About: Site-directed mutagenesis of residues in a conserved region of bovine aspartyl (asparaginyl) beta-hydroxylase: evidence that histidine 675 has a role in binding Fe2+

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About: Site-directed mutagenesis of residues in a conserved region of bovine aspartyl (asparaginyl) beta-hydroxylase: evidence that histidine 675 has a role in binding Fe2+ Goto Sponge NotDistinct Permalink

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scientific article published on 01 April 1996

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована у квітні 1996 (uk) article scientifique publié en 1996 (fr) artículu científicu espublizáu n'abril de 1996 (ast) scientific article published on 01 April 1996 (en) im April 1996 veröffentlicher wissenschaftlicher Artikel (de)
publication date	wds:Q71165576-2C3F1A3B-403B-447E-BEDE-A996A6B30568
publication date	1996-04-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q71165576-7ED23005-B4A1-4CAA-8E97-E4503ED08D38
language of work or name	English
author name string	wds:Q71165576-48C74290-CF13-40BA-9045-BAD48E80EBFB wds:Q71165576-72672345-5F6B-4975-B48E-69D1B72341FA wds:Q71165576-8CA1C9A1-3278-4559-9C5C-B139F4E1E36D wds:Q71165576-9FE1AB63-9A26-4CDB-B92A-3BBC4CF69C74 wds:Q71165576-A135AC64-A82B-4A8B-84FF-6562B5133C0B wds:Q71165576-DB0693BB-35DC-4EE2-B4BF-40B929188C48 wds:Q71165576-DB5EECE6-B1C0-42F2-8364-9174233832FC
author name string	Fu J Friedman PA McGinnis K Stern AM Garsky V VanDusen WJ Ku GM
rdfs:label	Site-directed mutagenesis of residues in a conserved region of bovine aspartyl (nl) Site-directed mutagenesis of residues in a conserved region of bovine aspartyl (asparaginyl) beta-hydroxylase: evidence that histidine 675 has a role in binding Fe2+ (en)
skos:prefLabel	Site-directed mutagenesis of residues in a conserved region of bovine aspartyl (nl) Site-directed mutagenesis of residues in a conserved region of bovine aspartyl (asparaginyl) beta-hydroxylase: evidence that histidine 675 has a role in binding Fe2+ (en)
name	Site-directed mutagenesis of residues in a conserved region of bovine aspartyl (nl) Site-directed mutagenesis of residues in a conserved region of bovine aspartyl (asparaginyl) beta-hydroxylase: evidence that histidine 675 has a role in binding Fe2+ (en)
title	wds:Q71165576-524AEBCB-0C77-4AD1-9A3C-57F6673CCFB1
title	Site-directed mutagenesis of residues in a conserved region of bovine aspartyl (asparaginyl) beta-hydroxylase: evidence that histidine 675 has a role in binding Fe2+ (en)
page(s)	wds:Q71165576-B111A8CE-E1CA-4A44-B321-3119275D4882
page(s)	3957-3962
instance of	wds:Q71165576-4AC9D7AB-89D9-4EAC-8C7F-9CC687684BF5
instance of	scholarly article
PubMed ID	wds:Q71165576-80E72428-C396-40B9-B591-B8D6735AD81B
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/8672427
PubMed ID	8672427
published in	wds:Q71165576-91794322-4010-4F9B-AF3B-D2612BEA4DEE
published in	Biochemistry
issue	wds:Q71165576-62BF8572-35DD-4FB2-93EC-484D8C9BB651
volume	wds:Q71165576-B1CE9685-9305-44E3-9F4B-70A459DB9770
issue	13
volume	35
DOI	wds:Q71165576-2D586441-F508-4553-A1E7-DD6BFA616E5D
DOI	http://dx.doi.org/10.1021/BI951520N
DOI	10.1021/BI951520N
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q71165576
