Ligand discrimination by TPR domains. Relevance and selectivity of EEVD-recognition in Hsp70 x Hop x Hsp90 complexes. - Wikidata - wikimedia - TriplyDB

Ligand discrimination by TPR domains. Relevance and selectivity of EEVD-recognition in Hsp70 x Hop x Hsp90 complexes.

Ligand discrimination by TPR domains. Relevance and selectivity of EEVD-recognition in Hsp70 x Hop x Hsp90 complexes.

http://www.wikidata.org/entity/Q30823415

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AIPL1, a protein implicated in Leber's congenital amaurosis, interacts with and aids in processing of farnesylated proteins A structure-based mutational analysis of cyclophilin 40 identifies key residues in the core tetratricopeptide repeat domain that mediate binding to Hsp90 Hepatitis C virus RNA replication is regulated by FKBP8 and Hsp90 Cofactor Tpr2 combines two TPR domains and a J domain to regulate the Hsp70/Hsp90 chaperone system Interaction of the Hsp90 cochaperone cyclophilin 40 with Hsc70 GCUNC-45 is a novel regulator for the progesterone receptor/hsp90 chaperoning pathway.Ferredoxin:NADPH oxidoreductase is recruited to thylakoids by binding to a polyproline type II helix in a pH-dependent manner Ligand binding by TPR domains An internal EELD domain facilitates mitochondrial targeting of Mcl-1 via a Tom70-dependent pathway GRP94: An HSP90-like protein specialized for protein folding and quality control in the endoplasmic reticulum Ex vivo promoter analysis of antiviral heat shock cognate 70B gene in Anopheles gambiae Electrostatic Interactions of Hsp-organizing Protein Tetratricopeptide Domains with Hsp70 and Hsp90: COMPUTATIONAL ANALYSIS AND PROTEIN ENGINEERING Redesign of a protein - peptide interaction: Characterization and applications A Structural Model of the Sgt2 Protein and Its Interactions with Chaperones and the Get4/Get5 Complex Chaperone ligand-discrimination by the TPR-domain protein Tah1.Cns1 is an activator of the Ssa1 ATPase activity.Defining the role for XAP2 in stabilization of the dioxin receptor An androgen receptor NH2-terminal conserved motif interacts with the COOH terminus of the Hsp70-interacting protein (CHIP)Allostery in the Hsp70 chaperone proteins C-terminal phosphorylation of Hsp70 and Hsp90 regulates alternate binding to co-chaperones CHIP and HOP to determine cellular protein folding/degradation balances The hexosamine signaling pathway: deciphering the "O-GlcNAc code"A brain-specific isoform of small glutamine-rich tetratricopeptide repeat-containing protein binds to Hsc70 and the cysteine string protein C-terminal sequences of hsp70 and hsp90 as non-specific anchors for tetratricopeptide repeat (TPR) proteins Binding of human nucleotide exchange factors to heat shock protein 70 (Hsp70) generates functionally distinct complexes in vitro HSPA8/HSC70 chaperone protein: structure, function, and chemical targeting.Heat shock proteins: cellular and molecular mechanisms in the central nervous system.Protein-Protein Interactions Modulate the Docking-Dependent E3-Ubiquitin Ligase Activity of Carboxy-Terminus of Hsc70-Interacting Protein (CHIP)The human TPR protein TTC4 is a putative Hsp90 co-chaperone which interacts with CDC6 and shows alterations in transformed cells.An AlphaScreen-based high-throughput screen to identify inhibitors of Hsp90-cochaperone interaction.Designed proteins to modulate cellular networks EEVD motif of heat shock cognate protein 70 contributes to bacterial uptake by trophoblast giant cells Synergistic regulation of competence development in Bacillus subtilis by two Rap-Phr systems.Differential impact of tetratricopeptide repeat proteins on the steroid hormone receptors Analysis of protein interactions at native chloroplast membranes by ellipsometry Tetratricopeptide repeat domain 9A negatively regulates estrogen receptor alpha activity Hsp90 functions in the targeting and outer membrane translocation steps of Tom70-mediated mitochondrial import.The molecular chaperone Hsp90 delivers precursor proteins to the chloroplast import receptor Toc64 Saccharomyces cerevisiae Hsp70 mutations affect [PSI+] prion propagation and cell growth differently and implicate Hsp40 and tetratricopeptide repeat cochaperones in impairment of [PSI+]Ligand recognition by the TPR domain of the import factor Toc64 from Arabidopsis thaliana.Client-loading conformation of the Hsp90 molecular chaperone revealed in the cryo-EM structure of the human Hsp90:Hop complex.

P2860

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P2860

Ligand discrimination by TPR domains. Relevance and selectivity of EEVD-recognition in Hsp70 x Hop x Hsp90 complexes.

http://www.wikidata.org/entity/Q30823415

description

2002 nî lūn-bûn

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2002 թուականի Մարտին հրատարակուած գիտական յօդուած

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2002 թվականի մարտին հրատարակված գիտական հոդված

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2002年の論文

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2002年論文

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2002年論文

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2002年論文

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2002年論文

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2002年論文

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2002年论文

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name

Ligand discrimination by TPR d ...... Hsp70 x Hop x Hsp90 complexes.

@ast

Ligand discrimination by TPR d ...... Hsp70 x Hop x Hsp90 complexes.

@en

type

label

Ligand discrimination by TPR d ...... Hsp70 x Hop x Hsp90 complexes.

@ast

Ligand discrimination by TPR d ...... Hsp70 x Hop x Hsp90 complexes.

@en

prefLabel

Ligand discrimination by TPR d ...... Hsp70 x Hop x Hsp90 complexes.

@ast

Ligand discrimination by TPR d ...... Hsp70 x Hop x Hsp90 complexes.

@en

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P1433

Journal of Biological Chemistry

P1476

Ligand discrimination by TPR d ...... Hsp70 x Hop x Hsp90 complexes.

@en

P2093

Achim Brinker

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

Burkhard Fleckenstein

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Christian Herrmann

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

Clemens Scheufler

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

Florian Von Der Mulbe

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

Gunther Jung

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

Ismail Moarefi

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P2860

Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions.

The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins

Hsp90: a specialized but essential protein-folding tool

Specific binding of tetratricopeptide repeat proteins to the C-terminal 12-kDa domain of hsp90

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

Structural basis of presequence recognition by the mitochondrial protein import receptor Tom20

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

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

Peroxisomal targeting signal-1 recognition by the TPR domains of human PEX5

The active N-terminal region of p67phox. Structure at 1.8 A resolution and biochemical characterizations of the A128V mutant implicated in chronic granulomatous disease

P304

19265-19275

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scholarly article

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10.1074/JBC.M109002200

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P433

22

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P478

277

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Franz-Ulrich Hartl

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2002-03-04T00:00:00Z

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P698

11877417

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