About: Identification and cDNA cloning of 35-kDa phosphatidic acid phosphatase (type 2) bound to plasma membranes. Polymerase chain reaction amplification of mouse H2O2-inducible hic53 clone yielded the cDNA encoding phosphatidic acid phosphatase

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About: Identification and cDNA cloning of 35-kDa phosphatidic acid phosphatase (type 2) bound to plasma membranes. Polymerase chain reaction amplification of mouse H2O2-inducible hic53 clone yielded the cDNA encoding phosphatidic acid phosphatase Goto Sponge NotDistinct Permalink

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description	artículu científicu espublizáu en 1996 (ast) vědecký článek publikovaný v roce 1996 (cs) наукова стаття, опублікована в серпні 1996 (uk) 1996 թվականի օգոստոսին հրատարակված գիտական հոդված (hy) 1996 թուականի Օգոստոսին հրատարակուած գիտական յօդուած (hyw) article publié dans la revue scientifique Journal of Biological Chemistry (fr) scientific journal article (en) im August 1996 veröffentlichter wissenschaftlicher Artikel (de) vedecký článok (publikovaný 1996/08/02) (sk) wetenschappelijk artikel (gepubliceerd op 1996/08/02) (nl) مقالة علمية (نشرت في 2-8-1996) (ar)
publication date	wds:Q28593858-B34A1E32-02C9-4BCC-AFFF-824375F24D16
publication date	1996-08-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q28593858-25430667-0F6C-454B-826A-64C25A4BF276
language of work or name	English
cites work	wds:Q28593858-10FB796E-5161-427B-A8F1-001D7FD34315 wds:Q28593858-1CC328C3-9E27-4BF7-A646-7096564DAFEE wds:Q28593858-438E5E01-5D9A-44D1-9182-6529AF81A106 wds:Q28593858-5545067A-ADBB-4B52-BC42-EE6D94F48617 wds:Q28593858-73542CDC-8889-47E7-8D49-502E93D8E5C0 wds:Q28593858-82FFF077-0778-46C3-9864-C05666076CBC wds:Q28593858-862BA2FC-1F87-4706-AF5D-B573B86474A4 wds:Q28593858-98FAB385-B58E-499B-921B-53BAD98E91D9 wds:Q28593858-A059EA10-65E9-4D29-8F08-9D2853ADB16B wds:Q28593858-B99070DC-F38D-49D9-8106-1C6D0CDEE09F wds:Q28593858-CC4F5D37-0934-4290-90CE-197C1A89BE41 wds:Q28593858-D005C8DC-4F46-4CB6-897B-72A427941585 wds:Q28593858-E000FD83-7FBD-4243-BBC7-75877573FD50 wds:Q28593858-E7214FA7-17E3-4347-A7F3-48568C63D26B wds:Q28593858-F53EDAA8-7D1E-4A77-8515-A95526AD3269
cites work	Molecular cloning of a novel diacylglycerol kinase isozyme with a pleckstrin homology domain and a C-terminal tail similar to those of the EPH family of protein-tyrosine kinases A rapid assay for measuring the activity and the Mg2+ and Ca2+ requirements of phosphatidate phosphohydrolase in cytosolic and microsomal fractions of rat liver. Purification and characterization of N-ethylmaleimide-insensitive phosphatidic acid phosphohydrolase (PAP2) from rat liver A simple method for displaying the hydropathic character of a protein The role of protein kinase C in cell surface signal transduction and tumour promotion Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4 DNA sequencing with chain-terminating inhibitors Compilation and analysis of sequences upstream from the translational start site in eukaryotic mRNAs Assembly of asparagine-linked oligosaccharides A method for the quantitative recovery of protein in dilute solution in the presence of detergents and lipids DISC ELECTROPHORESIS. II. METHOD AND APPLICATION TO HUMAN SERUM PROTEINS Isolation of a novel ras-recision gene that is induced by hydrogen peroxide from a mouse osteoblastic cell line, MC3T3-E1. Bimodal distribution of phosphatidic acid phosphohydrolase in NG108-15 cells. Modulation by the amphiphilic lipids oleic acid and sphingosine Effects of okadaic acid on the activities of two distinct phosphatidate phosphohydrolases in rat hepatocytes. Plasma membrane form of phosphatidate phosphohydrolase: a possible role in signal transduction during liver fibrogenesis.
author name string	wds:Q28593858-8AFC19E9-CA59-46A3-AE28-01FA343041A8 wds:Q28593858-C034CED8-3B34-46B2-A40A-CF5E74FF10A9 wds:Q28593858-C7A68BF5-A73E-44A6-B8F4-16CD40A62A4C
author name string	M Kai H Kanoh S Imai
rdfs:label	Identification and cDNA cloning of 35-kDa phosphatidic acid phosphatase (type 2) bound to plasma membranes. Polymerase chain reaction amplification of mouse H2O2-inducible hic53 clone yielded the cDNA encoding phosphatidic acid phosphatase (en) Identification and cDNA cloning of 35-kDa phosphatidic acid phosphatase (type 2) bound to plasma membranes. Polymerase chain reaction amplification of mouse H2O2-inducible hic53 clone yielded the cDNA encoding phosphatidic acid phosphatase (nl) Identification and cDNA cloning of 35-kDa phosphatidic acid phosphatase (type 2) bound to plasma membranes. Polymerase chain reaction amplification of mouse H2O2-inducible hic53 clone yielded the cDNA encoding phosphatidic acid phosphatase (ast)
