Protein Homeostasis in Amyotrophic Lateral Sclerosis: Therapeutic Opportunities?
Frontiers in Molecular Neuroscience, 2017 Protein homeostasis (proteostasis), the correct balance between production and degradation of proteins, is essential for the health and survival of cells.
Pamela J. Shaw +3 more
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Chaperonin Abundance Enhances Bacterial Fitness
Frontiers in Molecular Biosciences, 2021 The ability of chaperonins to buffer mutations that affect protein folding pathways suggests that their abundance should be evolutionarily advantageous. Here, we investigate the effect of chaperonin overproduction on cellular fitness in Escherichia coli.
C. M. Santosh Kumar +7 more
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A yeast two-hybrid screen reveals a strong interaction between the Legionella chaperonin Hsp60 and the host cell small heat shock protein Hsp10 [PDF]
, 2015 L. pneumophila is an intracellular bacterium that replicates inside a membrane-bound vacuole called Legionella-containing vacuole (LCV), where it plentifully liberates its HtpB chaperonin.
Nasrallah, Gheyath K.
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Overexpression of a Prefoldin β subunit gene reduces biomass recalcitrance in the bioenergy crop Populus. [PDF]
, 2020 Prefoldin (PFD) is a group II chaperonin that is ubiquitously present in the eukaryotic kingdom. Six subunits (PFD1-6) form a jellyfish-like heterohexameric PFD complex and function in protein folding and cytoskeleton organization.
Barry, Kerrie +20 more
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Comparative genomic analysis of mollicutes with and without a chaperonin system. [PDF]
PLoS ONE, 2018 The GroE chaperonin system, which comprises GroEL and GroES, assists protein folding in vivo and in vitro. It is conserved in all prokaryotes except in most, but not all, members of the class of mollicutes.
Dominik Schwarz +3 more
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Microbiology Spectrum, 2021 Almost 140 years after the identification of Mycobacterium tuberculosis as the etiological agent of tuberculosis, important aspects of its biology remain poorly described.
Joanna Houghton +7 more
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The role of molecular chaperonins in warm ischemia and reperfusion injury in the steatotic liver: A proteomic study [PDF]
, 2012 BACKGROUND: The molecular basis of the increased susceptibility of steatotic livers to warm ischemia/reperfusion (I/R) injury during transplantation remains undefined. Animal model for warm I/R injury was induced in obese Zucker rats.
Christopher D Anderson +12 more
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Extragenic Suppression analysis of TS mutations using Sec61p [PDF]
, 2007 During synthesis, secretory and membrane proteins are cotranslationally translocated into the lumen of the endoplasmic reticulum through an aqueous gated channel.
Sterling Smith
core +2 more sources
The Legionella pneumophila chaperonin – an unusual multifunctional protein in unusual locations
Frontiers in Cellular and Infection Microbiology, 2011 The L. pneumophila chaperonin, HtpB, was discovered as a highly immunogenic antigen, only a few years after the identification of L. pneumophila as the causative agent of Legionnaires’ disease.
Rafael A. eGarduno +3 more
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Frontiers in Plant Science, 2021 Microorganisms produce volatile compounds (VCs) with molecular masses of less than 300 Da that promote plant growth and photosynthesis. Recently, we have shown that small VCs of less than 45 Da other than CO2 are major determinants of plant responses to ...
Kinia Ameztoy +15 more
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