Results 41 to 50 of about 37,307 (249)
Chaperonin GroEL Reassembly: An Effect of Protein Ligands and Solvent Composition
Biomolecules, 2014 Chaperonin GroEL is a complex oligomeric heat shock protein (Hsp60) assisting the correct folding and assembly of other proteins in the cell. An intriguing question is how GroEL folds itself.
Nataliya Ryabova +3 more
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The Streptomyces coelicolor small ORF trpM stimulates growth and morphological development and exerts opposite effects on actinorhodin and calcium-dependent antibiotic production [PDF]
, 2020 In actinomycetes, antibiotic production is often associated with a morpho-physiological differentiation program that is regulated by complex molecular and metabolic networks. Many aspects of these regulatory circuits have been already elucidated and many
Alberto Vassallo +7 more
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Biomolecules, 2014 Numerous human diseases are caused by protein folding defects where the protein may become more susceptible to degradation or aggregation. Aberrant protein folding can affect the kinetic stability of the proteins even if these proteins appear to be ...
Ana R. Correia +3 more
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Frontiers in Molecular Biosciences, 2022 Recognition of diseases associated with mutations of the chaperone system genes, e.g., chaperonopathies, is on the rise. Hereditary and clinical aspects are established, but the impact of the mutation on the chaperone molecule and the mechanisms ...
Federica Scalia +26 more
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Extragenic Suppression analysis of TS mutations using Sec61p [PDF]
, 2007 During synthesis, secretory and membrane proteins are cotranslationally translocated into the lumen of the endoplasmic reticulum through an aqueous gated channel.
Sterling Smith
core +2 more sources
Heat Shock Protein 60 in Hepatocellular Carcinoma: Insights and Perspectives
Frontiers in Molecular Biosciences, 2020 Heat shock protein 60 (HSP60) is a mitochondrial chaperone that is implicated in physiological and pathological processes. For instance, it contributes to protein folding and stability, translocation of mitochondrial proteins, and apoptosis.
Abdullah Hoter +3 more
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Frontiers in Molecular Biosciences, 2023 Protein folding is often hampered by intermolecular protein aggregation, which can be prevented by a variety of chaperones in the cell. Bacterial chaperonin GroEL is a ring-shaped chaperone that forms complexes with its cochaperonin GroES, creating ...
Hideki Taguchi, Ayumi Koike-Takeshita
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Abstract OR-11: Conformations of a Viral Chaperonin in Different Nucleotide-Bound States [PDF]
International Journal of Biomedicine, 2019 Background: Chaperonins are protein complexes which assist nascent or misfolded proteins in attaining their native conformation. Several viral chaperonins have recently been found in the genomes of bacteriophages.
Tatiana B. Stanishneva-Konovalova +4 more
doaj +1 more source
The TRiCky Business of Protein Folding in Health and Disease
Frontiers in Cell and Developmental Biology, 2022 Maintenance of the cellular proteome or proteostasis is an essential process that when deregulated leads to diseases like neurological disorders and cancer.
Heba Ghozlan +5 more
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Oncogenic fusion protein BCR-FGFR1 requires the breakpoint cluster region-mediated oligomerization and chaperonin Hsp90 for activation. [PDF]
, 2020 Mutation and translocation of fibroblast growth factor receptors often lead to aberrant signaling and cancer. This work focuses on the t(8;22)(p11;q11) chromosomal translocation which creates the breakpoint cluster region (BCR) fibroblast growth factor ...
Bisom-Rapp, Ezra W +4 more
core +2 more sources