About: Alkyl-dihydroxyacetone phosphate synthase and dihydroxyacetone phosphate acyltransferase form a protein complex in peroxisomes

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description	artículu científicu espublizáu en 1999 (ast) vědecký článek publikovaný v roce 1999 (cs) مقالة علمية (نشرت في أبريل 1999) (ar) 1999 թվականի ապրիլին հրատարակված գիտական հոդված (hy) vedecký článok (publikovaný 1999/04/01) (sk) 1999 թուականի Ապրիլին հրատարակուած գիտական յօդուած (hyw) наукова стаття, опублікована у квітні 1999 (uk) scientific journal article (en) im April 1999 veröffentlichter wissenschaftlicher Artikel (de) wetenschappelijk artikel (gepubliceerd op 1999/04/01) (nl)
publication date	wds:Q28609399-CCD0AEF4-F1CC-4311-A1A3-C498FF1B2626
publication date	1999-04-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q28609399-AC03DF64-839D-40F0-B2BD-64A94D46A6E3
language of work or name	English
cites work	wds:Q28609399-0AFDF9E3-8BB5-41A1-ABCD-6015A5DF1556 wds:Q28609399-16743892-9162-4333-80CC-A1F77B3F3D04 wds:Q28609399-1C79C535-DA51-4AC3-AD56-74BB470E8C91 wds:Q28609399-25770D0E-F23F-421F-A262-4056F39BE6D5 wds:Q28609399-2B822A78-700E-4B31-A4EA-7FECEA8A8EE9 wds:Q28609399-39347902-BB9A-4ACB-AE07-3CC4BC67CB25 wds:Q28609399-47075948-6B4F-4D76-B7C8-9756C0A07105 wds:Q28609399-48A67AE0-B45E-4393-AE99-D712E8011CC6 wds:Q28609399-5FC6250D-22CC-40C8-BB85-B5F8FDC0C5B2 wds:Q28609399-7B5B60E6-9E5A-4BCD-8CE1-532567CCAD01 wds:Q28609399-8A8397A3-0C40-40F0-931E-6F9FEC97722F wds:Q28609399-9C86749E-8C15-4C30-BB19-7630D18055AA wds:Q28609399-A1141CE7-86C6-4021-9C08-3F45BD2C4397 wds:Q28609399-A653A757-5BC0-4C0C-99CE-8CC29BB3F365 wds:Q28609399-B54E05F1-9D65-4012-B558-D8A565E83C9C wds:Q28609399-CB9AE94B-A0D3-4AB5-87F5-2A830051794B wds:Q28609399-D9563D65-AD3A-4774-912A-743D6BEE9B28 wds:Q28609399-E175D777-2837-4846-B336-45BAE6848284 wds:Q28609399-F74C6594-7EBB-4907-97E2-A447B6204FFD wds:Q28609399-F9D8D955-1D98-4C5D-B1DB-C02B58253BE9 wds:Q28609399-FB01A7C2-CB02-4AF6-86A5-64F237B9BFC1 wds:Q28609399-FC6B9457-3673-4B11-AAF9-80AAE04D1561
cites work	Human PEX7 encodes the peroxisomal PTS2 receptor and is responsible for rhizomelic chondrodysplasia punctata Rhizomelic chondrodysplasia punctata is a peroxisomal protein targeting disease caused by a non-functional PTS2 receptor Rhizomelic chondrodysplasia punctata is caused by deficiency of human PEX7, a homologue of the yeast PTS2 receptor Biochemistry of peroxisomes Immunological localization and tissue distribution of alkyldihydroxyacetonephosphate synthase and deficiency of the enzyme in peroxisomal disorders The native molecular size of alkyl-dihydroxyacetonephosphate synthase and dihydroxyacetonephosphate acyltransferase. Differential protein import deficiencies in human peroxisome assembly disorders Severe plasmalogen deficiency in tissues of infants without peroxisomes (Zellweger syndrome). Acyl-CoA:dihydroxyacetonephosphate acyltransferase: cloning of the human cDNA and resolution of the molecular basis in rhizomelic chondrodysplasia punctata type 2 Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4 Identification of PAHX, a Refsum disease gene Refsum disease is caused by mutations in the phytanoyl-CoA hydroxylase gene Biochemical abnormalities in rhizomelic chondrodysplasia punctata A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Alkyl-dihydroxyacetonephosphate synthase. Fate in peroxisome biogenesis disorders and identification of the point mutation underlying a single enzyme deficiency Ether lipid biosynthesis: isolation and molecular characterization of human dihydroxyacetonephosphate acyltransferase Polymerase chain reaction-based cloning of alkyl-dihydroxyacetonephosphate synthase complementary DNA from guinea pig liver Nucleotide sequence of human alkyl-dihydroxyacetonephosphate synthase cDNA reveals the presence of a peroxisomal targeting signal 2. Peroxisomal fatty acid beta-oxidation in relation to the accumulation of very long chain fatty acids in cultured skin fibroblasts from patients with Zellweger syndrome and other peroxisomal disorders Acyl dihydroxyacetone phosphate: Precursor of alkyl ethers Differential deficiency of mevalonate kinase and phosphomevalonate kinase in patients with distinct defects in peroxisome biogenesis: evidence for a major role of peroxisomes in cholesterol biosynthesis. Rat liver dihydroxyacetone-phosphate acyltransferase: enzyme characteristics and localization studies.
