[NMR paper] Tyrosine Phosphorylation within the Intrinsically Disordered Cytosolic Domains of the B-Cell Receptor: An NMR-Based Structural Analysis.
Tyrosine Phosphorylation within the Intrinsically Disordered Cytosolic Domains of the B-Cell Receptor: An NMR-Based Structural Analysis.
Related Articles Tyrosine Phosphorylation within the Intrinsically Disordered Cytosolic Domains of the B-Cell Receptor: An NMR-Based Structural Analysis.
PLoS One. 2014;9(4):e96199
Authors: Rosenlöw J, Isaksson L, Mayzel M, Lengqvist J, Orekhov VY
Abstract
Intrinsically disordered proteins are found extensively in cell signaling pathways where they often are targets of posttranslational...
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[NMR paper] Unraveling a phosphorylation event in a folded protein by NMR spectroscopy: phosphorylation of the Pin1 WW domain by PKA.
Unraveling a phosphorylation event in a folded protein by NMR spectroscopy: phosphorylation of the Pin1 WW domain by PKA.
Unraveling a phosphorylation event in a folded protein by NMR spectroscopy: phosphorylation of the Pin1 WW domain by PKA.
J Biomol NMR. 2013 Mar 2;
Authors: Smet-Nocca C, Launay H, Wieruszeski JM, Lippens G, Landrieu I
Abstract
The Pin1 protein plays a critical role in the functional regulation of the hyperphosphorylated neuronal Tau protein in Alzheimer's disease and is by itself regulated by phosphorylation. We have...
Descriptive Review of Current NMR-Based Metabolomic Data Analysis Packages
Descriptive Review of Current NMR-Based Metabolomic Data Analysis Packages
Publication year: 2011
Source: Progress in Nuclear Magnetic Resonance Spectroscopy, In Press, Accepted Manuscript, Available online 21 February 2011</br>
Jose L., Izquierdo-García , Palmira, Villa , Angelos, Kyriazis , Laura del, Puerto-Nevado , Sandra, Pérez-Rial , ...</br>
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Review NMR-based investigation into protein phosphorylation - ScienceDirect.com
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