Backtracking on the folding landscape of the beta-trefoil protein interleukin-1beta? - Test2 - elhamkhani - TriplyDB

Backtracking on the folding landscape of the beta-trefoil protein interleukin-1beta?

Backtracking on the folding landscape of the beta-trefoil protein interleukin-1beta?

http://www.wikidata.org/entity/Q21045404

about

Knotted proteins: A tangled tale of Structural Biology Conformational frustration in calmodulin-target recognition.The Plasticity of the -Trefoil Fold Constitutes an Evolutionary Platform for Protease Inhibition Allosteric control in a metalloprotein dramatically alters function.Protein stability and dynamics modulation: the case of human frataxin Folding circular permutants of IL-1β: route selection driven by functional frustration Protein knotting through concatenation significantly reduces folding stability Blind protein structure prediction using accelerated free-energy simulations Allosteric switching of agonist/antagonist activity by a single point mutation in the interluekin-1 receptor antagonist, IL-1Ra Multi-scaled explorations of binding-induced folding of intrinsically disordered protein inhibitor IA3 to its target enzyme.Exploration of multi-state conformational dynamics and underlying global functional landscape of maltose binding protein.Energetics and mechanisms of folding and flipping the myristoyl switch in the {beta}-trefoil protein, hisactophilin Understanding the folding-function tradeoff in proteins.Interdomain communication revealed in the diabetes drug target mitoNEET Effects of knots on protein folding properties.Modulation of folding energy landscape by charge-charge interactions: linking experiments with computational modeling β-Bulge triggers route-switching on the functional landscape of interleukin-1β.Optimizing ring assembly reveals the strength of weak interactions.Geometrical Frustration in Interleukin-33 Decouples the Dynamics of the Functional Element from the Folding Transition State Ensemble Accelerating molecular simulations of proteins using Bayesian inference on weak information.Biomolecular dynamics: order-disorder transitions and energy landscapes Altered backbone and side-chain interactions result in route heterogeneity during the folding of interleukin-1β (IL-1β)Pro-interleukin (IL)-1beta shares a core region of stability as compared with mature IL-1beta while maintaining a distinctly different configurational landscape: a comparative hydrogen/deuterium exchange mass spectrometry study.Evidence for the principle of minimal frustration in the evolution of protein folding landscapes.Experimental support for the foldability-function tradeoff hypothesis: segregation of the folding nucleus and functional regions in fibroblast growth factor-1 Frozen in beta.Evolution of a protein folding nucleus Importance of contact persistence in denatured state loop formation: kinetic insights into sequence effects on nucleation early in folding.Chromophore packing leads to hysteresis in GFP.Steric confinement and enhanced local flexibility assist knotting in simple models of protein folding.Engineering carboxypeptidase G2 circular permutations for the design of an autoinhibited enzyme.Anomalous dimensionality dependence of diffusion in a rugged energy landscape: How pathological is one dimension?Circular permutation in proteins

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P2860

Backtracking on the folding landscape of the beta-trefoil protein interleukin-1beta?

http://www.wikidata.org/entity/Q21045404

description

2008 nî lūn-bûn

@nan

2008 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2008 թվականի սեպտեմբերին հրատարակված գիտական հոդված

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2008年の論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年论文

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name

Backtracking on the folding landscape of the beta-trefoil protein interleukin-1beta?

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Backtracking on the folding landscape of the beta-trefoil protein interleukin-1beta?

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Backtracking on the folding landscape of the beta-trefoil protein interleukin-1beta?

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Backtracking on the folding landscape of the beta-trefoil protein interleukin-1beta?

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type

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Backtracking on the folding landscape of the beta-trefoil protein interleukin-1beta?

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Backtracking on the folding landscape of the beta-trefoil protein interleukin-1beta?

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Backtracking on the folding landscape of the beta-trefoil protein interleukin-1beta?

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Backtracking on the folding landscape of the beta-trefoil protein interleukin-1beta?

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prefLabel

Backtracking on the folding landscape of the beta-trefoil protein interleukin-1beta?

@ast

Backtracking on the folding landscape of the beta-trefoil protein interleukin-1beta?

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Backtracking on the folding landscape of the beta-trefoil protein interleukin-1beta?

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Backtracking on the folding landscape of the beta-trefoil protein interleukin-1beta?

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Proceedings of the National Academy of Sciences of the United States of America

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Backtracking on the folding landscape of the beta-trefoil protein interleukin-1beta?

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Dominique T Capraro

http://www.w3.org/2001/XMLSchema#string

Melinda Roy

http://www.w3.org/2001/XMLSchema#string

Patricia A Jennings

http://www.w3.org/2001/XMLSchema#string

P2860

Circular and circularly permuted forms of bovine pancreatic trypsin inhibitor

Principles determining the structure of beta-sheet barrels in proteins. II. The observed structures

beta-Trefoil fold. Patterns of structure and sequence in the Kunitz inhibitors interleukins-1 beta and 1 alpha and fibroblast growth factors

Amyloid-like fibril formation in an all beta-barrel protein. Partially structured intermediate state(s) is a precursor for fibril formation.

Transition-state structure as a unifying basis in protein-folding mechanisms: contact order, chain topology, stability, and the extended nucleus mechanism.

Folding of circular and permuted chymotrypsin inhibitor 2: retention of the folding nucleus.

Toward the detection and validation of repeats in protein structure.

Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding.

Contact order, transition state placement and the refolding rates of single domain proteins.

Multiple routes lead to the native state in the energy landscape of the beta-trefoil family

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10.1073/PNAS.0807812105

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39

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105

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23271622

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18806223

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protein folding

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2567455

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