Results 41 to 50 of about 5,379 (199)
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 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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Reconstitution of Pure Chaperonin Hetero-Oligomer Preparations in Vitro by Temperature Modulation
Frontiers in Molecular Biosciences, 2018 Chaperonins are large, essential, oligomers that facilitate protein folding in chloroplasts, mitochondria, and eubacteria. Plant chloroplast chaperonins are comprised of multiple homologous subunits that exhibit unique properties.
Anna Vitlin Gruber +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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Mechanism and functional analysis of chaperonins of Mycobacterium marinum [PDF]
, 2023 Mycobacterial chaperonins have been demonstrated to play an important role in immunomodulation. Both the chaperonins of M. tuberculosis have been revealed to be involved directly or indirectly in pathology of tuberculosis.
Rafique Butt, Shahida
core +5 more sources
Structural basis for the structural dynamics of human mitochondrial chaperonin mHsp60
Scientific Reports, 2021 Human mitochondrial chaperonin mHsp60 is essential for mitochondrial function by assisting folding of mitochondrial proteins. Unlike the double-ring bacterial GroEL, mHsp60 exists as a heptameric ring that is unstable and dissociates to subunits.
Joseph Che-Yen Wang, Lingling Chen
doaj +1 more source
PLoS ONE, 2015 Chaperonins are large ring shaped oligomers that facilitate protein folding by encapsulation within a central cavity. All chaperonins possess flexible C-termini which protrude from the equatorial domain of each subunit into the central cavity ...
Kevin M Dalton +2 more
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The VHL tumor suppressor at the crossroad of protein folding, aggregation, and cancer
Molecular Oncology, EarlyView.Mutations, environmental stress, and chaperone dysfunction can destabilize pVHL, promoting its conversion from the native folded state into amyloid‐like assemblies. This transition may contribute to protein storage, cell dormancy, survival, and drug resistance.
Lara Abad +2 more
wiley +1 more source
Dynamics, flexibility, and allostery in molecular chaperonins [PDF]
, 2015 The chaperonins are a family of molecular chaperones present in all three kingdoms of life. They are classified into Group I and Group II. Group I consists of the bacterial variants (GroEL) and the eukaryotic ones from mitochondria and chloroplasts ...
Cuellar, Jorge +3 more
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Cryo-EM structure of human mitochondrial HSPD1
iScience, 2021 Summary: Chaperonins play an important role in folding newly synthesized or translocated proteins in all organisms. The bacterial chaperonin GroEL has served as a model system for the understanding of these proteins.
David P. Klebl +7 more
doaj +1 more source