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   Articles with "chaperone activity" as a keyword



Effect of evolution of the C‐terminal region on chaperone activity of Hsp70

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recommendations! Published in 2022 at "Protein Science"

DOI: 10.1002/pro.4549

Abstract: Dynamic interdomain interactions within the Hsp70 protein is the basis for the allosteric and functional properties of Hsp70s. While Hsp70s are generally conserved in terms of structure, allosteric behavior, and some overlapping functions, Hsp70s also… read more here.

Keywords: hsp70 members; terminal region; region; chaperone activity ... See more keywords

Cage-like polyhedrons of DegQ from Cytophaga hutchinsonii show stable proteolytic activity and strong chaperone activity

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recommendations! Published in 2020 at "Biochemical Engineering Journal"

DOI: 10.1016/j.bej.2020.107585

Abstract: Abstract DegQ is a member of highly conserved htrA family proteins, acting as a chaperone-protease facilitating refolding or degradation of periplasmic misfolded proteins. In the current regulatory model of DegQ, the resting state was inactive… read more here.

Keywords: cage like; like polyhedrons; chaperone activity; cage ... See more keywords

DJ-1 Molecular Chaperone Activity Depresses Tau Aggregation Propensity through Interaction with Monomers.

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recommendations! Published in 2023 at "Biochemistry"

DOI: 10.1021/acs.biochem.2c00581

Abstract: Tau aggregate-bearing lesions are pathological markers and potential mediators of tauopathic neurodegenerative diseases, including Alzheimer's disease. The molecular chaperone DJ-1 colocalizes with tau pathology in these disorders, but it has been unclear what functional link… read more here.

Keywords: chaperone; tau aggregation; chaperone activity; activity ... See more keywords

Conversion of a soluble protein into a potent chaperone in vivo

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recommendations! Published in 2019 at "Scientific Reports"

DOI: 10.1038/s41598-019-39158-6

Abstract: Molecular chaperones play an important role in cellular protein-folding assistance and aggregation inhibition. As a different but complementary model, we previously proposed that, in general, soluble cellular macromolecules with large excluded volume and surface charges… read more here.

Keywords: protein; conversion soluble; soluble protein; chaperone activity ... See more keywords

Disordered region encodes α-crystallin chaperone activity toward lens client γD-crystallin.

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recommendations! Published in 2023 at "Proceedings of the National Academy of Sciences of the United States of America"

DOI: 10.1073/pnas.2213765120

Abstract: Small heat-shock proteins (sHSPs) are a widely expressed family of ATP-independent molecular chaperones that are among the first responders to cellular stress. Mechanisms by which sHSPs delay aggregation of client proteins remain undefined. sHSPs have… read more here.

Keywords: hspb4 hspb5; activity toward; crystallin; chaperone ... See more keywords

A potential histone-chaperone activity for the MIER1 histone deacetylase complex.

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recommendations! Published in 2023 at "Nucleic acids research"

DOI: 10.1093/nar/gkad294

Abstract: Histone deacetylases 1 and 2 (HDAC1/2) serve as the catalytic subunit of six distinct families of nuclear complexes. These complexes repress gene transcription through removing acetyl groups from lysine residues in histone tails. In addition… read more here.

Keywords: activity mier1; histone; deacetylase; chaperone activity ... See more keywords

Role of Molecular Interactions and Oligomerization in Chaperone Activity of Recombinant Acr from Mycobacterium tuberculosis

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recommendations! Published in 2019 at "Iranian Journal of Biotechnology"

DOI: 10.29252/ijb.2370

Abstract: Background: The chaperone activity of Mycobacterium tuberculosis Acr is an important function that helps to prevent misfolding of protein substrates inside the host, especially in conditions of hypoxia. Objectives: The aim of this study was… read more here.

Keywords: gel filtered; recombinant acr; gel filtration; chaperone activity ... See more keywords

Large-Size Subunit Catalases Are Chimeric Proteins: A H2O2 Selecting Domain with Catalase Activity Fused to a Hsp31-Derived Domain Conferring Protein Stability and Chaperone Activity

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recommendations! Published in 2022 at "Antioxidants"

DOI: 10.3390/antiox11050979

Abstract: Bacterial and fungal large-size subunit catalases (LSCs) are like small-size subunit catalases (SSCs) but have an additional C-terminal domain (CT). The catalytic domain is conserved at both primary sequence and structural levels and its amino… read more here.

Keywords: subunit catalases; chaperone activity; domain; size subunit ... See more keywords

Chaperone Activity and Protective Effect against Aβ-Induced Cytotoxicity of Artocarpus camansi Blanco and Amaranthus dubius Mart. ex Thell Seed Protein Extracts

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recommendations! Published in 2023 at "Pharmaceuticals"

DOI: 10.3390/ph16060820

Abstract: Alzheimer’s disease (AD) is the most common type of dementia and is listed as the sixth-leading cause of death in the United States. Recent findings have linked AD to the aggregation of amyloid beta peptides… read more here.

Keywords: chaperone activity; seed; effect; protein extracts ... See more keywords