Results 81 to 90 of about 792,223 (273)

Organ‐specific redox imbalances in spinal muscular atrophy mice are partially rescued by SMN antisense oligonucleotides

FEBS Letters, EarlyView.
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

Stress-Induced Evolution of the Nucleolus: The Role of Ribosomal Intergenic Spacer (rIGS) Transcripts

Biomolecules
It became clear more than 20 years ago that the nucleolus not only performs the most important biological function of assembling ribonucleic particles but is also a key controller of many cellular processes, participating in cellular adaptation to stress.
Anastasia A. Gavrilova, Margarita V. Neklesova, Yuliya A. Zagryadskaya, Irina M. Kuznetsova, Konstantin K. Turoverov, Alexander V. Fonin   +5 more
doaj   +1 more source

Comparing the Folds of Prions and Other Pathogenic Amyloids

Pathogens, 2018
Pathogenic amyloids are the main feature of several neurodegenerative disorders, such as Creutzfeldt–Jakob disease, Alzheimer’s disease, and Parkinson’s disease. High resolution structures of tau paired helical filaments (PHFs), amyloid-
José Miguel Flores-Fernández, Vineet Rathod, Holger Wille   +2 more
doaj   +1 more source

Evolutionary Dynamics and Optimization: Neutral Networks as Model-Landscapes for RNA Secondary-Structure Folding-Landscapes

, 1995
We view the folding of RNA-sequences as a map that assigns a pattern of base pairings to each sequence, known as secondary structure. These preimages can be constructed as random graphs (i.e. the neutral networks associated to the structure $s$).
Christian Reidys, Christian V. Forst, Jacqueline Weber, Rna Secondary-structure Folding-landscapes   +3 more
core   +3 more sources

Effects of confinement and crowding on folding of model proteins

, 2008
We perform molecular dynamics simulations for a simple coarse-grained model of crambin placed inside of a softly repulsive sphere of radius R. The confinement makes folding at the optimal temperature slower and affects the folding scenarios, but both ...
Baruah, Baukmketner, Cheung, Cieplak, Cieplak, Cieplak, Duroux, Ellis, Go, Hartl, Hoang, Honeycutt, Jewett, Kwiecinska, Luisi, M. Wojciechowski, Marek Cieplak, Matzke, Melo, Moilanen, Murtas, Rathore, Sulkowska, Sulkowska, Szymczak, Szymczak, Takagi   +26 more
core   +1 more source

The planar cell polarity protein Vangl2 interacts with the PDZ‐domains of Scribble but not with a unique PDZ‐like domain in Inturned

FEBS Letters, EarlyView.
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, Jan Brysch, Carmen Gelze, Lilli Meier, Daniel Kümmel   +4 more
wiley   +1 more source

Native PLGA nanoparticles attenuate Aβ-seed induced tau aggregation under in vitro conditions: potential implication in Alzheimer’s disease pathology

Scientific Reports
Evidence suggests that beta-amyloid (Aβ)-induced phosphorylation/aggregation of tau protein plays a critical role in the degeneration of neurons and development of Alzheimer’s disease (AD), the most common cause of dementia affecting the elderly ...
Pallabi Sil Paul, Tark Patel, Jae-Young Cho, Allan Yarahmady, Aria Khalili, Valentyna Semenchenko, Holger Wille, Marianna Kulka, Sue-Ann Mok, Satyabrata Kar   +9 more
doaj   +1 more source

Calpain small subunit homodimerization is robust and calcium‐independent

FEBS Letters, EarlyView.
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, Trina Dykstra‐MacPherson, Mathias A. Bell, Peter L. Davies, Ruby May A. Sullan   +4 more
wiley   +1 more source

Criteria for folding in structure-based models of proteins

, 2016
In structure-based models of proteins, one often assumes that folding is accomplished when all contacts are established. This assumption may frequently lead to a conceptual problem that folding takes place in a temperature region of very low ...
Cieplak, Marek, Wołek, Karol
core   +1 more source

A methionine‐lined active site governs carbocation stabilization and product specificity in a bacterial terpene synthase

FEBS Letters, EarlyView.
This study reveals a unique active site enriched in methionine residues and demonstrates that these residues play a critical role by stabilizing carbocation intermediates through novel sulfur–cation interactions. Structure‐guided mutagenesis further revealed variants with significantly altered product profiles, enhancing pseudopterosin formation. These
Marion Ringel, Carl P. O. Helmer, Shani Zev, Ronja Driller, Emily Buhr, Markus Reinbold, Renana Schwartz, Gabriel Foley, Mikael Boden, Daniel Garbe, Gerhard Schenk, Dan Thomas Major, Bernhard Loll, Thomas Brück   +13 more
wiley   +1 more source