Tetratricopeptide-like repeats in type-III-secretion chaperones and regulators (Q47845290)

6 February 2018

title

Tetratricopeptide-like repeats in type-III-secretion chaperones and regulators (English)

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6 February 2018

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1

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6 February 2018

Matthew S. Francis

series ordinal

2

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6 February 2018

Klaus Fütterer

series ordinal

3

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6 February 2018

publication date

1 June 2003

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6 February 2018

FEMS Microbiology Letters

published in

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6 February 2018

volume

223

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6 February 2018

issue

1

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6 February 2018

page(s)

53-60

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6 February 2018

Yersinia type III secretion: send in the effectors

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Individual chaperones required for Yop secretion by Yersinia

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7 January 2021

How and when are substrates selected for type III secretion?

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7 January 2021

Structure of the Yersinia type III secretory system chaperone SycE

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7 January 2021

Yersinia pestis YscG protein is a Syc-like chaperone that directly binds yscE.

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7 January 2021

Three-dimensional structure of the type III secretion chaperone SycE from Yersinia pestis

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7 January 2021

Structural and biochemical characterization of the type III secretion chaperones CesT and SigE

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7 January 2021

Maintenance of an unfolded polypeptide by a cognate chaperone in bacterial type III secretion

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7 January 2021

The tetratricopeptide repeat: a structural motif mediating protein-protein interactions

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7 January 2021

The TPR snap helix: a novel protein repeat motif from mitosis to transcription

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7 January 2021

Tetratrico peptide repeat interactions: to TPR or not to TPR?

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7 January 2021

Molecular chaperones Hsp90 and Hsp70 deliver preproteins to the mitochondrial import receptor Tom70

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7 January 2021

The hsp90-based Chaperone System: Involvement in Signal Transduction from a Variety of Hormone and Growth Factor Receptors

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7 January 2021

Regulation of Hsp90 ATPase activity by tetratricopeptide repeat (TPR)-domain co-chaperones

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7 January 2021

The structure of the tetratricopeptide repeats of protein phosphatase 5: implications for TPR-mediated protein-protein interactions

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7 January 2021

Structure of the TPR domain of p67phox in complex with Rac.GTP

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7 January 2021

Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine

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7 January 2021

Two structures of cyclophilin 40: folding and fidelity in the TPR domains

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Gapped BLAST and PSI-BLAST: a new generation of protein database search programs

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7 January 2021

Comparative protein structure modeling of genes and genomes

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7 January 2021

Modelling protein docking using shape complementarity, electrostatics and biochemical information

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7 January 2021

Role of SycD, the chaperone of the Yersinia Yop translocators YopB and YopD.

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7 January 2021

A study of the YopD-lcrH interaction from Yersinia pseudotuberculosis reveals a role for hydrophobic residues within the amphipathic domain of YopD.

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7 January 2021

The Yersinia pestis YscY protein directly binds YscX, a secreted component of the type III secretion machinery

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7 January 2021

Identification of type III secreted products of the Pseudomonas aeruginosa exoenzyme S regulon

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7 January 2021

Genome sequence of the plant pathogen Ralstonia solanacearum

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7 January 2021

Homologs of the Shigella IpaB and IpaC invasins are required for Salmonella typhimurium entry into cultured epithelial cells

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7 January 2021

Complex function for SicA, a Salmonella enterica serovar typhimurium type III secretion-associated chaperone

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7 January 2021

Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae AR39.

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7 January 2021

EspB and EspD require a specific chaperone for proper secretion from enteropathogenicEscherichia coli

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7 January 2021

The type III secretion chaperone LcrH co-operates with YopD to establish a negative, regulatory loop for control of Yop synthesis in Yersinia pseudotuberculosis

1 reference

https://api.crossref.org/works/10.1016%2FS0378-1097%2803%2900344-6

7 January 2021

Conformational analysis by CD and NMR spectroscopy of a peptide encompassing the amphipathic domain of YopD from Yersinia

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https://api.crossref.org/works/10.1016%2FS0378-1097%2803%2900344-6

7 January 2021

The Salmonella pathogenicity island-1 type III secretion system

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7 January 2021

Evidence that the hrpB gene encodes a positive regulator of pathogenicity genes from Pseudomonas solanacearum

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7 January 2021

Competition between the Yops of Yersinia enterocolitica for delivery into eukaryotic cells: role of the SycE chaperone binding domain of YopE.

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7 January 2021

Topological characteristics of helical repeat proteins

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7 January 2021

Crystal structure of transcription factor MalT domain III: a novel helix repeat fold implicated in regulated oligomerization

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7 January 2021

Glucitol induction in Bacillus subtilis is mediated by a regulatory factor, GutR

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7 January 2021

Roles of glucitol in the GutR-mediated transcription activation process in Bacillus subtilis: tight binding of GutR to tis binding site

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7 January 2021

The crystal structure of Helicobacter pylori cysteine-rich protein B reveals a novel fold for a penicillin-binding protein

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7 January 2021

Identification of residues in the TPR domain of Ssn6 responsible for interaction with the Tup1 protein

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7 January 2021

Two distinct regions of the immunophilin-like protein XAP2 regulate dioxin receptor function and interaction with hsp90

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7 January 2021

Recognition of peroxisomal targeting signal type 1 by the import receptor Pex5p

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7 January 2021

A gain-of-function mutation in the second tetratricopeptide repeat of TFIIIC131 relieves autoinhibition of Brf1 binding

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7 January 2021

Role of rapsyn tetratricopeptide repeat and coiled-coil domains in self-association and nicotinic acetylcholine receptor clustering

1 reference

https://api.crossref.org/works/10.1016%2FS0378-1097%2803%2900344-6

7 January 2021

A structure-based mutational analysis of cyclophilin 40 identifies key residues in the core tetratricopeptide repeat domain that mediate binding to Hsp90

1 reference

https://api.crossref.org/works/10.1016%2FS0378-1097%2803%2900344-6

7 January 2021

The alpha-subunit of protein prenyltransferases is a member of the tetratricopeptide repeat family

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https://api.crossref.org/works/10.1016%2FS0378-1097%2803%2900344-6

7 January 2021

SWISS‐MODEL and the Swiss‐Pdb Viewer: An environment for comparative protein modeling

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https://api.crossref.org/works/10.1016%2FS0378-1097%2803%2900344-6

7 January 2021

10.1016/S0378-1097(03)00344-6

Identifiers

DOI

1 reference

6 February 2018

1 reference

6 February 2018