Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Greg Moorhead"'
Autor:
Joseph E Chambers, Lucy E Dalton, Hanna J Clarke, Elke Malzer, Caia S Dominicus, Vruti Patel, Greg Moorhead, David Ron, Stefan J Marciniak
Publikováno v:
eLife, Vol 4 (2015)
Four stress-sensing kinases phosphorylate the alpha subunit of eukaryotic translation initiation factor 2 (eIF2α) to activate the integrated stress response (ISR). In animals, the ISR is antagonised by selective eIF2α phosphatases comprising a cata
Externí odkaz:
https://doaj.org/article/cdfe0399553f43a3b9c0c2a15cc1ae87
Autor:
Catherine S. Smith, Dave Bridges, Carol MacKintosh, Nick Morrice, Greg Moorhead, Sarah E. M. Meek, Pauline Douglas
Publikováno v:
European Journal of Biochemistry. 270:1356-1362
An activity that inhibited both glutamine synthetase (GS) and nitrate reductase (NR) was highly purified from cauliflower (Brassica oleracea var. botrytis) extracts. The final preparation contained an acyl-CoA oxidase and a second protein of the plan
Autor:
Alastair Aitken, Jean Harthill, Pauline Douglas, Greg Moorhead, Uta Deiting, Mark Stitt, Carol MacKintosh, Marie Scarabel, Valérie Cotelle, Sarah E. M. Meek, Nick Morrice
Publikováno v:
The Plant Journal. 18:1-12
Far-Western overlays of soluble extracts of cauliflower revealed many proteins that bound to digoxygenin (DIG)-labelled 14-3-3 proteins. Binding to DIG-14-3-3s was prevented by prior dephosphorylation of the extract proteins or by competition with 14
Publikováno v:
University of Dundee
The form of protein phosphatase-1 associated with hepatic glycogen (PP1G) was purified to near homogeneity from rat liver by affinity chromatography on microcystin-Sepharose and gel-filtration. The enzyme is a heterodimer consisting of the catalytic
Autor:
Anna Kulma, Carol MacKintosh, Jean Harthill, Fiona C. Milne, Barry Hon Cheung Wong, Greg Moorhead, Valérie Cotelle, M. Pozuelo Rubio, D. Villadsen
Publikováno v:
Biochemical Society Transactions. 30:379-381
Many proteins that bind to a 14-3-3 column in competition with a 14-3-3-binding phospho-peptide have been purified from plant and mammalian cells and tissues. New 14-3-3 targets include enzymes of biosynthetic metabolism, vesicle trafficking, cell si
Autor:
Greg Moorhead
Publikováno v:
Protein Phosphatase Protocols
Contents Preface...v Contributors...xi Analysis Of Protein Phosphatases: Toolbox For Unraveling Cell Signaling Networks. Shirish Shenolikar...X A Brief Introduction To The Protein Phosphatase Families. Tomas Mustelin...X Small Molecule Inhibitors of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5908c6fcdc07264ec7a437cc2b55e779
https://doi.org/10.1385/159745267x
https://doi.org/10.1385/159745267x
Autor:
David Barford, Patricia T.W. Cohen, Marie Pierre Egloff, Philip Cohen, Greg Moorhead, Deborah F. Johnson
Publikováno v:
The EMBO journal. 16(8)
The diverse forms of protein phosphatase 1 in vivo result from the association of its catalytic subunit (PP1c) with different regulatory subunits, one of which is the G‐subunit (G M ) that targets PP1c to glycogen particles in muscle. Here we repor
Autor:
Deborah F. Johnson, F. Barry Caudwell, Philip Cohen, Patricia T.W. Cohen, Yu Hua Chen, Mao Xiang Chen, Greg Moorhead
Publikováno v:
European journal of biochemistry. 239(2)
The specificity of the catalytic subunit of protein phosphatase-1 (PP1c) is modified by regulatory subunits that target it to particular subcellular locations. Here, we identify PP1c-binding domains on GL and GM, the subunits that target PP1c to hepa
Publikováno v:
FEBS letters. 375(3)
A full-length cDNA encoding the putative hepatic glycogen-binding (GL) subunit of protein phosphatase-1 (PP1) was isolated from a rat liver library. The deduced amino acid sequence (284 residues, 32.6 kDa) was 23% identical (39% similar) to the N-ter
Publikováno v:
FEBS Letters. (3):141-144
Myosin is dephosphorylated by distinct forms of protein phosphatase 1 (PP1) in smooth muscle and skeletal muscle that are composed of PP1 complexed to different regulatory subunits. The smooth muscle myosin phosphatase (smPP1M) has been characterised