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Chaperone receptors: guiding proteins to intracellular compartments.

Chaperone receptors: guiding proteins to intracellular compartments.

http://www.wikidata.org/entity/Q37861008

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A central role for inducible heat-shock protein 70 in autoimmune vitiligo The heat shock protein/chaperone network and multiple stress resistance New insights into the mechanism of chloroplast protein import and its integration with protein quality control, organelle biogenesis and development.The Bam machine: a molecular cooper.Heat Shock Protein-70 Expression in Vitiligo and its Relation to the Disease Activity.AtTPR7 as part of the Arabidopsis Sec post-translocon.Chloroplast envelope protein targeting fidelity is independent of cytosolic components in dual organelle assays.A comparative glycoproteome study of developing endosperm in the hexose-deficient miniature1 (mn1) seed mutant and its wild type Mn1 in maize.Study of receptor-chaperone interactions using the optical technique of spectroscopic ellipsometry.Multiple PPR protein interactions are involved in the RNA editing system in Arabidopsis mitochondria and plastids.An antimicrobial origin of transit peptides accounts for early endosymbiotic events.

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Chaperone receptors: guiding proteins to intracellular compartments.

http://www.wikidata.org/entity/Q37861008

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on 03 April 2011

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Chaperone receptors: guiding proteins to intracellular compartments.

@en

Chaperone receptors: guiding proteins to intracellular compartments.

@nl

type

label

Chaperone receptors: guiding proteins to intracellular compartments.

@en

Chaperone receptors: guiding proteins to intracellular compartments.

@nl

prefLabel

Chaperone receptors: guiding proteins to intracellular compartments.

@en

Chaperone receptors: guiding proteins to intracellular compartments.

@nl

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Chaperone receptors: guiding proteins to intracellular compartments.

@en

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Ben M Abell

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Ottilie von Löffelholz

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P2860

Targeting of the tail-anchored peroxisomal membrane proteins PEX26 and PEX15 occurs through C-terminal PEX19-binding sites

AIP is a mitochondrial import mediator that binds to both import receptor Tom20 and preproteins

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

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.

Not all J domains are created equal: implications for the specificity of Hsp40-Hsp70 interactions

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

Substrate twinning activates the signal recognition particle and its receptor

Heterodimeric GTPase Core of the SRP Targeting Complex

The structural plasticity of Tom71 for mitochondrial precursor translocations

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s00709-011-0270-9

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21-30

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scholarly article

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10.1007/S00709-011-0270-9

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1

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249

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Ottilie von Löffelholz

Verena Kriechbaumer

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2011-04-03T00:00:00Z

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21461941

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molecular chaperones