Detecting folding intermediates of a protein as it passes through the bacterial translocation channel - Wikidata - wikimedia - TriplyDB

Detecting folding intermediates of a protein as it passes through the bacterial translocation channel

Detecting folding intermediates of a protein as it passes through the bacterial translocation channel

http://www.wikidata.org/entity/Q35004080

about

Disulfide-Bond-Forming Pathways in Gram-Positive Bacteria Disulfide bond formation in the bacterial periplasm: major achievements and challenges ahead Many roles of the bacterial envelope reducing pathways The Sec-dependent pathway Reducing systems protecting the bacterial cell envelope from oxidative damage Dissecting the Machinery That Introduces Disulfide Bonds in Pseudomonas aeruginosa Virtual Screening of Peptide and Peptidomimetic Fragments Targeted to Inhibit Bacterial Dithiol Oxidase DsbA Sequential unfolding of the hemolysin two-partner secretion domain from Proteus mirabilis.Protease homolog BepA (YfgC) promotes assembly and degradation of β-barrel membrane proteins in Escherichia coli.Disulfide rearrangement triggered by translocon assembly controls lipopolysaccharide export Selective ribosome profiling reveals the cotranslational chaperone action of trigger factor in vivo Diversity of the Epsilonproteobacteria Dsb (disulfide bond) systems.Directionality in protein fold prediction.Cotranslational protein folding and terminus hydrophobicity.Disulfide bond oxidoreductase DsbA2 of Legionella pneumophila exhibits protein disulfide isomerase activity Disulfide bond formation in prokaryotes: history, diversity and design Electron Transport Chain Is Biochemically Linked to Pilus Assembly Required for Polymicrobial Interactions and Biofilm Formation in the Gram-Positive Actinobacterium Actinomyces oris.The L-cysteine/L-cystine shuttle system provides reducing equivalents to the periplasm in Escherichia coli.Nonconsecutive disulfide bond formation in an essential integral outer membrane protein Novel proteomic tools reveal essential roles of SRP and importance of proper membrane protein biogenesis Glycosylation of pilin and nonpilin protein constructs by Pseudomonas aeruginosa 1244 Identification of disulfide bond isomerase substrates reveals bacterial virulence factors.Consequences of depletion of the signal recognition particle in Escherichia coli Protein folding in the cell: challenges and progress.Superfolder GFP is fluorescent in oxidizing environments when targeted via the Sec translocon TrbB from conjugative plasmid F is a structurally distinct disulfide isomerase that requires DsbD for redox state maintenance.Functional and bioinformatics analysis of two Campylobacter jejuni homologs of the thiol-disulfide oxidoreductase, DsbA.A Disulfide Bond-forming Machine Is Linked to the Sortase-mediated Pilus Assembly Pathway in the Gram-positive Bacterium Actinomyces oris DegP Chaperone Suppresses Toxic Inner Membrane Translocation Intermediates.Infrared and Fluorescence Assessment of Protein Dynamics: From Folding to Function.A thiol-disulfide oxidoreductase of the Gram-positive pathogen Corynebacterium diphtheriae is essential for viability, pilus assembly, toxin production and virulence.Mechanisms of oxidative protein folding in the bacterial cell envelope.Integrating protein homeostasis strategies in prokaryotes.Composition and function of cytochrome c biogenesis System II.SecA Cotranslationally Interacts with Nascent Substrate Proteins In Vivo.Oxidative folding: recent developments.Life Stage-specific Proteomes of Legionella pneumophila Reveal a Highly Differential Abundance of Virulence-associated Dot/Icm effectors.Protein folding in the cell envelope of Escherichia coli.Oxidative stress, protein damage and repair in bacteria.Redox pathway sensing bile salts activates virulence gene expression in Vibrio cholerae.

