Zobrazeno 1 - 10
of 16
pro vyhledávání: '"Joshua A. Jadwin"'
Autor:
Joshua A Jadwin, Dongmyung Oh, Timothy G Curran, Mari Ogiue-Ikeda, Lin Jia, Forest M White, Kazuya Machida, Ji Yu, Bruce J Mayer
Publikováno v:
eLife, Vol 5 (2016)
While the affinities and specificities of SH2 domain-phosphotyrosine interactions have been well characterized, spatio-temporal changes in phosphosite availability in response to signals, and their impact on recruitment of SH2-containing proteins in
Externí odkaz:
https://doaj.org/article/1fdecacfc0a547c680275964c20c628e
Publikováno v:
Journal of Biological Chemistry. 293:623-637
Phosphotyrosine (pTyr)-dependent signaling is critical for many cellular processes. It is highly dynamic, as signal output depends not only on phosphorylation and dephosphorylation rates but also on the rates of binding and dissociation of effectors
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ac55f9e573f94673f2c18887a5d09e45
https://doi.org/10.1074/jbc.m117.794412
https://doi.org/10.1074/jbc.m117.794412
Autor:
Vincent Dussupt, Melodi P Javid, Georges Abou-Jaoudé, Joshua A Jadwin, Jason de La Cruz, Kunio Nagashima, Fadila Bouamr
Publikováno v:
PLoS Pathogens, Vol 5, Iss 3, p e1000339 (2009)
HIV-1 release is mediated through two motifs in the p6 region of Gag, PTAP and LYPX(n)L, which recruit cellular proteins Tsg101 and Alix, respectively. The Nucleocapsid region of Gag (NC), which binds the Bro1 domain of Alix, also plays an important
Externí odkaz:
https://doaj.org/article/2cd65862e1f6449ebfbec35aa3ecc4e7
Publikováno v:
The Journal of biological chemistry. 293(2)
Phosphotyrosine (pTyr)-dependent signaling is critical for many cellular processes. It is highly dynamic, as signal output depends not only on phosphorylation and dephosphorylation rates but also on the rates of binding and dissociation of effectors
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::f0e9f0cfabdd4bca65e8df938edd2314
https://pubmed.ncbi.nlm.nih.gov/29162725
https://pubmed.ncbi.nlm.nih.gov/29162725
Autor:
Joshua A, Jadwin
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 1555
Over the last two decades there has been a significant effort in the field to characterize the phosphosite binding specificities of SH2 domains with the goal of deciphering the pY signaling code. Although high throughput studies in various formats us
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::b09b04e9917a684ab05d4860092bf513
https://pubmed.ncbi.nlm.nih.gov/28092051
https://pubmed.ncbi.nlm.nih.gov/28092051
Autor:
Joshua A. Jadwin
Publikováno v:
Methods in Molecular Biology ISBN: 9781493967605
Over the last two decades there has been a significant effort in the field to characterize the phosphosite binding specificities of SH2 domains with the goal of deciphering the pY signaling code. Although high throughput studies in various formats us
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c0cccec9b2660d6b63b41a610896bcf3
https://doi.org/10.1007/978-1-4939-6762-9_28
https://doi.org/10.1007/978-1-4939-6762-9_28
Autor:
Lin Jia, Ji Yu, Mari Ogiue-Ikeda, Forest M. White, Joshua A. Jadwin, Timothy G. Curran, Kazuya Machida, Bruce J. Mayer, Dongmyung Oh
Publikováno v:
eLife, Vol 5 (2016)
eLife Sciences Publications, Ltd.
eLife
eLife Sciences Publications, Ltd.
eLife
While the affinities and specificities of SH2 domain-phosphotyrosine interactions have been well characterized, spatio-temporal changes in phosphosite availability in response to signals, and their impact on recruitment of SH2-containing proteins in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::72d39dd35ff7bb1b8f067050cd23e0ac
https://elifesciences.org/articles/11835
https://elifesciences.org/articles/11835
Publikováno v:
Proceedings of the National Academy of Sciences. 109:14024-14029
Receptor tyrosine kinases (RTKs) control a host of biological functions by phosphorylating tyrosine residues of intracellular proteins upon extracellular ligand binding. The phosphotyrosines (p-Tyr) then recruit a subset of ∼100 Src homology 2 (SH2
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dd512c0e832b7d6a1aecf6e8bda71d69
https://doi.org/10.1073/pnas.1203397109
https://doi.org/10.1073/pnas.1203397109
Publikováno v:
Journal of Virology. 84:8181-8192
The p6 region of HIV-1 Gag contains two late (L) domains, PTAP and LYPX n L, that bind Tsg101 and Alix, respectively. Interactions with these two cellular proteins recruit members of the host's fission machinery (ESCRT) to facilitate HIV-1 release. O
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::039654525eefa247ea8def1feaa32baa
https://doi.org/10.1128/jvi.00634-10
https://doi.org/10.1128/jvi.00634-10