Intrinsic disorder as a mechanism to optimize allosteric coupling in proteins.
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Classification of intrinsically disordered regions and proteinsIntrinsically disordered proteins in a physics-based worldIntrinsically disordered proteins are potential drug targetsELM: the status of the 2010 eukaryotic linear motif resourceProtein Folding and Mechanisms of ProteostasisStructural and energetic basis of allosteryThe ensemble nature of allosteryPrinciples of allosteric interactions in cell signalingCommon Internal Allosteric Network Links Anesthetic Binding Sites in a Pentameric Ligand-Gated Ion ChannelLigand-Induced Dynamic Changes in Extended PDZ Domains from NHERF1Structural analysis of poly-SUMO chain recognition by the RNF4-SIMs domainAn intrinsically disordered entropic switch determines allostery in Phd-Doc regulationThe contribution of intrinsically disordered regions to protein function, cellular complexity, and human diseaseA progesterone receptor co-activator (JDP2) mediates activity through interaction with residues in the carboxyl-terminal extension of the DNA binding domainEzrin induces long-range interdomain allostery in the scaffolding protein NHERF1Quantifying Correlations Between Allosteric Sites in Thermodynamic EnsemblesElectrostatically accelerated encounter and folding for facile recognition of intrinsically disordered proteinsDisordered proteinaceous machinesGlobal distribution of conformational states derived from redundant models in the PDB points to non-uniqueness of the protein structure.Influence of sequence changes and environment on intrinsically disordered proteins.Conserved tertiary couplings stabilize elements in the PDZ fold, leading to characteristic patterns of domain conformational flexibility.On the mechanism of protein fold-switching by a molecular sensor.Conditionally disordered proteins: bringing the environment back into the fold.Drug export and allosteric coupling in a multidrug transporter revealed by molecular simulations.Cooperative folding of intrinsically disordered domains drives assembly of a strong elongated proteinDynamic allostery in the methionine repressor revealed by force distribution analysis.Van't Hoff global analyses of variable temperature isothermal titration calorimetry data.Fast dynamics perturbation analysis for prediction of protein functional sites.Allosteric signaling in the biotin repressor occurs via local folding coupled to global dampening of protein dynamics.A peek into tropomyosin binding and unfolding on the actin filament.Structure-based predictive models for allosteric hot spots.Regulating transcription regulators via allostery and flexibilityThe importance of being flexible: the case of basic region leucine zipper transcriptional regulators.Correlation of structural stability with functional remodeling of high-density lipoproteins: the importance of being disordered.Disordered allostery: lessons from glucocorticoid receptor.Detecting Allosteric Networks Using Molecular Dynamics SimulationImportance of protein dynamics during enzymatic C-H bond cleavage catalysis.Seven transmembrane receptors as shapeshifting proteins: the impact of allosteric modulation and functional selectivity on new drug discovery.Pathological unfoldomics of uncontrolled chaos: intrinsically disordered proteins and human diseasesNet charge per residue modulates conformational ensembles of intrinsically disordered proteins
P2860
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P2860
Intrinsic disorder as a mechanism to optimize allosteric coupling in proteins.
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
2007年论文
@zh
2007年论文
@zh-cn
name
Intrinsic disorder as a mechanism to optimize allosteric coupling in proteins.
@ast
Intrinsic disorder as a mechanism to optimize allosteric coupling in proteins.
@en
type
label
Intrinsic disorder as a mechanism to optimize allosteric coupling in proteins.
@ast
Intrinsic disorder as a mechanism to optimize allosteric coupling in proteins.
@en
prefLabel
Intrinsic disorder as a mechanism to optimize allosteric coupling in proteins.
@ast
Intrinsic disorder as a mechanism to optimize allosteric coupling in proteins.
@en
P2860
P356
P1476
Intrinsic disorder as a mechanism to optimize allosteric coupling in proteins.
@en
P2093
E Brad Thompson
Vincent J Hilser
P2860
P304
P356
10.1073/PNAS.0700329104
P407
P577
2007-05-09T00:00:00Z