Allostery without a conformational change? Revisiting the paradigm.
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NMR Methods to Study Dynamic AllosteryAllostery: An Overview of Its History, Concepts, Methods, and ApplicationsSelection on protein structure, interaction, and sequence.Conditionally disordered proteins: bringing the environment back into the fold.Allostery modulates the beat rate of a cardiac pacemakerAllosteric DNA nanoswitches for controlled release of a molecular cargo triggered by biological inputs.Discovery of a novel conformational equilibrium in urokinase-type plasminogen activator.Mapping the Free Energy Landscape of PKA Inhibition and Activation: A Double-Conformational Selection Model for the Tandem cAMP-Binding Domains of PKA RIα.Autism Linked to Increased Oncogene Mutations but Decreased Cancer Rate.Oncogenic mutations weaken the interactions that stabilize the p110α-p85α heterodimer in phosphatidylinositol 3-kinase α.Long-Range Signaling in MutS and MSH Homologs via Switching of Dynamic Communication PathwaysConformational diversity analysis reveals three functional mechanisms in proteins.Enzyme Selectivity Fine-Tuned through Dynamic Control of a LoopComputational approaches to detect allosteric pathways in transmembrane molecular machines.Solution NMR Spectroscopy for the Study of Enzyme Allostery.Chemical shift imprint of intersubunit communication in a symmetric homodimer.Protein Allostery and Conformational Dynamics.Allosteric regulation of Arf GTPases and their GEFs at the membrane interface.How do disordered regions achieve comparable functions to structured domains?Allosteric Dynamic Control of Binding.Computational investigation of conformational variability and allostery in cathepsin K and other related peptidases.Distinct dynamics and interaction patterns in H- and K-Ras oncogenic P-loop mutants.Exploiting computationally derived out-of-the-box protein conformations for drug design.Kinetic trapping - a strategy for directing the self-assembly of unique functional nanostructures.Intrinsic protein disorder in oncogenic KRAS signaling.Conformational Dynamics and Allostery in Pyruvate Kinase.Saturation transfer difference nuclear magnetic resonance titrations reveal complex multistep-binding of l-fucose to norovirus particles.Biased AllosterySite-to-site interdomain communication may mediate different loss-of-function mechanisms in a cancer-associated NQO1 polymorphism.The role of protein dynamics in allosteric effects-introduction.Altering the allosteric pathway in IGPS suppresses millisecond motions and catalytic activityAn engineered photoswitchable mammalian pyruvate kinase.Entropy redistribution controls allostery in a metalloregulatory protein.Remote electrochemical modulation of pKa in a rotaxane by co-conformational allostery.Molecular Dynamics Simulation Reveals Specific Interaction Sites between Scorpion Toxins and Kv1.2 Channel: Implications for Design of Highly Selective Drugs.Dependence of prevalence of contiguous pathways in proteins on structural complexity.Implications of short time scale dynamics on long time processes.Survey of solution dynamics in Src kinase reveals allosteric cross talk between the ligand binding and regulatory sites.Energetic redistribution in allostery to execute protein function.Dynamic Allostery Modulates Catalytic Activity by Modifying the Hydrogen Bonding Network in the Catalytic Site of Human Pin1.
P2860
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P2860
Allostery without a conformational change? Revisiting the paradigm.
description
2014 nî lūn-bûn
@nan
2014 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2014 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2014年の論文
@ja
2014年論文
@yue
2014年論文
@zh-hant
2014年論文
@zh-hk
2014年論文
@zh-mo
2014年論文
@zh-tw
2014年论文
@wuu
name
Allostery without a conformational change? Revisiting the paradigm.
@ast
Allostery without a conformational change? Revisiting the paradigm.
@en
type
label
Allostery without a conformational change? Revisiting the paradigm.
@ast
Allostery without a conformational change? Revisiting the paradigm.
@en
prefLabel
Allostery without a conformational change? Revisiting the paradigm.
@ast
Allostery without a conformational change? Revisiting the paradigm.
@en
P1476
Allostery without a conformational change? Revisiting the paradigm.
@en
P2093
Chung-Jung Tsai
P356
10.1016/J.SBI.2014.11.005
P577
2014-12-11T00:00:00Z