Results 51 to 60 of about 8,360 (214)
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
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
Single-molecule fluorescence polarization study of conformational change in archaeal group II chaperonin. [PDF]
PLoS ONE, 2011 Group II chaperonins found in archaea and in eukaryotic cytosol mediate protein folding without a GroES-like cofactor. The function of the cofactor is substituted by the helical protrusion at the tip of the apical domain, which forms a built-in lid on ...
Ryo Iizuka +3 more
doaj +1 more source
Journal of Integrative Plant Biology, EarlyView.Abscisic acid signaling homeostasis is essential for seed storability. The molecular chaperone OsCPN10a enhances rice seed storability by forming a trimeric chaperone complex with OsCPN20‐OsHSP60‐3B that attenuates abscisic acid signaling via direct interaction with OsPYL10‐OsABIL1, thereby maintaining starch integrity and offering a promising target ...
Sufeng Liao +13 more
wiley +1 more source
The refolding of recombinant human liver methylmalonyl-CoA mutase from inclusion bodies produced in Escherichia coli : a thesis presented in partial fulfilment of the requirements for the degree of Master of Science in Biochemistry at Massey University [PDF]
, 1998 Human methylmalonyl-CoA mutase (hMCM) is an adenosylcobalamin-dependent enzyme that catalyses the structural rearrangement of (R)-methylmalonyl-CoA to succinyl-CoA as pan of the catabolism of the branched chain amino acids valine, leucine and isoleucine,
Hayes, Michelle Marie
core
A comprehensive analysis of prefoldins and their implication in cancer
iScience, 2021 Summary: Prefoldins (PFDNs) are evolutionary conserved co-chaperones, initially discovered in archaea but universally present in eukaryotes. PFDNs are prevalently organized into hetero-hexameric complexes.
Irene Herranz-Montoya +2 more
doaj +1 more source
New Phytologist, EarlyView.Summary Experimental evolution under elevated temperatures has generated heat‐evolved (HE) strains of Symbiodiniaceae that enhance coral bleaching tolerance. However, the biomolecular mechanisms underlying this resilience remain poorly understood. We conducted a laboratory heat‐stress experiment and applied synchrotron‐based Fourier transform infrared (
Bede G. Johnston +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
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
Nature Communications, 2017 Chaperonins (CPNs) are ATP-dependent protein-folding machines. Here the authors present the open and closed crystal structures of a Group III CPN from the thermophilic bacterium Carboxydothermus hydrogenoformans, discuss its mechanism and structurally ...
Young Jun An +8 more
doaj +1 more source