About: Further characterization of the peroxisomal 3-hydroxyacyl-CoA dehydrogenases from rat liver. Relationship between the different dehydrogenases and evidence that fatty acids and the C27 bile acids di- and tri-hydroxycoprostanic acids are metabolized

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About: Further characterization of the peroxisomal 3-hydroxyacyl-CoA dehydrogenases from rat liver. Relationship between the different dehydrogenases and evidence that fatty acids and the C27 bile acids di- and tri-hydroxycoprostanic acids are metabolized Goto Sponge NotDistinct Permalink

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scientific article published on 01 September 1996

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована у вересні 1996 (uk) article scientifique publié en 1996 (fr) artículu científicu espublizáu en setiembre de 1996 (ast) scientific article published on 01 September 1996 (en)
publication date	wds:Q71652929-D371390C-81C9-428C-9E9F-B6E07FF3F524
publication date	1996-09-01 00:00:00Z (xsd:dateTime)
author name string	wds:Q71652929-1F9CB6DC-4539-4672-AC85-984EA1A1EA0D wds:Q71652929-360DA3D1-A7F2-4003-B679-5F79F2CE23B5 wds:Q71652929-52F28699-4622-436B-A1E7-C134402A608A wds:Q71652929-6E1412A6-732B-4849-BCB4-1442F2D32FF7 wds:Q71652929-7775F75A-27BE-44C1-B353-C9C136B72A51 wds:Q71652929-AC7D9A24-073D-4239-B564-E2BE126B8BD4 wds:Q71652929-D53593A3-3C9C-4ABE-AAA5-87B996A0666E wds:Q71652929-F428D18E-B19D-41E3-AC4A-266BBA39586B
author name string	J Vandekerckhove G P Mannaerts P P Van Veldhoven D Novikov E Baumgart M Goethals J C Vanhooren M Dieuaide-Noubhani
rdfs:label	Further characterization of the peroxisomal 3-hydroxyacyl-CoA dehydrogenases from rat liver. Relationship between the different dehydrogenases and evidence that fatty acids and the C27 bile acids di- and tri-hydroxycoprostanic acids are metabolized (en) Further characterization of the peroxisomal 3-hydroxyacyl-CoA dehydrogenases from rat liver. Relationship between the different dehydrogenases and evidence that fatty acids and the C27 bile acids di- and tri-hydroxycoprostanic acids are metabolized (nl)
skos:prefLabel	Further characterization of the peroxisomal 3-hydroxyacyl-CoA dehydrogenases from rat liver. Relationship between the different dehydrogenases and evidence that fatty acids and the C27 bile acids di- and tri-hydroxycoprostanic acids are metabolized (en) Further characterization of the peroxisomal 3-hydroxyacyl-CoA dehydrogenases from rat liver. Relationship between the different dehydrogenases and evidence that fatty acids and the C27 bile acids di- and tri-hydroxycoprostanic acids are metabolized (nl)
name	Further characterization of the peroxisomal 3-hydroxyacyl-CoA dehydrogenases from rat liver. Relationship between the different dehydrogenases and evidence that fatty acids and the C27 bile acids di- and tri-hydroxycoprostanic acids are metabolized (en) Further characterization of the peroxisomal 3-hydroxyacyl-CoA dehydrogenases from rat liver. Relationship between the different dehydrogenases and evidence that fatty acids and the C27 bile acids di- and tri-hydroxycoprostanic acids are metabolized (nl)
author	wds:Q71652929-1EC8E900-FD23-41F4-8100-63E2CC5D81C9
author	Marc Fransen
title	wds:Q71652929-908F5A1E-31C5-4AB1-8627-9384A2E3BB37
title	Further characterization of the peroxisomal 3-hydroxyacyl-CoA dehydrogenases from rat liver. Relationship between the different dehydrogenases and evidence that fatty acids and the C27 bile acids di- and tri-hydroxycoprostanic acids are metabolized by separate multifunctional proteins (en)
page(s)	wds:Q71652929-0C0E3514-21EF-423E-BA3F-A8EB3274153A
page(s)	660-666
instance of	wds:Q71652929-7F4A3DA1-721C-4BD4-950D-2246E48371E0
instance of	scholarly article
PubMed ID	wds:Q71652929-743DB669-29B6-4822-8876-E4911AEF3B3F
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/8856068
PubMed ID	8856068
published in	wds:Q71652929-CFDBBEE3-349D-4930-918E-F65DB454B288
published in	FEBS Journal
issue	wds:Q71652929-84D10149-ACF4-4D4C-BC08-3C5137C293B0
volume	wds:Q71652929-FDAF07BA-2F35-4053-AB62-49FC08BFF068
issue	3
volume	240
DOI	wds:Q71652929-09FF41DB-B033-44B8-A72A-3112342B714F
DOI	http://dx.doi.org/10.1111/J.1432-1033.1996.0660H.X
DOI	10.1111/J.1432-1033.1996.0660H.X
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q71652929
