Qingrong Yan, Ph.D.
Affiliations: | 2009 | Yeshiva University, New York, NY, United States |
Area:
Immunology, Cell BiologyGoogle:
"Qingrong Yan"Parents
Sign in to add mentorSteven C. Almo | grad student | (Chemistry Tree) | ||
Stanley G. Nathenson | grad student | 2009 | Yeshiva University | |
(Sequence, structure and immune functions: Structural basis for T cell regulation by SLAM, CD28/B7 and TIM family receptors.) | ||||
John Kuriyan | post-doc | UC Berkeley (Chemistry Tree) |
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Publications
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Mo J, Jin R, Yan Q, et al. (2018) Quantitative analysis of glycation and its impact on antigen binding. Mabs. 0 |
Ramagopal UA, Liu W, Garrett-Thomson SC, et al. (2017) Structural basis for cancer immunotherapy by the first-in-class checkpoint inhibitor ipilimumab. Proceedings of the National Academy of Sciences of the United States of America |
Visperas PR, Wilson CG, Winger JA, et al. (2016) Identification of Inhibitors of the Association of ZAP-70 with the T Cell Receptor by High-Throughput Screen. Journal of Biomolecular Screening |
Shah NH, Wang Q, Yan Q, et al. (2016) An electrostatic selection mechanism controls sequential kinase signaling downstream of the T cell receptor. Elife. 5 |
Mo J, Yan Q, So CK, et al. (2016) Understanding the Impact of Methionine Oxidation on the Biological Functions of IgG1 Antibodies Using Hydrogen/Deuterium Exchange Mass Spectrometry. Analytical Chemistry |
Huang WY, Yan Q, Lin WC, et al. (2016) Phosphotyrosine-mediated LAT assembly on membranes drives kinetic bifurcation in recruitment dynamics of the Ras activator SOS. Proceedings of the National Academy of Sciences of the United States of America |
Shah NH, Wang Q, Yan Q, et al. (2016) Author response: An electrostatic selection mechanism controls sequential kinase signaling downstream of the T cell receptor Elife |
Huang WY, Yan Q, Lin W, et al. (2016) Protein Assembly on Membrane Surface alters the Dynamical Spectrum of Downstream Signaling Reactions Biophysical Journal. 110: 88a |
Visperas PR, Winger JA, Horton TM, et al. (2015) Modification by covalent reaction or oxidation of cysteine residues in the tandem-SH2 domains of ZAP-70 and Syk can block phosphopeptide binding. The Biochemical Journal. 465: 149-61 |
Yan Q, Barros T, Visperas PR, et al. (2013) Structural basis for activation of ZAP-70 by phosphorylation of the SH2-kinase linker. Molecular and Cellular Biology. 33: 2188-201 |