(Q24316177)

5

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Jeffery W. Kelly

12

object named as

Jeffery W Kelly

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author name string

Xiaodong Wang

1

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John Venable

2

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Paul LaPointe

3

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Darren M Hutt

4

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Judith Coppinger

6

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Wendy Kellner

8

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Jeanne Matteson

9

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Helen Plutner

10

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John R Riordan

11

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John R Yates

13

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William E Balch

Hsp70 and Hsp90--a relay team for protein folding

14

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language of work or name

English

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publication date

17 November 2006

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published in

Cell

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volume

127

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issue

4

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page(s)

803-15

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cites work

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Therapy through chaperones: sense or antisense? Cystic fibrosis as a model disease

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Systems analyses reveal two chaperone networks with distinct functions in eukaryotic cells

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Structural features of the GroEL-GroES nano-cage required for rapid folding of encapsulated protein.

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Sequential quality-control checkpoints triage misfolded cystic fibrosis transmembrane conductance regulator

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More than folding: localized functions of cytosolic chaperones

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Fkbp8: novel isoforms, genomic organization, and characterization of a forebrain promoter in transgenic mice

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

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A model for random sampling and estimation of relative protein abundance in shotgun proteomics

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Native state kinetic stabilization as a strategy to ameliorate protein misfolding diseases: a focus on the transthyretin amyloidoses.

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The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation

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Large-scale analysis of the yeast proteome by multidimensional protein identification technology

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Structure of the Sec13/31 COPII coat cage

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Inherent calcineurin inhibitor FKBP38 targets Bcl-2 to mitochondria and inhibits apoptosis

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The integration of cell and chemical biology in protein folding

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New insights into cystic fibrosis: molecular switches that regulate CFTR

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The COPII cage: unifying principles of vesicle coat assembly

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Cystic fibrosis problem probed by proteolysis

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Structure of nucleotide-binding domain 1 of the cystic fibrosis transmembrane conductance regulator

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Aha1 competes with Hop, p50 and p23 for binding to the molecular chaperone Hsp90 and contributes to kinase and hormone receptor activation

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Localization and suppression of a kinetic defect in cystic fibrosis transmembrane conductance regulator folding

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Aha1 binds to the middle domain of Hsp90, contributes to client protein activation, and stimulates the ATPase activity of the molecular chaperone

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Regulation of the cytoplasmic quality control protein degradation pathway by BAG2

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COPII-dependent export of cystic fibrosis transmembrane conductance regulator from the ER uses a di-acidic exit code

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Regulation of longevity in Caenorhabditis elegans by heat shock factor and molecular chaperones

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The cochaperone HspBP1 inhibits the CHIP ubiquitin ligase and stimulates the maturation of the cystic fibrosis transmembrane conductance regulator

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Perturbation of Hsp90 interaction with nascent CFTR prevents its maturation and accelerates its degradation by the proteasome

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Roles of molecular chaperones in endoplasmic reticulum (ER) quality control and ER-associated degradation (ERAD)

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Pharmacologic rescue of conformationally-defective proteins: implications for the treatment of human disease

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Progressive disruption of cellular protein folding in models of polyglutamine diseases.

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Bi-directional protein transport between the ER and Golgi

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Assembly of functional CFTR chloride channels

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Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery

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7 January 2021

A new frontier in pharmacology: the endoplasmic reticulum as a regulated export pathway in health and disease

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