ATP-dependent chaperoning activity of reticulocyte lysate.
about
Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions.Human cyclophilin 40 is a heat shock protein that exhibits altered intracellular localization following heat shockComplexes between nascent polypeptides and their molecular chaperones in the cytosol of mammalian cellsRegulation of protein homeostasis in neurodegenerative diseases: the role of coding and non-coding genesMutational analysis of Hsp90 function: interactions with a steroid receptor and a protein kinase.The refolding activity of the yeast heat shock proteins Ssa1 and Ssa2 defines their role in protein translocationFolding in vivo of a newly translated yeast cytosolic enzyme is mediated by the SSA class of cytosolic yeast Hsp70 proteins.In vivo functions of the Saccharomyces cerevisiae Hsp90 chaperone.Identification of SSF1, CNS1, and HCH1 as multicopy suppressors of a Saccharomyces cerevisiae Hsp90 loss-of-function mutation.Functional requirement of p23 and Hsp90 in telomerase complexesTransportable, Chemical Genetic Methodology for the Small Molecule-Mediated Inhibition of Heat Shock Factor 1Reconstitution of a functional duck hepatitis B virus replication initiation complex from separate reverse transcriptase domains expressed in Escherichia coliA small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state.In vivo chaperone activity of heat shock protein 70 and thermotolerance.Chaperones rescue luciferase folding by separating its domains.In vitro reconstitution of functional hepadnavirus reverse transcriptase with cellular chaperone proteins.Hsp90 (heat shock protein 90) inhibitor occupancy is a direct determinant of client protein degradation and tumor growth arrest in vivoT antigens of simian virus 40: molecular chaperones for viral replication and tumorigenesisMaturation of the tyrosine kinase c-src as a kinase and as a substrate depends on the molecular chaperone Hsp90.Heat shock protein 90-independent activation of truncated hepadnavirus reverse transcriptase.Development of a high-throughput screening cancer cell-based luciferase refolding assay for identifying Hsp90 inhibitors.High-throughput screen of natural product libraries for hsp90 inhibitors.Search for Hsp90 inhibitors with potential anticancer activity: isolation and SAR studies of radicicol and monocillin I from two plant-associated fungi of the Sonoran desertHigh-throughput assay for the identification of Hsp90 inhibitors based on Hsp90-dependent refolding of firefly luciferase.Analysis of the tau-associated proteome reveals that exchange of Hsp70 for Hsp90 is involved in tau degradationMitochondrial Hsp90 is a ligand-activated molecular chaperone coupling ATP binding to dimer closure through a coiled-coil intermediate.Pharmacologic shifting of a balance between protein refolding and degradation mediated by Hsp90Inhibition of immunoglobulin folding and secretion by dominant negative BiP ATPase mutants.Requirement of heat shock protein 90 for human hepatitis B virus reverse transcriptase function.A small heat shock protein cooperates with heat shock protein 70 systems to reactivate a heat-denatured protein.Screening strategies to identify HSP70 modulators to treat Alzheimer's disease.Characterization of the UGA-recoding and SECIS-binding activities of SECIS-binding protein 2(-)-Epigallocatechin-3-gallate is a novel Hsp90 inhibitorHsp72 chaperone function is dispensable for protection against stress-induced apoptosisCompeting Pathways and Multiple Folding Nuclei in a Large Multidomain Protein, Luciferase.
P2860
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P2860
ATP-dependent chaperoning activity of reticulocyte lysate.
description
1994 nî lūn-bûn
@nan
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
1994年论文
@zh
1994年论文
@zh-cn
name
ATP-dependent chaperoning activity of reticulocyte lysate.
@en
type
label
ATP-dependent chaperoning activity of reticulocyte lysate.
@en
prefLabel
ATP-dependent chaperoning activity of reticulocyte lysate.
@en
P2093
P1476
ATP-dependent chaperoning activity of reticulocyte lysate.
@en
P2093
P304
P407
P577
1994-04-01T00:00:00Z