The state of cluster SH and S2- of aconitase during cluster interconversions and removal. A convenient preparation of apoenzyme.
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Kinetics and product analysis of the reaction catalysed by recombinant homoaconitase from Thermus thermophilusStructure of activated aconitase: formation of the [4Fe-4S] cluster in the crystalThe mechanism of aconitase: 1.8 A resolution crystal structure of the S642a:citrate complexA novel eukaryotic factor for cytosolic Fe-S cluster assemblyX-ray snapshots of possible intermediates in the time course of synthesis and degradation of protein-bound Fe4S4 clustersDre2, a conserved eukaryotic Fe/S cluster protein, functions in cytosolic Fe/S protein biogenesis.The acnD genes of Shewenella oneidensis and Vibrio cholerae encode a new Fe/S-dependent 2-methylcitrate dehydratase enzyme that requires prpF function in vivoCellular regulation of the iron-responsive element binding protein: disassembly of the cubane iron-sulfur cluster results in high-affinity RNA bindingInterplay between oxygen and Fe-S cluster biogenesis: insights from the Suf pathwayThe diabetes drug target MitoNEET governs a novel trafficking pathway to rebuild an Fe-S cluster into cytosolic aconitase/iron regulatory protein 1Mössbauer study of the inactive Fe3S4 and Fe3Se4 and the active Fe4Se4 forms of beef heart aconitaseIron regulatory factor expressed from recombinant baculovirus: conversion between the RNA-binding apoprotein and Fe-S cluster containing aconitaseNfu facilitates the maturation of iron-sulfur proteins and participates in virulence in Staphylococcus aureus.Reversible cycling between cysteine persulfide-ligated [2Fe-2S] and cysteine-ligated [4Fe-4S] clusters in the FNR regulatory protein.Separate FeS scaffold and carrier functions for SufB₂C₂ and SufA during in vitro maturation of [2Fe2S] FdxBacillithiol has a role in Fe-S cluster biogenesis in Staphylococcus aureus.Protection from superoxide damage associated with an increased level of the YggX protein in Salmonella enterica.Monothiol glutaredoxins and A-type proteins: partners in Fe-S cluster trafficking.The iron-sulfur cluster assembly machineries in plants: current knowledge and open questions.Reciprocal control of RNA-binding and aconitase activity in the regulation of the iron-responsive element binding protein: role of the iron-sulfur cluster.Monothiol glutaredoxins can bind linear [Fe3S4]+ and [Fe4S4]2+ clusters in addition to [Fe2S2]2+ clusters: spectroscopic characterization and functional implications.Purification and characterization of cytosolic aconitase from beef liver and its relationship to the iron-responsive element binding proteinA [3Fe-4S] cluster is required for tRNA thiolation in archaea and eukaryotes.Mutational analysis of the [4Fe-4S]-cluster converting iron regulatory factor from its RNA-binding form to cytoplasmic aconitase.A proposed role for the Azotobacter vinelandii NfuA protein as an intermediate iron-sulfur cluster carrier.Haem precursor delta-aminolaevulinic acid induces activation of the cytosolic iron regulatory protein 1.Cancer-Related NEET Proteins Transfer 2Fe-2S Clusters to Anamorsin, a Protein Required for Cytosolic Iron-Sulfur Cluster Biogenesis.Magnetic circular dichroism study of the selenium-substituted form (Fe3Se4) of bovine heart aconitaseThe SufBCD Fe-S scaffold complex interacts with SufA for Fe-S cluster transferExpression in Escherichia coli and characterization of a reconstituted recombinant 7Fe ferredoxin from Desulfovibrio africanus.Biochemical and spectroscopic characterization of Escherichia coli aconitases (AcnA and AcnB).The PrpF protein of Shewanella oneidensis MR-1 catalyzes the isomerization of 2-methyl-cis-aconitate during the catabolism of propionate via the AcnD-dependent 2-methylcitric acid cycle.
