Results 31 to 40 of about 18,856 (214)
Allosteric Inhibition of Factor XIIIa. Non-Saccharide Glycosaminoglycan Mimetics, but Not Glycosaminoglycans, Exhibit Promising Inhibition Profile [PDF]
, 2016 Factor XIIIa (FXIIIa) is a transglutaminase that catalyzes the last step in the coagulation process. Orthostery is the only approach that has been exploited to design FXIIIa inhibitors.
Afosa, Daniel K. +4 more
core +4 more sources
CABS-flex predictions of protein flexibility compared with NMR ensembles [PDF]
, 2014 Motivation: Identification of flexible regions of protein structures is important for understanding of their biological functions. Recently, we have developed a fast approach for predicting protein structure fluctuations from a single protein model: the ...
Jamroz, Michal +2 more
core +1 more source
Frontiers in Molecular Biosciences, 2023 Mesophilic and thermophilic enzyme counterparts are often studied to understand how proteins function under harsh conditions. To function well outside of standard temperature ranges, thermophiles often tightly regulate their structural ensemble through ...
Alexa L. Knight +2 more
doaj +1 more source
Activity modulation and allosteric control of a scaffolded DNAzyme using a dynamic DNA nanostructure. [PDF]
, 2016 Recognition of the fundamental importance of allosteric regulation in biology dates back to not long after its discovery in the 1960s. Our ability to rationally engineer this potentially useful property into normally non-allosteric catalysts, however ...
Fan, Chunhai +7 more
core +1 more source
PLoS Biology, 2013 Allostery is a fundamental process by which ligand binding to a protein alters its activity at a distinct site. There is growing evidence that allosteric cooperativity can be communicated by modulation of protein dynamics without conformational change ...
Thomas L Rodgers +8 more
doaj +1 more source
Detection of Side Chain Rearrangements Mediating the Motions of Transmembrane Helices in Molecular Dynamics Simulations of G Protein-Coupled Receptors. [PDF]
, 2017 Structure and dynamics are essential elements of protein function. Protein structure is constantly fluctuating and undergoing conformational changes, which are captured by molecular dynamics (MD) simulations.
Gaieb, Zied, Morikis, Dimitrios
core +2 more sources
Long-Range Signaling in MutS and MSH Homologs via Switching of Dynamic Communication Pathways. [PDF]
PLoS Computational Biology, 2016 Allostery is conformation regulation by propagating a signal from one site to another distal site. This study focuses on the long-range communication in DNA mismatch repair proteins MutS and its homologs where intramolecular signaling has to travel over ...
Beibei Wang +5 more
doaj +1 more source
Allo-network drugs: Extension of the allosteric drug concept to protein-protein interaction and signaling networks [PDF]
, 2013 Allosteric drugs are usually more specific and have fewer side effects than orthosteric drugs targeting the same protein. Here, we overview the current knowledge on allosteric signal transmission from the network point of view, and show that most ...
Csermely, Péter +2 more
core +2 more sources
Chemistry & Biology, 2004 Engineered RNAs have demonstrated remarkable properties of molecular recognition and allosteric function. Liu and colleagues now report the isolation and in vivo function of a ligand-dependent RNA-based transcription factor that opens wide the door for allosterically controllable aptamers.
openaire +2 more sources
Dynamically driven protein allostery [PDF]
Nature Structural & Molecular Biology, 2006 Allosteric interactions are typically considered to proceed through a series of discrete changes in bonding interactions that alter the protein conformation. Here we show that allostery can be mediated exclusively by transmitted changes in protein motions.
Nataliya, Popovych +3 more
openaire +2 more sources