Results 41 to 50 of about 8,317 (219)
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
Cetacean Host-Pathogen Interaction(s): Critical Knowledge Gaps [PDF]
, 2018 Within the broad range of viral and non-viral pathogens infecting cetaceans, Cetacean Morbillivirus (CeMV), Herpesvirus (HV), Brucella ceti, and Toxoplasma gondii are of special concern, due to their impact(s) on the health and conservation of free ...
Centelleghe, Cinzia +2 more
core +2 more sources
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
doaj +1 more source
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
Chaperonin-mediated Protein Folding [PDF]
Journal of Biological Chemistry, 2011 We have been studying chaperonins these past twenty years through an initial discovery of an action in protein folding, analysis of structure, and elucidation of mechanism. Some of the highlights of these studies were presented recently upon sharing the honor of the 2013 Herbert Tabor Award with my early collaborator, Ulrich Hartl, at the annual ...
openaire +3 more sources
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
doaj +1 more source
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
Proteostasis of organelles in aging and disease
The FEBS Journal, EarlyView.Cells rely on regulated proteostasis mechanisms to keep their internal compartments functioning properly. When these mechanisms fail, damaged proteins accumulate, disrupting organelles, such as the nucleus, mitochondria, endoplasmic reticulum, Golgi, and lysosomes, as well as membraneless organelles, such as stress granules, processing bodies, the ...
Yara Nabawi +5 more
wiley +1 more source
Soluble oligomerization provides a beneficial fitness effect on destabilizing mutations. [PDF]
, 2011 Protein stability is widely recognized as a major evolutionary constraint. However, the relation between mutation-induced perturbations of protein stability and biological fitness has remained elusive.
Eugene Shakhnovich, Shimon Bershtein
core +1 more source
Insect Molecular Biology, EarlyView.A small heat‐shock protein (HSP16) previously reported as insect‐derived in Bemisia tabaci actually originates from a fungal species of the genus Wallemia. BLAST, genome survey and phylogenetic analyses support the fungal origin and clarify persistent misattribution in the literature.
Jesús Navas‐Castillo +1 more
wiley +1 more source