Results 11 to 20 of about 8,317 (219)

Chaperonins [PDF]

open access: yesCurrent Biology, 1999
Gizachew, D.   +4 more
core   +4 more sources

Chaperonins [PDF]

open access: yesCurrent Opinion in Structural Biology, 1998
Molecular chaperones are essential to all living organisms. Their key role consists of mediating protein folding within the cell. Recent functional studies have provided more detailed information about the function and regulation of the chaperone network.
N A, Ranson, H E, White, H R, Saibil
openaire   +4 more sources

Local Flexibility of a New Single-Ring Chaperonin Encoded by Bacteriophage AR9 Bacillus subtilis

open access: yesBiomedicines, 2022
Chaperonins, a family of molecular chaperones, assist protein folding in all domains of life. They are classified into two groups: bacterial variants and those present in endosymbiotic organelles of eukaryotes belong to group I, while group II includes ...
Olga S. Sokolova   +7 more
doaj   +1 more source

The Possible Role of the Type I Chaperonins in Human Insulin Self-Association

open access: yesLife, 2022
Insulin is a hormone that attends to energy metabolism by regulating glucose levels in the bloodstream. It is synthesised within pancreas beta-cells where, before being released into the serum, it is stored in granules as hexamers coordinated by Zn2+ and
Federica Pizzo   +6 more
doaj   +1 more source

Back to GroEL-Assisted Protein Folding: GroES Binding-Induced Displacement of Denatured Proteins from GroEL to Bulk Solution

open access: yesBiomolecules, 2020
The main events in chaperone-assisted protein folding are the binding and ligand-induced release of substrate proteins. Here, we studied the location of denatured proteins previously bound to the GroEL chaperonin resulting from the action of the GroES co-
Victor Marchenkov   +4 more
doaj   +1 more source

Identification of elements that dictate the specificity of mitochondrial Hsp60 for its co-chaperonin. [PDF]

open access: yesPLoS ONE, 2012
Type I chaperonins (cpn60/Hsp60) are essential proteins that mediate the folding of proteins in bacteria, chloroplast and mitochondria. Despite the high sequence homology among chaperonins, the mitochondrial chaperonin system has developed unique ...
Avital Parnas   +8 more
doaj   +1 more source

Are Gastrointestinal Microorganisms Involved in the Onset and Development of Amyloid Neurodegenerative Diseases?

open access: yesMicrobiology Research, 2023
This review discusses a few examples of specific mechanisms mediating the contribution of the GIT microbiota to the development of amyloid neurodegenerative diseases caused by the pathologic transformation of prion protein, or alpha-synuclein. The effect
Vladimir I. Muronetz   +3 more
doaj   +1 more source

From lab to field : yield stability and shade avoidance genes are massively differentially expressed in the field [PDF]

open access: yes, 2020
To unravel molecular mechanisms with the ultimate goal to achieve improved stress resilience or increased yield, plants are often studied under highly controlled conditions in which stresses are applied and in which growth‐ or architecture‐related traits
De Block, Jolien   +6 more
core   +2 more sources

Single-Ring Intermediates Are Essential for Some Chaperonins

open access: yesFrontiers in Molecular Biosciences, 2018
Chaperonins are macromolecular complexes found throughout all kingdoms of life that assist unfolded proteins reach a biologically active state. Historically, chaperonins have been classified into two groups based on sequence, subunit structure, and the ...
Jay M. Bhatt   +6 more
doaj   +1 more source

Antagonistic Regulation by CPN60A and CLPC1 of TRXL1 that Regulates MDH Activity Leading to Plant Disease Resistance and Thermotolerance

open access: yesCell Reports, 2020
Summary: Global warming and emerging plant diseases challenge agricultural food/feed production. We identify mechanism(s) regulating both plant thermotolerance and disease resistance.
Bikram Datt Pant   +4 more
doaj   +1 more source

Home - About - Disclaimer - Privacy