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Characterization of AtBAG2 as a Novel Molecular Chaperone [PDF]
Bcl-2-associated anthanogene (BAG) family proteins regulate plant defense against biotic and abiotic stresses; however, the function and precise mechanism of action of each individual BAG protein are not yet clear.
Chang Ho Kang +6 more
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Functional Characterization of an Arabidopsis Profilin Protein as a Molecular Chaperone under Heat Shock Stress [PDF]
Profilins (PFNs) are actin monomer-binding proteins that function as antimicrobial agents in plant phloem sap. Although the roles of Arabidopsis thaliana profilin protein isoforms (AtPFNs) in regulating actin polymerization have already been described ...
Hyosuk Son +6 more
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Calnexin, More Than Just a Molecular Chaperone [PDF]
Calnexin is a type I integral endoplasmic reticulum (ER) membrane protein with an N-terminal domain that resides in the lumen of the ER and a C-terminal domain that extends into the cytosol.
Tautvydas Paskevicius +3 more
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Targeting extracellular Hsp90: A unique frontier against cancer
The molecular chaperone Heat Shock Protein-90 (Hsp90) is known to interact with over 300 client proteins as well as regulatory factors (eg. nucleotide and proteins) that facilitate execution of its role as a chaperone and, ultimately, client protein ...
Rebecca A. Sager +19 more
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Expression patterns of molecular chaperone genes in Antarctic psychrophilic yeast, Glaciozyma antarctica PI12 in response to heat stress [PDF]
Microbes living in the polar regions have some common and unique strategies to respond to thermal stress. Nevertheless, the amount of information available, especially at the molecular level is lacking for some organisms such as Antarctic psychrophilic ...
Nur Athirah Yusof +7 more
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HSP10 as a Chaperone for Neurodegenerative Amyloid Fibrils
Neurodegenerative diseases (NDs) are associated with accumulated misfolded proteins (MPs). MPs oligomerize and form multiple forms of amyloid fibril polymorphs that dictate fibril propagation and cellular dysfunction.
Johan N. K. Larsson +2 more
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The chaperone (or chaperoning) system (CS) constitutes molecular chaperones, co-chaperones, and chaperone co-factors, interactors and receptors, and its canonical role is protein quality control.
Federica Scalia +5 more
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The dysfunction of the proteostasis network is a molecular hallmark of neurodegenerative diseases such as Alzheimer’s disease, Parkinson’s disease, Huntington’s disease, and amyotrophic lateral sclerosis. Molecular chaperones are a major component of the
Lisha Wang +4 more
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Among the several tetratricopeptide (TPR) repeat-containing proteins encoded by the Arabidopsis thaliana genome, AtTPR10 exhibits an atypical structure with three TPR domain repeats at the C-terminus in addition to seven ankyrin (ANK) domain repeats at ...
Seol Ki Paeng +9 more
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The APE2 Exonuclease Is a Client of the Hsp70–Hsp90 Axis in Yeast and Mammalian Cells
Molecular chaperones such as Hsp70 and Hsp90 help fold and activate proteins in important signal transduction pathways that include DNA damage response (DDR).
Siddhi Omkar +4 more
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