P2860

Q26773784-355D2E76-BBA1-4A7C-A75F-E712F7588979 Q26823827-1F7E0B6C-BC6A-4B90-A45B-1717B636CBF8 Q27007462-1A458FD8-5382-443E-A1B6-4695D81AAC2B Q27010633-26D5511A-4F78-4D79-BE4A-5ED79CBC0775 Q27015968-8448C519-4576-426C-8EA7-01B001FFCD0A Q27680864-4A85E23F-929D-4AD8-BFCA-1603893C6AFA Q28546904-E30A8549-ECF5-42B7-8806-FCF76F8C5FF4 Q30152834-B040E9B2-2A2D-4563-A9B3-3803EE9A6996 Q30153518-63AB92DD-B490-46F9-8D9C-7459CCB1D438 Q30155243-5C05779B-09E7-4BC7-9C96-BFF1C33EFF63 Q30155411-EDF920F6-C4DB-4D53-9FCA-86EA925773E3 Q30376017-0C113569-C631-4FD1-A9DB-3A84B36E82A5 Q30387760-77A68710-35FF-4042-9B82-5AFF84E9E9A4 Q30404033-62DB4FEC-A193-4B31-9AB8-DAA525EE16E5 Q30416941-FA60978D-2AB9-428A-931D-1E0B9BA0D5CC Q33723782-0BD14A82-1CAE-400F-93F5-129119927840 Q33820093-8C137EDA-3C20-4D98-B854-0607732929F7 Q33885138-7D943979-D729-40D1-9198-1AA3C151E824 Q33982252-A472FF4A-B64A-43FD-8998-15B58761011D Q34059311-7C7CC93B-64F6-40E1-9375-57B3E2774793 Q34291197-CF08ADC5-0AC0-470B-86C6-744CFBF9E4B9 Q34490362-7185451C-410B-4558-8663-BB3C22ABFA4E Q34575625-EFE5A778-5A55-4408-B7BA-71098000B437 Q34768822-23196523-E8A0-4A47-BA05-A9A227793362 Q34816912-2B54CF14-3568-4478-84E8-890D0DC1E5D5 Q35192535-640C3D68-F9C3-4EE8-BA1D-0A2E8DC9A390 Q35236867-6BFDCCBF-BD56-4B54-BF6B-699C030DFFCE Q36065069-A50D5B16-9336-4E6D-BA33-A8CAD832FC0D Q36132158-39A93E18-C660-4EC5-B5CA-78F777E94C9E Q37013963-45F8EF98-B58F-4343-B839-525BBC5DE5B3 Q37168806-F3978831-BAA6-402B-AFDD-06DB51F6DE2A Q37724253-7B525EC2-0BE6-43F9-BC14-37DDC07956AE Q37858328-186F471B-710A-424C-B7CB-04F6970E229E Q37940091-A89BA15A-F3B5-4B44-9452-36465E1DBE9E Q38290386-39924324-49C4-4132-95A5-164D9CC6C777 Q38472604-8B634227-ABC9-458E-A83C-0018A2263149 Q38587508-CD036285-4D35-4FCE-AFAE-C05F54D023EB Q38940176-4837ECFA-3C7C-4F62-BE13-5AEDB9ECAB35 Q39249467-E1F7DEF9-2ABC-4BBB-89C9-70E2EBFB8D10 Q39407748-070D5EAE-C6A1-4A66-A4DC-D9C2BD07E4F6

P2860

Detecting folding intermediates of a protein as it passes through the bacterial translocation channel

http://www.wikidata.org/entity/Q35004080

description

2009 nî lūn-bûn

@nan

2009 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2009 թվականի սեպտեմբերին հրատարակված գիտական հոդված

