Hsp90 functions in the targeting and outer membrane translocation steps of Tom70-mediated mitochondrial import (Q34565583)

3 August 2017

Hsp90 functions in the targeting and outer membrane translocation steps of Tom70-mediated mitochondrial import (English)

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3 August 2017

Anna C Y Fan

1

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3 August 2017

Melanie K Bhangoo

series ordinal

2

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3 August 2017

Jason C Young

series ordinal

3

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3 August 2017

language of work or name

English

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publication date

12 September 2006

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Journal of Biological Chemistry

3 August 2017

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3 August 2017

281

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3 August 2017

44

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3 August 2017

33313-33324

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Mitochondriomics or what makes us breathe.

3 August 2017

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https://api.crossref.org/works/10.1074%2FJBC.M605250200

New developments in mitochondrial assembly

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M605250200

The protein import machinery of mitochondria

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M605250200

A mitochondrial import receptor for the ADP/ATP carrier

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M605250200

The requirement of heat shock cognate 70 protein for mitochondrial import varies among precursor proteins and depends on precursor length

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M605250200

The mitochondrial import receptor Tom70: identification of a 25 kDa core domain with a specific binding site for preproteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M605250200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M605250200

A biophysical analysis of the tetratricopeptide repeat-rich mitochondrial import receptor, Tom70, reveals an elongated monomer that is inherently flexible, unstable, and unfolds via a multistate pathway

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M605250200

The C-terminal TPR Domain of Tom70 Defines a Family of Mitochondrial Protein Import Receptors Found only in Animals and Fungi

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M605250200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M605250200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M605250200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M605250200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M605250200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M605250200

Molecular chaperones in the cytosol: from nascent chain to folded protein

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M605250200

Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M605250200

Pathways of chaperone-mediated protein folding in the cytosol

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M605250200

Hsp70 chaperones: cellular functions and molecular mechanism

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M605250200

The TOM core complex: the general protein import pore of the outer membrane of mitochondria.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M605250200

Tom40, the pore-forming component of the protein-conducting TOM channel in the outer membrane of mitochondria

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M605250200

Membrane-embedded C-terminal segment of rat mitochondrial TOM40 constitutes protein-conducting pore with enriched beta-structure

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M605250200

Tim9p, an essential partner subunit of Tim10p for the import of mitochondrial carrier proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M605250200

Different import pathways through the mitochondrial intermembrane space for inner membrane proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M605250200

Functional reconstitution of the import of the yeast ADP/ATP carrier mediated by the TIM10 complex

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M605250200

The Tim9p-Tim10p complex binds to the transmembrane domains of the ADP/ATP carrier

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M605250200

Mitochondrial import of the ADP/ATP carrier: the essential TIM complex of the intermembrane space is required for precursor release from the TOM complex

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M605250200

Organization and function of the small Tim complexes acting along the import pathway of metabolite carriers into mammalian mitochondria

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M605250200

Crystal structure of the mitochondrial chaperone TIM9.10 reveals a six-bladed alpha-propeller

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M605250200

Import of carrier proteins into the mitochondrial inner membrane mediated by Tim22.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M605250200

Transport of the ADP/ATP carrier of mitochondria from the TOM complex to the TIM22.54 complex

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M605250200

The mitochondrial TIM22 preprotein translocase is highly conserved throughout the eukaryotic kingdom

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M605250200

Tim22, the essential core of the mitochondrial protein insertion complex, forms a voltage-activated and signal-gated channel

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M605250200

Protein insertion into the mitochondrial inner membrane by a twin-pore translocase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M605250200

Reconstituted TOM core complex and Tim9/Tim10 complex of mitochondria are sufficient for translocation of the ADP/ATP carrier across membranes

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M605250200

Functional staging of ADP/ATP carrier translocation across the outer mitochondrial membrane

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M605250200

The three modules of ADP/ATP carrier cooperate in receptor recruitment and translocation into mitochondria

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M605250200

Hsp90: a specialized but essential protein-folding tool

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M605250200

Hsp90: chaperoning signal transduction

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M605250200

Heat-shock protein 90, a chaperone for folding and regulation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M605250200

Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M605250200

The amino-terminal domain of heat shock protein 90 (hsp90) that binds geldanamycin is an ATP/ADP switch domain that regulates hsp90 conformation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M605250200

ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M605250200

In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysis

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M605250200

The ATPase cycle of Hsp90 drives a molecular 'clamp' via transient dimerization of the N-terminal domains

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M605250200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M605250200

Dimerization and N-terminal domain proximity underlie the function of the molecular chaperone heat shock protein 90

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M605250200

Surface charge and hydrophobicity determine ErbB2 binding to the Hsp90 chaperone complex.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M605250200

Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complex

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M605250200

More than folding: localized functions of cytosolic chaperones

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M605250200

HSP90 and the chaperoning of cancer

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M605250200

Inhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: essential role for stress proteins in oncogenic transformation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M605250200

Pharmacologic shifting of a balance between protein refolding and degradation mediated by Hsp90

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M605250200

Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M605250200

The heat shock protein 90 antagonist novobiocin interacts with a previously unrecognized ATP-binding domain in the carboxyl terminus of the chaperone

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M605250200

Nucleotide binding states of hsp70 and hsp90 during sequential steps in the process of glucocorticoid receptor.hsp90 heterocomplex assembly

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M605250200

Novobiocin induces a distinct conformation of Hsp90 and alters Hsp90-cochaperone-client interactions

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M605250200

Modulation of chaperone function and cochaperone interaction by novobiocin in the C-terminal domain of Hsp90: evidence that coumarin antibiotics disrupt Hsp90 dimerization

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M605250200

New mitochondrial carriers: an overview.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M605250200

Functional analysis of human mitochondrial receptor Tom20 for protein import into mitochondria

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M605250200

Identification and functional analysis of human Tom22 for protein import into mitochondria

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M605250200

Functional analysis of human metaxin in mitochondrial protein import in cultured cells and its relationship with the Tom complex

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M605250200

Mitochondrial ATP synthasome. Cristae-enriched membranes and a multiwell detergent screening assay yield dispersed single complexes containing the ATP synthase and carriers for Pi and ADP/ATP.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M605250200

Navigating the chaperone network: an integrative map of physical and genetic interactions mediated by the hsp90 chaperone

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M605250200

Isolation of intracellular membranes by means of sodium carbonate treatment: application to endoplasmic reticulum

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M605250200

Signal-anchored proteins follow a unique insertion pathway into the outer membrane of mitochondria

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M605250200

21 January 2018

Identifiers

DOI

10.1074/JBC.M605250200

1 reference

3 August 2017

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