Random-coil chemical shifts of phosphorylated amino acids.
about
Characterization of protein secondary structure from NMR chemical shiftsNMR Meets Tau: Insights into Its Function and PathologyTyrosine phosphorylation within the intrinsically disordered cytosolic domains of the B-cell receptor: an NMR-based structural analysisDetection of methylation, acetylation and glycosylation of protein residues by monitoring (13)C chemical-shift changes: A quantum-chemical studyCell signaling, post-translational protein modifications and NMR spectroscopyβ-Sheet nanocrystalline domains formed from phosphorylated serine-rich motifs in caddisfly larval silk: a solid state NMR and XRD study.Light-regulated sampling of protein tyrosine kinase activity.Multisite phosphorylation disrupts arginine-glutamate salt bridge networks required for binding of cytoplasmic linker-associated protein 2 (CLASP2) to end-binding protein 1 (EB1).Physicochemical characterization of casein phosphopeptide-amorphous calcium phosphate nanocomplexes.Overexpression of post-translationally modified peptides in Escherichia coli by co-expression with modifying enzymes.Phosphorylation induces sequence-specific conformational switches in the RNA polymerase II C-terminal domain.Gradual phosphorylation regulates PC4 coactivator function.The affinity of Ets-1 for DNA is modulated by phosphorylation through transient interactions of an unstructured region.Phosphorylation in intrinsically disordered regions regulates the activity of Neurogenin2.Structural and Dynamic Features of F-recruitment Site Driven Substrate Phosphorylation by ERK2.Characterization of Neuronal Tau Protein as a Target of Extracellular Signal-regulated KinaseStructure of phosphorylated UBL domain and insights into PINK1-orchestrated parkin activation.Time-resolved multidimensional NMR with non-uniform sampling.CFTR regulatory region interacts with NBD1 predominantly via multiple transient helicesUbiquitin S65 phosphorylation engenders a pH-sensitive conformational switch.Extended string-like binding of the phosphorylated HP1α N-terminal tail to the lysine 9-methylated histone H3 tailNuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins.OGlcNAcylation and phosphorylation have opposing structural effects in tau: phosphothreonine induces particular conformational order.OGlcNAcylation and phosphorylation have similar structural effects in α-helices: post-translational modifications as inducible start and stop signals in α-helices, with greater structural effects on threonine modification.Molecular Dynamics Simulation of Tau Peptides for the Investigation of Conformational Changes Induced by Specific Phosphorylation Patterns.Spectroscopic studies of GSK3{beta} phosphorylation of the neuronal tau protein and its interaction with the N-terminal domain of apolipoprotein E.A mechanistic design principle for protein tyrosine kinase sensors: application to a validated cancer target.The PNT domain from Drosophila pointed-P2 contains a dynamic N-terminal helix preceded by a disordered phosphoacceptor sequence.Opposing effects of Elk-1 multisite phosphorylation shape its response to ERK activationComparative analysis of Erk phosphorylation suggests a mixed strategy for measuring phospho-form distributions.Interfacial enzyme kinetics of a membrane bound kinase analyzed by real-time MAS-NMR.pH-dependent random coil (1)H, (13)C, and (15)N chemical shifts of the ionizable amino acids: a guide for protein pK a measurements.Site-specific NMR mapping and time-resolved monitoring of serine and threonine phosphorylation in reconstituted kinase reactions and mammalian cell extracts.Protein dynamics of bovine dentin phosphophoryn.CDK4/6 Inhibition Augments Anti-Tumor Immunity by Enhancing T Cell Activation.The Study of Posttranslational Modifications of Tau Protein by Nuclear Magnetic Resonance Spectroscopy: Phosphorylation of Tau Protein by ERK2 Recombinant Kinase and Rat Brain Extract, and Acetylation by Recombinant Creb-Binding Protein.Impact of different ionization states of phosphorylated Serine-65 on ubiquitin structure and interactions.Structural evaluations of tau protein conformation: methodologies and approaches.Random coil chemical shift for intrinsically disordered proteins: effects of temperature and pH.Structural characterization by nuclear magnetic resonance of the impact of phosphorylation in the proline-rich region of the disordered Tau protein.
