The molecular chaperone Hsp90 delivers precursor proteins to the chloroplast import receptor Toc64 - Wikidata - awgldk - TriplyDB

The molecular chaperone Hsp90 delivers precursor proteins to the chloroplast import receptor Toc64

The molecular chaperone Hsp90 delivers precursor proteins to the chloroplast import receptor Toc64

http://www.wikidata.org/entity/Q34590484

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The similarity between N-terminal targeting signals for protein import into different organelles and its evolutionary relevance Specific targeting of proteins to outer envelope membranes of endosymbiotic organelles, chloroplasts, and mitochondria The POTRA domains of Toc75 exhibit chaperone-like function to facilitate import into chloroplasts.New insights into the mechanism of chloroplast protein import and its integration with protein quality control, organelle biogenesis and development.Tic62: a protein family from metabolism to protein translocation.An optimized transit peptide for effective targeting of diverse foreign proteins into chloroplasts in rice.In silico identification of carboxylate clamp type tetratricopeptide repeat proteins in Arabidopsis and rice as putative co-chaperones of Hsp90/Hsp70 Analysis of protein interactions at native chloroplast membranes by ellipsometry The Hsp90-dependent proteome is conserved and enriched for hub proteins with high levels of protein-protein connectivity.The protein translocation systems in plants - composition and variability on the example of Solanum lycopersicum The C-terminus of Bienertia sinuspersici Toc159 contains essential elements for its targeting and anchorage to the chloroplast outer membrane.Ligand recognition by the TPR domain of the import factor Toc64 from Arabidopsis thaliana.Protein-protein interactions visualized by bimolecular fluorescence complementation in tobacco protoplasts and leaves.Chloroplast biogenesis: the use of mutants to study the etioplast-chloroplast transition.Mitochondrial biogenesis and function in Arabidopsis.Chloroplast biogenesis: control of plastid development, protein import, division and inheritance.Energetic cost of protein import across the envelope membranes of chloroplasts.An essential role for chloroplast heat shock protein 90 (Hsp90C) in protein import into chloroplasts.Protein import into chloroplasts: new aspects of a well-known topic.Protein transport in organelles: The Toc complex way of preprotein import.Molecular interactions within the plant TOC complex.Tail-anchored membrane proteins: exploring the complex diversity of tail-anchored-protein targeting in plant cells.Chaperone receptors: guiding proteins to intracellular compartments.Protein import into chloroplasts: dealing with the (membrane) integration problem.Direct targeting of proteins from the cytosol to organelles: the ER versus endosymbiotic organelles.The chloroplast protein translocation complexes of Chlamydomonas reinhardtii: a bioinformatic comparison of Toc and Tic components in plants, green algae and red algae AtTPR7 as part of the Arabidopsis Sec post-translocon.Import of Soluble Proteins into Chloroplasts and Potential Regulatory Mechanisms Early stages in the biogenesis of eukaryotic β-barrel proteins.Sequence Motifs in Transit Peptides Act as Independent Functional Units and Can Be Transferred to New Sequence Contexts.OEP61 is a chaperone receptor at the plastid outer envelope.Chloroplast envelope protein targeting fidelity is independent of cytosolic components in dual organelle assays.Quantification of interaction strengths between chaperones and tetratricopeptide repeat domain-containing membrane proteins.Study of receptor-chaperone interactions using the optical technique of spectroscopic ellipsometry.Arabidopsis thaliana Oxa proteins locate to mitochondria and fulfill essential roles during embryo development.Toc33 and Toc64-III cooperate in precursor protein import into the chloroplasts of Arabidopsis thaliana.Multiple sequence motifs in the rubisco small subunit transit peptide independently contribute to Toc159-dependent import of proteins into chloroplasts.REP27, a tetratricopeptide repeat nuclear-encoded and chloroplast-localized protein, functions in D1/32-kD reaction center protein turnover and photosystem II repair from photodamage.Cytosolic HSP90 regulates the heat shock response that is responsible for heat acclimation in Arabidopsis thaliana.The integration of chloroplast protein targeting with plant developmental and stress responses.

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The molecular chaperone Hsp90 delivers precursor proteins to the chloroplast import receptor Toc64

http://www.wikidata.org/entity/Q34590484

description

2006 nî lūn-bûn

@nan

2006 թուականի Ապրիլին հրատարակուած գիտական յօդուած

@hyw

2006 թվականի ապրիլին հրատարակված գիտական հոդված

@hy

2006年の論文

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2006年論文

@yue

2006年論文

@zh-hant

2006年論文

@zh-hk

2006年論文

@zh-mo

2006年論文

@zh-tw

2006年论文

@wuu

name

The molecular chaperone Hsp90 ...... oroplast import receptor Toc64

@en

The molecular chaperone Hsp90 ...... oroplast import receptor Toc64

@nl

type

label

The molecular chaperone Hsp90 ...... oroplast import receptor Toc64

@en

The molecular chaperone Hsp90 ...... oroplast import receptor Toc64

@nl

prefLabel

The molecular chaperone Hsp90 ...... oroplast import receptor Toc64

@en

The molecular chaperone Hsp90 ...... oroplast import receptor Toc64

@nl

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SJ.EMBOJ.7601091

P1433

The EMBO Journal

P1476

The molecular chaperone Hsp90 ...... oroplast import receptor Toc64

@en

P2093

Ivo Tews

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

Jürgen Soll

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

Oliver Mirus

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

Soumya Qbadou

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

Thomas Becker

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

P2860

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

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

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

WHAT IF: a molecular modeling and drug design program

Pathways of chaperone-mediated protein folding in the cytosol

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

Getting newly synthesized proteins into shape.

Protein import into yeast mitochondria is accelerated by the outer membrane protein MAS70.

Polypeptide release by Hsp90 involves ATP hydrolysis and is enhanced by the co-chaperone p23.

A GTP-driven motor moves proteins across the outer envelope of chloroplasts.

P304

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scholarly article

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10.1038/SJ.EMBOJ.7601091

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P433

9

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25

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Enrico Schleiff

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2006-04-13T00:00:00Z

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7161268

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16619024

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P921

molecular chaperones

P932

1456943

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