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Diversity of Allosteric Regulation in Proteases

ACS Chemical Biology, 2012
Allostery is a fundamental regulatory mechanism that is based on a functional modulation of a site by a distant site. Allosteric regulation can be triggered by binding of diverse allosteric effectors, ranging from small molecules to macromolecules, and is therefore offering promising opportunities for functional modulation in a wide range of ...
Merdanovic, Melisa   +3 more
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Selecting Allosteric Ribozymes

2012
Allosteric ribozymes can be designed to respond to virtually any molecule of choice. The resulting species may be used for example as synthetic regulators of gene expression or alternatively as biosensors. In vitro selection techniques allow the isolation of active molecules from libraries as large as 10(15) different molecules.
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Simulations of allosteric transitions

Current Opinion in Structural Biology, 2011
Allosteric transitions are one of the subtler mechanisms used by nature to fine tune protein activity. Effector binding to a specific site on the protein surface induces significant activity change, and initiates a conformational transition that frequently includes domain motions and is very large.
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Advances in NMR Methods to Identify Allosteric Sites and Allosteric Ligands

2019
NMR allows assessment of protein structure in solution. Unlike conventional X-ray crystallography that provides snapshots of protein conformations, all conformational states are simultaneously accessible to analysis by NMR. This is a significant advantage for discovery and characterization of allosteric effects.
Hazem, Abdelkarim   +3 more
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Allosteric modulation of neurotransmission

Biochemical Pharmacology
The therapeutic effects of allosteric modulators on neurotransmission are described. The two unique features of allosteric modulators are: (1) separate binding sites on proteins, and (2) the production of altered receptor conformation upon binding.
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Kinetics of Allosteric Activation

2009
Although enzyme inhibition results in most cases from the competing effect of a ligand with substrate, the ability of ligands to enhance enzyme function requires binding to a site distinct from the active site. This is the basis of allosteric activation of enzyme activity, documented most conspicuously in the vast family of enzymes activated by ...
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Along the allostery stream: Recent advances in computational methods for allosteric drug discovery

Wiley Interdisciplinary Reviews: Computational Molecular Science, 2022
Duan Ni, Zongtao Chai, Shaoyong Lu
exaly  

Rational design of allosteric modulators: Challenges and successes

Wiley Interdisciplinary Reviews: Computational Molecular Science, 2021
Alexios Chatzigoulas, Zoe Cournia
exaly  

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