The protein-disulfide isomerase DsbC cooperates with SurA and DsbA in the assembly of the essential β-barrel protein LptD.
about
Disulfide bond formation in the bacterial periplasm: major achievements and challenges aheadMany roles of the bacterial envelope reducing pathwaysReducing systems protecting the bacterial cell envelope from oxidative damageCrystal Structure of the Outer Membrane Protein RcsF, a New Substrate for the Periplasmic Protein-disulfide Isomerase DsbCStructural basis for lipopolysaccharide insertion in the bacterial outer membraneProtease homolog BepA (YfgC) promotes assembly and degradation of β-barrel membrane proteins in Escherichia coli.Outer membrane biogenesis in Escherichia coli, Neisseria meningitidis, and Helicobacter pylori: paradigm deviations in H. pyloriROSics: chemistry and proteomics of cysteine modifications in redox biology.Disulfide bond oxidoreductase DsbA2 of Legionella pneumophila exhibits protein disulfide isomerase activityBacterial thiol oxidoreductases - from basic research to new antibacterial strategiesA new family of membrane electron transporters and its substrates, including a new cell envelope peroxiredoxin, reveal a broadened reductive capacity of the oxidative bacterial cell envelopeSilver enhances antibiotic activity against gram-negative bacteria.Identification of disulfide bond isomerase substrates reveals bacterial virulence factors.The Interferon-Inducible Mouse Apolipoprotein L9 and Prohibitins Cooperate to Restrict Theiler's Virus ReplicationA comparison of the endotoxin biosynthesis and protein oxidation pathways in the biogenesis of the outer membrane of Escherichia coli and Neisseria meningitidis.Lipopolysaccharide transport and assembly at the outer membrane: the PEZ modelTransport of lipopolysaccharide to the Gram-negative bacterial cell surface.The LptD chaperone LptE is not directly involved in lipopolysaccharide transport in Neisseria meningitidisA new role for Escherichia coli DsbC protein in protection against oxidative stressProduction of anti-cancer immunotoxins in algae: ribosome inactivating proteins as fusion partners.Oxidative stress, protein damage and repair in bacteria.Nanoparticles as Efflux Pump and Biofilm Inhibitor to Rejuvenate Bactericidal Effect of Conventional Antibiotics.The Disulfide Bond Formation Pathway Is Essential for Anaerobic Growth of Escherichia coli.Impact of selected amino acids of HP0377 (Helicobacter pylori thiol oxidoreductase) on its functioning as a CcmG (cytochrome c maturation) protein and Dsb (disulfide bond) isomerase.A novel mechanism of RNase L inhibition: Theiler's virus L* protein prevents 2-5A from binding to RNase L.Structural Basis for the Lipopolysaccharide Export Activity of the Bacterial Lipopolysaccharide Transport System
P2860
Q26823827-7C48F4D4-C95B-41AF-8636-C868E833F5C4Q27007462-65297D5C-20AE-47E1-9218-EF0428E6AC36Q27015968-110E9D53-15E3-478D-A8F2-4C8BC56ED279Q27667359-28008B39-3800-4924-B5C4-66523E07AEC0Q28493206-5C4FBD9D-DCC5-4490-AE45-DF152ABF3487Q30153518-1CBAB197-2A8E-438D-AFF0-69043DB5F0EBQ30155248-A25BDCDE-A186-48C8-8155-62438B83323EQ30363450-5868EA1A-2EF5-4E95-8DFD-7D893CA5DB2CQ30416941-8DFD8A4B-ECD7-4B56-A6E2-9604CB7E538DQ33599927-F2C53375-D15A-4882-994D-8A3F4F1D14ACQ34228037-5F7D8CA6-BE00-427E-A29A-1C8F852F4A84Q34352180-2CB2ECCA-F617-4CD1-A6B9-509F1F176E51Q34490362-9E97AAC7-E7CC-4CAB-8BCE-A9590D508D79Q35702392-8F276138-33A1-4948-B240-95796F0C46DCQ36479175-B8D035A5-F522-4CAB-8FF1-9A39F6517018Q37077552-379B7E44-A6BE-4374-9A21-2F18677A810BQ38514161-2F0E3783-FBF1-4F6F-BF7E-DC90548C6ABCQ38672707-538EEC6C-9166-4953-BA7A-8944079876E1Q39145574-D9126B0B-6E66-488C-9168-5142EEB03167Q39146031-BF8DF016-CF0A-493F-AA16-C8343F9160F3Q39249467-357F4589-F524-4A0E-890E-1574A1226077Q39435559-2CDF9F3C-0B72-45C5-A12C-D19FA9A71232Q50301904-04BA2917-1D8B-46C6-A8EB-A56E3507A6ABQ52314279-E8FC4E19-9B5B-4A02-AD93-6D96FD545B71Q52589873-83DE1254-34DF-4BEB-9B72-D18794EADDDCQ58753224-8D81C5C0-7E91-4954-9B03-9595E4131140
P2860
The protein-disulfide isomerase DsbC cooperates with SurA and DsbA in the assembly of the essential β-barrel protein LptD.
description
2010 nî lūn-bûn
@nan
2010 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
The protein-disulfide isomeras ...... sential β-barrel protein LptD.
@ast
The protein-disulfide isomeras ...... sential β-barrel protein LptD.
@en
type
label
The protein-disulfide isomeras ...... sential β-barrel protein LptD.
@ast
The protein-disulfide isomeras ...... sential β-barrel protein LptD.
@en
prefLabel
The protein-disulfide isomeras ...... sential β-barrel protein LptD.
@ast
The protein-disulfide isomeras ...... sential β-barrel protein LptD.
@en
P2860
P356
P1476
The protein-disulfide isomeras ...... sential β-barrel protein LptD.
@en
P2093
Eunok Paek
Katleen Denoncin
P2860
P304
29425-29433
P356
10.1074/JBC.M110.119321
P407
P577
2010-07-07T00:00:00Z