author name string	wds:Q28609399-5EB0C3AA-5C24-4016-BB66-25357FE1A5AC wds:Q28609399-CE741E33-3B4A-4ECB-95A1-465F249405AB wds:Q28609399-FBDF9070-2B76-46B1-B4E6-9F0C977EAF58 wds:Q28609399-FC906FD3-FD11-4CDC-8F35-18D724F45D38
author name string	R. J. Wanders W. W. Just H. Van Den Bosch J. Biermann
rdfs:label	Alkyl-dihydroxyacetone phosphate synthase and dihydroxyacetone phosphate acyltransferase form a protein complex in peroxisomes (en) Alkyl-dihydroxyacetone phosphate synthase and dihydroxyacetone phosphate acyltransferase form a protein complex in peroxisomes (nl) Alkyl-dihydroxyacetone phosphate synthase and dihydroxyacetone phosphate acyltransferase form a protein complex in peroxisomes (ast)
skos:prefLabel	Alkyl-dihydroxyacetone phosphate synthase and dihydroxyacetone phosphate acyltransferase form a protein complex in peroxisomes (en) Alkyl-dihydroxyacetone phosphate synthase and dihydroxyacetone phosphate acyltransferase form a protein complex in peroxisomes (nl) Alkyl-dihydroxyacetone phosphate synthase and dihydroxyacetone phosphate acyltransferase form a protein complex in peroxisomes (ast)
name	Alkyl-dihydroxyacetone phosphate synthase and dihydroxyacetone phosphate acyltransferase form a protein complex in peroxisomes (en) Alkyl-dihydroxyacetone phosphate synthase and dihydroxyacetone phosphate acyltransferase form a protein complex in peroxisomes (nl) Alkyl-dihydroxyacetone phosphate synthase and dihydroxyacetone phosphate acyltransferase form a protein complex in peroxisomes (ast)
title	wds:Q28609399-584E689B-FDCC-46DD-B8AB-DAC27489BD74
title	Alkyl-dihydroxyacetone phosphate synthase and dihydroxyacetone phosphate acyltransferase form a protein complex in peroxisomes (en)
page(s)	wds:Q28609399-9D5C927F-272F-41E8-87DB-DDC0BD7372FC
page(s)	492–499
instance of	wds:Q28609399-D42DC44B-1D1E-4F3B-9FEA-30DE850DA04A
instance of	scholarly article
PubMed ID	wds:Q28609399-AC094E75-C333-4A4A-9ADA-FA086ED3A815
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/10215861
PubMed ID	10215861
published in	wds:Q28609399-3C47270C-145C-41C6-BCDD-EEFACB15EF3E
published in	FEBS Journal
issue	wds:Q28609399-057358F5-6814-4FD1-8949-EBE866414319
volume	wds:Q28609399-F5210534-E5E5-4C23-8807-02EC3E9D04E2
issue	2
volume	261
DOI	wds:Q28609399-448FB27D-C7C5-4B78-8C6F-A599EF07529A
DOI	http://dx.doi.org/10.1046/J.1432-1327.1999.00295.X
DOI	10.1046/J.1432-1327.1999.00295.X
ResearchGate publication ID	wds:Q28609399-D81EC0B4-902C-4363-A3A7-7A7E0E1A4F2C
ResearchGate publication ID	13082253
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q28609399
is cites work of	Leishmania major expresses a single dihydroxyacetone phosphate acyltransferase localized in the glycosome, important for rapid growth and survival at high cell density and essential for virulence. Plasmalogens: biosynthesis and functions Induction of the peroxisomal glycerolipid-synthesizing enzymes during differentiation of 3T3-L1 adipocytes. Role in triacylglycerol synthesis

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