skos:prefLabel	Identification and cDNA cloning of 35-kDa phosphatidic acid phosphatase (type 2) bound to plasma membranes. Polymerase chain reaction amplification of mouse H2O2-inducible hic53 clone yielded the cDNA encoding phosphatidic acid phosphatase (en) Identification and cDNA cloning of 35-kDa phosphatidic acid phosphatase (type 2) bound to plasma membranes. Polymerase chain reaction amplification of mouse H2O2-inducible hic53 clone yielded the cDNA encoding phosphatidic acid phosphatase (nl) Identification and cDNA cloning of 35-kDa phosphatidic acid phosphatase (type 2) bound to plasma membranes. Polymerase chain reaction amplification of mouse H2O2-inducible hic53 clone yielded the cDNA encoding phosphatidic acid phosphatase (ast)
name	Identification and cDNA cloning of 35-kDa phosphatidic acid phosphatase (type 2) bound to plasma membranes. Polymerase chain reaction amplification of mouse H2O2-inducible hic53 clone yielded the cDNA encoding phosphatidic acid phosphatase (en) Identification and cDNA cloning of 35-kDa phosphatidic acid phosphatase (type 2) bound to plasma membranes. Polymerase chain reaction amplification of mouse H2O2-inducible hic53 clone yielded the cDNA encoding phosphatidic acid phosphatase (nl) Identification and cDNA cloning of 35-kDa phosphatidic acid phosphatase (type 2) bound to plasma membranes. Polymerase chain reaction amplification of mouse H2O2-inducible hic53 clone yielded the cDNA encoding phosphatidic acid phosphatase (ast)
author	wds:Q28593858-59F910AF-6E95-44A0-8A93-9F157C18411F wds:Q28593858-C42543FC-2007-4522-9834-3F86CD64B54B
author	Ikuo Wada Fumio Sakane
title	wds:Q28593858-4F23E7C8-5776-4465-A753-D969F23DB5D0
title	Identification and cDNA cloning of 35-kDa phosphatidic acid phosphatase (type 2) bound to plasma membranes. Polymerase chain reaction amplification of mouse H2O2-inducible hic53 clone yielded the cDNA encoding phosphatidic acid phosphatase (en)
page(s)	wds:Q28593858-BEDFD456-903E-4B35-AA32-B75160A490CC
page(s)	18931-18938
instance of	wds:Q28593858-B9D9298D-1CDF-40FF-B562-EE407F627C0F
instance of	scholarly article
main subject	wds:Q28593858-49B20DD6-57E9-4307-9814-584566B92636 wds:Q28593858-B0897F6F-FF1D-4BBA-BC79-5E6545501F00
main subject	molecular mass Phospholipid phosphatase 1
PubMed ID	wds:Q28593858-2C9D4D51-7FCD-482E-97B3-B9C7EE5BD51C
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/8702556
PubMed ID	8702556
published in	wds:Q28593858-66B87F2B-6382-4FF6-BEEC-A03318BC27CD
published in	Journal of Biological Chemistry
issue	wds:Q28593858-9648BCD0-3217-416D-9581-7A2D8898C4BD
volume	wds:Q28593858-56E2A729-B700-466B-A8DB-BDF29B4A5DDB
issue	31
volume	271
DOI	wds:Q28593858-BDD8E6FD-5995-4DF4-A417-18F031B3714B
DOI	http://dx.doi.org/10.1074/JBC.271.31.18931
DOI	10.1074/JBC.271.31.18931
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q28593858
is cites work of	Lipid phosphate phosphatase 3 stabilization of beta-catenin induces endothelial cell migration and formation of branching point structures Differential translation and fragile X syndrome Enzymatic analysis of lipid phosphate phosphatases Isolation and characterization of the Saccharomyces cerevisiae DPP1 gene encoding diacylglycerol pyrophosphate phosphatase. An unexpected structural relationship between integral membrane phosphatases and soluble haloperoxidases The Drosophila protein Wunen repels migrating germ cells. Cloning and characterization of two human isozymes of Mg2+-independent phosphatidic acid phosphatase Human type 2 phosphatidic acid phosphohydrolases. Substrate specificity of the type 2a, 2b, and 2c enzymes and cell surface activity of the 2a isoform Phospholipid biosynthesis in the yeast Saccharomyces cerevisiae and interrelationship with other metabolic processes Mammalian Mg2+-independent phosphatidate phosphatase (PAP2) displays diacylglycerol pyrophosphate phosphatase activity Lipid phosphate phosphatase (LPP3) and vascular development The CWH8 gene encodes a dolichyl pyrophosphate phosphatase with a luminally oriented active site in the endoplasmic reticulum of Saccharomyces cerevisiae

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