About: Protein Kinase CK2 Mutants Defective in Substrate Recognition

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scientific article published in Journal of Biological Chemistry

Attributes	Values
rdf:type	Item
description	artículu científicu (ast) wetenschappelijk artikel (nl) наукова стаття, опублікована в травні 1996 (uk) article publié dans la revue scientifique Journal of Biological Chemistry (fr) im Mai 1996 veröffentlichter wissenschaftlicher Artikel (de) scientific article published in Journal of Biological Chemistry (en)
publication date	wds:Q58194450-F2BC36EF-58C1-4F38-98F0-9A7B8B9CE745
publication date	1996-05-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q58194450-1B5A2979-1E96-4DCD-8ABD-F82DDEB41A73
language of work or name	English
cites work	wds:Q58194450-0385F1B8-9EB7-4AAF-8ADA-CD368DF0C0BA wds:Q58194450-2243947A-0279-467C-93BC-852039F6F84E wds:Q58194450-26AC41A6-0BAB-4FD7-9BED-572F26B24A10 wds:Q58194450-286521BD-9A77-485F-A4DD-63CA391BDA39 wds:Q58194450-2BA528CE-9BE2-4B42-B11D-EB5B617677C4 wds:Q58194450-2D87A26D-6F7C-4107-8781-2CAB7BA10161 wds:Q58194450-36C2F684-0493-4194-A59B-221A45490110 wds:Q58194450-38BF3C87-A1D7-4EBD-9669-B92D927935CD wds:Q58194450-4052F7F6-EA9F-41CE-A6B6-ABCEE13E39FE wds:Q58194450-40E8D8F2-F2F9-410A-AB59-4CBFCB16D389 wds:Q58194450-50F7E46C-E5A8-49C4-9189-AFE8201D0523 wds:Q58194450-6AA01CEC-41F8-45E1-84BC-6F529B8F76A1 wds:Q58194450-7B762BE0-EB1F-4E9B-8769-909A4FED267A wds:Q58194450-81014622-1C62-4593-AD68-3BCFF5655D14 wds:Q58194450-86FD4139-B842-46A4-BE42-2A0DB1A5F04C wds:Q58194450-89E5BEB2-5AC8-49D8-A495-A9869DADA1FB wds:Q58194450-930DA4C8-0F92-48BF-8B9E-4E9D5FAC339C wds:Q58194450-9AB78FCA-D554-491D-A179-ED000B1EBDF1 wds:Q58194450-AD176C9A-2CEF-422E-B0B1-32C43F44A960 wds:Q58194450-B75D63C6-A3C9-4C57-81C1-8DB0E60773DC wds:Q58194450-BB8790D0-D4E7-48C3-AE3F-9A44748CB04D wds:Q58194450-BE32BDD3-F083-4833-9000-B17948455B74 wds:Q58194450-C360B4C1-2AA9-45CF-8F3B-ABD58074977F wds:Q58194450-C6E7E607-1242-4D2D-BC1D-C3C11CEF3697 wds:Q58194450-C82EA51B-5EF0-4D60-B769-DA26919070FB wds:Q58194450-CA9C2CC9-6C31-4F74-BE44-BF34320B70C8 wds:Q58194450-D53AA6D3-C580-4E83-A232-B31A195787C0 wds:Q58194450-DE848EF0-7B25-4C3E-9513-9BE9A3D05D07 wds:Q58194450-E87E9EBA-56E6-40C5-810E-BF6A9A4FBAD0 wds:Q58194450-EEF78B0B-739B-4CD1-8D79-860D0C58BF70 wds:Q58194450-F910627A-00EC-4DAA-9235-671E0E1A17A8 wds:Q58194450-FC972765-718B-40F7-84AD-D036E775C04E wds:Q58194450-FF89427C-FEF8-4C57-9FA3-D137EEE2D8DC
cites work	Ca2+ phospholipid-dependent and independent phosphorylation of synthetic peptide substrates by protein kinase C Protein kinase catalytic domain sequence database: identification of conserved features of primary structure and classification of family members Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4 Casein kinase 2: an 'eminence grise' in cellular regulation? Casein kinases: pleiotropic mediators of cellular regulation Casein kinase II alpha transgene-induced murine lymphoma: relation to theileriosis in cattle. Reconstitution of normal and hyperactivated forms of casein kinase-2 by variably mutated beta-subunits. Isolation and characterization of recombinant human casein kinase II subunits alpha and beta from bacteria. Subunit structure and autophosphorylation mechanism of casein kinase-TS (type-2) from rat liver cytosol The consensus sequences for cdc2 kinase and for casein kinase-2 are mutually incompatible. A study with peptides derived from the beta-subunit of casein kinase-2 Role of the beta subunit of casein kinase-2 on the stability and specificity of the recombinant reconstituted holoenzyme Structure of a peptide inhibitor