Results 71 to 80 of about 18,856 (214)
Ligand‐driven modulation of chaperone–cochaperone networks shapes proteostasis outcomes
Protein Science, Volume 35, Issue 5, May 2026.Abstract Protein homeostasis depends on a delicate interplay between folding and degradation, orchestrated by molecular chaperones. Among them, Hsp90 is a central hub, regulating nearly 10% of the proteome through ATP‐driven conformational cycles and selective interactions with cochaperones.
Andrea Magni +9 more
wiley +1 more source
PLoS Computational Biology, 2018 Intrinsically disordered proteins/regions (IDPs/IDRs) are prevalent in allosteric regulation. It was previously thought that intrinsic disorder is favorable for maximizing the allosteric coupling.
Luhao Zhang, Maodong Li, Zhirong Liu
doaj +1 more source
Detecting Repetitions and Periodicities in Proteins by Tiling the Structural Space [PDF]
, 2013 The notion of energy landscapes provides conceptual tools for understanding the complexities of protein folding and function. Energy Landscape Theory indicates that it is much easier to find sequences that satisfy the "Principle of Minimal Frustration ...
Espada, Rocío +4 more
core +2 more sources
MAVISp: A modular structure‐based framework for protein variant effects
Protein Science, Volume 35, Issue 5, May 2026.Abstract The role of genomic variants in disease has expanded significantly with the advent of advanced sequencing techniques. The rapid increase in identified genomic variants has led to many variants being classified as Variants of Uncertain Significance or as having conflicting evidence, posing challenges for their interpretation and ...
Matteo Arnaudi +32 more
wiley +1 more source
, 2008 Citation: 'allostery' in the IUPAC Compendium of Chemical Terminology, 3rd ed.; International Union of Pure and Applied Chemistry; 2006. Online version 3.0.1, 2019. 10.1351/goldbook.A00241 • License: The IUPAC Gold Book is licensed under Creative Commons Attribution-ShareAlike CC BY-SA 4.0 International for individual terms.
openaire +2 more sources
Ligand Binding Introduces Significant Allosteric Shifts in the Locations of Protein Fluctuations
Frontiers in Molecular Biosciences, 2021 Allostery is usually considered to be a mechanism for transmission of signals associated with physical or dynamic changes in some part of a protein. Here, we investigate the changes in fluctuations across the protein upon ligand binding based on the ...
Ambuj Kumar, Robert L. Jernigan
doaj +1 more source
, 2011 S-adenosylhomocysteine hydrolase (SAHH), a cellular enzyme that plays a key role in methylation reactions including those required for maturation of viral mRNA, is an important drug target in the discovery of antiviral agents.
Choi, Sun +3 more
core +1 more source
Protein Science, Volume 35, Issue 5, May 2026.Abstract In cyanobacteria, the redox‐sensitive protein OpcA acts as a metabolic switch for G6PDH, enabling rapid adjustment of reducing power generation from glycogen catabolism and thereby precisely regulating carbon flux between anabolic and catabolic pathways.
Hoshin Kim +7 more
wiley +1 more source
Mechanisms of DNA-Mediated Allostery
Physical Review Letters, 2023 Proteins often regulate their activities via allostery - or action at a distance - in which the binding of a ligand at one binding site influences the affinity for another ligand at a distal site. Although less studied than in proteins, allosteric effects have been observed in experiments with DNA as well. In these experiments two or more proteins bind
Segers, Midas +3 more
openaire +4 more sources
PLoS Computational Biology, 2014 Complex networks of interacting residues and microdomains in the structures of biomolecular systems underlie the reliable propagation of information from an input signal, such as the concentration of a ligand, to sites that generate the appropriate ...
Michael V LeVine, Harel Weinstein
doaj +1 more source