The Chaperoning Properties of Mouse Grp170, a Member of the Third Family of Hsp70 Related Proteins
- 22 November 2003
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 42 (50), 14893-14902
- https://doi.org/10.1021/bi030122e
Abstract
No abstract availableKeywords
This publication has 10 references indexed in Scilit:
- LHS1 and SIL1 provide a lumenal function that is essential for protein translocation into the endoplasmic reticulumThe EMBO Journal, 2000
- Prefoldin–Nascent Chain Complexes in the Folding of Cytoskeletal ProteinsThe Journal of cell biology, 1999
- The Hsp70 Homologue Lhs1p Is Involved in a Novel Function of the Yeast Endoplasmic Reticulum, Refolding and Stabilization of Heat-denatured Protein AggregatesThe Journal of cell biology, 1997
- Multiple Molecular Chaperones Complex with Misfolded Large Oligomeric Glycoproteins in the Endoplasmic ReticulumJournal of Biological Chemistry, 1997
- Regulation of the Heat-shock Protein 70 Reaction Cycle by the Mammalian DnaJ Homolog, Hsp40Journal of Biological Chemistry, 1996
- Purification and Characterization of a Novel Stress Protein, the 150-kDa Oxygen-regulated Protein (ORP150), from Cultured Rat Astrocytes and Its Expression in Ischemic Mouse BrainPublished by Elsevier BV ,1996
- The 170 kDa glucose regulated stress protein is a large HSP70‐ HSP110‐like protein of the endoplasmic reticulumFEBS Letters, 1996
- The 23-kDa Acidic Protein in Reticulocyte Lysate Is the Weakly Bound Component of the hsp Foldosome That Is Required for Assembly of the Glucocorticoid Receptor into a Functional Heterocomplex with hsp90Journal of Biological Chemistry, 1995
- Identification of a Major Subfamily of Large hsp70-like Proteins through the Cloning of the Mammalian 110-kDa Heat Shock ProteinPublished by Elsevier BV ,1995
- [5] Bioinorganic spectroscopyMethods in enzymology, 1995