Weill Medical College  of Cornell University
Weill Medical College  of Cornell University Cornell University
Department of Physiology and Biophysics
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Lei Shi

Publications:

Journal articles (# indicates equal contribution)

Guo W, Urizar E, Kralikova M, Mobarec JC, Shi L, Filizola M, Javitch JA. Dopamine D2 receptors form higher order oligomers at physiological expression levels. EMBO J. 2008 July 31. [pubmed]

Wang D, Yang H, Shi L, Ma L, Fujii T, Engelstad K, Pascual JM, De Vivo DC. Functional studies of the T295M mutation Causing Glut1 Deficiency: Glucose efflux preferentially affected by T295M. Pediatr Res. 2008 Jul 3. [pubmed]

Shi L, Quick M, Zhao Y, Weinstein H, and Javitch JA The mechanism of a neurotransmitter:sodium symporter—inward release of Na+ and substrate is triggered by substrate in a second binding site. Mol Cell. 2008 Jun 20;30(6):667-77. [pubmed] [cover] [press release]

Beuming T, Kniazeff J, Bergmann ML, Shi L, Gracia L, Raniszewska K, Newman AH, Javitch JA, Weinstein H, Gether U, and Loland CJ. The binding sites for cocaine and dopamine in the dopamine transporter overlap. Nat Neurosci. 2008 Jul;11(7):780-9. Epub 2008 Jun 22. [pubmed] [press release]

#Kniazeff J, #Shi L, Loland CJ, Javitch JA, Weinstein H, Gether U. An intracellular interaction network regulates conformational transitions in the dopamine transporter. J Biol Chem. 2008 Jun 20;283(25):17691-701. Epub 2008 Apr 21. [pubmed]

Pascual JM, Wang D, Yang R, Shi L, Yang H, De Vivo DC. Structural signatures and membrane helix 4 in GLUT1: Inferences from human blood brain glucose transport mutants. J Biol Chem. 2008 Jun 13;283(24):16732-42. Epub 2008 Apr 3. [pubmed]

#Beuming T, #Shi L, Javitch JA, and Weinstein H. 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. Mol Pharmacol. 2006 Nov;70(5):1630-42. Epub 2006 Jul 31. [pubmed][TRAC]

Quick M, Yano H, Goldberg NR, Duan L, Beuming T, Shi L, Weinstein H, and Javitch JA. State-dependent conformations of the translocation pathway in the tyrosine transporter Tyt1, a novel neurotransmitter: sodium symporter from Fusobacterium nucleatum. J Biol Chem. 2006, Jun 23. [pubmed]

Shi L and Javitch JA. Information collection, management, and integration in structure-function studies of G-protein coupled receptors. Curr Pharm Des. 2006, 12(14):1771-83. [pubmed]

Hao G, Derakhshan B, Shi L, Campagne F, and Gross SS. SNOSID, a proteomic method for identification of cysteine S-nitrosylation sites in complex protein mixtures. Proc. Natl. Acad. Sci. USA 2006, 103(4):1012-7. [pubmed] [press release]

Guo W, #Shi L, #Filizola M, Weinstein H, Javitch JA. A structural context for functional crosstalk in G-protein-coupled receptors: dynamic changes at the homodimer interface in the transmembrane domain determine activation. Proc. Natl. Acad. Sci. USA 2005, 102(48):17495-500. [pubmed] [press release] [“from the cover”] [jpet cover]

Sen N, Shi L, Beuming T, Weinstein H, and Javitch JA. A pincer-like configuration of TM2 in the human dopamine transporter is responsible for indirect effects on cocaine binding. Neuropharmacology 2005, 49(6):780-90. [pubmed]

Carter M, Chen X, Minnerath S, Slowinska B, Shi L, Champagne F, Weinstein H, and Ross ME. Crooked tail (Cd) model of human folate responsive NTD is mutated in Wnt co-receptor, Lrp6. Proc. Natl. Acad. Sci. USA 2005, 102(36):12843-8. [pubmed]

Palma M, Zurita J, Ferreras J, Worgall S, Larone DH, Shi L, Campagne F, and Quadri LE. Pseudomonas aeruginosa SoxR does not conform to the archetypal paradigm for SoxR-dependent regulation of the bacterial oxidative stress adaptive response. Infection and Immunity 2005, 73(5):2958-66.  [pubmed]

