All in the family: atypical Hsp70 chaperones are conserved modulators of Hsp70 activity.
about
Quality control and fate determination of Hsp90 client proteinsThe delicate balance between secreted protein folding and endoplasmic reticulum-associated degradation in human physiologyThe Endoplasmic Reticulum Chaperone GRP170: From Immunobiology to Cancer TherapeuticsSelective targeting of the stress chaperome as a therapeutic strategyThe master regulator of the cellular stress response (HSF1) is critical for orthopoxvirus infectionLarge-Scale Conformational Transitions and Dimerization Are Encoded in the Amino-Acid Sequences of Hsp70 ChaperonesHsp90 and co-chaperones twist the functions of diverse client proteins.Hierarchical functional specificity of cytosolic heat shock protein 70 (Hsp70) nucleotide exchange factors in yeast.The endoplasmic reticulum protein folding factory and its chaperones: new targets for drug discovery?Hsp110 chaperones control client fate determination in the hsp70-Hsp90 chaperone systemExpression of a malarial Hsp70 improves defects in chaperone-dependent activities in ssa1 mutant yeast.Heat shock protein 70 (hsp70) as an emerging drug target.J domain co-chaperone specificity defines the role of BiP during protein translocationHeteromeric complexes of heat shock protein 70 (HSP70) family members, including Hsp70B', in differentiated human neuronal cells.Meta-analysis of heat- and chemically upregulated chaperone genes in plant and human cells.Direct association of heat shock protein 20 (HSPB6) with phosphoinositide 3-kinase (PI3K) in human hepatocellular carcinoma: regulation of the PI3K activity.HSP70s: From Tumor Transformation to Cancer Therapy.A functional DnaK dimer is essential for the efficient interaction with Hsp40 heat shock proteinBlocking Hsp70 enhances the efficiency of amphotericin B treatment against resistant Aspergillus terreus strains.Molecular Chaperones of Leishmania: Central Players in Many Stress-Related and -Unrelated Physiological Processes.The response to heat shock and oxidative stress in Saccharomyces cerevisiaeComputational Analysis of Residue Interaction Networks and Coevolutionary Relationships in the Hsp70 Chaperones: A Community-Hopping Model of Allosteric Regulation and CommunicationHsp70 and Hsp90 multichaperone complexes sequentially regulate thiazide-sensitive cotransporter endoplasmic reticulum-associated degradation and biogenesis.The Lhs1/GRP170 chaperones facilitate the endoplasmic reticulum-associated degradation of the epithelial sodium channelHsp70 targets a cytoplasmic quality control substrate to the San1p ubiquitin ligaseThe activities and function of molecular chaperones in the endoplasmic reticulum.RDJ2 (DNAJA2) chaperones neural G protein signaling pathways.Multiple hsp70 isoforms in the eukaryotic cytosol: mere redundancy or functional specificity?The complex evolutionary dynamics of Hsp70s: a genomic and functional perspective.The large Hsp70 Grp170 binds to unfolded protein substrates in vivo with a regulation distinct from conventional Hsp70s.HSP110 promotes colorectal cancer growth through STAT3 activation.The Molecular Chaperone Hsc70 Interacts with Tyrosine Hydroxylase to Regulate Enzyme Activity and Synaptic Vesicle Localization.Affinity purification probes of potential use to investigate the endogenous Hsp70 interactome in cancer.Label-free nondestructive discrimination of colon carcinoma sublines and biomolecular insights into their differential Hsp70 expression: DNA/RNA nucleobase specific changes.Ydj1 protects nascent protein kinases from degradation and controls the rate of their maturation.Ssz1 restores endoplasmic reticulum-associated protein degradation in cells expressing defective cdc48-ufd1-npl4 complex by upregulating cdc48.The endoplasmic reticulum Grp170 acts as a nucleotide exchange factor of Hsp70 via a mechanism similar to that of the cytosolic Hsp110.Swapping nucleotides, tuning Hsp70.Unique peptide substrate binding properties of 110-kDa heat-shock protein (Hsp110) determine its distinct chaperone activityA protective Hsp70-TLR4 pathway in lethal oxidant lung injury.
P2860
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P2860
All in the family: atypical Hsp70 chaperones are conserved modulators of Hsp70 activity.
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
2007年论文
@zh
2007年论文
@zh-cn
name
All in the family: atypical Hsp70 chaperones are conserved modulators of Hsp70 activity.
@ast
All in the family: atypical Hsp70 chaperones are conserved modulators of Hsp70 activity.
@en
type
label
All in the family: atypical Hsp70 chaperones are conserved modulators of Hsp70 activity.
@ast
All in the family: atypical Hsp70 chaperones are conserved modulators of Hsp70 activity.
@en
prefLabel
All in the family: atypical Hsp70 chaperones are conserved modulators of Hsp70 activity.
@ast
All in the family: atypical Hsp70 chaperones are conserved modulators of Hsp70 activity.
@en
P2860
P356
P1476
All in the family: atypical Hsp70 chaperones are conserved modulators of Hsp70 activity
@en
P2093
Lance Shaner
P2860
P2888
P356
10.1379/CSC-245R.1
P577
2007-01-01T00:00:00Z
P5875
P6179
1008953181