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Wyszukujesz frazę ""Yan, Qingrong"" wg kryterium: Autor


Tytuł :
Structural basis for cancer immunotherapy by the first-in-class checkpoint inhibitor ipilimumab
Autorzy :
Ramagopal Udupi A.
Liu Weifeng
Garrett-Thomson Sarah C.
Bonanno Jeffrey B.
Yan Qingrong
Srinivasan Mohan
Wong Susan C.
Bell Alasdair
Mankikar Shilpa
Rangan Vangipuram S.
Deshpande Shrikant
Korman Alan J.
Almo Steven C.
Pokaż więcej
Źródło :
Proceedings of the National Academy of Sciences of the United States of America. 114(21):E4223-E4232
Dostęp URL :
https://www.jstor.org/stable/26483333
Czasopismo naukowe
Tytuł :
An electrostatic selection mechanism controls sequential kinase signaling downstream of the T cell receptor.
Autorzy :
Weiss, Arthur
Kuriyan, John
Shah, Neel H
Wang, Qi
Yan, Qingrong
Karandur, Deepti
Kadlecek, Theresa A
Fallahee, Ian R
Russ, William P
Ranganathan, Rama
Pokaż więcej
Temat :
T-Cell
Biotechnology
Biochemistry and Cell Biology
Research Article
Lymphocyte Specific Protein Tyrosine Kinase p56(lck)
ZAP-70
E. coli
tyrosine kinase
Lck
Substrate Specificity
Static Electricity
hemic and immune systems
structural biology
HEK293 Cells
immunology
biophysics
LAT
Biophysics and Structural Biology
Receptors
Signal Transduction
Antigen
T cell receptor
chemical and pharmacologic phenomena
ZAP-70 Protein-Tyrosine Kinase
bacterial surface display
Humans
Źródło :
eLife, vol 5, iss OCTOBER2016
Shah, NH; Wang, Q; Yan, Q; Karandur, D; Kadlecek, TA; Fallahee, IR; et al.(2016). An electrostatic selection mechanism controls sequential kinase signaling downstream of the T cell receptor. eLife, 5(OCTOBER2016). doi: 10.7554/eLife.20105. UCSF: Retrieved from: http://www.escholarship.org/uc/item/2st6657q
Opis pliku :
application/pdf
Tytuł :
Phosphotyrosine-mediated LAT assembly on membranes drives kinetic bifurcation in recruitment dynamics of the Ras activator SOS
Autorzy :
Huang, William YC
Yan, Qingrong
Lin, Wan-Chen
Chung, Jean K
Hansen, Scott D
Christensen, Sune M
Tu, Hsiung-Lin
Kuriyan, John
Groves, Jay T
Pokaż więcej
Temat :
T-Cell
Receptors
signal transduction
Signal Transducing
kinetic proofreading
Antigen
Adaptor Proteins
GRB2 Adaptor Protein
protein assembly
Biological Sciences
Phosphotyrosine
Membranes
membrane dwell time
single molecule
Artificial
Membrane Proteins
Generic Health Relevance
Son of Sevenless Proteins
ras Proteins
Kinetics
Źródło :
Proceedings of the National Academy of Sciences of the United States of America, vol 113, iss 29
Huang, WYC; Yan, Q; Lin, WC; Chung, JK; Hansen, SD; Christensen, SM; 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, 113(29), 8218 - 8223. doi: 10.1073/pnas.1602602113. UC Berkeley: Retrieved from: http://www.escholarship.org/uc/item/8hh6r18f
Opis pliku :
application/pdf
Tytuł :
Modification by covalent reaction or oxidation of cysteine residues in the Tandem-SH2 Domains of ZAP-70 and Syk Can Block Phosphopeptide Binding
Autorzy :
Visperas, Patrick R
Winger, Jonathan A
Horton, Timothy M
Shah, Neel H
Aum, Diane J
Tao, Alyssa
Barros, Tiago
Yan, Qingrong
Wilson, Christopher G
Arkin, Michelle R
Weiss, Arthur
Kuriyan, John
Pokaż więcej
Temat :
T-cell
Protein-Tyrosine Kinases
Biochemistry & Molecular Biology
Cysteine
Phosphopeptides
B-cell
Phosphotyrosine
Small Molecule Libraries
Syk Kinase
covalent small-molecule inhibitor
hemic and immune systems
Oxidation-Reduction
Molecular
Phosphorylation
src Homology Domains
Binding Sites
Models
hydrogen peroxide
Sulfhydryl Compounds
Chemical Sciences
Protein Binding
immunoreceptor tyrosine-based activation motif
Biological Sciences
Article
Medical and Health Sciences
Amino Acid Motifs
chemical and pharmacologic phenomena
ZAP-70 Protein-Tyrosine Kinase
Humans
Intracellular Signaling Peptides and Proteins
Źródło :
Visperas, PR; Winger, JA; Horton, TM; Shah, NH; Aum, DJ; Tao, A; 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. Biochemical Journal, 465, 149 - 161. doi: 10.1042/BJ20140793. UCSF: Retrieved from: http://www.escholarship.org/uc/item/5192668r
The Biochemical journal, vol 465, iss 1
Opis pliku :
application/pdf

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