Stress-inducible, murine protein mSTI1. Characterization of binding domains for heat shock proteins and in vitro phosphorylation by different kinases.
about
A structure-based mutational analysis of cyclophilin 40 identifies key residues in the core tetratricopeptide repeat domain that mediate binding to Hsp90Post-transcriptional regulation of thioredoxin by the stress inducible heterogenous ribonucleoprotein A18.Ubiquilin4 is an adaptor protein that recruits Ubiquilin1 to the autophagy machineryInteraction of the Hsp90 cochaperone cyclophilin 40 with Hsc70Stress-inducible protein 1 is a cell surface ligand for cellular prion that triggers neuroprotection.Electrostatic Interactions of Hsp-organizing Protein Tetratricopeptide Domains with Hsp70 and Hsp90: COMPUTATIONAL ANALYSIS AND PROTEIN ENGINEERINGSBA1 encodes a yeast hsp90 cochaperone that is homologous to vertebrate p23 proteinsThe phosphatase Ppt1 is a dedicated regulator of the molecular chaperone Hsp90Plasmodium falciparum Hop (PfHop) Interacts with the Hsp70 Chaperone in a Nucleotide-Dependent Fashion and Exhibits Ligand SelectivitySpecific interaction of the 70-kDa heat shock cognate protein with the tetratricopeptide repeatsThe ubiquitin-related BAG-1 provides a link between the molecular chaperones Hsc70/Hsp70 and the proteasomeHop modulates Hsp70/Hsp90 interactions in protein foldingCharacterisation of the Plasmodium falciparum Hsp70-Hsp90 organising protein (PfHop)Ligand discrimination by TPR domains. Relevance and selectivity of EEVD-recognition in Hsp70 x Hop x Hsp90 complexes.The common tetratricopeptide repeat acceptor site for steroid receptor-associated immunophilins and hop is located in the dimerization domain of Hsp90.The Hsp70/Hsp90 Chaperone Machinery in Neurodegenerative DiseasesIn silico identification of carboxylate clamp type tetratricopeptide repeat proteins in Arabidopsis and rice as putative co-chaperones of Hsp90/Hsp70Genistein induces deleterious effects during its acute exposure in Swiss mice.A family of ubiquitin-like proteins binds the ATPase domain of Hsp70-like Stch.Hsp104 interacts with Hsp90 cochaperones in respiring yeastThe Hsp90 co-chaperones Cdc37 and Sti1 interact physically and genetically.Independent regulation of Hsp70 and Hsp90 chaperones by Hsp70/Hsp90-organizing protein Sti1 (Hop1).Involvement of tumor necrosis factor receptor-associated protein 1 (TRAP1) in apoptosis induced by beta-hydroxyisovalerylshikonin.Versatile TPR domains accommodate different modes of target protein recognition and functionPost-translational modifications of Hsp90 and their contributions to chaperone regulationTetratricopeptide repeat cochaperones in steroid receptor complexesThe cellular prion protein (PrP(C)): its physiological function and role in diseaseThe regulation of proteasome degradation by multi-ubiquitin chain binding proteins.Polymyxin B inhibits the chaperone activity of Plasmodium falciparum Hsp70.Differential proteomics analysis of synaptic proteins identifies potential cellular targets and protein mediators of synaptic neuroprotection conferred by the slow Wallerian degeneration (Wlds) gene.Tumor-intrinsic and tumor-extrinsic factors impacting hsp90- targeted therapy.Bovine spongiform encephalopathy in Japan: history and recent studies on oxidative stress in prion diseases.Ubiquilin/Dsk2 promotes inclusion body formation and vacuole (lysosome)-mediated disposal of mutated huntingtinEndocytosis of prion protein is required for ERK1/2 signaling induced by stress-inducible protein 1.Molecular correlates of axonal and synaptic pathology in mouse models of Batten disease.A proteomic approach for the discovery of protease substrates.Chaperone receptors: guiding proteins to intracellular compartments.Different combinations of the heat-shock cognate protein 70 (hsc70) C-terminal functional groups are utilized to interact with distinct tetratricopeptide repeat-containing proteins.Tetratricopeptide repeat motif-mediated Hsc70-mSTI1 interaction. Molecular characterization of the critical contacts for successful binding and specificity.The chaperone cofactor Hop/p60 interacts with the cytosolic chaperonin-containing TCP-1 and affects its nucleotide exchange and protein folding activities.
P2860
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P2860
Stress-inducible, murine protein mSTI1. Characterization of binding domains for heat shock proteins and in vitro phosphorylation by different kinases.
description
1997 nî lūn-bûn
@nan
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
1997年论文
@zh
1997年论文
@zh-cn
name
Stress-inducible, murine prote ...... rylation by different kinases.
@en
Stress-inducible, murine prote ...... rylation by different kinases.
@nl
type
label
Stress-inducible, murine prote ...... rylation by different kinases.
@en
Stress-inducible, murine prote ...... rylation by different kinases.
@nl
prefLabel
Stress-inducible, murine prote ...... rylation by different kinases.
@en
Stress-inducible, murine prote ...... rylation by different kinases.
@nl
P2093
P2860
P356
P1476
Stress-inducible, murine prote ...... rylation by different kinases.
@en
P2093
P2860
P304
P356
10.1074/JBC.272.3.1876
P407
P577
1997-01-01T00:00:00Z