The dynamics of the catalytic site in small GTPases, variations on a common motif.
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Noncanonical Myo9b-RhoGAP Accelerates RhoA GTP Hydrolysis by a Dual-Arginine-Finger MechanismDeciphering the Molecular and Functional Basis of RHOGAP Family Proteins: A SYSTEMATIC APPROACH TOWARD SELECTIVE INACTIVATION OF RHO FAMILY PROTEINS.The carbonate/bicarbonate system as a pH indicator for infrared spectroscopy.Rab proteins and the compartmentalization of the endosomal systemPatients with Griscelli syndrome and normal pigmentation identify RAB27A mutations that selectively disrupt MUNC13-4 binding.Overview of simulation studies on the enzymatic activity and conformational dynamics of the GTPase Ras.Site-specific monoubiquitination activates Ras by impeding GTPase-activating protein functionInvited review: Small GTPases and their GAPs.Rho GTPases, their post-translational modifications, disease-associated mutations and pharmacological inhibitors.Integration of Fourier Transform Infrared Spectroscopy, Fluorescence Spectroscopy, Steady-state Kinetics and Molecular Dynamics Simulations of Gαi1 Distinguishes between the GTP Hydrolysis and GDP Release Mechanism.
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P2860
The dynamics of the catalytic site in small GTPases, variations on a common motif.
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article científic
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article scientifique
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articol științific
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articolo scientifico
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artigo científico
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artigo científico
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The dynamics of the catalytic site in small GTPases, variations on a common motif.
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label
The dynamics of the catalytic site in small GTPases, variations on a common motif.
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prefLabel
The dynamics of the catalytic site in small GTPases, variations on a common motif.
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P2860
P1433
P1476
The dynamics of the catalytic site in small GTPases, variations on a common motif.
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P2093
Carsten Kötting
P2860
P304
P356
10.1016/J.FEBSLET.2013.05.021
P407
P577
2013-05-16T00:00:00Z