Results 261 to 270 of about 137,279 (309)
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Computational elucidation of allosteric communication in proteins for allosteric drug design

Drug Discovery Today, 2022
Allosteric modulators target topologically distal allosteric sites in order to modulate orthosteric sites, providing enhanced specificity and physiochemical properties. Harnessing allostery for drug discovery is an emerging paradigm in modern pharmaceutics.
Duan Ni, Ren Kong, Shaoyong Lu
exaly   +3 more sources

Allosteric repression: An Analysis

Journal of Theoretical Biology, 1977
Abstract A kinetic analysis of repression is presented based on the accepted sequence of molecular events and the assumption that the co-repressor-repressor interaction involves an allosteric transition. This leads to an expression which relates the two experimentally accessible variables—enzyme and signal—when the system is operating in vivo .
J A, Burns, H, Kacser
openaire   +2 more sources

Olfaction: Allosteric modulation

Current Biology, 2023
New research indicates that the odor-evoked responses of human olfactory receptors can be enhanced via the non-competitive binding of an allosteric modulator. This modulatory mechanism adds an additional layer of complexity to the peripheral encoding of odors.
Samuel, Caton, Adam, Dewan
openaire   +2 more sources

An Allosteric Hammerhead Ribozyme

Nature Biotechnology, 1995
We have constructed an RNA molecule containing a hammerhead ribozyme that is under allosteric control. In the inactive state, the RNA enzyme is unable to cleave a suitable substrate. The formation of the active state of the ribozyme is triggered by a specific interaction with a DNA oligonucleotide effector that is complementary to a single-stranded ...
H, Porta, P M, Lizardi
openaire   +2 more sources

Artificial Allosteric Receptors

Chemistry – A European Journal, 2013
AbstractCooperative effects in the binding of two or more substrates to different binding sites of a receptor that are a result of a conformational change caused by the binding of the first substrate—also referred to as the effector—are called allosteric effects.
Christopher, Kremer, Arne, Lützen
openaire   +2 more sources

Allosteric regulation of chaperonins

Current Opinion in Structural Biology, 2005
Chaperonins are molecular machines that facilitate protein folding by undergoing energy (ATP)-dependent movements that are coordinated in time and space by complex allosteric regulation. Recently, progress has been made in describing the various functional (allosteric) states of these machines, the pathways by which they interconvert, and the coupling ...
Horovitz, A, Willison, KR
openaire   +3 more sources

Neurotensin Receptor Allosterism Revealed in Complex with a Biased Allosteric Modulator

Biochemistry, 2023
The NTSR1 neurotensin receptor (NTSR1) is a G protein-coupled receptor (GPCR) found in the brain and peripheral tissues with neurotensin (NTS) being its endogenous peptide ligand. In the brain, NTS modulates dopamine neuronal activity, induces opioid-independent analgesia, and regulates food intake.
Brian E. Krumm   +14 more
openaire   +2 more sources

Progress in Allosteric Database

2019
An allosteric mechanism refers to the biological regulation process wherein macromolecules propagate the effect of ligand binding at one site to a spatially distant orthosteric locus, thus affecting activity. The theory has remained a trending topic in biology research for over 50 years, since the understanding of allostery is fundamental for gleaning ...
Kun, Song, Jian, Zhang, Shaoyong, Lu
openaire   +2 more sources

Aptamers for allosteric regulation

Nature Chemical Biology, 2011
Aptamers are useful for allosteric regulation because they are nucleic acid-based structures in which ligand binding induces conformational changes that may alter the function of a connected oligonucleotide at a distant site. Through this approach, a specific input is efficiently converted into an altered output.
Vinkenborg, J.   +2 more
openaire   +3 more sources

Overview of Receptor Allosterism

Current Protocols in Pharmacology, 2010
AbstractIn addition to the orthosteric site, which recognizes endogenous ligands, most G protein–coupled receptors (GPCRs) possess topographically distinct allosteric sites that can be recognized by small molecules and accessory cellular proteins. Ligand binding to allosteric sites promotes a conformational change in the GPCR that can alter orthosteric
Karen J, Gregory   +2 more
openaire   +2 more sources

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