Structure and function of DsbA, a key bacterial oxidative folding catalyst.
about
Targeting Bacterial Dsb Proteins for the Development of Anti-Virulence AgentsDisulfide bond formation in the bacterial periplasm: major achievements and challenges aheadCytochrome c biogenesis System I: an intricate process catalyzed by a maturase supercomplex?Structure analysis of the extracellular domain reveals disulfide bond forming-protein properties of Mycobacterium tuberculosis Rv2969cDisarming Burkholderia pseudomallei : Structural and Functional Characterization of a Disulfide Oxidoreductase (DsbA) Required for Virulence In VivoComparative Sequence, Structure and Redox Analyses of Klebsiella pneumoniae DsbA Show That Anti-Virulence Target DsbA Enzymes Fall into Distinct ClassesThe Multidrug Resistance IncA/C Transferable Plasmid Encodes a Novel Domain-swapped Dimeric Protein-disulfide IsomeraseThe 1.2 Å resolution crystal structure of TcpG, the Vibrio cholerae DsbA disulfide-forming protein required for pilus and cholera-toxin productionCrystal Structure of the Dithiol Oxidase DsbA Enzyme from Proteus Mirabilis Bound Non-covalently to an Active Site Peptide LigandStructure of the Acinetobacter baumannii Dithiol Oxidase DsbA Bound to Elongation Factor EF-Tu Reveals a Novel Protein Interaction SiteStructural and Biochemical Characterization of Chlamydia trachomatis DsbA Reveals a Cysteine-Rich and Weakly Oxidising OxidoreductaseVirtual Screening of Peptide and Peptidomimetic Fragments Targeted to Inhibit Bacterial Dithiol Oxidase DsbALegionella pneumophila utilizes a single-player disulfide-bond oxidoreductase system to manage disulfide bond formation and isomerizationDiversity of the Epsilonproteobacteria Dsb (disulfide bond) systems.Disulfide bond oxidoreductase DsbA2 of Legionella pneumophila exhibits protein disulfide isomerase activityBacterial thiol oxidoreductases - from basic research to new antibacterial strategiesStructure of a DsbF homologue from Corynebacterium diphtheriae.Vital dye reaction and granule localization in periplasm of Escherichia coliCytochrome c assembly.Genetic and proteomic characterization of rpoB mutations and their effect on nematicidal activity in Photorhabdus luminescens LN2.Developmental stage oxidoreductive states of Chlamydia and infected host cells.Purification, crystallization and preliminary crystallographic investigation of FrnE, a disulfide oxidoreductase from Deinococcus radiodurans.How periplasmic thioredoxin TlpA reduces bacterial copper chaperone ScoI and cytochrome oxidase subunit II (CoxB) prior to metallation.Biosynthesis of colabomycin E, a new manumycin-family metabolite, involves an unusual chain-length factor.Organocatalysts of oxidative protein folding inspired by protein disulfide isomerase.Crystal Structure of DsbA from Corynebacterium diphtheriae and Its Functional Implications for CueP in Gram-Positive BacteriaA Disulfide Bond-forming Machine Is Linked to the Sortase-mediated Pilus Assembly Pathway in the Gram-positive Bacterium Actinomyces orisFunctional and evolutionary analyses of Helicobacter pylori HP0231 (DsbK) protein with strong oxidative and chaperone activity characterized by a highly diverged dimerization domainDiversity and Expression of Bacterial Metacaspases in an Aquatic Ecosystem.Engineering of Helicobacter pylori Dimeric Oxidoreductase DsbK (HP0231)A thiol-disulfide oxidoreductase of the Gram-positive pathogen Corynebacterium diphtheriae is essential for viability, pilus assembly, toxin production and virulence.Cytochrome c biogenesis System I.Protein Machineries Involved in the Attachment of Heme to Cytochrome c: Protein Structures and Molecular Mechanisms.The interplay between the disulfide bond formation pathway and cytochrome c maturation in Escherichia coli.Absence of Thiol-Disulfide Oxidoreductase DsbA Impairs cbb3-Type Cytochrome c Oxidase Biogenesis in Rhodobacter capsulatus.INHIBITION OF DIVERSE DsbA ENZYMES IN MULTI-DsbA ENCODING PATHOGENS.The Multiple Localized Glyceraldehyde-3-Phosphate Dehydrogenase Contributes to the Attenuation of the Francisella tularensis dsbA Deletion Mutant.Dual Role for DsbA in Attacking and Targeted Bacterial Cells during Type VI Secretion System-Mediated Competition.Virulence of the melioidosis pathogen Burkholderia pseudomallei requires the oxidoreductase membrane protein DsbB.Structural basis of a thiol-disulfide oxidoreductase in the hedgehog-forming actinobacterium Corynebacterium matruchotii.
