Zobrazeno 1 - 10
of 27
pro vyhledávání: '"Valsan Mandiyan"'
Autor:
Anil R. Ekkati, Valsan Mandiyan, Jae Hyun Bae, Krishna P. Ravindranathan, Joseph Schlessinger, William L. Jorgensen
Publikováno v:
Tetrahedron Letters. 52:2228-2231
Optimization of thienopyrimidinone derivatives as FGFR1 kinase inhibitors is being pursued. The present results confirm predictions of computational modeling that an aryl substituent can be introduced at the 2-position in structure 3. The substituent
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::656dda439d0f89d8029888818f964764
https://doi.org/10.1016/j.tetlet.2010.12.081
https://doi.org/10.1016/j.tetlet.2010.12.081
Autor:
William L. Jorgensen, Krishna P. Ravindranathan, Anil R. Ekkati, Valsan Mandiyan, Jae Hyun Bae, Joseph Schlessinger
Publikováno v:
Journal of Medicinal Chemistry. 53:1662-1672
Fibroblast growth factors (FGFs) play important roles in embryonic development, angiogenesis, wound healing, and cell proliferation and differentiation. In search of inhibitors of FGFR1 kinase, 2.2 million compounds were docked into the ATP binding s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2f4ec7e08627f8f9b58cca1aea4e9681
https://doi.org/10.1021/jm901386e
https://doi.org/10.1021/jm901386e
Autor:
Yarden Opatowsky, Valsan Mandiyan, Zhongtao Zhang, Irit Lax, Joseph Schlessinger, Satoru Yuzawa
Publikováno v:
Cell. 130:323-334
SummaryStem Cell Factor (SCF) initiates its multiple cellular responses by binding to the ectodomain of KIT, resulting in tyrosine kinase activation. We describe the crystal structure of the entire ectodomain of KIT before and after SCF stimulation.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::47e2366285a330638cba5d5b8a2c60eb
https://doi.org/10.1016/j.cell.2007.05.055
https://doi.org/10.1016/j.cell.2007.05.055
Autor:
Koji Nagata, Joseph Schlessinger, Yukiko Hachimori, Motohiko Nishida, Kenji Ogura, Valsan Mandiyan, Fuyuhiko Inagaki, Masataka Horiuchi
Publikováno v:
The EMBO Journal. 20:2995-3007
Vav is a guanine nucleotide exchange factor for the Rho/Rac family that is expressed exclusively in hematopoietic cells. Growth factor receptor-bound protein 2 (Grb2) has been proposed to play important roles in the membrane localization and activati
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::356c046079473f022beef8c27db9f2a3
https://doi.org/10.1093/emboj/20.12.2995
https://doi.org/10.1093/emboj/20.12.2995
Autor:
Masashi Yokochi, Kenji Ogura, Joseph Schlessinger, Hideki Hatanaka, Satoru Yuzawa, Mikio Kataoka, Valsan Mandiyan, Fuyuhiko Inagaki, Kin-ichiro Miura
Publikováno v:
Journal of Molecular Biology. 306:527-537
Grb2 is an adaptor protein composed of a single SH2 domain flanked by two SH3 domains. Grb2 functions as an important evolutionary conserved link between a variety of cell membrane receptors and the Ras/MAP kinase-signaling cascade. Here, we describe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d4be18e0d0fde46be903c807260beeab
https://doi.org/10.1006/jmbi.2000.4396
https://doi.org/10.1006/jmbi.2000.4396
Publikováno v:
The EMBO Journal. 18:6890-6898
ADP ribosylation factors (ARFs), which are members of the Ras superfamily of GTP-binding proteins, are critical components of vesicular trafficking pathways in eukaryotes. Like Ras, ARFs are active in their GTP-bound form, and their duration of activ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::667780e903599fef08e7d5ae575d8652
https://doi.org/10.1093/emboj/18.24.6890
https://doi.org/10.1093/emboj/18.24.6890
Autor:
Valsan Mandiyan, Fuyuhiko Inagaki, Saburo Aimoto, Hiromichi Ohta, Kenji Ogura, Hiroaki Terasawa, Shigeo Tsuchiya, Hideki Hatanaka, Koji Nagata, Joseph Schlessinger
Publikováno v:
Journal of Biochemistry. 125:1151-1159
1H, 13C, and 15N NMR resonances of the SH2 domain of Grb2/Ash in both the free form and the form complexed with a phosphotyrosine-containing peptide derived from the EGF receptor were assigned by analysis of multi-dimensional, double- and triple-reso
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::53272f07693e21d3e285a6538b9baa07
https://doi.org/10.1093/oxfordjournals.jbchem.a022398
https://doi.org/10.1093/oxfordjournals.jbchem.a022398
Autor:
Kenji Ogura, Satoru Yuzawa, Shigeo Tsuchiya, Valsan Mandiyan, Fuyuhiko Inagaki, Hiroaki Terasawa, Joseph Schlessinger, Hideki Hatanaka
Publikováno v:
Journal of Molecular Biology. 289:439-445
The solution structure of growth factor receptor-bound protein 2 (Grb2) SH2 complexed with a Shc-derived phosphotyrosine (pTyr)-containing peptide was determined by nuclear magnetic resonance (NMR) spectroscopy. The pTyr binding site of Grb2 SH2 was
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::162717efa6e7dfa55a5be921066ac58e
https://doi.org/10.1006/jmbi.1999.2792
https://doi.org/10.1006/jmbi.1999.2792
Autor:
Valsan Mandiyan, Min Zhou, Julian M. Sturtevant, Joseph Schlessinger, Ben Margolis, Ronan O'Brien, Mark A. Lemmon
Publikováno v:
Journal of Biological Chemistry. 271:4770-4775
The N-terminal 200 amino acids of SHC constitute a unique phosphotyrosine (Tyr(P)) interaction (PI) domain that shows no significant sequence similarity to the other Tyr(P)-recognizing module, the SH2 domain. We describe the thermodynamic parameters
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c5e8718950e45d3e0158cb29a9ebd5c3
https://doi.org/10.1074/jbc.271.9.4770
https://doi.org/10.1074/jbc.271.9.4770
Publikováno v:
Europe PubMed Central
Scopus-Elsevier
Scopus-Elsevier
Grb2, composed entirely of SH2 and SH3 domains, serves as an adaptor protein in signaling from growth factor-activated tyrosine kinase receptors. It interacts via its SH2 domain with the autophosphorylated carboxyl-terminal tail of activated epiderma
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::30c84b450d1534727bd6d7de41ede603
https://doi.org/10.1016/s0021-9258(18)31745-9
https://doi.org/10.1016/s0021-9258(18)31745-9