98%
921
2 minutes
20
Calcium and protons exert control over the formation and activity of the cytoskeleton, usually by modulating an associated motor protein or one that affects the structural organization of the polymer.
Download full-text PDF |
Source |
---|---|
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4704593 | PMC |
http://dx.doi.org/10.1104/pp.15.01506 | DOI Listing |
Front Biosci (Landmark Ed)
August 2025
University of Angers, MitoLab, Unité MITOVASC, UMR CNRS 6015, INSERM U1083, SFR ICAT, 49330 Angers, France.
The bioenergetic machinery of the cell is protected and structured within two layers of mitochondrial membranes. The mitochondrial inner membrane is extremely rich in proteins, including respiratory chain complexes, substrate transport proteins, ion exchangers, and structural fusion proteins. These proteins participate directly or indirectly in shaping the membrane's curvature and facilitating its folding, as well as promoting the formation of nanotubes, and proton-rich pockets known as cristae.
View Article and Find Full Text PDFFront Genet
August 2025
Department of Prosthodontics, Yonsei University College of Dentistry, Seoul, Republic of Korea.
Introduction: Although peg-shaped lateral incisors are a common dental anomaly, the genetic mechanisms governing peg lateralis are poorly understood, particularly in cases where other associated anomalies are absent. Here, we aimed to identify potential candidate genes contributing to the development of non-syndromic peg lateralis via whole-exome sequencing (WES).
Methods: Saliva samples were collected from 20 unrelated Korean individuals with non-syndromic peg lateralis.
Int J Mol Sci
August 2025
Department of Biological Sciences, Faculty of Science, Beirut Arab University, Tripoli P.O. Box 11-5020, Lebanon.
The state of the art in the thermodynamics of calix[4]resorcinarene derivatives and its metal ion complexes is briefly discussed in the introduction. This is followed by the synthesis and characterization of a recyclable calix[4]resorcinarene amide derivative (L). The 1H NMR analyses in CD3CN and CD3OD showed solvent-dependent conformational changes with a notable downfield chemical shift in the aromatic proton (H-2) in moving from deuterated methanol to acetonitrile, indicating an interaction of the solvent within the ligand cavity as suggested by molecular dynamic simulations.
View Article and Find Full Text PDFSci Rep
August 2025
Photobiology Laboratory, Institute of Biophysics SB RAS, Federal Research Center "Krasnoyarsk Science Center SB RAS", Krasnoyarsk, Russia.
Coelenterazine is the most common substrate for light-emitting reactions identified in luminous marine organisms. Among bioluminescent proteins engaging coelenterazine as a luciferin, Ca-regulated photoproteins form stable enzyme-substrate complexes offering thereby a unique opportunity to study their bioluminescence reactions in detail. Here, we used stopped-flow kinetics to investigate the formation of the emitters of recombinant aequorin, obelin, and W92F obelin activated with coelenterazine, as well as aequorin activated with coelenterazine-e.
View Article and Find Full Text PDF