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Volumn 352, Issue 3, 2000, Pages 651-658
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The C-terminus of NIPP1 (nuclear inhibitor of protein phosphatase-1) contains a novel binding site for protein phosphatase-1 that is controlled by tyrosine phosphorylation and RNA binding
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Author keywords
Dephosphorylation; Lyn; mRNA splicing; Substrate specificity; Targeting
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Indexed keywords
ENZYME INHIBITOR;
MESSENGER RNA;
MYELIN BASIC PROTEIN;
PHOSPHOPROTEIN PHOSPHATASE 1;
PROTEIN NIPP 1;
RNA BINDING PROTEIN;
UNCLASSIFIED DRUG;
ANIMAL CELL;
ARTICLE;
BINDING SITE;
CARBOXY TERMINAL SEQUENCE;
CHEMICAL MUTAGENESIS;
CONTROLLED STUDY;
DEPHOSPHORYLATION;
ENZYME ACTIVE SITE;
ENZYME ACTIVITY;
ENZYME BINDING;
ENZYME INHIBITION;
ENZYME SPECIFICITY;
ENZYME SUBUNIT;
NONHUMAN;
PRIORITY JOURNAL;
PROTEIN PHOSPHORYLATION;
PROTEIN PROTEIN INTERACTION;
PROTEIN RNA BINDING;
PROTEIN TARGETING;
RNA SPLICING;
AMINO ACID SEQUENCE;
BINDING SITES;
CARRIER PROTEINS;
INTRACELLULAR SIGNALING PEPTIDES AND PROTEINS;
MODELS, BIOLOGICAL;
MOLECULAR SEQUENCE DATA;
MUTATION;
OSMOLAR CONCENTRATION;
PEPTIDE FRAGMENTS;
PHOSPHOPROTEIN PHOSPHATASE;
PHOSPHORYLATION;
PHOSPHOTYROSINE;
PROTEIN BINDING;
PROTEIN STRUCTURE, TERTIARY;
PROTEIN SUBUNITS;
RNA;
RNA-BINDING PROTEINS;
SEQUENCE ALIGNMENT;
SRC-FAMILY KINASES;
ANIMALIA;
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EID: 0034672212
PISSN: 02646021
EISSN: None
Source Type: Journal
DOI: 10.1042/0264-6021:3520651 Document Type: Article |
Times cited : (61)
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References (24)
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