bound to the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Crystal Structure of the Catalytic Subunit of Cyclic Adenosine Monophosphate-Dependent Protein Kinase Protein kinases--structure and function. Site specificity of casein kinase-2 (TS) from rat liver cytosol. A study with model peptide substrates Design and synthesis of two new peptide substrates for the specific and sensitive monitoring of casein kinases-1 and -2 Substrate and pseudosubstrate interactions with protein kinases: determinants of specificity Three protein kinase structures define a common motif Identification of electrostatic interactions that determine the phosphorylation site specificity of the cAMP-dependent protein kinase Dissection of the dual function of the beta-subunit of protein kinase CK2 ('casein kinase-2'): a synthetic peptide reproducing the carboxyl-terminal domain mimicks the positive but not the negative effects of the whole protein Isolation of phosphorylated peptides and proteins on ion exchange papers Casein kinase 2 down-regulation and activation by polybasic peptides are mediated by acidic residues in the 55-64 region of the beta-subunit. A study with calmodulin as phosphorylatable substrate Activity of the E75E76 mutant of the alpha subunit of casein kinase II from Xenopus laevis. Mapping the residues of protein kinase CK2 α subunit responsible for responsiveness to polyanionic inhibitors Mapping the residues of protein kinase CK2 implicated in substrate recognition: mutagenesis of conserved basic residues in the alpha-subunit Casein kinase-2 structure-function relationship: creation of a set of mutants of the beta subunit that variably surrogate the wildtype beta subunit function Substrate recognition by casein kinase-II: the role of histidine-160. Mutations on 170Glu, a substrate recognition residue in mouse cAMP-dependent protein kinase, generate enzymes with altered substrate affinity and biological functions Identification of the substrate and pseudosubstrate binding sites of phosphorylase kinase gamma-subunit Phosphoserine in peptide substrates can specify casein kinase II action Role of phosphorylated aminoacyl residues in generating atypical consensus sequences which are recognized by casein kinase-2 but not by casein kinase-1 Random tyrosine and glutamic acid-containing polymers are very powerful inhibitors of casein kinase-2
author name string	wds:Q58194450-39B22905-403F-4089-BFD4-FE0BA88CED86 wds:Q58194450-BBEC7BC0-3F4F-48F5-A245-709F09E16F48 wds:Q58194450-C741BC16-AF08-43AC-9620-53A6DC859755
author name string	O G Issinger L A Pinna F Meggio
rdfs:label	Protein Kinase CK2 Mutants Defective in Substrate Recognition (en) Protein Kinase CK2 Mutants Defective in Substrate Recognition (nl)
skos:prefLabel	Protein Kinase CK2 Mutants Defective in Substrate Recognition (en) Protein Kinase CK2 Mutants Defective in Substrate Recognition (nl)
name	Protein Kinase CK2 Mutants Defective in Substrate Recognition (en) Protein Kinase CK2 Mutants Defective in Substrate Recognition (nl)
author	wds:Q58194450-81415D89-207B-465C-85A1-B18179761E49 wds:Q58194450-F7CE6C55-CF47-47A8-A061-1FEA7B35D2F1
author	Stefania Sarno Philippe Vaglio
title	wds:Q58194450-BDD75E8F-EB46-4ADB-972C-FFF9E786CC39
title	Protein kinase CK2 mutants defective in substrate recognition. Purification and kinetic analysis (en)
page(s)	wds:Q58194450-AFF58474-9968-4B51-99AE-98C85E375A13
page(s)	10595-10601
instance of	wds:Q58194450-9002353F-1C7C-4BFE-949B-3EFAB4157557
instance of	scholarly article
PubMed ID	wds:Q58194450-8696B3CA-C40F-40D5-AF2D-931E598B380B

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