Results 31 to 40 of about 8,317 (219)
A human CCT5 gene mutation causing distal neuropathy impairs hexadecamer assembly in an archaeal model [PDF]
, 2014 Chaperonins mediate protein folding in a cavity formed by multisubunit rings. The human CCT has eight non-identical subunits and the His147Arg mutation in one subunit, CCT5, causes neuropathy.
ALMERICO, Anna Maria +10 more
core +1 more source
Novel insights into the Thaumarchaeota in the deepest oceans: their metabolism and potential adaptation mechanisms [PDF]
, 2020 Background: Marine Group I (MGI) Thaumarchaeota, which play key roles in the global biogeochemical cycling of nitrogen and carbon (ammonia oxidizers), thrive in the aphotic deep sea with massive populations.
Lehtovirta-Morley, Laura +8 more
core +2 more sources
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
doaj +1 more source
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
doaj +1 more source
Protein sorting to mitochondria [PDF]
, 1990 According to the endosymbiont hypothesis, mitochondria have lost the autonomy of their prokaryotic ancestors. They have to import most of their proteins from the cytosol because the mitochondrial genome codes for only a small percentage of the ...
Hartl, Franz-Ulrich, Neupert, Walter
core +1 more source
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
doaj +1 more source
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
doaj +1 more source
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
Chaperonin-Inspired pH Protection by Mesoporous Silica SBA-15 on Myoglobin and Lysozyme [PDF]
, 2016 While enzymes are valuable tools in many fields of biotechnology, they are fragile and must be protected against denaturing conditions such as unfavorable solution pH.
Coppens, MO, Liu, J, Lynch, MM, Nigra, M
core +1 more source
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
doaj +1 more source