LAUSR

About LAUSR
Donate
Contact Us

Follow us:

You are not signed in:

Sign Up!


   Articles with "molecular chaperone" as a keyword



The components of the AhR‐molecular chaperone complex differ depending on whether the ligands are toxic or non‐toxic

Sign Up to like & get
recommendations! Published in 2024 at "FEBS Letters"

DOI: 10.1002/1873-3468.14871

Abstract: The aryl hydrocarbon receptor (AhR) forms a complex with the HSP90‐XAP2‐p23 molecular chaperone when the cells are exposed to toxic compounds. Recently, 1,4‐dihydroxy‐2‐naphthoic acid (DHNA) was reported to be an AhR ligand. Here, we investigated… read more here.

Keywords: molecular chaperone; hsp90 xap2; ahr molecular; chaperone ... See more keywords

GHCU, a Molecular Chaperone, Regulates Leaf Curling by Modulating the Distribution of KNGH1 in Cotton (Adv. Sci. 26/2024)

Sign Up to like & get
recommendations! Published in 2024 at "Advanced Science"

DOI: 10.1002/advs.202470154

Abstract: Chaperonin Protein In article number 2402816, Yan Hu, Tianzhen Zhang, and co‐workers report a chaperonin protein controls upward‐curling leaves margin. They explain this phenotype that had existed for nearly a century. Chaperonin protein GHCU, homeodomain… read more here.

Keywords: molecular chaperone; chaperonin protein; protein; chaperone regulates ... See more keywords

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

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

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

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

Conserved molecular chaperone PrsA stimulates protective immunity against group A Streptococcus

Sign Up to like & get
recommendations! Published in 2024 at "NPJ Vaccines"

DOI: 10.1038/s41541-024-00839-7

Abstract: Group A Streptococcus (GAS) is a significant human pathogen that poses a global health concern. However, the development of a GAS vaccine has been challenging due to the multitude of diverse M-types and the risk… read more here.

Keywords: molecular chaperone; prsa1 prsa2; gas; group streptococcus ... See more keywords

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

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

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

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