Results 21 to 30 of about 4,302 (172)
Scientific Reports, 2021 Plasmodium falciparum harbors group 1 and group 2 chaperonin systems to mediate the folding of cellular proteins in different cellular locations. Two distinct group 1 chaperonins operate in the organelles of mitochondria and apicoplasts, while group 2 ...
Brian Nguyen +4 more
doaj +1 more source
Frontiers in Microbiology, 2017 Chaperonin GroEL (Cpn60) requires cofactor GroES (Cpn10) for protein refolding in bacteria that possess single groEL and groES genes in a bicistronic groESL operon.
Yue-zhong Li +6 more
doaj +1 more source
The ribosome modulates folding inside the ribosomal exit tunnel
Communications Biology, 2021 Wruck et al. investigate the folding of the small zinc-finger domain ADR1a inside and at the vestibule of the ribosomal tunnel, using optical tweezers, single-molecule FRET, and molecular dynamics simulations.
Florian Wruck +6 more
doaj +1 more source
Biomolecules, 2021 Group I chaperonins are a highly conserved family of essential proteins that self-assemble into molecular nanoboxes that mediate the folding of cytoplasmic proteins in bacteria and organelles.
Karla N. Valenzuela-Valderas +3 more
doaj +1 more source
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
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
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
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
doaj +1 more source