Articles with "molecular chaperone" as a keyword



Photo from wikipedia

New insights into molecular chaperone TRAP1 as a feasible target for future cancer treatments.

Sign Up to like & get
recommendations!
Published in 2020 at "Life sciences"

DOI: 10.1016/j.lfs.2020.117737

Abstract: Tumor necrosis factor receptor-associated protein 1 (TRAP1), a molecular chaperone, is a major member of the mitochondrial heat shock protein 90 (Hsp90) family. Studies have shown that TRAP1 can prevent hypoxia-induced damage to cardiomyocytes, maintain… read more here.

Keywords: chaperone; chaperone trap1; cancer; molecular chaperone ... See more keywords
Photo from wikipedia

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

Sign Up to like & get
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
Photo from wikipedia

Conformational dynamics modulate the catalytic activity of the molecular chaperone Hsp90

Sign Up to like & get
recommendations!
Published in 2020 at "Nature Communications"

DOI: 10.1038/s41467-020-15050-0

Abstract: The heat shock protein 90 (Hsp90) is a molecular chaperone that employs the free energy of ATP hydrolysis to control the folding and activation of several client proteins in the eukaryotic cell. To elucidate how… read more here.

Keywords: conformational dynamics; chaperone; chaperone hsp90; catalytic activity ... See more keywords
Photo by robbie36 from unsplash

Catalysis of proline isomerization and molecular chaperone activity in a tug-of-war

Sign Up to like & get
recommendations!
Published in 2020 at "Nature Communications"

DOI: 10.1038/s41467-020-19844-0

Abstract: Catalysis of cis/trans isomerization of prolines is important for the activity and misfolding of intrinsically disordered proteins. Catalysis is achieved by peptidylprolyl isomerases, a superfamily of molecular chaperones. Here, we provide atomic insight into a… read more here.

Keywords: proline isomerization; molecular chaperone; activity; catalysis ... See more keywords
Photo from wikipedia

Antagonistic evolution of an antibiotic and its molecular chaperone: how to maintain a vital ectosymbiosis in a highly fluctuating habitat

Sign Up to like & get
recommendations!
Published in 2017 at "Scientific Reports"

DOI: 10.1038/s41598-017-01626-2

Abstract: Evolution of antimicrobial peptides (AMPs) has been shown to be driven by recurrent duplications and balancing/positive selection in response to new or altered bacterial pathogens. We use Alvinella pompejana, the most eurythermal animal known on… read more here.

Keywords: chaperone; antagonistic evolution; vital ectosymbiosis; molecular chaperone ... See more keywords
Photo by clemono from unsplash

Active-site plasticity revealed in the asymmetric dimer of AnPrx6 the 1-Cys peroxiredoxin and molecular chaperone from Anabaena sp. PCC 7120

Sign Up to like & get
recommendations!
Published in 2017 at "Scientific Reports"

DOI: 10.1038/s41598-017-17044-3

Abstract: Peroxiredoxins (Prxs) are vital regulators of intracellular reactive oxygen species levels in all living organisms. Their activity depends on one or two catalytically active cysteine residues, the peroxidatic Cys (CP) and, if present, the resolving… read more here.

Keywords: cys; anabaena; active site; prxs ... See more keywords
Photo from wikipedia

Molecular chaperone prefoldin-assisted biosynthesis of gold nanoparticles with improved size distribution and dispersion.

Sign Up to like & get
recommendations!
Published in 2019 at "Biomaterials science"

DOI: 10.1039/c8bm01026a

Abstract: Here we report a novel aspect of molecular chaperone prefoldin (PFD) as a biomaterial in the biocatalytic synthesis of gold nanoparticles (AuNPs) using glycerol dehydrogenase (GLD). We found that PFD could inhibit the aggregation of… read more here.

Keywords: size distribution; molecular chaperone; gold nanoparticles; chaperone prefoldin ... See more keywords
Photo by dkoi from unsplash

The molecular chaperone Hsp90α deficiency causes retinal degeneration by disrupting Golgi organization and vesicle transportation in photoreceptors

Sign Up to like & get
recommendations!
Published in 2019 at "Journal of Molecular Cell Biology"

DOI: 10.1093/jmcb/mjz048

Abstract: Abstract Heat shock protein 90 (Hsp90) is an abundant molecular chaperone with two isoforms, Hsp90α and Hsp90β. Hsp90β deficiency causes embryonic lethality, whereas Hsp90α deficiency causes few abnormities except male sterility. In this paper, we… read more here.

Keywords: hsp90; deficiency causes; molecular chaperone; vesicle transportation ... See more keywords
Photo by marissacristina from unsplash

The molecular chaperone Hsp90 maintains Golgi organization and vesicular trafficking by regulating microtubule stability

Sign Up to like & get
recommendations!
Published in 2019 at "Journal of Molecular Cell Biology"

DOI: 10.1093/jmcb/mjz093

Abstract: Abstract Hsp90 is an abundant and special molecular chaperone considered to be the regulator of many transcription factors and signaling kinases. Its high abundance is indicative of its involvement in some more fundamental processes. In… read more here.

Keywords: microtubule; hsp90; organization vesicular; golgi organization ... See more keywords
Photo from wikipedia

HspB1 phosphorylation regulates its intramolecular dynamics and mechanosensitive molecular chaperone interaction with filamin C

Sign Up to like & get
recommendations!
Published in 2019 at "Science Advances"

DOI: 10.1126/sciadv.aav8421

Abstract: The molecular chaperone HspB1 regulates the biomechanical extension of the heart muscle protein filamin C upon stress. Mechanical force–induced conformational changes in proteins underpin a variety of physiological functions, typified in muscle contractile machinery. Mutations… read more here.

Keywords: chaperone; filamin; hspb1 phosphorylation; interaction ... See more keywords
Photo from wikipedia

Prognostic model and immunotherapy prediction based on molecular chaperone-related lncRNAs in lung adenocarcinoma

Sign Up to like & get
recommendations!
Published in 2022 at "Frontiers in Genetics"

DOI: 10.3389/fgene.2022.975905

Abstract: Introduction: Molecular chaperones and long non-coding RNAs (lncRNAs) have been confirmed to be closely related to the occurrence and development of tumors, especially lung cancer. Our study aimed to construct a kind of molecular chaperone-related… read more here.

Keywords: immunotherapy; analysis; risk; model ... See more keywords