is cites work of	Characterization of rat 17 beta-hydroxysteroid dehydrogenase type 1 gene and mRNA transcripts. Participation of two members of the very long-chain acyl-CoA synthetase family in bile acid synthesis and recycling 17Beta-hydroxysteroid dehydrogenases in normal human mammary epithelial cells and breast tissue. Peroxisomal L-bifunctional enzyme (Ehhadh) is essential for the production of medium-chain dicarboxylic acids Lipid metabolism in peroxisomes in relation to human disease Peroxisomal beta-oxidation enzymes Enoyl-CoA hydratase deficiency: identification of a new type of D-bifunctional protein deficiency Peroxisomal D-hydroxyacyl-CoA dehydrogenase deficiency: resolution of the enzyme defect and its molecular basis in bifunctional protein deficiency Crystal structure of 2-enoyl-CoA hydratase 2 from human peroxisomal multifunctional enzyme type 2 Recombinant 2-enoyl-CoA hydratase derived from rat peroxisomal multifunctional enzyme 2: role of the hydratase reaction in bile acid synthesis Binary structure of the two-domain (3R)-hydroxyacyl-CoA dehydrogenase from rat peroxisomal multifunctional enzyme type 2 at 2.38 A resolution The biochemistry of peroxisomal beta-oxidation in the yeast Saccharomyces cerevisiae Molecular basis of d-bifunctional protein deficiency Evidence that multifunctional protein 2, and not multifunctional protein 1, is involved in the peroxisomal beta-oxidation of pristanic acid Human peroxisomal multifunctional enzyme type 2. Site-directed mutagenesis studies show the importance of two protic residues for 2-enoyl-CoA hydratase 2 activity Prenatal and postnatal development of peroxisomal lipid-metabolizing pathways in the mouse Specific combination of compound heterozygous mutations in 17β-hydroxysteroid dehydrogenase type 4 (HSD17B4) defines a new subtype of D-bifunctional protein deficiency beta-oxidation - strategies for the metabolism of a wide variety of acyl-CoA esters Peroxisomal bifunctional protein deficiency revisited: resolution of its true enzymatic and molecular basis Peroxisome targeting of porcine 17beta-hydroxysteroid dehydrogenase type IV/D-specific multifunctional protein 2 is mediated by its C-terminal tripeptide AKI. Characterization of the HSD17B4 gene: D-specific multifunctional protein 2/17beta-hydroxysteroid dehydrogenase IV Human brain short chain L-3-hydroxyacyl coenzyme A dehydrogenase is a single-domain multifunctional enzyme. Characterization of a novel 17beta-hydroxysteroid dehydrogenase Peroxisomal beta-oxidation of polyunsaturated fatty acids in Saccharomyces cerevisiae: isocitrate dehydrogenase provides NADPH for reduction of double bonds at even positions Yeast peroxisomal multifunctional enzyme: (3R)-hydroxyacyl-CoA dehydrogenase domains A and B are required for optimal growth on oleic acid The human peroxisomal multifunctional protein involved in bile acid synthesis: activity measurement, deficiency in Zellweger syndrome and chromosome mapping Evolution of 17beta-HSD type 4, a multifunctional protein of beta-oxidation Differential regulation by a peroxisome proliferator of the different multifunctional proteins in guinea pig: cDNA cloning of the guinea pig D-specific multifunctional protein 2. Sterol carrier protein-2 Cloning of mouse 17beta-hydroxysteroid dehydrogenase type 2, and analysing expression of the mRNAs for types 1, 2, 3, 4 and 5 in mouse embryos and adult tissues The role of alpha-methylacyl-CoA racemase in bile acid synthesis Human metabolism of phytanic acid and pristanic acid Mechanisms of estradiol inactivation in primate endometrium Peroxisomal disorders: clinical, biochemical, and molecular aspects Pristanic acid beta-oxidation in peroxisomal disorders: studies in cultured human fibroblasts Cell biology of peroxisomes and their characteristics in aquatic organisms Conjugation reactions catalyzed by bifunctional proteins related to beta-oxidation in bile acid biosynthesis Identification and characterization of the 2-enoyl-CoA hydratases involved in peroxisomal beta-oxidation in rat liver Identification of a substrate-binding site in a peroxisomal beta-oxidation enzyme by photoaffinity labeling with a novel palmitoyl derivative The beta-3 adrenergic agonist (CL-316,243) restores the expression of down-regulated fatty acid oxidation genes in type 2 diabetic mice
is cites work of	wds:Q24337779-B9DAA665-D21B-403F-9DEE-A58C8144C0AE wds:Q24530588-B42FA1E4-8DA6-4EC3-9FE5-6AE1D274D054 wds:Q31875444-176F5A96-B296-4626-A493-5B6D7731F74C wds:Q33889081-3435F58A-3DD5-4BE0-A647-E399BF286251 wds:Q41033062-BE35AA61-BD38-415D-B08E-EC4569D6D2B3 wds:Q24295748-B8B30892-5904-48CB-B439-2B8C3ABDA890 wds:Q28144146-71CA560F-FA6C-44D4-9C40-C33C53D01042 wds:Q42660411-D3BBE2BE-DFB6-492D-8F61-38693E2A3F6A wds:Q77596072-FB7325BD-5D39-4CC5-9E23-082C66C02FCB wds:Q73441782-97FCB225-19A8-4C4D-88DE-03BE7CE531D4

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