Results 31 to 40 of about 19,917 (239)

Current updates of CRISPR/Cas9‐mediated genome editing and targeting within tumor cells: an innovative strategy of cancer management

open access: yesCancer Communications, Volume 42, Issue 12, Page 1257-1287, December 2022., 2022
Abstract Clustered regularly interspaced short palindromic repeats‐associated protein (CRISPR/Cas9), an adaptive microbial immune system, has been exploited as a robust, accurate, efficient and programmable method for genome targeting and editing. This innovative and revolutionary technique can play a significant role in animal modeling, in vivo genome
Khaled S. Allemailem   +6 more
wiley   +1 more source

Computational study on the inhibitor binding mode and allosteric regulation mechanism in hepatitis C virus NS3/4A protein.

open access: yesPLoS ONE, 2014
HCV NS3/4A protein is an attractive therapeutic target responsible for harboring serine protease and RNA helicase activities during the viral replication.
Weiwei Xue   +4 more
doaj   +1 more source

Dimeric allostery mechanism of the plant circadian clock photoreceptor ZEITLUPE.

open access: yesPLoS Computational Biology, 2021
In Arabidopsis thaliana, the Light-Oxygen-Voltage (LOV) domain containing protein ZEITLUPE (ZTL) integrates light quality, intensity, and duration into regulation of the circadian clock.
Francesco Trozzi   +4 more
doaj   +1 more source

Allosteric modulation of G protein-coupled receptor signaling

open access: yesFrontiers in Endocrinology, 2023
G protein-coupled receptors (GPCRs), the largest family of transmembrane proteins, regulate a wide array of physiological processes in response to extracellular signals. Although these receptors have proven to be the most successful class of drug targets,
Siyuan Shen   +6 more
doaj   +1 more source

The energy landscape analysis of cancer mutations in protein kinases. [PDF]

open access: yesPLoS ONE, 2011
The growing interest in quantifying the molecular basis of protein kinase activation and allosteric regulation by cancer mutations has fueled computational studies of allosteric signaling in protein kinases.
Anshuman Dixit, Gennady M Verkhivker
doaj   +1 more source

Prediction of protein allosteric signalling pathways and functional residues through paths of optimised propensity [PDF]

open access: yesarXiv, 2022
Allostery commonly refers to the mechanism that regulates protein activity through the binding of a molecule at a different, usually distal, site from the orthosteric site. The omnipresence of allosteric regulation in nature and its potential for drug design and screening render the study of allostery invaluable.
arxiv  

Statistical Mechanics of Allosteric Enzymes [PDF]

open access: yesJournal Physical Chemistry B 120 (2016) 6021-6037, 2017
The concept of allostery in which macromolecules switch between two different conformations is a central theme in biological processes ranging from gene regulation to cell signaling to enzymology. Allosteric enzymes pervade metabolic processes, yet a simple and unified treatment of the effects of allostery in enzymes has been lacking.
arxiv   +1 more source

Real-time observation of ligand-induced allosteric transitions in a PDZ domain [PDF]

open access: yesProc. Natl. Acad. Sci. USA 117, 26031-26039 (2020), 2020
While allostery is of paramount importance for protein regulation, the underlying dynamical process of ligand (un)binding at one site, resulting time evolution of the protein structure, and change of the binding affinity at a remote site is not well understood.
arxiv   +1 more source

The structural basis of ATP as an allosteric modulator. [PDF]

open access: yesPLoS Computational Biology, 2014
Adenosine-5'-triphosphate (ATP) is generally regarded as a substrate for energy currency and protein modification. Recent findings uncovered the allosteric function of ATP in cellular signal transduction but little is understood about this critical ...
Shaoyong Lu   +6 more
doaj   +1 more source

A non-equilibrium dynamic mechanism for the allosteric effect [PDF]

open access: yesPhys. Rev. Lett. 99, 168103 (2007), 2007
Allosteric regulation is often viewed as thermodynamic in nature. However protein internal motions during an enzymatic reaction cycle can be slow hopping processes over numerous potential barriers. We propose that regulating molecules may function by modifying the nonequilibrium protein dynamics.
arxiv   +1 more source

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