Results 181 to 190 of about 10,740 (213)
Allostery in Disease and in Drug Discovery
Cell, 2013 Allostery is largely associated with conformational and functional transitions in individual proteins. This concept can be extended to consider the impact of conformational perturbations on cellular function and disease states.
Ruth Nussinov, Chung-Jung Tsai
exaly +2 more sources
Hidden electrostatic basis of dynamic allostery in a PDZ domain
Proceedings of the National Academy of Sciences of the United States of America, 2017 Significance Allosteric regulation is a crucial component in biochemical pathways, where ligand binding to an allosteric site modulates the enzymatic activity at a distant functional site.
Amit Kumawat, Suman Chakrabarty
exaly +2 more sources
Some of the next articles are maybe not open access.
Related searches:
Related searches:
Physical Chemistry Chemical Physics, 2007
Thrombin is a Na(+)-activated, allosteric serine protease that plays multiple functional roles in blood pathophysiology. Binding of Na(+) is the major driving force behind the procoagulant, prothrombotic and signaling functions of the enzyme. This review summarizes our current understanding of the molecular basis of thrombin allostery with special ...
Enrico, Di Cera +4 more
openaire +2 more sources
Thrombin is a Na(+)-activated, allosteric serine protease that plays multiple functional roles in blood pathophysiology. Binding of Na(+) is the major driving force behind the procoagulant, prothrombotic and signaling functions of the enzyme. This review summarizes our current understanding of the molecular basis of thrombin allostery with special ...
Enrico, Di Cera +4 more
openaire +2 more sources
The ‘allosteron’ model for entropic allostery of self-assembly [PDF]
Philosophical Transactions of the Royal Society B: Biological Sciences, 2018 Using the simple ‘allosteron’ model, we show that it is possible, in principle, to elicit pathways by which fluctuation allostery affects self-assembly of protein complexes.
T C B Mcleish, Charley Schaefer
exaly +2 more sources
EXERCER, 2021
À côté des travaux de recherche originaux, ce numéro d’exercer propose l’analyse commentée d’un récent article du Lancet, rédigée de main de maître par Denis Pouchain1.Curieusement, cette méta-analyse consacrée aux effets des traitements de l’hypertension artérielle n’a eu pour l’instant qu’un retentissement limité.
openaire +1 more source
À côté des travaux de recherche originaux, ce numéro d’exercer propose l’analyse commentée d’un récent article du Lancet, rédigée de main de maître par Denis Pouchain1.Curieusement, cette méta-analyse consacrée aux effets des traitements de l’hypertension artérielle n’a eu pour l’instant qu’un retentissement limité.
openaire +1 more source
Global low-frequency motions in protein allostery: CAP as a model system
Biophysical Reviews, 2015 Allostery is a fundamental process by which ligand binding to a protein alters its activity at a distant site. There is considerable evidence that allosteric cooperativity can be communicated by the modulation of protein dynamics without conformational ...
Philip D Townsend +2 more
exaly +3 more sources
Hemoglobin allostery and pharmacology
Molecular Aspects of Medicine, 2022The oxygen demands of the human body require the constant circulation of blood carrying an enormous concentration of hemoglobin (Hb). Oxygen transport depends not only on the amount of Hb, but also on the control over the affinity of the protein for the gas, which can be optimized for the environmental conditions by changes in the concentration of ...
Andrea Bellelli, Jeremy R.H. Tame
openaire +2 more sources
Allostery: The Rebound of Proteins
2020The discovery of hemoglobin allosteric properties is briefly summarized and contextualized in the frame of the main biochemical revelations that characterized the first half of the XX century. In particular, the historical background of DNA, RNA, and protein structure research is recalled and the new role that protein-protein interaction may have on ...
Alessandro, Finazzi Agrò +1 more
openaire +2 more sources
Protein topology and allostery
Current Opinion in Structural Biology, 2020Allostery plays important roles in many biological processes. Although all non-fibrous proteins may be allosteric, currently only a limited number of allosteric proteins are known. How allosteric regulation depends on protein topology and what are the preferred folds in allosteric proteins need to be explored.
Juan, Xie, Luhua, Lai
openaire +2 more sources
Correlating allostery with rigidity
Molecular BioSystems, 2010Abstract Allosteric proteins demonstrate the phenomenon of a ligand binding to a protein at a regulatory or effector site and thereby changing the chemical affinity of the catalytic site. As such, allostery is extremely important biologically as a regulatory mechanism for molecular concentrations in many cellular processes.
A J, Rader, Stephen M, Brown
openaire +2 more sources