Shi L and Campagne F. Building a protein name dictionary from full text: a machine learning term extraction approach. BMC bioinformatics 2005, 6(1):88. [pubmed]

Shi L and Javitch JA. The second extracellular loop of the dopamine D2 receptor lines the binding-site crevice. Proc. Natl. Acad. Sci. USA 2004, 101(1):440-5. [pubmed]

Yu Y, Shi L, and Karlin A. Structural effects of quinacrine binding in the open channel of the acetylcholine receptor. Proc. Natl. Acad. Sci. USA 2003, 100(7):3907-12. [pubmed]

Li J, Shi L, and Karlin A. A photochemical approach to the lipid accessibility of engineered cysteinyl residues. Proc. Natl. Acad. Sci. USA 2003, 100(3):886-91. [pubmed]

Guo W, Shi L, and Javitch JA. The fourth transmembrane segment forms the dopamine D2 receptor homodimer interface. J. Biol. Chem. 2003, 278(7):4385-8. [pubmed] [press release]

#Shi L, #Liapakis G, Xu R, Guarnieri F, Ballesteros JA, and Javitch JA. β2 Adrenergic Receptor Activation: Modulation of the Proline Kink in TM6 by a Rotamer Toggle Switch. J. Biol. Chem. 2002, 277(43):40989-96. [pubmed]

Shi L and Javitch JA. The binding site of aminergic G-protein-coupled receptors: the transmembrane segments and second extracellular loop. Annu. Rev. Pharmacol. Toxicol. 2002, 42:437-67. [pubmed]

Javitch JA, Shi L, and Liapakis G. Use of the substituted-cysteine accessibility method (SCAM) to study the structure and function of G-protein-coupled receptors. Methods Enzymol. 2002, 343:137-56. [pubmed]

Shi L, Simpson MM, Ballesteros JA, and Javitch JA. The first transmembrane segment of the dopamine D2 receptor: accessibility in the binding-site crevice and position in the transmembrane bundle. Biochemistry 2001, 40(41): 12339-48. [pubmed]

Xu W, Li J, Chen C, Huang P, Weinstein H, Javitch JA, Shi L, Riel JK, and Liu-Chen L. Comparison of the amino acid residues in the sixth transmembrane domains accessible in binding-site crevices of m, d and k opioid receptors. Biochemistry 2001, 40(27):8018-29. [pubmed]

#Ballesteros J A, #Shi L, and Javitch JA. Structural mimicry in G-protein-coupled receptors: implications of the high-resolution structure of rhodopsin for structure-function analysis of rhodopsin-like receptors. Mol. Pharmacol. 2001, 60(1):1-19.  [pubmed] [cover]

Ballesteros JA, Jensen AD, Liapakis G, Rasmussen SG, Shi L, Gether U, and Jonathan A. Javitch, JA. Activation of the β2 adrenergic receptor involves disruption of an ionic lock between the cytoplasmic ends of transmembrane segments 3 and 6. J. Biol. Chem. 2001, 276(31):29171-7. [pubmed]

Javitch JA, Shi L, Simpson MM, Chen J, Chiappa V, Visiers I, Weinstein H, and Ballesteros JA. The fourth transmembrane segment of the dopamine D2 receptor: accessibility in the binding-site crevice and position in the transmembrane bundle. Biochemistry 2000, 39(40):12190-9. [pubmed]

Saunders C, Ferrer JV, Shi L, Chen J, Merrill G, Lamb ME, Leeb-Lundberg LM, Carvelli L, Javitch JA, and Galli A. Amphetamine-induced loss of human dopamine transporter activity: An internalization-dependent and cocaine-sensitive mechanism. Proc. Natl. Acad. Sci. USA 2000, 97(12): 6850-6855. [pubmed]

Book chapters

Deupi X, Govaerts C, Shi L, Javitch J, Pardo L, and Ballesteros JA. Conformational plasticity of GPCR binding sites: structural basis for evolutionary diversity in ligand recognition. The G Protein-Coupled Receptors Handbook, Humana Press, Totowa, NJ 2005

Shi L and Javitch JA. The binding pocket of G protein-coupled receptors for biogenic amines, retinal, and other ligands. Handbook of Cell Signaling, Academic Press, San Diego, CA 2003.

physiology@med.cornell.edu | last updated: Friday, September 30, 2005