Molecular Modeling of the Structural and Dynamical Changes in Calcium Channel TRPV5 Induced by the African-Specific A563T Variation
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Deprotonation states of the two active site water molecules regulate the binding of protein phosphatase 5 with its substrate: a molecular dynamics study.The L530R variation associated with recurrent kidney stones impairs the structure and function of TRPV5.Activation mechanisms of αVβ3 integrin by binding to fibronectin: A computational study.Phosphorylation of KLHL3 at serine 433 impairs its interaction with the acidic motif of WNK4: a molecular dynamics study.
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Molecular Modeling of the Structural and Dynamical Changes in Calcium Channel TRPV5 Induced by the African-Specific A563T Variation
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article científic
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article scientifique
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articolo scientifico
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artigo científico
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bilimsel makale
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scientific article published on 03 February 2016
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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Molecular Modeling of the Stru ...... rican-Specific A563T Variation
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Molecular Modeling of the Stru ...... ican-Specific A563T Variation.
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label
Molecular Modeling of the Stru ...... rican-Specific A563T Variation
@en
Molecular Modeling of the Stru ...... ican-Specific A563T Variation.
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prefLabel
Molecular Modeling of the Stru ...... rican-Specific A563T Variation
@en
Molecular Modeling of the Stru ...... ican-Specific A563T Variation.
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P2860
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Molecular Modeling of the Stru ...... rican-Specific A563T Variation
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P2093
Ji-Bin Peng
Lingyun Wang
P2860
P304
P356
10.1021/ACS.BIOCHEM.5B00732
P407
P577
2016-02-03T00:00:00Z