About: Importance of the β12-β13 Loop in Protein Phosphatase-1 Catalytic Subunit for Inhibition by Toxins and Mammalian Protein Inhibitors

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About: Importance of the β12-β13 Loop in Protein Phosphatase-1 Catalytic Subunit for Inhibition by Toxins and Mammalian Protein Inhibitors Goto Sponge NotDistinct Permalink

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scientific article published in Journal of Biological Chemistry

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rdf:type	Item
description	artículu científicu (ast) wetenschappelijk artikel (nl) наукова стаття, опублікована в серпні 1999 (uk) article publié dans la revue scientifique Journal of Biological Chemistry (fr) im August 1999 veröffentlichter wissenschaftlicher Artikel (de) scientific article published in Journal of Biological Chemistry (en)
publication date	wds:Q56766180-838D79BC-7CCE-40A7-961D-4C72284663BE
publication date	1999-08-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q56766180-B2C500EB-CDC6-4C6B-8397-FD3BEB2F98AF
language of work or name	English
cites work	wds:Q56766180-0BA96853-DB2D-4D64-9573-3FB2240FEF03 wds:Q56766180-0C81842C-0032-4634-BE24-87B76B58F18C wds:Q56766180-12DFAB76-35F5-4187-88D4-81F91674105E wds:Q56766180-1D89F9F7-A6BF-4425-ADD5-75AC3BF21D6C wds:Q56766180-2DFCFB77-4B99-49EF-BFF4-FA23C6D9E6CF wds:Q56766180-3FBB6DA3-8589-4E4B-BDF4-55D73716FE98 wds:Q56766180-3FBD2275-BA10-41A9-9ED3-B20D744CE8F7 wds:Q56766180-6DE95D89-EF69-4A03-9D08-F9CB58A47B87 wds:Q56766180-7DCE6BEE-8709-463C-9E41-4AF4218EE4AE wds:Q56766180-7FF973AC-D373-4389-AAA4-E944FF0A5FAC wds:Q56766180-8699497F-5A77-4100-963A-2E68F6593E63 wds:Q56766180-912A97E8-2486-440C-9C30-1E0A2CDAB911 wds:Q56766180-933411F4-1642-4E58-87A0-190CAF72F85F wds:Q56766180-A405293E-A0C1-4F7D-AA33-6778E0342AF2 wds:Q56766180-ADE9EBDA-A112-46B8-A17F-21691E60407A wds:Q56766180-D9D136A5-B51F-4E24-909B-26F3C55C2147 wds:Q56766180-E62B5D94-1E61-4722-A405-8674FEEB9FAF wds:Q56766180-E6E96F98-D2C1-4935-BDCC-6D2EDE0DBE2B wds:Q56766180-EDF82E7B-6B58-462D-AF88-EC35F998F142 wds:Q56766180-FADD6FAC-A973-4F25-B515-C51B058DFD41 wds:Q56766180-FD55C8D7-8366-4C39-9289-E9EE9B9A7F6A wds:Q56766180-FFC15A0B-2A4E-4BA8-8FEF-08405766D385
cites work	Localization of the gene encoding a type I protein phosphatase catalytic subunit to human chromosome band 11q13 Identification of protein phosphatase-1-binding proteins by microcystin-biotin affinity chromatography Inhibitor-2 functions like a chaperone to fold three expressed isoforms of mammalian protein phosphatase-1 into a conformation with the specificity and regulatory properties of the native enzyme. Multiple structural elements define the specificity of recombinant human inhibitor-1 as a protein phosphatase-1 inhibitor Structural basis for the recognition of regulatory subunits by the catalytic subunit of protein phosphatase 1 Characterization of the interaction between DARPP-32 and protein phosphatase 1 (PP-1): DARPP-32 peptides antagonize the interaction of PP-1 with binding proteins Three-dimensional structure of the catalytic subunit of protein serine/threonine phosphatase-1 Physiologic importance of protein phosphatase inhibitors DARPP-32: regulator of the efficacy of dopaminergic neurotransmission Molecular determinants of nuclear protein phosphatase-1 regulation by NIPP-1. Conversion of Protein Phosphatase 1 Catalytic Subunit to a Mn2+-Dependent Enzyme Impairs Its Regulation by Inhibitor 1† Protein phosphatase type-1 and glycogen bind to a domain in the skeletal muscle regulatory subunit containing conserved hydrophobic sequence motif Cloning and chromosomal localization of Drosophila cDNA encoding the catalytic subunit of protein phosphatase 1 alpha. High conservation between mammalian and insect sequences Conservation analysis and structure prediction of the protein serine/threonine phosphatases. Sequence similarity with diadenosine tetraphosphatase from Escherichia coli suggests homology to the protein phosphatases. In vivo and