Results 41 to 50 of about 19,683 (209)

Single-molecule fluorescence studies of Protein Folding and Molecular Chaperones [PDF]

open access: yes, 2011
Folding of newly synthesized proteins is an essential part of protein biosynthesis and misfolding can result in protein aggregation which can also lead to several severe diseases.
Sikor, Martin
core   +1 more source

Probing the functional mechanism of Escherichia coli GroEL using circular permutation. [PDF]

open access: yesPLoS ONE, 2011
BACKGROUND: The Escherichia coli chaperonin GroEL subunit consists of three domains linked via two hinge regions, and each domain is responsible for a specific role in the functional mechanism.
Tomohiro Mizobata   +5 more
doaj   +1 more source

Myxococcus xanthus DK1622 Coordinates Expressions of the Duplicate groEL and Single groES Genes for Synergistic Functions of GroELs and GroES

open access: yesFrontiers 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

In Vivo Incorporation of Photoproteins into GroEL Chaperonin Retaining Major Structural and Functional Properties

open access: yesMolecules, 2023
The incorporation of photoproteins into proteins of interest allows the study of either their localization or intermolecular interactions in the cell.
Victor Marchenkov   +8 more
doaj   +1 more source

Groel

open access: yes, 2015
Alignment of the Buchnera Groel from ...
Don G. Miller (3313983)   +9 more
core   +1 more source

The Functional Differences between the GroEL Chaperonin of Escherichia coli and the HtpB Chaperonin of Legionella pneumophila Can Be Mapped to Specific Amino Acid Residues

open access: yesBiomolecules, 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

The Chaperonin GroEL Is Destabilized by Binding of ADP [PDF]

open access: yesJournal of Biological Chemistry, 1995
The urea-induced dissociation and subsequent conformational transitions of the nucleotide-bound form of GroEL were studied by light scattering, 4,4'-bis(1-anilino-8- naphthalenesulfonic acid) binding, and intrinsic tyrosine fluorescence. Magnesium ion alone (10 mM) stabilizes GroEL and leads to coordination of the structural transitions monitored by ...
B M, Gorovits, P M, Horowitz
openaire   +2 more sources

Engineering Microbial Particles for Next‐Generation Biomedical Platforms

open access: yesAdvanced Science, EarlyView.
Microbe‐derived particles (MDPs), which include extracellular vesicles, outer membrane vesicles, inclusion bodies, polysaccharide particles, and virus‐like particles, represent a rapidly expanding category of bioinspired nanomaterials. With their natural origin, intrinsic biocompatibility, and highly programmable functionality, MDPs serve as a ...
Yuting Li   +7 more
wiley   +1 more source

Heat Stress and Gut Microbiome Dynamics in Poultry: Interplay, Consequences, and Mitigation Strategies

open access: yesAnimal Research and One Health, EarlyView.
Heat stress disrupts gut microbial balance in poultry, impairing nutrient absorption and immunity. This review outlines the interplay between thermal stress and microbiome dynamics and discusses integrative mitigation strategies, probiotics, phytogenics, cooling systems, and genetic adaptation to enhance poultry resilience.
O. E. Oke   +9 more
wiley   +1 more source

Suppression of amyloid fibrils using the GroEL apical domain [PDF]

open access: yes
In E. coli cells, rescue of non-native proteins and promotion of native state structure is assisted by the chaperonin GroEL. An important key to this activity lies in the structure of the apical domain of GroEL (GroEL-AD) (residue 191–376), which ...
80335504   +21 more
core   +1 more source

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