Ma;Jun Qin;Chuanyue Wu;Edward F. Plow

  • Autophosphorylation in the Activation Loop Is Required for Full Kinase Activity In Vivo of Human and Yeast Eukaryotic Initiation Factor 2α Kinases PKR and GCN2

    Patrick R. Romano;Minerva T. Garcia-Barrio;Xiaolong Zhang;Qizhi Wang

  • The lipid whisker model of the structure of oxidized cell membranes

    Michael E. Greenberg;Xin Min Li;Bogdan G. Gugiu;Xiaodong Gu

  • Structural Basis for the Autoinhibition of Talin in Regulating Integrin Activation

    Esen Goksoy;Yan Qing Ma;Xiaoxia Wang;Xiangming Kong

  • Solution structure of human thioredoxin in a mixed disulfide intermediate complex with its target peptide from the transcription factor NFκB

    Jun Qin;G.Marius Clore;WM Poindexter Kennedy;Jeffrey R Huth

  • A robust methodology to subclassify pseudokinases based on their nucleotide-binding properties.

    James M. Murphy;James M. Murphy;Qingwei Zhang;Samuel N. Young;Michael L. Reese

  • Protein indentification using mass spectrometric information

    David Fenyö;Jun Qin;Brian T. Chait

  • The Impact of Direct Refinement against 13Cα and 13Cβ Chemical Shifts on Protein Structure Determination by NMR

    J. Kuszewski;Jun Qin;A. M. Gronenborn;G. M. Clore

  • Mechanism of magnesium activation of calcium-activated potassium channels

    Jingyi Shi;Gayathri Krishnamoorthy;Yanwu Yang;Lei Hu

  • Integrin bidirectional signaling: a molecular view.

    Jun-jun Qin;Olga Vinogradova;Edward F. Plow

  • Identification of a Translation Initiation Factor 3 (eIF3) Core Complex, Conserved in Yeast and Mammals, That Interacts with eIF5

    Lon Phan;Xiaolong Zhang;Katsura Asano;James Anderson

  • Platelet integrin alpha(IIb)beta(3): activation mechanisms.

    Y. Q. Ma;Jun Qin;Edward F Plow

  • The Pseudoactive Site of ILK Is Essential for Its Binding to α-Parvin and Localization to Focal Adhesions

    Koichi Fukuda;Sudhiranjan Gupta;Ka Chen;Chuanyue Wu

  • Identification and Characterization of Posttranslational Modifications of Proteins by MALDI Ion Trap Mass Spectrometry

    Jun Qin;Brian T. Chait

Frequent Co-Authors

Edward F. Plow
Edward F. Plow Cleveland Clinic Lerner College of Medicine
Chuanyue Wu
Chuanyue Wu University of Pittsburgh
Tatiana V. Byzova
Tatiana V. Byzova Cleveland Clinic Lerner College of Medicine
Angela M. Gronenborn
Angela M. Gronenborn University of Pittsburgh
Xiaoxia Li
Xiaoxia Li Cleveland Clinic Lerner College of Medicine
Markus Moser
Markus Moser Technical University of Munich
Ganes C. Sen
Ganes C. Sen Case Western Reserve University
G. Marius Clore
G. Marius Clore National Institutes of Health
Paul E. DiCorleto
Paul E. DiCorleto Kent State University
Lucia R. Languino
Lucia R. Languino Thomas Jefferson University

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