Results 191 to 200 of about 24,211 (206)
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Conformational states of ribulose bisphosphate carboxylase and their interaction with chaperonin 60
Biochemistry, 1992Conformational states of ribulosebisphosphate carboxylase (Rubisco) from Rhodospirillum rubrum were examined by far-UV circular dichroism (CD), tryptophan fluorescence, and 1-anilino-naphthalenesulfonate (ANS) binding. At pH 2 and low ionic strength (I = 0.01), Rubisco adopts an unfolded, monomeric conformation (UA1 state) as judged by far-UV CD and ...
S M, van der Vies +4 more
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Chaperonin 60 and mitochondrial disease in Dictyostelium.
Journal of muscle research and cell motility, 2003The single Dictyostelium chaperonin 60 gene, hspA, was cloned, sequenced and characterized. Sequence comparisons and a three-dimensional model for the structure of the encoded protein showed that it exhibits the conserved sequence and structural features expected for its role as the Dictyostelium mitochondrial chaperonin 60. Dictyostelium hspA contains
Kotsifas, Martha. +4 more
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Chaperonin 60 regulation of SOX9 ubiquitination mitigates the development of knee osteoarthritis
Journal of Molecular Medicine, 2016Articular cartilage integrity loss is a prominently deleterious feature of osteoarthritis (OA). The mechanistic underlying the development of OA warrants characterization. Heat shock proteins (HSPs), members of the chaperone family, reportedly orchestrate tissue homeostasis and remodeling in response to detrimental stress.
Jih-Yang, Ko +3 more
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Insect Symbiotic Bacterial GroEL (Chaperonin 60) and Plant Virus Transmission
2013GroEL is a multifunctional protein belonging to the conspicuous family of chaperones active in prokaryotic and eukaryotic cells. GroEL of Escherichia coli is a heat shock-like protein (Hsp60). It is involved in the correct folding of newly synthesized proteins, and participates in protein aggregation and in repair of damaged proteins.
Rena Gorovits, Henryk Czosnek
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Histoplasma capsulatum Chaperonin 60: A Novel Adhesin and Vaccine Candidate
2013HSP60 has a key role in immunoregulation and the abundance of HSP60 proteins in mammalian and microbial cells impacts diverse biological functions in both. Therefore, it may be essential for innate immune cells to distinguish HSP60 proteins by their endogenous or infectious origin.
Joshua Daniel Nosanchuk +1 more
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Implication de la chaperonine 60 (HSP60) dans la sécrétion pancréatique
1996Mémoire numérisé par la Direction des bibliothèques de l'Université de Montréal.
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Mycobacterium tuberculosis Chaperonin 60 Paralogues Contribute to Virulence in Tuberculosis
2013With the human population reaching seven billion it is estimated that one third of this population are infected with the causative agent of tuberculosis, Mycobacterium tuberculosis. Curiously, this bacterium has evolved to survive within the macrophage, a key cell population involved in cell-mediated immunity to infectious bacteria.
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Evaluation of Heat Shock Protein 60 (HSP60) Chaperonin in Oncology
2019Heat shock proteins (Hsp) are a group of chaperonin that are increased production at cellular level in cellular stress situations. These stress include such as heat, infection, inflammation, many toxins such as ethanol, arsenic, some metals, ultraviolet light, some oncogenes.
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[17] Purification of yeast mitochondrial chaperonin 60 and co-chaperonin 10
1998Yves Dubaquié +2 more
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