is cites work of	Cloning and characterization of a low molecular weight prolyl 4-hydroxylase from Arabidopsis thaliana. Effective hydroxylation of proline-rich, collagen-like, and hypoxia-inducible transcription factor alpha-like peptides Characterization of the iron- and 2-oxoglutarate-binding sites of human prolyl 4-hydroxylase Chemical modification and site-directed mutagenesis of conserved HXXH and PP-loop motif arginines and histidines in the murine bifunctional ATP sulfurylase/adenosine 5'-phosphosulfate kinase Deciphering tissue-induced Klebsiella pneumoniae lipid A structure. An inner membrane dioxygenase that generates the 2-hydroxymyristate moiety of Salmonella lipid A. Site-directed Mutagenesis of 2,4-Dichlorophenoxyacetic Acid/α-Ketoglutarate Dioxygenase Aspartate β-Hydroxylase expression promotes a malignant pancreatic cellular phenotype Antisense oligodeoxynucleotides directed against aspartyl (asparaginyl) β-hydroxylase suppress migration of cholangiocarcinoma cells Intrinsic tryptophan fluorescence as a probe of metal and alpha-ketoglutarate binding to TfdA, a mononuclear non-heme iron dioxygenase Potential Role of Phosphorylation as a Regulator of Aspartyl-(asparaginyl)-β-hydroxylase: Relevance to Infiltrative Spread of Human Hepatocellular Carcinoma Phosphorylation Modulates Aspartyl-(Asparaginyl)-β Hydroxylase Protein Expression, Catalytic Activity and Migration in Human Immature Neuronal Cerebellar Cells. Recent advances in research on aspartate β-hydroxylase (ASPH) in pancreatic cancer: A brief update Stringency of the 2-His-1-Asp active-site motif in prolyl 4-hydroxylase Hydroxylase Activity of ASPH Promotes Hepatocellular Carcinoma Metastasis Through Epithelial-to-Mesenchymal Transition Pathway. Kinetic parameters of human aspartate/asparagine-β-hydroxylase suggest that it has a possible function in oxygen sensing The five cysteine residues located in the active site region of bovine aspartyl (asparaginyl) beta-hydroxylase are not essential for catalysis Aspartate/asparagine-β-hydroxylase: a high-throughput mass spectrometric assay for discovery of small molecule inhibitors Co-operative intermolecular kinetics of 2-oxoglutarate dependent dioxygenases may be essential for system-level regulation of plant cell physiology. Optimized Expression and Purification of Humbug in Pichia pastoris and Its Monoclonal Antibody Preparation
is cites work of	wds:Q42051705-F90116EF-E1F4-4275-90EB-F4CD2DB02818 wds:Q44284961-084CB952-FC8E-4031-8C25-310E68FD69D1 wds:Q57831109-3C585715-D43C-4C8E-95B5-0E254BAB6582 wds:Q89926103-3D53C90C-056D-4832-857B-4D4E7224E1D1 wds:Q35176052-2535EE8B-C107-46BC-986A-4AC2259D7B46 wds:Q28201030-3B5BEAD9-7CC8-4B1B-A2DC-30F522ED5F3B wds:Q53092252-048A960D-0C69-41B0-9F6D-1A8CBC304C2C wds:Q77333927-36DFE59F-F017-4AE5-BBEF-206C487AC29E wds:Q95840325-9ABC970D-FF0A-4EBC-AD34-37F099495FCA wds:Q41120528-7F3AF71C-F05B-44F5-B4B2-19CE93528AFC wds:Q28471783-32C207EE-388F-49DD-ACFD-3C349C6B0D98 wds:Q37259730-8F365507-4D7C-4514-8CA5-C948C2519436 wds:Q40667135-E7991336-9910-4100-98B5-874688A520FA wds:Q55378664-A7D94EEE-24AC-44B2-A764-5F2FC7D95448 wds:Q73041125-D312BE80-B15E-40DF-9182-0046E6C06F75 wds:Q36306056-9622E018-3044-4ADE-BFED-9988098B703F wds:Q36170624-C1349C34-2938-436F-8078-6EE2F3FCB171 wds:Q36495723-2CB6F4A8-6C59-49CA-B53C-C23EB794D2A0 wds:Q59329484-9A92B5DD-8435-4509-9664-6DF85E774FA1

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