(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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3

Erik L Snapp

1 reference

19 August 2017

Olga Ostrovsky

1

1 reference

19 August 2017

Catherine A Makarewich

series ordinal

2

1 reference

19 August 2017

Yair Argon

series ordinal

4

1 reference

19 August 2017

language of work or name

English

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publication date

24 June 2009

1 reference

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

19 August 2017

1 reference

19 August 2017

106

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19 August 2017

11600-11605

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19 August 2017

28

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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

1 reference