Molecular Simulations Reveal an Unresolved Conformationof the Type IA Protein Kinase A Regulatory Subunit and Suggest ItsRole in the cAMP Regulatory Mechanism
Molecular Simulations Reveal an Unresolved Conformationof the Type IA Protein Kinase A Regulatory Subunit and Suggest ItsRole in the cAMP Regulatory Mechanism
[NMR paper] Ca2+-induced PRE-NMR changes in the troponin complex reveal the possessive nature of the cardiac isoform for its regulatory switch.
Ca2+-induced PRE-NMR changes in the troponin complex reveal the possessive nature of the cardiac isoform for its regulatory switch.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.plosone.org-images-pone_120x30.png http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.ncbi.nlm.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Ca2+-induced PRE-NMR changes in the troponin complex reveal the possessive nature of the cardiac isoform for its regulatory switch.
PLoS One. 2014;9(11):e112976
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[NMR paper] Structural Dynamics and Conformational Equilibria of SERCA Regulatory Proteins in Membranes by Solid-State NMR Restrained Simulations.
Structural Dynamics and Conformational Equilibria of SERCA Regulatory Proteins in Membranes by Solid-State NMR Restrained Simulations.
Related Articles Structural Dynamics and Conformational Equilibria of SERCA Regulatory Proteins in Membranes by Solid-State NMR Restrained Simulations.
Biophys J. 2014 Jun 17;106(12):2566-2576
Authors: De Simone A, Mote KR, Veglia G
Abstract
Solid-state NMR spectroscopy is emerging as a powerful approach to determine structure, topology, and conformational dynamics of membrane proteins at the...
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Structural Dynamics and Conformational Equilibria of SERCA Regulatory Proteins in Membranes by Solid-State NMR Restrained Simulations
Structural Dynamics and Conformational Equilibria of SERCA Regulatory Proteins in Membranes by Solid-State NMR Restrained Simulations
Publication date: 17 June 2014
Source:Biophysical Journal, Volume 106, Issue 12</br>
Author(s): Alfonso De*Simone , Kaustubh*R. Mote , Gianluigi Veglia</br>
Solid-state NMR spectroscopy is emerging as a powerful approach to determine structure, topology, and conformational dynamics of membrane proteins at the atomic level. Conformational dynamics are often inferred and quantified from the motional averaging of the NMR parameters....
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[NMR paper] Tapping the translation potential of cAMP signalling: molecular basis for selectivity in cAMP agonism and antagonism as revealed by NMR.
Tapping the translation potential of cAMP signalling: molecular basis for selectivity in cAMP agonism and antagonism as revealed by NMR.
Related Articles Tapping the translation potential of cAMP signalling: molecular basis for selectivity in cAMP agonism and antagonism as revealed by NMR.
Biochem Soc Trans. 2014 Apr 1;42(2):302-7
Authors: Boulton S, Akimoto M, Vanschouwen B, Moleschi K, Selvaratnam R, Giri R, Melacini G
Abstract
Eukaryotic CBDs (cAMP-binding domains) control multiple cellular functions (e.g. phosphorylation, guanine...
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[NMR paper] NMR Binding and Crystal Structure Reveal that Intrinsically-unstructured Regulatory Domain Auto-inhibits PAK4 by a Mechanism Different for that of PAK1.
NMR Binding and Crystal Structure Reveal that Intrinsically-unstructured Regulatory Domain Auto-inhibits PAK4 by a Mechanism Different for that of PAK1.
NMR Binding and Crystal Structure Reveal that Intrinsically-unstructured Regulatory Domain Auto-inhibits PAK4 by a Mechanism Different for that of PAK1.
Biochem Biophys Res Commun. 2013 Jul 19;
Authors: Wang W, Lim L, Baskaran Y, Manser E, Song J
Abstract
Six human PAK members are classified into groups I (PAKs 1-3) and II (PAK4-6). Previously, only group I PAKs were thought to be...
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Discovered a new regulatory mechanism of c-Src, the human protein bound to ... - HealthCanal.com
Discovered a new regulatory mechanism of c-Src, the human protein bound to ... - HealthCanal.com
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Discovered a new regulatory mechanism of c-Src, the human protein bound to ...
HealthCanal.com
... leader of the Biomolecular Nuclear Magnetic Resonance (NMR) Research Group, affiliated with the Department of Organic Chemistry of the UB, â??the discovery of a new regulatory mechanism in such a relevant and extensively studied protein proves the ...
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[NMR paper] NMR structure of the HIV-1 regulatory protein VPR.
NMR structure of the HIV-1 regulatory protein VPR.
Related Articles NMR structure of the HIV-1 regulatory protein VPR.
J Mol Biol. 2003 Mar 14;327(1):215-27
Authors: Morellet N, Bouaziz S, Petitjean P, Roques BP
The human immunodeficiency virus type 1 (HIV-1) genome encodes a highly conserved regulatory gene product, Vpr (96 residues, 14kDa), which is incorporated into virions. In the infected cells, Vpr, expressed late in the virus cycle, is believed to function in the early phases of HIV-1 replication, such as nuclear migration of...
Molecular Simulations Reveal an Unresolved Conformationof the Type IA Protein Kinase A Regulatory Subunit and Suggest ItsRole in the cAMP Regulatory Mechanism
Linear Mode
