Succinate dehydrogenase and fumarate reductase from Escherichia coli.
about
Host-pathogen interactions of Actinobacillus pleuropneumoniae with porcine lung and tracheal epithelial cellsChannelling and formation of 'active' formaldehyde in dimethylglycine oxidaseGlucose repression of the Escherichia coli sdhCDAB operon, revisited: regulation by the CRP*cAMP complex.Structure of Escherichia coli Succinate:Quinone Oxidoreductase with an Occupied and Empty Quinone-binding SitePerturbation of the Quinone-binding Site of Complex II Alters the Electronic Properties of the Proximal [3Fe-4S] Iron-Sulfur ClusterStructural and computational analysis of the quinone-binding site of complex II (succinate-ubiquinone oxidoreductase): a mechanism of electron transfer and proton conduction during ubiquinone reductionThe iron-sulfur clusters in Escherichia coli succinate dehydrogenase direct electron flowSuccinate dehydrogenase is the regulator of respiration in Mycobacterium tuberculosisThe bacterial flagellar switch complex is getting more complex.CRISPR-Cas gene-editing reveals RsmA and RsmC act through FlhDC to repress the SdhE flavinylation factor and control motility and prodigiosin production in Serratia.Fumarate reductase activity maintains an energized membrane in anaerobic Mycobacterium tuberculosis.Using gene expression data and network topology to detect substantial pathways, clusters and switches during oxygen deprivation of Escherichia coliBactericidal actions of a silver ion solution on Escherichia coli, studied by energy-filtering transmission electron microscopy and proteomic analysis.Genome evolution and the emergence of fruiting body development in Myxococcus xanthus.A split and rearranged nuclear gene encoding the iron-sulfur subunit of mitochondrial succinate dehydrogenase in Euglenozoa.Phylogenetic detection of horizontal gene transfer during the step-wise genesis of Mycobacterium tuberculosisThe functional microbiome of arthropodsMutation of the heme axial ligand of Escherichia coli succinate-quinone reductase: implications for heme ligation in mitochondrial complex II from yeastThe quinone-binding and catalytic site of complex II.The quaternary structure of the Saccharomyces cerevisiae succinate dehydrogenase. Homology modeling, cofactor docking, and molecular dynamics simulation studies.Mechanism of superoxide and hydrogen peroxide formation by fumarate reductase, succinate dehydrogenase, and aspartate oxidase.Flavogenomics--a genomic and structural view of flavin-dependent proteins.The Genome of Nitrospina gracilis Illuminates the Metabolism and Evolution of the Major Marine Nitrite OxidizerRole of gluconeogenesis and the tricarboxylic acid cycle in the virulence of Salmonella enterica serovar Typhimurium in BALB/c miceEnergetics of Respiration and Oxidative Phosphorylation in Mycobacteria.Kinetic evidence against partitioning of the ubiquinone pool and the catalytic relevance of respiratory-chain supercomplexes.The genome-sequenced variant of Campylobacter jejuni NCTC 11168 and the original clonal clinical isolate differ markedly in colonization, gene expression, and virulence-associated phenotypes.Expression of a metagenome-derived fumarate reductase from marine microorganisms and its characterization.Crystallization of mitochondrial respiratory complex II from chicken heart: a membrane-protein complex diffracting to 2.0 AMnSOD deficiency results in elevated oxidative stress and decreased mitochondrial function but does not lead to muscle atrophy during agingA synthetic system links FeFe-hydrogenases to essential E. coli sulfur metabolismVariation in proton donor/acceptor pathways in succinate:quinone oxidoreductases.A conserved lysine residue controls iron-sulfur cluster redox chemistry in Escherichia coli fumarate reductase.SDH mutations in tumorigenesis and inherited endocrine tumours: lesson from the phaeochromocytoma-paraganglioma syndromesInvestigating the thermostability of succinate: quinone oxidoreductase enzymes by direct electrochemistry at SWNTs-modified electrodes and FTIR spectroscopyRole of intragenic binding of cAMP responsive protein (CRP) in regulation of the succinate dehydrogenase genes Rv0249c-Rv0247c in TB complex mycobacteriaFumarate-Mediated Persistence of Escherichia coli against Antibiotics.Robust bioengineered 3D functional human intestinal epitheliumProtein-mediated assembly of succinate dehydrogenase and its cofactorsA Salmonella enterica serovar typhimurium succinate dehydrogenase/fumarate reductase double mutant is avirulent and immunogenic in BALB/c mice.