in vitro binding of microcystin to protein phosphatases 1 and 2A. Inhibitor-1 interaction domain that mediates the inhibition of protein phosphatase-1. Fostriecin, an antitumor antibiotic with inhibitory activity against serine/threonine protein phosphatases types 1 (PP1) and 2A (PP2A), is highly selective for PP2A. Remarkable similarities between yeast and mammalian protein phosphatases Characterization of the PP2A alpha gene mutation in okadaic acid-resistant variants of CHO-K1 cells Protein phosphatase regulation by endogenous inhibitors Expression of recombinant inhibitor-2 in E. coli and its utilization for the affinity chromatography of protein phosphatase-1. Purification of the catalytic subunit of protein phosphatase-1 from Drosophila melanogaster.
author name string	wds:Q56766180-48CFDCF2-8CBC-40BA-8995-B4074B2715AB wds:Q56766180-8CC627B5-A022-4D3B-B295-CF2915F1B8F4 wds:Q56766180-9694449C-3EEA-4CD1-ABC0-6E2458076997 wds:Q56766180-F140C6E8-956B-48C1-8A99-34AACD561758
author name string	S Shenolikar S Barik R E Honkanen T Kleeman
rdfs:label	Importance of the β12-β13 Loop in Protein Phosphatase-1 Catalytic Subunit for Inhibition by Toxins and Mammalian Protein Inhibitors (en) Importance of the β12-β13 Loop in Protein Phosphatase-1 Catalytic Subunit for Inhibition by Toxins and Mammalian Protein Inhibitors (nl)
skos:prefLabel	Importance of the β12-β13 Loop in Protein Phosphatase-1 Catalytic Subunit for Inhibition by Toxins and Mammalian Protein Inhibitors (en) Importance of the β12-β13 Loop in Protein Phosphatase-1 Catalytic Subunit for Inhibition by Toxins and Mammalian Protein Inhibitors (nl)
name	Importance of the β12-β13 Loop in Protein Phosphatase-1 Catalytic Subunit for Inhibition by Toxins and Mammalian Protein Inhibitors (en) Importance of the β12-β13 Loop in Protein Phosphatase-1 Catalytic Subunit for Inhibition by Toxins and Mammalian Protein Inhibitors (nl)
author	wds:Q56766180-C17E2010-07EC-4036-AF48-93073FE6536D
author	John Connor
title	wds:Q56766180-9EEAC15E-18F5-483E-9C23-BECECCBD77D0
title	Importance of the beta12-beta13 loop in protein phosphatase-1 catalytic subunit for inhibition by toxins and mammalian protein inhibitors (en)
page(s)	wds:Q56766180-C2D12094-FB1D-4FD7-8350-628777F4E7CE
page(s)	22366-22372
instance of	wds:Q56766180-4C6C4532-06DC-4962-A197-5829C0E69F60
instance of	scholarly article
PubMed ID	wds:Q56766180-CA7DCCDB-2F58-4A5A-AB5B-4DDB3E6AD7A4
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/10428807
PubMed ID	10428807
published in	wds:Q56766180-19943EDB-BBB1-4F9A-8727-4A7C57EE99EB
published in	Journal of Biological Chemistry
issue	wds:Q56766180-F93AD7DF-0D3F-4AD8-AB7C-4DDFC8A0A1F1
volume	wds:Q56766180-75FBF4AD-F702-4D51-8613-F746195E8158
issue	32
volume	274
DOI	wds:Q56766180-7E4D9A1A-A6F3-4AD0-838D-DBDE031C657E
DOI	http://dx.doi.org/10.1074/JBC.274.32.22366
DOI	10.1074/JBC.274.32.22366
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q56766180
is cites work of	Interaction of inhibitor-2 with the catalytic subunit of type 1 protein phosphatase. Identification of a sequence analogous to the consensus type 1 protein phosphatase-binding motif Neurabins recruit protein phosphatase-1 and inhibitor-2 to the actin cytoskeleton Structural basis for the catalytic activity of human serine/threonine protein phosphatase-5. Growth arrest and DNA damage-inducible protein GADD34 assembles a novel signaling complex containing protein phosphatase 1 and inhibitor 1. Crystal structure of the tumor-promoter okadaic acid bound to protein phosphatase-1 Crystal structure of the complex between calyculin A and the catalytic subunit of protein phosphatase 1 Structural basis of protein phosphatase 1 regulation Binding of the concave surface of the Sds22 superhelix to the alpha 4/alpha 5/alpha 6-triangle of protein phosphatase-1. WNK3 bypasses the tonicity requirement for K-Cl cotransporter activation via a phosphatase-dependent pathway Combinatorial control of protein phosphatase-1

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