Results 71 to 80 of about 391,837 (318)
Synucleinopathies, including Parkinson's disease (PD), multiple system atrophy (MSA), and dementia with Lewy bodies (DLB), are neurodegenerative disorders caused by the accumulation of misfolded alpha‐synuclein protein.
Jose Miguel Flores‐Fernandez +13 more
doaj +1 more source
This paper aims to define the influencing design criteria for compliant folding mechanisms with pneumatically actuated hinges consisting of fiber-reinforced plastic (FRP).
Mona Mühlich +6 more
doaj +1 more source
We identified a systemic, progressive loss of protein S‐glutathionylation—detected by nonreducing western blotting—alongside dysregulation of glutathione‐cycle enzymes in both neuronal and peripheral tissues of Taiwanese SMA mice. These alterations were partially rescued by SMN antisense oligonucleotide therapy, revealing persistent redox imbalance as ...
Sofia Vrettou, Brunhilde Wirth
wiley +1 more source
Video of the Miura-ori origami structure self-folding into its initial stable state and subsequently reconfigured to its second stable ...
Salvador Rojas (13861903) +2 more
core +1 more source
Structural and biochemical characterisations show that the planar cell polarity (PCP) protein Inturned harbours a unique PDZ‐like domain that does not bind canonical PDZ‐binding motifs (PBMs) like that of another PCP protein Vangl2. In contrast, the apical‐basal polarity protein Scribble contains four PDZ domains that bind Vangl2, but one PDZ domain ...
Stephan Wilmes +4 more
wiley +1 more source
Ribonuclease P (RNase P) is a universal RNA-protein endonuclease that catalyzes 5’ precursor-tRNA (ptRNA) processing. The RNase P RNA plays the catalytic role in ptRNA processing; however, the RNase P protein is required for catalysis in vivo and ...
Danyun Zeng +4 more
doaj +1 more source
Calpain small subunit homodimerization is robust and calcium‐independent
Calpains dimerize via penta‐EF‐hand (PEF) domains. Using single‐molecule force spectroscopy, we measured the strength and kinetics of PEF–PEF homodimer binding. The interaction is robust, shows a transient conformational step before dissociation, and remains largely insensitive to Ca2+.
Nesha May O. Andoy +4 more
wiley +1 more source
Proteome-Wide Analyis of Chaperonin-Dependent Protein Folding in Escherichia coli [PDF]
In Escherichia coli, the cylindrical chaperonin GroEL and its cofactor GroES promote the folding of a fraction of newly synthesized polypeptide chains by acting as an Anfinsen cage.
Maier, T., Maier, Tobias
core
meleetrimble/robust-folding-paper-support: Initial Release
Notebooks and data for the paper "Robust folding of elastic ...
meleetrimble
core +1 more source
Structure and Conformational Properties of d-Glucose/d-Galactose-Binding Protein in Crowded Milieu
Conformational changes of d-glucose/d-galactose-binding protein (GGBP) were studied under molecular crowding conditions modeled by concentrated solutions of polyethylene glycols (PEG-12000, PEG-4000, and PEG-600), Ficoll-70, and Dextran-70, addition of ...
Alexander V. Fonin +5 more
doaj +1 more source

