World's Best Scientists 2026 revealed!

D-Index & Metrics

Biology and Biochemistry

D-Index
66
Citations
18073
World Ranking
8562
National Ranking
3847

Overview

Lei Shi is affiliated with the National Institute on Drug Abuse in the United States and has contributed extensively to research in biochemistry, genetics, molecular biology, and neuroscience. Their body of work spans molecular biology, cellular and molecular neuroscience, computational theory and mathematics, pharmacology, and cell biology.

The scientist's research primarily focuses on receptor mechanisms and signaling, as well as neuropeptides and animal physiology. Other major topics include neurotransmitter receptor influence on behavior, pharmacological receptor mechanisms and effects, neuroscience and neuropharmacology research, computational drug discovery methods, and monoclonal and polyclonal antibodies research.

Shi's recent publications include the following papers:

  • GPCR-mediated β-arrestin activation deconvoluted with single-molecule precision, 2022, Cell
  • The mechanism of a high-affinity allosteric inhibitor of the serotonin transporter, 2020, Nature Communications
  • A structural basis for how ligand binding site changes can allosterically regulate GPCR signaling and engender functional selectivity, 2020, Science Signaling
  • Methods of study on conformation of polysaccharides from natural products: A review, 2024, International Journal of Biological Macromolecules
  • Distinct inactive conformations of the dopamine D2 and D3 receptors correspond to different extents of inverse agonism, 2020, eLife

Shi frequently publishes in venues such as bioRxiv (Cold Spring Harbor Laboratory), Journal of Pharmacology and Experimental Therapeutics, ACS Chemical Neuroscience, Journal of Medicinal Chemistry, and Journal of Chemical Information and Modeling.

The scientist has collaborated often with several researchers, including Kuo Hao Lee, David R. Sibley, R. Benjamin Free, Amy Hauck Newman, and Bing Xie.

Best Publications

  • Structure of the human dopamine d3 receptor in complex with a d2/d3 selective antagonist.

    Ellen Y. T. Chien;Wei Liu;Qiang Zhao;Vsevolod Katritch

  • Activation of the β2-Adrenergic Receptor Involves Disruption of an Ionic Lock between the Cytoplasmic Ends of Transmembrane Segments 3 and 6

    Juan A. Ballesteros;Anne D. Jensen;George Liapakis;George Liapakis;Søren G.F. Rasmussen

  • Acetyl-CoA and the regulation of metabolism: mechanisms and consequences

    Lei Shi;Benjamin P Tu

  • Structural mimicry in G protein-coupled receptors: implications of the high-resolution structure of rhodopsin for structure-function analysis of rhodopsin-like receptors.

    Juan A. Ballesteros;Lei Shi;Jonathan A. Javitch

  • β2 Adrenergic Receptor Activation MODULATION OF THE PROLINE KINK IN TRANSMEMBRANE 6 BY A ROTAMER TOGGLE SWITCH

    Lei Shi;George Liapakis;Rui Xu;Frank Guarnieri

  • Amphetamine-induced loss of human dopamine transporter activity: an internalization-dependent and cocaine-sensitive mechanism.

    Christine Saunders;Jasmine V. Ferrer;Lei Shi;Jiayun Chen

  • The mechanism of a neurotransmitter:sodium symporter--inward release of Na+ and substrate is triggered by substrate in a second binding site.

    Lei Shi;Matthias Quick;Yongfang Zhao;Harel Weinstein

  • The binding sites for cocaine and dopamine in the dopamine transporter overlap

    Thijs Beuming;Julie Kniazeff;Marianne L Bergmann;Lei Shi

  • The binding site of aminergic G protein-coupled receptors: the transmembrane segments and second extracellular loop.

    Lei Shi;Jonathan A Javitch

  • Mannose-binding Lectin-deficient Mice Are Susceptible to Infection with Staphylococcus aureus

    Lei Shi;Kazue Takahashi;Joseph Dundee;Sarit Shahroor-Karni

  • Dopamine D2 receptors form higher order oligomers at physiological expression levels

    Wen Guo;Eneko Urizar;Michaela Kralikova;Juan Carlos Mobarec

  • A comprehensive structure-based alignment of prokaryotic and eukaryotic neurotransmitter/Na+ symporters (NSS) aids in the use of the LeuT structure to probe NSS structure and function.

    Thijs Beuming;Lei Shi;Jonathan A. Javitch;Harel Weinstein

  • SNOSID, a proteomic method for identification of cysteine S-nitrosylation sites in complex protein mixtures.

    Gang Hao;Behrad Derakhshan;Lei Shi;Fabien Campagne

  • The fourth transmembrane segment forms the interface of the dopamine D2 receptor homodimer.

    Wen Guo;Lei Shi;Jonathan A. Javitch

  • Crosstalk in G protein-coupled receptors: Changes at the transmembrane homodimer interface determine activation

    Wen Guo;Lei Shi;Marta Filizola;Harel Weinstein

  • Mannose-Binding Lectin Is a Regulator of Inflammation That Accompanies Myocardial Ischemia and Reperfusion Injury

    Mary C. Walsh;Todd Bourcier;Kazue Takahashi;Lei Shi

  • Mannose-Binding Lectin-Deficient Mice Display Defective Apoptotic Cell Clearance but No Autoimmune Phenotype

    Lynda M. Stuart;Lynda M. Stuart;Kazue Takahashi;Lei Shi;John Savill

  • Substrate-modulated gating dynamics in a Na + -coupled neurotransmitter transporter homologue

    Yongfang Zhao;Daniel S. Terry;Lei Shi;Matthias Quick

  • TAS-120 Overcomes Resistance to ATP-Competitive FGFR Inhibitors in Patients with FGFR2 Fusion–Positive Intrahepatic Cholangiocarcinoma

    Lipika Goyal;Lei Shi;Leah Y Liu;Ferran Fece de la Cruz

  • P085. SNOSID, a proteomic method for identification of cysteine S-nitrosylation sites in complex protein mixtures

    Steven S. Gross;Gang Hao;Behrad Derakhshan;M. Carrie Garceau

Frequent Co-Authors

Jonathan A. Javitch
Jonathan A. Javitch Columbia University
Harel Weinstein
Harel Weinstein Cornell University
Amy Hauck Newman
Amy Hauck Newman National Institutes of Health
Ulrik Gether
Ulrik Gether University of Copenhagen
Kazue Takahashi
Kazue Takahashi Harvard University
Benjamin P. Tu
Benjamin P. Tu The University of Texas Southwestern Medical Center
Hassane S. Mchaourab
Hassane S. Mchaourab Vanderbilt University
R. Alan B. Ezekowitz
R. Alan B. Ezekowitz Harvard University
Carl Nathan
Carl Nathan Cornell University
Cheryl H. Arrowsmith
Cheryl H. Arrowsmith Structural Genomics Consortium

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