Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Peter Trenh"'
Autor:
Sascha Lange, Marissa Bylsma, Marek Wieczorek, Abigail I Guce, Christian Freund, Lawrence J. Stern, Elizabeth D. Mellins, Liusong Yin, Wei Jiang, Peter Trenh, Jana Sticht
Publikováno v:
Journal of Biological Chemistry. 289:23449-23464
HLA-DM mediates the exchange of peptides loaded onto MHCII molecules during antigen presentation by a mechanism that remains unclear and controversial. Here, we investigated the sequence and structural determinants of HLA-DM interaction. Peptides int
Autor:
Brian R Duke, Priya G. Huseby, Lawrence J. Stern, Brian D. Stadinski, Guoqi Li, Peter Trenh, Eric S. Huseby
Publikováno v:
The Journal of Immunology. 192:6071-6082
The mature T cell repertoire has the ability to orchestrate immunity to a wide range of potential pathogen challenges. This ability stems from thymic development producing individual T cell clonotypes that express TCRs with unique patterns of Ag reac
Autor:
Priya G. Huseby, Brian D. Stadinski, Lawrence J. Stern, Rebecca Smith, Guoqi Li, Bianca Bautista, Peter Trenh, Eric S. Huseby
Publikováno v:
Immunity. 35:694-704
Summary A limited set of T cell receptor (TCR) variable (V) gene segments are used to create a repertoire of TCRs that recognize all major histocompatibility complex (MHC) ligands within a species. How individual αβTCRs are constructed to specifica
Autor:
Stephen Lyle, Giles F. Whalen, Ramesh C. Kovi, Steven R. Grossman, M.W. Straza, Peter Trenh, Seema Paliwal, Daniel Parker, Celia A. Schiffer, Barur R. Rajeshkumar
The CtBP transcriptional corepressors promote cancer cell survival and migration/invasion. CtBP senses cellular metabolism via a regulatory dehydrogenase domain, and is antagonized by p14/p19(ARF) tumor suppressors. The CtBP dehydrogenase substrate 4
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3490b737765bf57f6a96ce72cb65ff48
https://europepmc.org/articles/PMC3047800/
https://europepmc.org/articles/PMC3047800/
Publikováno v:
Immunity. 36:889-890
The letter by Garcia et al. (2012) suggests our conclusions that (1) TCRα chain pairing can modify the TCRβ chain binding reaction with MHC and (2) by pairing with a different TCR Vα domain, a TCRβ loop conformation changed and created an altered
Publikováno v:
The Journal of Immunology. 190:41.8-41.8
HLA-DM (DM) mediates the exchange of peptides loaded onto MHC II. However, the determinants of DM-mediated peptide release remain unclear and controversial. In this study, we synthesized a series of peptides derived from HLA-A2104-117 and measured th