P2860
Q24649700-03DABD1E-8F9A-424D-B235-A05C48544FA4Q26747418-8DA3C567-32B5-4E60-A8E4-176AD9E47FF4Q28538256-37C17ECB-5FFF-4CCB-AB2B-A154A77BBD12Q28828681-05AF4535-4FE9-4488-9BE6-1C1A2CDBCBD5Q28830783-709E89D0-2C93-4E5C-B6DA-064BA4B21DF0Q30427747-CC87752A-F7C0-4FBA-82B3-C0A20968E36EQ30486657-2E3AC990-87BE-4E37-A2D7-62E366601584Q30514537-F89AB833-922D-49ED-87ED-AE7A0469039FQ33210997-649BC694-52C3-4D70-A6D2-31DBE306759CQ33308396-99A06E25-6880-496D-A13D-7648551BE629Q33705708-5B3CEE24-8272-4C7B-A80E-AB7D93F6F926Q34524536-908DAD58-63A7-4AC4-AE57-60B857AEC297Q34806524-3C851605-5B7C-4110-AE78-99F0EC29EED6Q35397840-9242489C-BE2B-422B-9176-BA389CAF6753Q35693224-77F60F4A-51FF-4FEA-BBAB-98EB3423B738Q36755114-BA1737B1-22F8-4EC0-93D8-C9B578ED598EQ37589985-BA18D5FA-6F2E-484D-AE38-4C1E3FF1FB92Q37594147-139865AC-487D-4289-9A81-870DBDE9A12BQ37618800-ACC4F5F0-4338-4FDB-92AA-C58642B0C42BQ38727017-9DC40DC4-3B49-4048-8364-5B39362F6960Q38743946-E1BB6DD7-29B0-4527-A357-5A4F6C5F1F77Q39036047-114BECFC-2058-4657-9463-FC6F1F21FFE1Q39045088-C69D1642-7954-4CCF-AF83-03C74043A442Q39045464-BB74FBC6-4A58-4AF8-8A93-5E0A152BAD5DQ39099836-4837880E-E2EF-4E73-805F-FF252100628BQ41771621-3D594384-708C-4D68-8B3D-DC89DA80EAECQ41840642-9DD974A2-FC83-432B-A237-977D68FD08BDQ41971847-1F5DF45C-0222-41C0-BBFF-2E00964F72E5Q42320390-771C84AC-ACBE-4E65-A3DA-ED2B9ACE2935Q42735782-E7BC0E32-33EA-455F-B5AC-E36C9D2D0A8EQ43893115-8DE06CDB-9902-4919-9ED6-0C679782FC3DQ44914553-2AE7399D-E0F3-4DD0-9C71-11304F1F96FBQ45738787-C00ACB95-23AE-4D60-BA3D-819E99952587Q46283468-E889EAB6-5C27-4B71-ACE8-119446D9578EQ47443248-C0FF1075-B058-424F-9279-1F2A148BE7A7Q48395326-5E4E3567-50CF-4D01-ACA1-93DAEF542473Q49436375-78BD3FD0-6E6F-4EE2-9439-4290CE0CFAEEQ51104104-7A27407D-3C24-4A31-8FA9-28A1D7722FE6Q53079294-8F9725A3-A18D-4B75-B63D-F0C2785C6F24Q53323738-B9647B2E-338A-40BF-8504-B8D667A45E33
P2860
Random-coil chemical shifts of phosphorylated amino acids.
description
1999 nî lūn-bûn
@nan
1999 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Random-coil chemical shifts of phosphorylated amino acids.
@ast
Random-coil chemical shifts of phosphorylated amino acids.
@en
type
label
Random-coil chemical shifts of phosphorylated amino acids.
@ast
Random-coil chemical shifts of phosphorylated amino acids.
@en
prefLabel
Random-coil chemical shifts of phosphorylated amino acids.
@ast
Random-coil chemical shifts of phosphorylated amino acids.
@en
P356
P1476
Random-coil chemical shifts of phosphorylated amino acids
@en
P2093
Bienkiewicz EA
P2888
P304
P356
10.1023/A:1008375029746
P577
1999-11-01T00:00:00Z
P6179
1018945939