An essential role for ATP binding and hydrolysis in the chaperone activity of GRP94 in cells (Q37261639)

19 August 2017

An essential role for ATP binding and hydrolysis in the chaperone activity of GRP94 in cells (English)

1 reference

19 August 2017

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Erik L Snapp

1 reference

19 August 2017

Olga Ostrovsky

1 reference

19 August 2017

Catherine A Makarewich

series ordinal

1 reference

19 August 2017

Yair Argon

series ordinal

1 reference

19 August 2017

language of work or name

English

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publication date

24 June 2009

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Proceedings of the National Academy of Sciences of the United States of America

19 August 2017

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19 August 2017

106

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19 August 2017

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19 August 2017

11600-11605

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Measuring protein mobility by photobleaching GFP chimeras in living cells

19 August 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2710619

Structures of GRP94-nucleotide complexes reveal mechanistic differences between the hsp90 chaperones

6 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2710619

GRP94 is essential for mesoderm induction and muscle development because it regulates insulin-like growth factor secretion

6 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2710619

Heat shock protein gp96 is a master chaperone for toll-like receptors and is important in the innate function of macrophages

6 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2710619

Identification of novel quaternary domain interactions in the Hsp90 chaperone, GRP94.

6 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2710619

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

6 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2710619

Monitoring chaperone engagement of substrates in the endoplasmic reticulum of live cells

6 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2710619

Improved monomeric red, orange and yellow fluorescent proteins derived from Discosoma sp. red fluorescent protein

6 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2710619

Ligand-induced conformational shift in the N-terminal domain of GRP94, an Hsp90 chaperone

6 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2710619

Formation of stacked ER cisternae by low affinity protein interactions

6 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2710619

Structure of the N-terminal domain of GRP94. Basis for ligand specificity and regulation

6 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2710619

Structural and functional analysis of the middle segment of hsp90: implications for ATP hydrolysis and client protein and cochaperone interactions

6 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2710619

Aha1 binds to the middle domain of Hsp90, contributes to client protein activation, and stimulates the ATPase activity of the molecular chaperone

6 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2710619

SHEPHERD is the Arabidopsis GRP94 responsible for the formation of functional CLAVATA proteins

6 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2710619

Endoplasmic reticulum chaperone gp96 is required for innate immunity but not cell viability

6 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2710619

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

6 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2710619

Diffusion in inhomogeneous media: theory and simulations applied to whole cell photobleach recovery

6 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2710619

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

6 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2710619

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

6 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2710619

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

6 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2710619

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

6 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2710619

Two chaperone sites in Hsp90 differing in substrate specificity and ATP dependence

6 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2710619

Endoplasmic reticulum chaperone GRP94 subunit assembly is regulated through a defined oligomerization domain.

6 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2710619

Tumor rejection antigen gp96/grp94 is an ATPase: implications for protein folding and antigen presentation

6 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2710619

The peptide-binding activity of GRP94 is regulated by calcium.

6 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2710619

Interaction of radicicol with members of the heat shock protein 90 family of molecular chaperones

14 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2710619

ATP-binding Properties of Human Hsp90

28 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2710619

The ATPase cycle of the endoplasmic chaperone Grp94.

28 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2710619

Structure of unliganded GRP94, the endoplasmic reticulum Hsp90. Basis for nucleotide-induced conformational change

3 September 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2710619

Co-chaperone regulation of conformational switching in the Hsp90 ATPase cycle

3 September 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2710619

Identification of the N-terminal peptide binding site of glucose-regulated protein 94.

3 September 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2710619

Structural transitions accompanying the activation of peptide binding to the endoplasmic reticulum Hsp90 chaperone GRP94.

3 September 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2710619

Assessment of the ATP binding properties of Hsp90.

3 September 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2710619

The chaperone activity of GRP94 toward insulin-like growth factor II is necessary for the stress response to serum deprivation

3 September 2018

1 reference

Crossref

https://api.crossref.org/works/10.1073%2FPNAS.0902626106

Dynamics and retention of misfolded proteins in native ER membranes

21 January 2018

1 reference

Crossref

https://api.crossref.org/works/10.1073%2FPNAS.0902626106

Sequential interaction of the chaperones BiP and GRP94 with immunoglobulin chains in the endoplasmic reticulum

21 January 2018

1 reference

Crossref

https://api.crossref.org/works/10.1073%2FPNAS.0902626106

The N-terminal fragment of GRP94 is sufficient for peptide presentation via professional antigen-presenting cells

21 January 2018

1 reference

12 December 2020

Quantitative proteomics analysis of the secretory pathway

1 reference

12 December 2020

Ligand interactions in the adenosine nucleotide-binding domain of the Hsp90 chaperone, GRP94. I. Evidence for allosteric regulation of ligand binding

1 reference

12 December 2020

Ligand interactions in the adenosine nucleotide-binding domain of the Hsp90 chaperone, GRP94. II. Ligand-mediated activation of GRP94 molecular chaperone and peptide binding activity

1 reference

12 December 2020

Polyglutamine protein aggregates are dynamic

1 reference

12 December 2020

Radicicol-sensitive peptide binding to the N-terminal portion of GRP94

1 reference

12 December 2020

Interaction of Endoplasmic Reticulum Chaperone GRP94 with Peptide Substrates Is Adenine Nucleotide-independent

1 reference

12 December 2020

Immunotherapy of Tumors with Autologous Tumor-Derived Heat Shock Protein Preparations

1 reference

12 December 2020

The importance of ATP binding and hydrolysis by hsp90 in formation and function of protein heterocomplexes

1 reference

12 December 2020

Identifiers

DOI

10.1073/PNAS.0902626106

1 reference

19 August 2017

0 references

1 reference

19 August 2017

PubMed publication ID

19553200

1 reference