T. Gheyi

发表

Structure of the C‐terminal domain of Saccharomyces cerevisiae Nup133, a component of the nuclear pore complex

Seung Joong Kim, Josef D. Franke, A. Sali, 2011, Proteins.

Structures of the autoproteolytic domain from the Saccharomyces cerevisiae nuclear pore complex component, Nup145

Seung Joong Kim, Josef D. Franke, A. Sali, 2010, Proteins.

Atomic structure of the nuclear pore complex targeting domain of a Nup116 homologue from the yeast, Candida glabrata

Seung Joong Kim, Josef D. Franke, A. Sali, 2012, Proteins.

Structure of a putative BenF‐like porin from Pseudomonas fluorescens Pf‐5 at 2.6 Å resolution

D. Baker, A. Sali, J. M. Sauder, 2010, Proteins.

Protein production and purification

K. Gunsalus, G. Montelione, J. Bray, 2008, Nature Methods.

Evolution of enzymatic activities in the enolase superfamily: stereochemically distinct mechanisms in two families of cis,cis-muconate lactonizing enzymes.

Patricia C Babbitt, Stephen K Burley, Ayano Sakai, 2009, Biochemistry.

Liver Fatty Acid-binding Protein Initiates Budding of Pre-chylomicron Transport Vesicles from Intestinal Endoplasmic Reticulum*

T. Gheyi, J. Storch, C. Mansbach, 2007, Journal of Biological Chemistry.

STRUCTURE NOTE Structure of the C-terminal domain of Saccharomyces cerevisiae Nup133, a component of the nuclear pore complex

Seung Joong Kim, Josef D. Franke, A. Sali, 2011 .

Crystal structure of uncharacterized protein BH1478 from Bacillus halodurans

J. M. Sauder, S. Almo, S. Burley, 2007 .

Second-Harmonic Generation (SHG) for Conformational Measurements: Assay Development, Optimization, and Screening.

T. Gheyi, J. J. Carrillo, J. Salafsky, 2018, Methods in enzymology.

Anionic Clays as Potential Slow-Release Fertilizers: Nitrate Ion Exchange

S. Komarneni, T. Gheyi, Dongsheng Li, 2003 .

Acetaldehyde dissociates the PTP1B-E-cadherin-beta-catenin complex in Caco-2 cell monolayers by a phosphorylation-dependent mechanism.

T. Gheyi, D. Desiderio, R. Rao, 2007, The Biochemical journal.

The 2.5 Å crystal structure of the SIRT1 catalytic domain bound to nicotinamide adenine dinucleotide (NAD+) and an indole (EX527 analogue) reveals a novel mechanism of histone deacetylase inhibition.

J. Luz, Y. Qian, T. Gheyi, 2013, Journal of medicinal chemistry.

Structures of PHR domains from Mus musculus Phr1 (Mycbp2) explain the loss-of-function mutation (Gly1092-->Glu) of the C. elegans ortholog RPM-1.

Kevin T Bain, Stephen K Burley, Shane Atwell, 2010, Journal of molecular biology.

Crystal structure of the human PRMT5:MEP50 complex

Aiping Zhang, Spencer Emtage, Bomie Han, 2012, Proceedings of the National Academy of Sciences.

Structural Context of Disease-Associated Mutations and Putative Mechanism of Autoinhibition Revealed by X-Ray Crystallographic Analysis of the EZH2-SET Domain

J. Bonanno, T. Gheyi, L. Rodgers, 2013, PloS one.

Structural Bases of PAS Domain-regulated Kinase (PASK) Activation in the Absence of Activation Loop Phosphorylation*

J. M. Sauder, S. Burley, B. Turk, 2010, The Journal of Biological Chemistry.

LLY-507, a Cell-active, Potent, and Selective Inhibitor of Protein-lysine Methyltransferase SMYD2

B. Garcia, R. Campbell, C. Arrowsmith, 2015, The Journal of Biological Chemistry.

Structures of a minimal human CFTR first nucleotide-binding domain as a monomer, head-to-tail homodimer, and pathogenic mutant.

John F Hunt, Diana Wetmore, Spencer Emtage, 2010, Protein engineering, design & selection : PEDS.

The catalase activity of diiron adenine deaminase

J. M. Sauder, F. Raushel, S. Burley, 2011, Protein science : a publication of the Protein Society.

Mass spectrometry guided in situ proteolysis to obtain crystals for X-ray structure determination

J. M. Sauder, S. Burley, T. Gheyi, 2010, Journal of the American Society for Mass Spectrometry.

High throughput protein production and crystallization at NYSGXRC.

Stephen K Burley, Kevin Bain, Spencer Emtage, 2008, Methods in molecular biology.

Structural basis for GPR40 allosteric agonism and incretin stimulation

A. R. Miller, B. Chau, T. Gheyi, 2018, Nature Communications.