Literature DB >> 24084862

Q-bodies monitor the quinary state of the protein fold.

Daniela Martino Roth1, William E Balch.   

Abstract

Cytoplasmic compartments containing misfolded proteins targeted for degradation, named Q-bodies, have been identified. Q-body formation is a dynamic process that actively manages the metastable state of the protein fold through small heat shock proteins and the Hsp70-Hsp90-Hsp110 proteostasis system to promote cellular fitness under both physiological and stress conditions.

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Year:  2013        PMID: 24084862     DOI: 10.1038/ncb2857

Source DB:  PubMed          Journal:  Nat Cell Biol        ISSN: 1465-7392            Impact factor:   28.824


  23 in total

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Journal:  Curr Enzym Inhib       Date:  2013-01-01

Review 5.  Protein homeostasis in models of aging and age-related conformational disease.

Authors:  Elise A Kikis; Tali Gidalevitz; Richard I Morimoto
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7.  The molecular chaperone Hsp90 modulates intermediate steps of amyloid assembly of the Parkinson-related protein alpha-synuclein.

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8.  A class of membrane proteins shaping the tubular endoplasmic reticulum.

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9.  A chaperone trap contributes to the onset of cystic fibrosis.

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10.  Spatial sequestration of misfolded proteins by a dynamic chaperone pathway enhances cellular fitness during stress.

Authors:  Stéphanie Escusa-Toret; Willianne I M Vonk; Judith Frydman
Journal:  Nat Cell Biol       Date:  2013-09-15       Impact factor: 28.824

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Review 3.  Ferritinophagy and α-Synuclein: Pharmacological Targeting of Autophagy to Restore Iron Regulation in Parkinson's Disease.

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Review 4.  Direct and/or Indirect Roles for SUMO in Modulating Alpha-Synuclein Toxicity.

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5.  The ER Stress Surveillance (ERSU) pathway regulates daughter cell ER protein aggregate inheritance.

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