Articles with "chaperone like" as a keyword



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Glycosylation differentially modulates membranolytic and chaperone-like activities of PDC-109, the major protein of bovine seminal plasma.

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Published in 2019 at "Biochemical and biophysical research communications"

DOI: 10.1016/j.bbrc.2019.02.002

Abstract: The major bovine seminal plasma protein, PDC-109, is a mixture of glycosylated (BSP-A1) and non-glycosylated (BSP-A2) isoforms of a 109-residue long polypeptide. It binds to spermatozoa by specifically recognizing choline phospholipids on the plasma membrane… read more here.

Keywords: like activities; pdc 109; chaperone like; membrane ... See more keywords
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Chaperone-like Activity of Calnuc Prevents Amyloid Aggregation.

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Published in 2017 at "Biochemistry"

DOI: 10.1021/acs.biochem.6b00660

Abstract: Calnuc is a ubiquitously expressed protein of the EF-hand Ca2+-binding superfamily. Previous studies have implicated it in Ca2+-sensitive physiological processes, whereas details of its function and involvement in human diseases are lacking. Drawing upon the… read more here.

Keywords: aggregation; disease; chaperone like; activity ... See more keywords
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Stabilization of Immobilized Enzymes via the Chaperone-Like Activity of Mixed Lipid Bilayers.

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Published in 2018 at "ACS applied materials & interfaces"

DOI: 10.1021/acsami.8b05523

Abstract: Biomimetic lipid bilayers represent intriguing materials for enzyme immobilization, which is critical for many biotechnological applications. Here, through the creation of mixed lipid bilayers, the retention of immobilized enzyme structures and catalytic activity are dramatically… read more here.

Keywords: like activity; activity mixed; lipid bilayers; mixed lipid ... See more keywords
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Discerning Modulation of α-Synuclein Amyloid Assembly by α-Crystallin.

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Published in 2023 at "ACS chemical neuroscience"

DOI: 10.1021/acschemneuro.3c00052

Abstract: Altered protein folding leading to the formation of structured aggregates such as amyloid fibrils has gained significant attention due to its association with neurodegenerative diseases. α-Synuclein, a small intrinsically disordered protein, gets transformed into amyloid… read more here.

Keywords: crystallin; modulation synuclein; chaperone like; synuclein amyloid ... See more keywords
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The chaperone-like activity of the hepatitis C virus IRES and CRE elements regulates genome dimerization

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Published in 2017 at "Scientific Reports"

DOI: 10.1038/srep43415

Abstract: The RNA genome of the hepatitis C virus (HCV) establishes a network of long-distance RNA-RNA interactions that direct the progression of the infective cycle. This work shows that the dimerization of the viral genome, which… read more here.

Keywords: ires cre; genome dimerization; hepatitis virus; chaperone like ... See more keywords
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Ocular protein optineurin shows reversibility from unfolded states and exhibits chaperone-like activity

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Published in 2023 at "RSC Advances"

DOI: 10.1039/d2ra07931c

Abstract: Optineurin (OPTN) is a multifunctional, ubiquitously expressed cytoplasmic protein, mutants of which are associated with primary open-angle glaucoma (POAG) and amyotrophic lateral sclerosis (ALS). The most abundant heat shock protein crystallin, known for its remarkable… read more here.

Keywords: ocular tissues; ocular protein; chaperone like; activity ... See more keywords
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Investigating Chaperone like Activity of Green Silver Nanoparticles: Possible Implications in Drug Development

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Published in 2022 at "Molecules"

DOI: 10.3390/molecules27030944

Abstract: Protein aggregation and amyloidogenesis have been associated with several neurodegenerative disorders like Alzheimer’s, Parkinson’s etc. Unfortunately, there are still no proper drugs and no effective treatment available. Due to the unique properties of noble metallic… read more here.

Keywords: aggregation; chaperone like; silver nanoparticles; green silver ... See more keywords