P2860
Q24548588-FA18BF25-CAD0-43DC-85AD-CA31E6271A59Q24614444-0401AA01-1E5C-4977-945C-B4A97401758CQ24672826-AEBAA9EB-327C-4FF5-BE5F-A077D735EF21Q24685689-85A84FFD-92FA-4D10-8E0B-388E9A29BD3BQ27677436-E1CF166F-3800-4784-BB98-662AE0145BC0Q27938813-0040C116-6EE7-4ED3-A3B9-756BE0F1A955Q28487962-E8C627F8-18E0-4E38-8327-1C056020B3D3Q28910479-F126807F-0C86-4650-BBF2-5CEF53C2C003Q34230475-C4890DF3-AD65-40D8-9D14-12157ED51CA5Q34317253-4AB63AD9-1418-480C-83F3-607F2B95A6D7Q34325468-FE3DCCD1-5212-4175-8E93-C6BB0EEEC6DDQ34977298-BBE6F585-6560-48F5-9DF1-72C404DFAF70Q35596266-850949D2-D3FE-4CD6-875A-822420AB6F04Q36300810-A75BF455-F2BD-41A1-B5E6-62259E97F504Q36354561-56D0E2EB-DA90-4E54-87B4-AB4ABDCB6990Q36441404-3816FC38-E7AD-4414-9933-0C8B79A275B8Q36536735-6C4D8CE3-E410-4A9D-93F5-F2E57835E65CQ36627228-81273BA2-0F14-4E83-A875-F158B56FDAC3Q37040353-49650009-CB6B-4E1E-A4C6-C617B8B12C5BQ37153706-D629A2D7-888F-479B-8F0D-1C0F07CECAABQ37331542-157C34E5-EB19-40DD-A59A-A10D77F793D4Q37336988-B1322A8B-F718-464A-B8DA-48D7B9E1BE27Q37417854-FB066811-AA03-4A9D-9B8E-3D1AF1E03F1FQ37628036-3440C67C-5EA0-41B3-BF39-B330D7A0D7F0Q38291272-C75FA14A-1000-40F3-8F47-C13EBEC63735Q41067962-D42EA846-C882-4569-8FAD-29092AB4C31DQ41105227-A3830941-F004-4A91-8C1A-9817F798BAC8Q42118063-4B409000-6DA0-4D15-A7FF-62CBFA0C7005Q42671806-863EFC68-59AE-4E27-AB23-917A7F5D4A05Q42981074-3EE07F40-A49F-47D9-B97B-1909A0640CD5Q42995327-D3418E78-4A48-4AF2-9BB6-9C3D707F9FABQ47148388-7CC8CA8F-2D56-4D93-A0C2-5910A4D144B5
P2860
The state of cluster SH and S2- of aconitase during cluster interconversions and removal. A convenient preparation of apoenzyme.
description
1988 nî lūn-bûn
@nan
1988 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
1988 թվականի հունիսին հրատարակված գիտական հոդված
@hy
1988年の論文
@ja
1988年論文
@yue
1988年論文
@zh-hant
1988年論文
@zh-hk
1988年論文
@zh-mo
1988年論文
@zh-tw
1988年论文
@wuu
name
The state of cluster SH and S2 ...... ient preparation of apoenzyme.
@ast
The state of cluster SH and S2 ...... ient preparation of apoenzyme.
@en
type
label
The state of cluster SH and S2 ...... ient preparation of apoenzyme.
@ast
The state of cluster SH and S2 ...... ient preparation of apoenzyme.
@en
prefLabel
The state of cluster SH and S2 ...... ient preparation of apoenzyme.
@ast
The state of cluster SH and S2 ...... ient preparation of apoenzyme.
@en
P1476
The state of cluster SH and S2 ...... nient preparation of apoenzyme
@en
P2093
M C Kennedy
P304
P407
P577
1988-06-01T00:00:00Z