Zobrazeno 1 - 10 of 10 pro vyhledávání: '"Beth L. Murray"'
1
15 years of PhosphoSitePlus®: integrating post-translationally modified sites, disease variants and isoforms
Autor: Travis J. Wheeler, Peter Hornbeck, Jon M. Kornhauser, Beth L. Murray, Latham, Bin Zhang, Florian Gnad, Nandhikonda, Alexander Nord, Elzbieta Skrzypek
Publikováno v: Nucleic Acids Research
For 15 years the mission of PhosphoSitePlus® (PSP, https://www.phosphosite.org) has been to provide comprehensive information and tools for the study of mammalian post-translational modifications (PTMs). The number of unique PTMs in PSP is now more
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b514388a921d85153f16986dd69854c4
https://pubmed.ncbi.nlm.nih.gov/30445427
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2
PhosphoSitePlus, 2014: mutations, PTMs and recalibrations
Autor: Peter Hornbeck, Jon M. Kornhauser, Elzbieta Skrzypek, Vaughan Latham, Beth L. Murray, Bin Zhang
Publikováno v: Nucleic Acids Research
PhosphoSitePlus(®) (PSP, http://www.phosphosite.org/), a knowledgebase dedicated to mammalian post-translational modifications (PTMs), contains over 330,000 non-redundant PTMs, including phospho, acetyl, ubiquityl and methyl groups. Over 95% of the
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8e9b4186e63e242e2fddd811c3330dee
https://doi.org/10.1093/nar/gku1267
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3
PhosphoSitePlus: a comprehensive resource for investigating the structure and function of experimentally determined post-translational modifications in man and mouse
Autor: Bin Zhang, Sasha Tkachev, Vaughan Latham, Jon M. Kornhauser, Beth L. Murray, Peter Hornbeck, Elzbieta Skrzypek, Michael Sullivan
Publikováno v: Nucleic Acids Research
PhosphoSitePlus (http://www.phosphosite.org) is an open, comprehensive, manually curated and interactive resource for studying experimentally observed post-translational modifications, primarily of human and mouse proteins. It encompasses 1,30,000 no
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ea5d9763fe0764a92cb00ab8db6d4b5b
https://doi.org/10.1093/nar/gkr1122
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4
Murine peptidoglycan recognition proteins PglyrpIα and PglyrpIβ are encoded in the epidermal differentiation complex and are expressed in epidermal and hematopoietic tissues
Autor: Normand Allaire, John P. Carulli, Thomas Crowell, Beth L. Murray, Punam Mathur, Yen-Ming Hsu, Greg Thill, Humphrey Gardner
Publikováno v: Genomics. 83:1151-1163
Peptidoglycan recognition proteins (PGRPs or PGLYRPs) are pattern recognition molecules that are found in insects and mammals and are critical for innate immune responses. PGRPs bind peptidoglycan, a ubiquitous component of bacterial cell walls, and
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c2ad6c52dc25c621a2d09d8cdd057b04
https://doi.org/10.1016/j.ygeno.2004.01.003
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7
TAJ/TROY, an orphan TNF receptor family member, binds Nogo-66 receptor 1 and regulates axonal regeneration
Autor: Melissa Levesque, Sveltlana Shulga-Morskaya, Zhaohui Shao, Greg Thill, Xinhua Lee, R. Blake Pepinsky, John M. Mccoy, Dinah W. Y. Sah, Sha Mi, Jeffrey L. Browning, Beth L. Murray, Vincent Jung, Norm Allaire, Martin L. Scott
Publikováno v: Neuron. 45(3)
SummaryMyelin-associated inhibitory factors (MAIFs) are inhibitors of CNS axonal regeneration following injury. The Nogo receptor complex, composed of the Nogo-66 receptor 1 (NgR1), neurotrophin p75 receptor (p75), and LINGO-1, represses axon regener
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a778b4cbe80bf1a3d817488432fa207e
https://pubmed.ncbi.nlm.nih.gov/15694322
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8
Abstract 5146: Phosphositeplus® and protein modifications in cancer, a case study: profiling tyrosine phosphorylated sites in AML and CML
Autor: Elzbieta Skrzypek, Bin Zhang, Jon M. Kornhauser, Peter Hornbeck, Vaughan Latham, Beth L. Murray
Publikováno v: Cancer Research. 73:5146-5146
Proceedings: AACR 104th Annual Meeting 2013; Apr 6-10, 2013; Washington, DC PhosphoSitePlus® (PSP) is an open, comprehensive, manually curated, and interactive resource for studying experimentally observed post-translational modifications, primarily
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::50d80a1878da7c5852f730e03dacf679
https://doi.org/10.1158/1538-7445.am2013-5146
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9
Profiling post-translational modifications of proteins that regulate gene expression
Autor: Ela Skrzypek, Vaughan Latham, Bin Zhang, Peter Hornbeck, Sasha Tkachev, Beth L. Murray, Jon M. Kornhauser
Publikováno v: Genome Biology
Background The aggregation of over 100,000 non-redundant, experimentally-determined post-translational modification sites on human proteins in PhosphoSitePlus (PSP) has enabled system-wide analyses of modification sites on proteins that regulate gene
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a8fb0de190e75a4f01bb9ff6b27bed19
https://doi.org/10.1186/gb-2010-11-s1-p19
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10
ANALYSIS OF STRUCTURAL REQUIREMENTS FOR FACTOR VIII FUNCTION USING SITE-DIRECTED MUTAGENESIS
Autor: Beth L. Murray, Debra D. Pittman, Randal J. Kaufman, Jack H. Wang, Louise C. Wasley
Publikováno v: XIth International Congress on Thrombosis and Haemostasis.
Factor VIII (fVIII) functions in the intrinsic pathway of coagulation as the cofactor for Factor IXa proteolytic activation of Factor X. fVIII contains multiple sites which are susceptible to cleavage by thrombin, Factor Xa, and activate) protein C.
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::80900f332f34c63291789dda4083bcff
https://doi.org/10.1055/s-0038-1644044
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