@hy

2009年の論文

@ja

2009年論文

@yue

2009年論文

@zh-hant

2009年論文

@zh-hk

2009年論文

@zh-mo

2009年論文

@zh-tw

2009年论文

@wuu

name

Detecting folding intermediate ...... acterial translocation channel

@ast

Detecting folding intermediate ...... acterial translocation channel

@en

type

label

Detecting folding intermediate ...... acterial translocation channel

@ast

Detecting folding intermediate ...... acterial translocation channel

@en

prefLabel

Detecting folding intermediate ...... acterial translocation channel

@ast

Detecting folding intermediate ...... acterial translocation channel

@en

P1433

Q35004080-1BA92FA1-8414-4CFF-9535-C99905C9D02F

P1476

Q35004080-AB228A94-8283-4F1A-9E5B-A53871B41F6C

P2093

Q35004080-3E8DA52C-FE32-4192-96FA-1873D4C70E4C

Q35004080-57F29065-A3E7-4FED-9210-26F933C1BEB0

P2860

Q35004080-04AA43A6-B0D7-4B68-83AE-63854813FDA4

Q35004080-05721565-E595-48F6-A455-16A3D2BF0090

Q35004080-0617A275-6433-4C12-8F66-3AA7F66DA3FD

Q35004080-08BBC283-B591-4140-A5D3-7CD54833E5DB

Q35004080-09DA1BBB-1CF3-4CB3-B9CB-71ED4C5DE322

Q35004080-0AAFF23F-3B66-44E2-BCF5-28C911B76F48

Q35004080-11292856-5E38-4A26-9AD2-201A7DBB64DD

Q35004080-11C2A226-137C-47E5-A38B-39FBCC5B7746

Q35004080-18ECC8BD-ADA3-4362-97CF-A9CAEC40EB66

Q35004080-3012CC58-1D02-4470-888D-DADD8BE6343E

P304

Q35004080-8A3891C8-54C0-4D28-966D-5F37D9BC0375

P31

Q35004080-A9D6630F-6F00-4606-8F7A-42F2376A4989

P356

Q35004080-0F1DB790-0FEA-4FB0-B0D6-132D78D9CEB2

P407

Q35004080-B3A62FA8-41A9-4C6F-85B2-F3C74614C735

P433

Q35004080-AACFAC65-0610-440F-A53D-7665DD7778BD

P478

Q35004080-5DEF58E3-11DC-4B62-A6CA-551B3AE3E3BF

P577

Q35004080-0713601D-F165-4435-AB53-C39A68E5B0FD

P5875

Q35004080-126292D6-5E31-4555-89DD-BFE88121E827

P698

Q35004080-314BB415-B785-42DA-88D0-8B396641265D

P921

Q35004080-2C5FB801-8502-4464-8415-B7B073E9D042

P932

Q35004080-A4F7443D-A594-4A76-A374-4B35E7755E48

P356

J.CELL.2009.07.030

P1433

P1476

Detecting folding intermediate ...... acterial translocation channel

@en

P2093

Hiroshi Kadokura

http://www.w3.org/2001/XMLSchema#string

Jon Beckwith

http://www.w3.org/2001/XMLSchema#string

P2860

The oxidase DsbA folds a protein with a nonconsecutive disulfide

Systems analyses reveal two chaperone networks with distinct functions in eukaryotic cells.

The complete general secretory pathway in gram-negative bacteria

Kinetic analysis of the assembly of the outer membrane protein LamB in Escherichia coli mutants each lacking a secretion or targeting factor in a different cellular compartment.

Azide-resistant mutants of Escherichia coli alter the SecA protein, an azide-sensitive component of the protein export machinery.

Identification and characterization of an Escherichia coli gene required for the formation of correctly folded alkaline phosphatase, a periplasmic enzyme.

Mixed-disulfide folding intermediates between thyroglobulin and endoplasmic reticulum resident oxidoreductases ERp57 and protein disulfide isomerase.

Protein disulfide bond formation in prokaryotes.

Amino acid sequence of Escherichia coli alkaline phosphatase.

Preferential binding of an unfolded protein to DsbA.

P304

1164-1173

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1016/J.CELL.2009.07.030

http://www.w3.org/2001/XMLSchema#string

P407

P433

6

http://www.w3.org/2001/XMLSchema#string

P478

138

http://www.w3.org/2001/XMLSchema#string

P577

2009-09-01T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

26824042

http://www.w3.org/2001/XMLSchema#string

P698

19766568

http://www.w3.org/2001/XMLSchema#string

P921

protein folding

P932

2750780

http://www.w3.org/2001/XMLSchema#string