P2860
Q26738760-7157E128-A159-4C3D-A543-8FEBAE65D2D4Q26823827-74C34CC8-EB4D-4095-91B3-787406989E0AQ27003123-264C84C9-AA6B-467B-BDBD-BA39367A0130Q27678934-204C8038-7C3E-45F6-B308-36B1C4389839Q27679294-028D74F2-79E7-4D74-AA25-122EBBE805F7Q27680624-61CCEE86-F054-4FCB-BC64-992876A7AE7CQ27680786-0A1718C3-D5D8-4E70-8CB3-9448742BA289Q27682316-CE74119A-3F88-4426-8855-AD7D05E1C528Q27683799-B2E55AEB-469E-4A4A-BD39-EC84AA1FAD3BQ27683945-E05ED085-7F0F-43B1-A3B9-62C6E6E2331EQ28468521-BE3CF300-154C-4191-A5C5-125BFEDBBCFDQ28546904-EEB62C3E-EB02-419C-A5F0-1BA5E80BF43EQ30301079-567762C7-BD0E-47A8-B063-29AD5670A68AQ30376017-F67A5A7F-4DEC-4754-B79F-268E59F38434Q30416941-892A682B-0575-47B6-8DB1-1B5FA2312509Q33599927-F24FF9F9-4E87-47DD-9ABD-E212D79E6004Q34147966-A71ADCE1-53EF-4A93-A6B8-BCADE570BF64Q34295902-8FA7DC74-E05D-434A-99A9-9A50EA5749AEQ34323819-F12DAA13-85B2-4151-847B-24134394C5C2Q34389310-0D94D534-4961-400A-8774-4C01BF1398D3Q34440868-9B658F97-577F-45E2-886F-7D72ED6A6DE6Q34510590-2DD9BD5A-D642-409A-BE38-9582DC38F7A7Q34552524-29CDE4B9-B819-4D21-ABD7-43723AB23443Q35170571-4BE96015-D02A-4F8B-BD12-A612F32A5A65Q35285491-495604E3-8EE0-4168-9138-476A21A6CCA5Q35988882-FAAF3917-1EA1-429B-945C-3805B440912DQ36065069-CFAA7954-144E-4E1E-B3AD-37F26E885E46Q36133918-4D902178-2E2C-492A-8ABE-BF76333F578EQ37067079-89627798-5428-4642-943F-9EB6BB47ED25Q37124378-D09A433D-3C71-4024-BE88-AD195B8C12A9Q37168806-A4229945-3128-47C7-A382-663A8D03367FQ37940545-3B80454D-CCBF-479E-BA57-B50B6604445BQ38181141-2453B598-59F0-42A7-9B25-092743C73CB2Q41767891-DD713AE4-5029-4405-9312-661C422DB317Q47221449-3A1B75D2-5073-4F81-AEEC-2DA9C0D735C2Q47297144-34E22393-AC38-47C6-9EEC-FE5CB1816FC8Q47417123-8A699284-7E11-463D-84AE-048852C54346Q49326490-97BB393F-0903-4E47-B4A3-6627906A1AD5Q50026707-D70E12CE-F1E1-4178-9786-483D9022397EQ50027206-3B8CA0FF-B153-4F76-A4CA-909D1603D9CA
P2860
Structure and function of DsbA, a key bacterial oxidative folding catalyst.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on 17 January 2011
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Structure and function of DsbA, a key bacterial oxidative folding catalyst.
@en
Structure and function of DsbA, a key bacterial oxidative folding catalyst.
@nl
type
label
Structure and function of DsbA, a key bacterial oxidative folding catalyst.
@en
Structure and function of DsbA, a key bacterial oxidative folding catalyst.
@nl
prefLabel
Structure and function of DsbA, a key bacterial oxidative folding catalyst.
@en
Structure and function of DsbA, a key bacterial oxidative folding catalyst.
@nl
P2093
P50
P356
P1476
Structure and function of DsbA, a key bacterial oxidative folding catalyst.
@en
P2093
Begoña Heras
Patricia M Walden
Stephen R Shouldice
P304
P356
10.1089/ARS.2010.3344
P577
2011-01-17T00:00:00Z