Results 31 to 40 of about 140,081 (117)

Updates on Aβ Processing by Hsp90, BRICHOS, and Newly Reported Distinctive Chaperones

Biomolecules, 2023
Alzheimer’s disease (AD) is an extremely devastating neurodegenerative disease, and there is no cure for it. AD is specified as the misfolding and aggregation of amyloid-β protein (Aβ) and abnormalities in hyperphosphorylated tau protein.
Mohammed Iqbal, Shea-Lorane Lewis, Shivani Padhye, Umesh Kumar Jinwal   +3 more
doaj   +1 more source

Epitopes of Immunoreactive Proteins of Streptococcus Agalactiae: Enolase, Inosine 5′-Monophosphate Dehydrogenase and Molecular Chaperone GroEL

Frontiers in Cellular and Infection Microbiology, 2018
Three Streptococcus agalactiae (group B streptococci, GBS) immunoreactive proteins: enolase (47.4 kDa), inosine 5′-monophosphate dehydrogenase (IMPDH) (53 kDa) and molecular chaperone GroEL (57 kDa) were subjected to investigation.
Anna Dobrut, Ewa Brzozowska, Sabina Górska, Marcelina Pyclik, Andrzej Gamian, Małgorzata Bulanda, Elzbieta Majewska, Monika Brzychczy-Włoch   +7 more
doaj   +1 more source

Alpha-Hemoglobin-Stabilizing Protein: An Erythroid Molecular Chaperone

Biochemistry Research International, 2011
Alpha-hemoglobin-stabilizing protein (AHSP) is an erythroid-specific protein that acts as a molecular chaperone for the free α chains of hemoglobin. Evidence strongly suggests that AHSP participates in hemoglobin synthesis and may act to neutralize the ...
Maria Emília Favero, Fernando Ferreira Costa   +1 more
doaj   +1 more source

Prediction of recombinant Mycobacterium tuberculosis α-crystallin oligomer chaperone activity using polynomial graphs [version 2; peer review: 2 approved]

F1000Research, 2020
Background: Mycobacterial α-crystallin (Acr) is a chaperone that prevents misfolding of proteins when Mycobacterium tuberculosis is found in a latent form in the host tissue. Methods: Using insulin as a model substrate and utilizing polynomial graphs, we
Gautam Krishnan, Utpal Roy
doaj   +1 more source

Enhanced Extracellular Type III Pullulan Hydrolase Production by Co-expressing Molecular Chaperone in Brevibacillus choshinensis and Fermentation Optimization

Shipin gongye ke-ji
This study aimed to increase the expression and secretion of type III pullulan hydrolase (TK-PUL) by Brevibacillus choshinensis through the co-expression of molecular chaperone proteins and the optimization of fermentation conditions.
Jing ZENG, Jianjun GUO, Tong WANG, Lin YUAN   +3 more
doaj   +1 more source

Small Heat Shock Proteins, Big Impact on Protein Aggregation in Neurodegenerative Disease

Frontiers in Pharmacology, 2019
Misfolding, aggregation, and aberrant accumulation of proteins are central components in the progression of neurodegenerative disease. Cellular molecular chaperone systems modulate proteostasis, and, therefore, are primed to influence aberrant protein ...
Jack M. Webster, April L. Darling, Vladimir N. Uversky, Laura J. Blair   +3 more
doaj   +1 more source

Calmodulin regulates protease versus co-chaperone activity of a metacaspase

Cell Reports, 2023
Summary: Metacaspases are ancestral homologs of caspases that can either promote cell death or confer cytoprotection. Furthermore, yeast (Saccharomyces cerevisiae) metacaspase Mca1 possesses dual biochemical activity: proteolytic activity causing cell ...
Anna Maria Eisele-Bürger, Frederik Eisele, Sandra Malmgren Hill, Xinxin Hao, Kara L. Schneider, Rahmi Imamoglu, David Balchin, Beidong Liu, F. Ulrich Hartl, Peter V. Bozhkov, Thomas Nyström   +10 more
doaj   +1 more source

Aggregation Prevention Assay for Chaperone Activity of Proteins Using Spectroflurometry

Bio-Protocol, 2017
The ability to stabilize other proteins against thermal aggregation is one of the major characteristics of chaperone proteins. Molecular chaperones bind to nonnative conformations of proteins.
Manish Bhuwan, Madhuri Suragani, Nasreen Ehtesham, Seyed Hasnain   +3 more
doaj   +1 more source

Universal Stress Protein exhibits a redox-dependent chaperone function in Arabidopsis and enhances plant tolerance to heat shock and oxidative stress

Frontiers in Plant Science, 2015
Although a wide range of physiological information on Universal Stress Proteins (USPs) is available from many organisms, their biochemical and molecular functions remain unidentified.
Jung eYoung Jun, Sarah Mae Boyles Melencion, Lee eEun Seon, Park eJoung Hun, Cresilda Vergara Alinapon, Hun Taek eOh, Dae-Jin eYun, Yong Hun eChi, Sang Yeol eLee   +8 more
doaj   +1 more source

An increase in surface hydrophobicity mediates chaperone activity in N-chlorinated RidA

Redox Biology, 2022
Under physiological conditions, Escherichia coli RidA is an enamine/imine deaminase, which promotes the release of ammonia from reactive enamine/imine intermediates.
Marharyta Varatnitskaya, Julia Fasel, Alexandra Müller, Natalie Lupilov, Yunlong Shi, Kristin Fuchs, Marco Krewing, Christoph Jung, Timo Jacob, Barbara Sitek, Julia E. Bandow, Kate S. Carroll, Eckhard Hofmann, Lars I. Leichert   +13 more
doaj   +1 more source