About: Proximal regions of the catalytic gamma and regulatory beta subunits on the interior lobe face of phosphorylase kinase are structurally coupled to each other and with enzyme activation

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About: Proximal regions of the catalytic gamma and regulatory beta subunits on the interior lobe face of phosphorylase kinase are structurally coupled to each other and with enzyme activation Goto Sponge NotDistinct Permalink

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scientific article published on 01 January 1997

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в січні 1997 (uk) articolo scientifico (pubblicato il 1997) (it) im Januar 1997 veröffentlichter wissenschaftlicher Artikel (de) artículu científicu espublizáu en xineru de 1997 (ast) artikull shkencor i botuar më 01 janar 1997 (sq) scientific article published on 01 January 1997 (en)
publication date	wds:Q73033822-456EB0B5-286E-4940-9626-593CC5B3AD41
publication date	1997-01-01 00:00:00Z (xsd:dateTime)
author name string	wds:Q73033822-097ECD70-5D83-411C-B812-DE889F3E3995 wds:Q73033822-0BAB741C-E458-4512-B196-497890C9B3AA wds:Q73033822-156B401B-E3DA-4D0E-A0FC-679B121A38DF wds:Q73033822-4FAAC6CC-5DAB-47F4-B30E-AFFB1ABC219A wds:Q73033822-736B12B4-55DA-4DAC-8545-7188AE1BC3A3 wds:Q73033822-9F68AAAC-77DD-4C78-B5CF-3661DFCA6931
author name string	Marion TN Tillman DM Carlson GM Wilkinson DA Norcum MT Fizgerald TJ
rdfs:label	Proximal regions of the catalytic gamma and regulatory beta subunits on the interior lobe face of phosphorylase kinase are structurally coupled to each other and with enzyme activation (en) Proximal regions of the catalytic gamma and regulatory beta subunits on the interior lobe face of phosphorylase kinase are structurally coupled to each other and with enzyme activation (nl) Proximal regions of the catalytic gamma and regulatory beta subunits on the interior lobe face of phosphorylase kinase are structurally coupled to each other and with enzyme activation (sq)
skos:prefLabel	Proximal regions of the catalytic gamma and regulatory beta subunits on the interior lobe face of phosphorylase kinase are structurally coupled to each other and with enzyme activation (en) Proximal regions of the catalytic gamma and regulatory beta subunits on the interior lobe face of phosphorylase kinase are structurally coupled to each other and with enzyme activation (nl) Proximal regions of the catalytic gamma and regulatory beta subunits on the interior lobe face of phosphorylase kinase are structurally coupled to each other and with enzyme activation (sq)
name	Proximal regions of the catalytic gamma and regulatory beta subunits on the interior lobe face of phosphorylase kinase are structurally coupled to each other and with enzyme activation (en) Proximal regions of the catalytic gamma and regulatory beta subunits on the interior lobe face of phosphorylase kinase are structurally coupled to each other and with enzyme activation (nl) Proximal regions of the catalytic gamma and regulatory beta subunits on the interior lobe face of phosphorylase kinase are structurally coupled to each other and with enzyme activation (sq)
title	wds:Q73033822-6657B799-37F2-4315-9847-D8D36F910598
title	Proximal regions of the catalytic gamma and regulatory beta subunits on the interior lobe face of phosphorylase kinase are structurally coupled to each other and with enzyme activation (en)
page(s)	wds:Q73033822-10381F0F-A3DE-45C2-9EA7-AD073438485C
page(s)	319-329
instance of	wds:Q73033822-6D28D040-754F-487D-B387-1654EA76F018
instance of	scholarly article
PubMed ID	wds:Q73033822-B564F086-A04A-4708-98F3-FFA1AE67B1E8
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/9018046
PubMed ID	9018046
published in	wds:Q73033822-2F582642-A520-4F0F-8DA3-A9B9806E965C
published in	Journal of Molecular Biology
issue	wds:Q73033822-20443E96-58CF-4333-A3F2-B0C69A5C3F20
volume	wds:Q73033822-141565F6-9655-460B-9C4A-1F4D0A1FC5BC
issue	3
volume	265
DOI	wds:Q73033822-6FA7DF1D-2829-4DEB-A3C9-1D5551BC2632
DOI	http://dx.doi.org/10.1006/JMBI.1996.0739
DOI	10.1006/JMBI.1996.0739
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q73033822
