Results 261 to 270 of about 151,004 (296)

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
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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
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Kinetics of Allosteric Enzymes

Annual Review of Biophysics and Bioengineering, 1974
Within the cell, hundreds of different chemical reactions go on simultaneously, each requiring different substrates and producing different products. This array of rea,ctions must be carefully regulated in order to maintain the orderly function of a cell.
G G, Hammes, C W, Wu
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Allosteric Agonist Modulators

Journal of Receptors and Signal Transduction, 2007
This article discusses a model to describe the effects of molecules that bind to a site on the receptor separate from that of the endogenous agonist to actively produce receptor signals (direct agonism). In addition, these molecules also modify the biological responses of the endogenous agonist (either potentiation or antagonism).
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Allosteric Disulfide Bonds

Biochemistry, 2006
Disulfide bonds have been generally considered to be either structural or catalytic. Structural bonds stabilize a protein, while catalytic bonds mediate thiol-disulfide interchange reactions in substrate proteins. There is emerging evidence for a third type of disulfide bond that can control protein function by triggering a conformational change when ...
Bryan, Schmidt, Lorraine, Ho, Philip J, Hogg   +2 more
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Allosteric modulation of caspases

Pharmacology & Therapeutics, 2011
Caspases are proteolytic enzymes mainly involved in the induction and execution phases of apoptosis. This type of programmed cell death is an essential regulatory process required to maintain the integrity and homeostasis of multicellular organisms. Inappropriate apoptosis is attributed a key role in many human diseases, including neurodegenerative ...
Hans-Georg, Häcker, Mihiret Tekeste, Sisay, Michael, Gütschow   +2 more
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Allosteric Disulfide Bonds

2011
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Hogg, Philip J., Wong, Jason W.H.
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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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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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