Zobrazeno 1 - 10
of 228
pro vyhledávání: '"Michael J. Begley"'
Publikováno v:
Cell Death & Differentiation. 24:238-250
Death-associated protein kinase 1 (DAPK1) has been shown to have important roles in neuronal cell death in several model systems and has been implicated in multiple diseases, including Alzheimer's disease (AD). However, little is known about the mole
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::619f5b40e15067e63562f7db77ad8354
https://doi.org/10.1038/cdd.2016.114
https://doi.org/10.1038/cdd.2016.114
Autor:
Ana Lako, Lewis C. Cantley, Jean J. Zhao, Timothy J. Mitchison, Yubao Wang, Michael J. Eck, Nathanael S. Gray, Michael J. Begley, Qing Li, Hai-Tsang Huang
Publikováno v:
Proceedings of the National Academy of Sciences. 113:9810-9815
The protein kinase maternal and embryonic leucine zipper kinase (MELK) is critical for mitotic progression of cancer cells; however, its mechanisms of action remain largely unknown. By combined approaches of immunoprecipitation/mass spectrometry and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::66dc3799f23e23a78202a08b0a8083ea
https://doi.org/10.1073/pnas.1606862113
https://doi.org/10.1073/pnas.1606862113
Autor:
Michael J. Begley, Lewis C. Cantley, Apostolou Irina, Michael J. Eck, Cai-Hong Yun, Christina A. Gewinner, Jared L. Johnson, Anthony J. Coyle, John M. Asara
Publikováno v:
Nature Structural & Molecular Biology. 22:983-990
Aberrant activation of the EGF receptor (EGFR) contributes to many human cancers by activating the Ras-MAPK pathway and other pathways. EGFR signaling is augmented by Src-family kinases, but the mechanism is poorly understood. Here, we show that huma
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::52feec0752a62f78fa6a10615dfbb876
https://doi.org/10.1038/nsmb.3117
https://doi.org/10.1038/nsmb.3117
Autor:
Xuemei Yang, Norbert Perrimon, Pengyu Hong, Maria I. Kontaridis, Jessica Lauriol, Michael J. Begley, John M. Asara, Meghana M. Kulkarni, Lewis C. Cantley, Alexa B. Turke, Jie Qi, Yu-Hsin Chiu, Min Yuan, Jeffrey A. Engelman, Susanne B. Breitkopf
Publikováno v:
Scientific Reports
Using a series of immunoprecipitation (IP) – tandem mass spectrometry (LC-MS/MS) experiments and reciprocal BLAST, we conducted a fly-human cross-species comparison of the phosphoinositide-3-kinase (PI3K) interactome in a drosophila S2R+ cell line
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2b8d4044a22ed3b4134ddd6cce5073f3
https://doi.org/10.1038/srep20471
https://doi.org/10.1038/srep20471
Autor:
Michale Bouskila, Noor Esoof, Laurie Gay, Emily H. Fang, Maria Deak, Michael J. Begley, Lewis C. Cantley, Alan Prescott, Kate G. Storey, Dario R. Alessi
Publikováno v:
Biochemical Journal. 437:157-167
Mutations that truncate the C-terminal non-catalytic moiety of TTBK2 (tau tubulin kinase 2) cause the inherited, autosomal dominant, SCA11 (spinocerebellar ataxia type 11) movement disorder. In the present study we first assess the substrate specific
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b72b462ace679710d7094f63218e3da8
https://doi.org/10.1042/bj20110276
https://doi.org/10.1042/bj20110276
Autor:
Gregory S. Taylor, Michael J. Begley, Partho Ghosh, Melissa A. Brock, Virgil L. Woods, Jack E. Dixon
Publikováno v:
Proceedings of the National Academy of Sciences. 103:927-932
Myotubularins, a large family of catalytically active and inactive proteins, belong to a unique subgroup of protein tyrosine phosphatases that use inositol phospholipids, rather than phosphoproteins, as physiological substrates. Here, by integrating
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::04bb94507ac3cbe0c272a48060c9fc7e
https://doi.org/10.1073/pnas.0510006103
https://doi.org/10.1073/pnas.0510006103
Autor:
Michael J. Begley, Jack E. Dixon
Publikováno v:
Current Opinion in Structural Biology. 15:614-620
The human neuromuscular diseases X-linked myotubular myopathy and Charcot-Marie-Tooth disease type 4B are caused by mutations in myotubularin family proteins. The myotubularins are a unique subfamily of protein tyrosine phosphatases that utilize inos
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4981c7a07f512a46fef4af18f5613990
https://doi.org/10.1016/j.sbi.2005.10.016
https://doi.org/10.1016/j.sbi.2005.10.016
Autor:
Gregory S. Taylor, Donna M. Veine, Jack E. Dixon, Michael J. Begley, Jeanne A. Stuckey, Soo Kim
Publikováno v:
Molecular Cell. 12(6):1391-1402
Myotubularin-related proteins are a large subfamily of protein tyrosine phosphatases (PTPs) that dephosphorylate D3-phosphorylated inositol lipids. Mutations in members of the myotubularin family cause the human neuromuscular disorders myotubular myo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dd4da4ad8c6e7bdff491a222e64d616f
Autor:
Xin Huang, Paul E. Rose, Yan Gu, Huilin Zhao, Xiaotian Zhu, Michael J. Begley, Kurt Morgenstern
Publikováno v:
Structure. 11:21-30
Akt/PKB represents a subfamily of three isoforms from the AGC serine/threonine kinase family. Amplification of Akt activity has been implicated in diseases that involve inappropriate cell survival, including a number of human malignancies. The struct
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3fbe315abde921f6e9b27449356bbe34
https://doi.org/10.1016/s0969-2126(02)00937-1
https://doi.org/10.1016/s0969-2126(02)00937-1
Autor:
Michael J. Begley, Andrei S. Batsanov, Claire E. Russell, Paul H. Walton, Michael W. George, Peter Hubberstey, Meguma Munakata
Publikováno v:
Journal of the Chemical Society, Dalton Transactions. :4251-4259
Regardless of conditions, reaction of [Cu(NCMe)4][BF4] with pyridazine (pydz) or 3-methylpyridazine (Mepydz) in MeCN or with pydz in PhCN invariably gave tris-bridged dinuclear cations, [{Cu(NCR)}2(µ-diimine)3]2+. Structural analysis, by single crys
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::895c51b74da058f865a4d0dc20b5eaf3
https://doi.org/10.1039/a906192d
https://doi.org/10.1039/a906192d