Results 21 to 30 of about 136,024 (249)

Gymnastics of Molecular Chaperones [PDF]

Molecular Cell, 2010
Molecular chaperones assist folding processes and conformational changes in many proteins. In order to do so, they progress through complex conformational cycles themselves. In this review, I discuss the diverse conformational dynamics of the ATP-dependent chaperones of the Hsp60, Hsp70, Hsp90, and Hsp100 families.
openaire   +2 more sources

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

Hsp83/Hsp90 Physically Associates with Insulin Receptor to Promote Neural Stem Cell Reactivation

Stem Cell Reports, 2018
Summary: Neural stem cells (NSCs) have the ability to exit quiescence and reactivate in response to physiological stimuli. In the Drosophila brain, insulin receptor (InR)/phosphatidylinositol 3-kinase (PI3K)/Akt pathway triggers NSC reactivation. However,
Jiawen Huang, Hongyan Wang
doaj   +1 more source

Ensemble-based modeling and rigidity decomposition of allosteric interaction networks and communication pathways in cyclin-dependent kinases: Differentiating kinase clients of the Hsp90-Cdc37 chaperone. [PDF]

PLoS ONE, 2017
The overarching goal of delineating molecular principles underlying differentiation of protein kinase clients and chaperone-based modulation of kinase activity is fundamental to understanding activity of many oncogenic kinases that require chaperoning of
Gabrielle Stetz, Amanda Tse, Gennady M Verkhivker   +2 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