is cites work of	Structural evidence for co-evolution of the regulation of contraction and energy production in skeletal muscle Three-dimensional structure of phosphorylase kinase at 22 A resolution and its complex with glycogen phosphorylase b Cryoelectron microscopy reveals new features in the three-dimensional structure of phosphorylase kinase The structure of phosphorylase kinase holoenzyme at 9.9 angstroms resolution and location of the catalytic subunit and the substrate glycogen phosphorylase Mass Spectrometric Analysis of Surface-Exposed Regions in the Hexadecameric Phosphorylase Kinase Complex Structure and location of the regulatory β subunits in the (αβγδ)4 phosphorylase kinase complex Mass spectrometry reveals differences in stability and subunit interactions between activated and nonactivated conformers of the (αβγδ)4 phosphorylase kinase complex Effector-sensitive cross-linking of phosphorylase b kinase by the novel cross-linker 4-phenyl-1,2,4-triazoline-3,5-dione Evidence for the location of the allosteric activation switch in the multisubunit phosphorylase kinase complex from mass spectrometric identification of chemically crosslinked peptides. The structural effects of endogenous and exogenous Ca2+/calmodulin on phosphorylase kinase A Ca(2+)-dependent global conformational change in the 3D structure of phosphorylase kinase obtained from electron microscopy Self-association of the alpha subunit of phosphorylase kinase as determined by two-hybrid screening The regulatory beta subunit of phosphorylase kinase interacts with glyceraldehyde-3-phosphate dehydrogenase Single molecule analyses of the conformational substates of calmodulin bound to the phosphorylase kinase complex Physicochemical changes in phosphorylase kinase associated with its activation Glycogen storage disease type IX: High variability in clinical phenotype Expressed phosphorylase b kinase and its alphagammadelta subcomplex as regulatory models for the rabbit skeletal muscle holoenzyme The glucoamylase inhibitor acarbose is a direct activator of phosphorylase kinase A model for activation of the hexadecameric phosphorylase kinase complex deduced from zero-length oxidative crosslinking The regulation of glycogenolysis in the brain. CrossSearch, a user-friendly search engine for detecting chemically cross-linked peptides in conjugated proteins. Mg2+ induces conformational changes in the catalytic subunit of phosphorylase kinase, whether by itself or as part of the holoenzyme complex A review of methods used for identifying structural changes in a large protein complex Physicochemical changes in phosphorylase kinase induced by its cationic activator Mg(2+). Structural characterization of the catalytic γ and regulatory β subunits of phosphorylase kinase in the context of the hexadecameric enzyme complex. The regulatory α and β subunits of phosphorylase kinase directly interact with its substrate, glycogen phosphorylase. Activation of Phosphorylase Kinase by Physiological Temperature.
is cites work of	wds:Q28831025-63BAA28B-11B5-453F-AF62-AF922C980ECD wds:Q33343232-8E80CDF3-35C4-4A93-8D48-2688EE095B1B wds:Q36990635-8897C190-6C98-4535-A4AF-2E3AB7F7FDC9 wds:Q39945994-E7D20E20-F7FD-413A-A189-F9E145D33F82 wds:Q54124317-4D144860-86F6-4D77-A121-3785872E6F17 wds:Q24655096-A5745014-1FBC-4CE1-9EE6-69C9FA801F99 wds:Q28215772-4BBE7AB6-E95E-401B-B64A-6E848E36AFA9 wds:Q36749277-BCF887D0-A041-4E3E-BFC2-C6D7A81B32ED wds:Q73797141-A363E132-AD57-4062-971D-C13D0EDA6020 wds:Q36455657-E719C510-3C3B-476F-806C-BE52297F6EC3 wds:Q36722234-00095C01-E33A-4E9D-B0C1-780209A65AF9 wds:Q47446194-B4A50ED8-7DBF-4CAA-8374-D8006956955D wds:Q36540772-69D3CE82-F153-4331-95AE-8B9B39A98F1B wds:Q77763447-0C66E57F-1F86-4B23-8D51-0E53C617A707 wds:Q42114605-4BAA5A43-2CF6-4295-BB32-A68542767223 wds:Q41985378-94D36446-61A5-4AE6-89AA-9404C4F6B567 wds:Q24644307-D9926D26-E3E6-4E2B-AF44-DD7FA004FA76 wds:Q41950866-B232B08F-346C-4365-9BCB-7AF2DD0FEBA3 wds:Q47161542-D4FC9D88-57BD-43E9-82C8-6ACF2CBB644D wds:Q77503649-41D99A86-BDDB-4013-83B6-83784D94C1E6 wds:Q36684998-AC56F75A-0ACA-42F7-B583-13B59C551161 wds:Q37952606-87F5A76C-4500-4836-BF23-02B5D200797E wds:Q31438184-7B7AE497-D5CA-4F2E-AD3B-3CA510E0D667

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