How potassium affects the activity of the molecular chaperone Hsc70. I. Potassium is required for optimal ATPase activity.
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Biochemical and structural studies on the high affinity of Hsp70 for ADPLysine 71 of the chaperone protein Hsc70 Is essential for ATP hydrolysisThe nucleotide exchange factor MGE exerts a key function in the ATP-dependent cycle of mt-Hsp70-Tim44 interaction driving mitochondrial protein import.Regulation of Hsp90 ATPase activity by tetratricopeptide repeat (TPR)-domain co-chaperones.Nucleotide binding states of hsp70 and hsp90 during sequential steps in the process of glucocorticoid receptor.hsp90 heterocomplex assemblyAllostery in the Hsp70 chaperone proteinsUsing ¹⁵N-ammonium to characterise and map potassium binding sites in proteins by NMR spectroscopy.Measurement and interpretation of 15N-1H residual dipolar couplings in larger proteins.Monitoring charge flux to quantify unusual ligand-induced ion channel activity for use in biological nanopore-based sensorsAbility of Sit4p to promote K+ efflux via Nha1p is modulated by Sap155p and Sap185p.The membrane-bound DnaJ protein located at the cytosolic site of glyoxysomes specifically binds the cytosolic isoform 1 of Hsp70 but not other Hsp70 species.ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo.LacZ β-galactosidase: structure and function of an enzyme of historical and molecular biological importance.Defining the potassium binding region in an apple terpene synthase.An RNA aptamer specific to Hsp70-ATP conformation inhibits its ATPase activity independent of Hsp40.Identification of yeast genes involved in k homeostasis: loss of membrane traffic genes affects k uptake.Hsc66 and Hsc20, a new heat shock cognate molecular chaperone system from Escherichia coli.A structural perspective on enzymes activated by monovalent cations.Role of Na+ and K+ in enzyme function.A role for molecular chaperone Hsc70 in reovirus outer capsid disassemblyThrombin.HscA and HscB stimulate [2Fe-2S] cluster transfer from IscU to apoferredoxin in an ATP-dependent reaction.Specific molecular chaperone interactions and an ATP-dependent conformational change are required during posttranslational protein translocation into the yeast ER.Bacterial expression and purification of interleukin-2 tyrosine kinase: single step separation of the chaperonin impurityMolecular Mechanisms of Enzyme Activation by Monovalent Cations.The Hsp70 peptide-binding domain determines the interaction of the ATPase domain with Tim44 in mitochondriaTranscription of the archaeal trkA homolog in Methanosarcina mazei S-6.Intracellular potassium stabilizes human ether-à-go-go-related gene channels for export from endoplasmic reticulum.PDBSiteScan: a program for searching for active, binding and posttranslational modification sites in the 3D structures of proteins.Sulfatide-Hsp70 interaction promotes Hsp70 clustering and stabilizes binding to unfolded protein.Structural features required for the interaction of the Hsp70 molecular chaperone DnaK with its cochaperone DnaJ.Kinetic characterization of the ATPase cycle of the molecular chaperone Hsc66 from Escherichia coli.Measurement of 15N longitudinal relaxation rates in 15NH4+ spin systems to characterise rotational correlation times and chemical exchange.Mechanism of Na(+) binding to thrombin resolved by ultra-rapid kinetics.Heteronuclear transverse and longitudinal relaxation in AX4 spin systems: application to (15)N relaxations in (15)NH4(+).Destabilization of peptide binding and interdomain communication by an E543K mutation in the bovine 70-kDa heat shock cognate protein, a molecular chaperone.Crystal structure of an ATPase-active form of Rad51 homolog from Methanococcus voltae. Insights into potassium dependence.Potassium is involved in apatite biomineralization.Disrupted hydrogen bond network and impaired ATPase activity in an Hsc70 cysteine mutant.Real time kinetics of the DnaK/DnaJ/GrpE molecular chaperone machine action.
P2860
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P2860
How potassium affects the activity of the molecular chaperone Hsc70. I. Potassium is required for optimal ATPase activity.
description
1995 nî lūn-bûn
@nan
1995年の論文
@ja
1995年学术文章
@wuu
1995年学术文章
@zh-cn
1995年学术文章
@zh-hans
1995年学术文章
@zh-my
1995年学术文章
@zh-sg
1995年學術文章
@yue
1995年學術文章
@zh
1995年學術文章
@zh-hant
name
How potassium affects the acti ...... d for optimal ATPase activity.
@en
How potassium affects the acti ...... d for optimal ATPase activity.
@nl
type
label
How potassium affects the acti ...... d for optimal ATPase activity.
@en
How potassium affects the acti ...... d for optimal ATPase activity.
@nl
prefLabel
How potassium affects the acti ...... d for optimal ATPase activity.
@en
How potassium affects the acti ...... d for optimal ATPase activity.
@nl
P2860
P356
P1476
How potassium affects the acti ...... d for optimal ATPase activity.
@en
P2093
P2860
P304
P356
10.1074/JBC.270.5.2247
P407
P577
1995-02-01T00:00:00Z