Results 71 to 80 of about 30,272 (208)

Putting handcuffs on the chaperonin GroEL [PDF]

open access: yesProceedings of the National Academy of Sciences, 2013
Oligomeric, ring-shaped nano-machines that are fueled by ATP are ubiquitous in all three kingdoms of life and are involved in a wide range of processes that include, for example, protein folding, protein degradation, DNA and RNA remodeling, and protein insertion into membranes (for review, see ref. 1).
openaire   +2 more sources

Detection of Anaplasma phagocytophilum and Babesia aktasi in a wild bezoar goat (Capra aegagrus): Overlap with domestic goat strains

open access: yesMedical and Veterinary Entomology, Volume 40, Issue 1, Page 190-197, March 2026.
This study provides the first molecular detection of tick‐borne pathogens in Capra aegagrus. Genetic analysis reveals similarities between Babesia aktasi and Anaplasma phagocytophilum strains in bezoar and domestic goats, indicating potential pathogen exchange.
Aykut Zerek   +4 more
wiley   +1 more source

GroEL/GroES Mechanism of Action and Formation of Complexes During Reaction Cycle: A Matter of Debate [PDF]

open access: yesJournal of Stress Physiology & Biochemistry
The bacterial chaperonin GroEL alongwith its cochaperonin GroES is the paradigmatic molecular chaperone machine for protein folding. Most bacterial proteins require the GroEL chaperonin for proper folding.
Sutrisha Kundu   +2 more
doaj  

Epitopes of Immunoreactive Proteins of Streptococcus Agalactiae: Enolase, Inosine 5′-Monophosphate Dehydrogenase and Molecular Chaperone GroEL

open access: yesFrontiers in Cellular and Infection Microbiology, 2018
Three Streptococcus agalactiae (group B streptococci, GBS) immunoreactive proteins: enolase (47.4 kDa), inosine 5′-monophosphate dehydrogenase (IMPDH) (53 kDa) and molecular chaperone GroEL (57 kDa) were subjected to investigation.
Anna Dobrut   +7 more
doaj   +1 more source

GroEL Secreted from Bacillus subtilis Natto Exerted a Crucial Role for Anti-Inflammatory IL-10 Induction in THP-1 Cells

open access: yesMicroorganisms, 2023
Although diverse immunomodulatory reactions of probiotic bacteria have been reported, this effect via Bacillus subtilis natto remains unclear, despite its long consumption history in Japan and usage in Natto production.
Taisuke Uesugi   +3 more
doaj   +1 more source

Adaptive response of neonatal sepsis-derived Group B Streptococcus to bilirubin [PDF]

open access: yes, 2018
This work was funded by the Neonatal Unit Endowment Fund, Aberdeen Maternity Hospital. RH is funded by a career researcher fellowship from NHS Research Scotland. SG was funded by the MRC Flagship PhD programme.
Berry, Susan   +10 more
core   +4 more sources

Ticks and tick‐borne bacterial pathogens found on hard ticks (Acari: Ixodidae) on cattle in the Central River region of The Gambia

open access: yesMedical and Veterinary Entomology, Volume 40, Issue 1, Page 91-100, March 2026.
First detection of Ehrlichia minasensis, Anaplasma marginale and hemotropic Mycoplasma spp. in cattle in The Gambia. Identification of four tick species, with Hyalomma marginatum being the most common. 15.6% of ticks tested positive for tick‐borne pathogens, including Ehrlichia spp., A. marginale and hemotropic Mycoplasma spp.
Alpha Kargbo   +9 more
wiley   +1 more source

Revealing taxonomy, activity, and substrate assimilation in mixed bacterial communities by GroEL-proteotyping-based stable isotope probing

open access: yesiScience
Summary: Protein-based stable isotope probing (protein-SIP) can link microbial taxa to substrate assimilation. Traditionally, protein-SIP requires a sample-specific metagenome-derived database for samples with unknown composition. Here, we describe GroEL-
Simon Klaes   +4 more
doaj   +1 more source

Antifolding activity of hsp60 couples protein import into the mitochondrial matrix with export to the intermembrane space [PDF]

open access: yes, 1992
Cytochrome b2 reaches the intermembrane space of mitochondria by transport into the matrix followed by export across the inner membrane. While in the matrix, the protein interacts with hsp60, which arrests its folding prior to export.
Guiard, Bernard   +6 more
core   +1 more source

GroEL Binds Artificial Proteins with Random Sequences [PDF]

open access: yesJournal of Biological Chemistry, 2000
Chaperonin GroEL from Escherichia coli binds to the non-native states of many unrelated proteins, and GroEL-recognizable structural features have been argued. As model substrate proteins of GroEL, we used seven artificial proteins (138 approximately 141 residues), each of which has a unique but randomly chosen amino acid sequence and no propensity to ...
Katsuhiko Aoki   +4 more
openaire   +2 more sources

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