Uncovering a region of heat shock protein 90 important for client binding in E. coli and chaperone function in yeast. - Wikidata - wikimedia - TriplyDB

Uncovering a region of heat shock protein 90 important for client binding in E. coli and chaperone function in yeast.

Uncovering a region of heat shock protein 90 important for client binding in E. coli and chaperone function in yeast.

http://www.wikidata.org/entity/Q36604957

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Glucocorticoid receptor function regulated by coordinated action of the Hsp90 and Hsp70 chaperone cycles Hsp90-Tau complex reveals molecular basis for specificity in chaperone action Chaperone machines for protein folding, unfolding and disaggregation Structural Asymmetry in the Closed State of Mitochondrial Hsp90 (TRAP1) Supports a Two-Step ATP Hydrolysis Mechanism Atomic structure of Hsp90-Cdc37-Cdk4 reveals that Hsp90 traps and stabilizes an unfolded kinase The Hsp90 cochaperones Cpr6, Cpr7, and Cns1 interact with the intact ribosome Mechanistic Asymmetry in Hsp90 Dimers Differential modulation of functional dynamics and allosteric interactions in the Hsp90-cochaperone complexes with p23 and Aha1: a computational study.Computational modeling of allosteric regulation in the hsp90 chaperones: a statistical ensemble analysis of protein structure networks and allosteric communications.An Hsp90 co-chaperone protein in yeast is functionally replaced by site-specific posttranslational modification in humans Genome-scale co-evolutionary inference identifies functions and clients of bacterial Hsp90 Heat Shock Protein 90 Associates with the Per-Arnt-Sim Domain of Heme-free Soluble Guanylate Cyclase: IMplications for Enzyme Maturation.Hsp70 and Hsp90 of E. coli Directly Interact for Collaboration in Protein Remodeling.Human J-protein DnaJB6b Cures a Subset of Saccharomyces cerevisiae Prions and Selectively Blocks Assembly of Structurally Related Amyloids.Interaction of heat shock protein 90 and the co-chaperone Cpr6 with Ura2, a bifunctional enzyme required for pyrimidine biosynthesis Elucidating the mechanism of substrate recognition by the bacterial Hsp90 molecular chaperone.Mutational Analysis of Glycogen Synthase Kinase 3β Protein Kinase Together with Kinome-Wide Binding and Stability Studies Suggests Context-Dependent Recognition of Kinases by the Chaperone Heat Shock Protein 90.Activation of Hsp90 Enzymatic Activity and Conformational Dynamics through Rationally Designed Allosteric Ligands.A C-terminal HSP90 inhibitor restores glucocorticoid sensitivity and relieves a mouse allograft model of Cushing disease.Molecular Dynamics Simulations Reveal the Mechanisms of Allosteric Activation of Hsp90 by Designed Ligands.Interactions of Escherichia coli molecular chaperone HtpG with DnaA replication initiator DNA.Symmetry broken and rebroken during the ATP hydrolysis cycle of the mitochondrial Hsp90 TRAP1.How Hsp90 and Cdc37 Lubricate Kinase Molecular Switches.Characterization of the Grp94/OS-9 chaperone-lectin complex.Hsp90·Cdc37 Complexes with Protein Kinases Form Cooperatively with Multiple Distinct Interaction Sites.A novel N-terminal extension in mitochondrial TRAP1 serves as a thermal regulator of chaperone activity.Hsp104 disaggregase at normal levels cures many [PSI+] prion variants in a process promoted by Sti1p, Hsp90, and Sis1p.Atomistic simulations and network-based modeling of the Hsp90-Cdc37 chaperone binding with Cdk4 client protein: A mechanism of chaperoning kinase clients by exploiting weak spots of intrinsically dynamic kinase domains.Evidence for Hsp90 Co-chaperones in Regulating Hsp90 Function and Promoting Client Protein Folding.Computational Modeling of the Hsp90 Interactions with Cochaperones and Small-Molecule Inhibitors.Bacterial Hsp90 ATPase Assays.Determination of Hsp90 Activity Through Activation of Glucocorticoid Receptors in Yeast.Functional and physical interaction between yeast Hsp90 and Hsp70.The HSP90 chaperone machinery.Interaction of E. coli Hsp90 with DnaK Involves the DnaJ Binding Region of DnaK.A switch point in the molecular chaperone Hsp90 responding to client interaction.Mutation of essential Hsp90 co-chaperones SGT1 or CNS1 renders yeast hypersensitive to overexpression of other co-chaperones.Dihydropyridines Allosterically Modulate Hsp90 Providing a Novel Mechanism for Heat Shock Protein Co-induction and Neuroprotection.

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P2860

Uncovering a region of heat shock protein 90 important for client binding in E. coli and chaperone function in yeast.

http://www.wikidata.org/entity/Q36604957

description

2012 nî lūn-bûn

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2012年の論文

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name

Uncovering a region of heat sh ...... d chaperone function in yeast.

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Uncovering a region of heat sh ...... d chaperone function in yeast.

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type

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Uncovering a region of heat sh ...... d chaperone function in yeast.

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Uncovering a region of heat sh ...... d chaperone function in yeast.

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Uncovering a region of heat sh ...... d chaperone function in yeast.

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Uncovering a region of heat sh ...... d chaperone function in yeast.

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Uncovering a region of heat sh ...... nd chaperone function in yeast

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Daniel C Masison

http://www.w3.org/2001/XMLSchema#string

David A Agard

http://www.w3.org/2001/XMLSchema#string

Jodi L Camberg

http://www.w3.org/2001/XMLSchema#string

Joel R Hoskins

http://www.w3.org/2001/XMLSchema#string

Olivier Genest

http://www.w3.org/2001/XMLSchema#string

Sue Wickner

http://www.w3.org/2001/XMLSchema#string

Timothy O Street

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P2860

Activation of the ATPase activity of hsp90 by the stress-regulated cochaperone aha1

Large-scale identification of protein-protein interaction of Escherichia coli K-12

The ATPase cycle of Hsp90 drives a molecular 'clamp' via transient dimerization of the N-terminal domains

Structural and functional analysis of the middle segment of hsp90: implications for ATP hydrolysis and client protein and cochaperone interactions

Mutational analysis of Hsp90 function: interactions with a steroid receptor and a protein kinase.

Hsp90 is regulated by a switch point in the C-terminal domain

Regulation of Hsp90 ATPase activity by tetratricopeptide repeat (TPR)-domain co-chaperones.

The Hsp90 chaperone machinery: conformational dynamics and regulation by co-chaperones

Interaction network containing conserved and essential protein complexes in Escherichia coli

HSP90 at the hub of protein homeostasis: emerging mechanistic insights

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3

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23260660

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Escherichia coli

molecular chaperones

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3570620

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