Cargando…

Tyrosine Phosphorylation within the Intrinsically Disordered Cytosolic Domains of the B-Cell Receptor: An NMR-Based Structural Analysis

Intrinsically disordered proteins are found extensively in cell signaling pathways where they often are targets of posttranslational modifications e.g. phosphorylation. Such modifications can sometimes induce or disrupt secondary structure elements present in the modified protein. CD79a and CD79b ar...

Descripción completa

Detalles Bibliográficos
Autores principales:	Rosenlöw, Joakim, Isaksson, Linnéa, Mayzel, Maxim, Lengqvist, Johan, Orekhov, Vladislav Y.
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	Public Library of Science 2014
Materias:	Research Article
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4000212/ https://www.ncbi.nlm.nih.gov/pubmed/24769851 http://dx.doi.org/10.1371/journal.pone.0096199

Ejemplares similares

Time-resolved multidimensional NMR with non-uniform sampling
por: Mayzel, Maxim, et al.
Publicado: (2014)

Highly Efficient NMR Assignment of Intrinsically Disordered Proteins: Application to B- and T Cell Receptor Domains
por: Isaksson, Linnéa, et al.
Publicado: (2013)

XLSY: Extra‐Large NMR Spectroscopy
por: Pustovalova, Yulia, et al.
Publicado: (2018)

Backbone Assignment of the MALT1 Paracaspase by Solution NMR
por: Unnerståle, Sofia, et al.
Publicado: (2016)

Measurement of protein backbone (13)CO and (15)N relaxation dispersion at high resolution
por: Mayzel, Maxim, et al.
Publicado: (2017)

Unambiguous Tracking of Protein Phosphorylation by Fast High‐Resolution FOSY NMR
por: Lesovoy, Dmitry M., et al.
Publicado: (2021)

Role of Phosphorylation in the Modulation of the Glucocorticoid Receptor’s Intrinsically Disordered Domain
por: Kumar, Raj, et al.
Publicado: (2019)

Tyrosine Phosphorylation of Botulinum Neurotoxin Protease Domains
por: Toth, Stephen, et al.
Publicado: (2012)

Solution NMR of MPS-1 Reveals a Random Coil Cytosolic Domain Structure
por: Li, Pan, et al.
Publicado: (2014)

An NMR study on the intrinsically disordered core transactivation domain of human glucocorticoid receptor
por: Kim, Do-Hyoung, et al.
Publicado: (2017)

Tyrosine phosphorylation within the SH3 domain regulates CAS subcellular localization, cell migration, and invasiveness
por: Janoštiak, Radoslav, et al.
Publicado: (2011)

Rapid Biophysical Characterization and NMR Spectroscopy Structural Analysis of Small Proteins from Bacteria and Archaea
por: Kubatova, Nina, et al.
Publicado: (2020)

A Population Shift between Sparsely Populated Folding Intermediates Determines Amyloidogenicity
por: Karamanos, Theodoros K., et al.
Publicado: (2016)

Role of Phosphorylation Sites and the C2 Domain in Regulation of Cytosolic Phospholipase A(2)
por: Gijón, Miguel A., et al.
Publicado: (1999)

Effects of NMR Spectral Resolution on Protein Structure Calculation
por: Tikole, Suhas, et al.
Publicado: (2013)

Backbone and side chain NMR assignments for the intrinsically disordered cytoplasmic domain of human neuroligin-3
por: Wood, Kathleen, et al.
Publicado: (2011)

SH3 Domain Tyrosine Phosphorylation – Sites, Role and Evolution
por: Tatárová, Zuzana, et al.
Publicado: (2012)

Measurement of cytosolic calcium using 19F NMR.
por: Murphy, E, et al.
Publicado: (1990)

Site-specific phosphorylation regulates the structure and function of an intrinsically disordered domain of the glucocorticoid receptor
por: Khan, Shagufta H., et al.
Publicado: (2017)

Iterative Tyrosine Phosphorylation Controls Non-canonical Domain Utilization in Crk
por: Sriram, Ganapathy, et al.
Publicado: (2014)

Intrinsic disorder within an AKAP-protein kinase A complex guides local substrate phosphorylation
por: Smith, F Donelson, et al.
Publicado: (2013)

Structural Characterization of Intrinsically Disordered Proteins by NMR Spectroscopy
por: Kosol, Simone, et al.
Publicado: (2013)

NMR Lineshape Analysis of Intrinsically Disordered Protein Interactions
por: Waudby, Christopher A., et al.
Publicado: (2020)

Dataset for the NMR structure of the intrinsically disordered acidic region of XPC bound to the PH domain of TFIIH p62
por: Okuda, Masahiko, et al.
Publicado: (2016)

Role of cytosolic, tyrosine‐insensitive prephenate dehydrogenase in Medicago truncatula
por: Schenck, Craig A., et al.
Publicado: (2020)

Folding and Intrinsic Disorder of the Receptor Tyrosine Kinase KIT Insert Domain Seen by Conventional Molecular Dynamics Simulations
por: Ledoux, Julie, et al.
Publicado: (2021)

Phosphorylation of Intrinsically Disordered Regions in Remorin Proteins
por: Marín, Macarena, et al.
Publicado: (2012)

NMR contributions to structural dynamics studies of intrinsically disordered proteins()
por: Konrat, Robert
Publicado: (2014)

Altered localization and cytoplasmic domain-binding properties of tyrosine-phosphorylated beta 1 integrin
Publicado: (1994)

Dual regulation of cytosolic ascorbate peroxidase (APX) by tyrosine nitration and S-nitrosylation
por: Begara-Morales, Juan C., et al.
Publicado: (2014)

NMR Structure of Integrin α4 Cytosolic Tail and Its Interactions with Paxillin
por: Chua, Geok-Lin, et al.
Publicado: (2013)

Spectrin redistributes to the cytosol and is phosphorylated during mitosis in cultured cells
Publicado: (1992)

Tyrosine phosphorylation and bacterial virulence
por: Whitmore, Sarah E, et al.
Publicado: (2012)

Wide-line NMR and DSC studies on intrinsically disordered p53 transactivation domain and its helically pre-structured segment
por: Tompa, Peter, et al.
Publicado: (2016)

Ensemble description of the intrinsically disordered N-terminal domain of the Nipah virus P/V protein from combined NMR and SAXS
por: Schiavina, Marco, et al.
Publicado: (2020)

Resolution enhancement of NMR by decoupling with the low-rank Hankel model
por: Qiu, Tianyu, et al.
Publicado: (2023)

A Method for Systematic Assessment of Intrinsically Disordered Protein Regions by NMR
por: Goda, Natsuko, et al.
Publicado: (2015)

NMR characterization of solvent accessibility and transient structure in intrinsically disordered proteins
por: Hartlmüller, Christoph, et al.
Publicado: (2019)

Troubleshooting Guide to Expressing Intrinsically Disordered Proteins for Use in NMR Experiments
por: Graether, Steffen P.
Publicado: (2019)

Synergies of Single Molecule Fluorescence and NMR for the Study of Intrinsically Disordered Proteins
por: Naudi-Fabra, Samuel, et al.
Publicado: (2021)

Cannot write session to /tmp/vufind_sessions/sess_cu4l82veks0nd7bd0o7qm73m8i