P2860
Q24650118-BFFC4CCB-7876-488D-8381-436699688876Q24671918-641FAF93-3A7F-4243-82E5-93DCFD7B5E5EQ24813790-B38AAD74-72CF-4A85-A667-9116E826BB6EQ27657195-3E76D094-8FCC-469F-B433-BBC8EDB9D598Q27666928-6B4FBE43-75A1-4CE6-9CE1-1F9075B27BF7Q28291140-17537D44-E3B4-4DAC-B7E5-CA26DBCDCA8BQ28492481-C9A87AD5-886E-49C6-9E82-EFB1F0DB7F62Q28545101-F56AC8F5-DDB3-40A3-9D2A-CCDE500DFEE8Q30481718-31C30D08-38AD-4F8C-BBD6-3EE2B39E5408Q30816486-2C777E3A-9033-4B20-BA6F-AC6CCB484FCFQ31036537-B395566C-0FDF-44F2-8A02-CBC95E1808A0Q31111982-CA9945BC-7C7A-402F-B9D8-865D563C8954Q33226585-423BEA24-043E-458E-ABBE-FCFFD5B420FDQ33312359-59DF431E-1E81-46C7-82F3-97A98F27D25BQ33405458-9A8E27C9-198B-4BDC-8656-C145842CBC0DQ33491861-4189992C-ACB1-4C85-90CB-8E52868A855BQ33643015-43312F65-16E8-42E4-B9A0-482AF8D7899CQ33926010-B7B78A18-6E75-463D-BB81-7CCE70D75231Q33937869-F568C91B-4934-4F1B-AB83-AAA1CA30353FQ33974538-181720E7-7EBE-4BD3-839A-339D4D5BDCD6Q34146499-C047F26C-7299-4126-8E6B-4B35C1591FB2Q34189187-41282120-2504-4483-97CA-525A9869E431Q34329676-78FB1CCA-84E2-482B-9153-379D1327D7CCQ34334340-31673F12-1CD0-4AEF-AA0B-572BE42ED81FQ34383371-7B6EE134-7EEE-41D0-8331-B58753BCE752Q34480885-A8713918-FBEE-4A61-A69C-C2E2948D67E1Q34674816-EB37D305-1E8A-434D-BC99-5B9D108D496DQ34716343-7F39EE77-9646-44D7-814A-27AAF51F325EQ34977198-B74534B8-DA9A-4E24-ACE2-15D0B7872AEAQ34981154-7C704DAA-DBDC-4059-9894-DA3DD12CD3F9Q35089085-6AECEC2D-D0B6-4772-B2B7-64DAE2380AE3Q35146219-3B9E61A7-9686-4EF8-9B45-5EF65AD33CCFQ35162513-30A6ECD1-A70C-41FE-A6CB-5219C648A1DFQ35185252-E62D5B01-8A6A-4105-BCF4-54F5AC7ECB67Q35206817-B659A1C9-A6A2-46C9-A4F4-1BE100C06ACBQ35770624-FC570244-DDCE-43EC-BCFF-7673BFBA0B75Q35904442-6B004155-F18C-4198-9875-ED614BFEE315Q36064532-E7089F5F-8B90-4227-93AE-A8897413BDBBQ36300096-92577638-AA68-4012-AAC5-F7A8C4057203Q36483591-B13A8A96-EFC2-420B-8363-70794DF3CA28
P2860
Succinate dehydrogenase and fumarate reductase from Escherichia coli.
description
2002 nî lūn-bûn
@nan
2002 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年学术文章
@wuu
2002年学术文章
@zh-cn
2002年学术文章
@zh-hans
2002年学术文章
@zh-my
2002年学术文章
@zh-sg
2002年學術文章
@yue
name
Succinate dehydrogenase and fumarate reductase from Escherichia coli.
@ast
Succinate dehydrogenase and fumarate reductase from Escherichia coli.
@en
type
label
Succinate dehydrogenase and fumarate reductase from Escherichia coli.
@ast
Succinate dehydrogenase and fumarate reductase from Escherichia coli.
@en
prefLabel
Succinate dehydrogenase and fumarate reductase from Escherichia coli.
@ast
Succinate dehydrogenase and fumarate reductase from Escherichia coli.
@en
P2093
P1476
Succinate dehydrogenase and fumarate reductase from Escherichia coli.
@en
P2093
Elena Maklashina
Gary Cecchini
Imke Schröder
Robert P Gunsalus
P304
P356
10.1016/S0005-2728(01)00238-9
P407
P577
2002-01-01T00:00:00Z