Related references
Note: Only part of the references are listed.The Chaperone Activity of GRP94 Toward Insulin-like Growth Factor II Is Necessary for the Stress Response to Serum Deprivation
Olga Ostrovsky et al.
MOLECULAR BIOLOGY OF THE CELL (2009)
The ATPase cycle of the endoplasmic chaperone Grp94
Stephan Frey et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2007)
Structures of GRP94-Nucleotide complexes reveal mechanistic differences between the hsp90 chaperones
D. Eric Dollins et al.
MOLECULAR CELL (2007)
GRP94 is essential for mesoderm induction and muscle development because it regulates insulin-like growth factor Secretion
Sherry Wanderling et al.
MOLECULAR BIOLOGY OF THE CELL (2007)
The peptide-binding activity of GRP94 is regulated by calcium
Chhanda Biswas et al.
BIOCHEMICAL JOURNAL (2007)
Heat shock protein gp96 is a master chaperone for toll-like receptors and is important in the innate function of macrophages
Yi Yang et al.
IMMUNITY (2007)
Quantitative proteomics analysis of the secretory pathway
Annalyn Gilchrist et al.
CELL (2006)
The N-terminal fragment of GRP94 is sufficient for peptide presentation via professional antigen-presenting cells
Chhanda Biswas et al.
INTERNATIONAL IMMUNOLOGY (2006)
Identification of novel quaternary domain interactions in the Hsp90 chaperone, GRP94
Feixia Chu et al.
PROTEIN SCIENCE (2006)
Monitoring chaperone engagement of substrates in the endoplasmic reticulum of live cells
EL Snapp et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2006)
Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complex
MMU Ali et al.
NATURE (2006)
Structure of unliganded GRP94, the endoplasmic reticulum Hsp90 - Basis for nucleotide-induced conformational change
DE Dollins et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2005)
Identification of the N-terminal peptide binding site of glucose-regulated protein 94
T Gidalevitz et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2004)
Co-chaperone regulation of conformational switching in the Hsp90 ATPase cycle
G Siligardi et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2004)
Improved monomeric red, orange and yellow fluorescent proteins derived from Discosoma sp red fluorescent protein
NC Shaner et al.
NATURE BIOTECHNOLOGY (2004)
Ligand-induced conformational shift in the N-terminal domain of GRP94, an Hsp90 chaperone
RM Immormino et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2004)
Structure of the N-terminal domain of GRP94 - Basis for ligand specificity and regulation
KL Soldano et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2003)
Formation of stacked ER cisternae by low affinity protein interactions
EL Snapp et al.
JOURNAL OF CELL BIOLOGY (2003)
Aha1 binds to the middle domain of Hsp90, contributes to client protein activation, and stimulates the ATPase activity of the molecular chaperone
GP Lotz et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2003)
Structural and functional analysis of the middle segment of Hsp90: Implications for ATP hydrolysis and client protein and cochaperone interactions
P Meyer et al.
MOLECULAR CELL (2003)
Radicicol-sensitive peptide binding to the N-terminal portion of GRP94
S Vogen et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2002)
Polyglutamine protein aggregates are dynamic
S Kim et al.
NATURE CELL BIOLOGY (2002)
SHEPHERD is the Arabidopsis GRP94 responsible for the formation of functional CLAVATA proteins
S Ishiguro et al.
EMBO JOURNAL (2002)
Endoplasmic reticulum chaperone gp96 is required for innate immunity but not cell viability
F Randow et al.
NATURE CELL BIOLOGY (2001)
Polypeptide release by Hsp90 involves ATP hydrolysis and is enhanced by the co-chaperone p23
JC Young et al.
EMBO JOURNAL (2000)
Diffusion in inhomogeneous media: Theory and simulations applied to whole cell photobleach recovery
ED Siggia et al.
BIOPHYSICAL JOURNAL (2000)
Ligand interactions in the adenosine nucleotide-binding domain of the Hsp90 chaperone, GRP94 I. Evidence for allosteric regulation of ligand binding
MFN Rosser et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2000)
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
JJ Wassenberg et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2000)
Structure of TPR domain-peptide complexes: Critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine
C Scheufler et al.
CELL (2000)
Dynamics and retention of misfolded proteins in native ER membranes
S Nehls et al.
NATURE CELL BIOLOGY (2000)
Share Paper
