Direct effects of phosphorylation on the preferred backbone conformation of peptides: a nuclear magnetic resonance study.
about
Tyrosine phosphorylation of the well packed ephrinB cytoplasmic beta-hairpin for reverse signaling. Structural consequences and binding propertiesConformational changes in protein loops and helices induced by post-translational phosphorylation.AMBER force-field parameters for phosphorylated amino acids in different protonation states: phosphoserine, phosphothreonine, phosphotyrosine, and phosphohistidine.The natively disordered loop of Bcl-2 undergoes phosphorylation-dependent conformational change and interacts with Pin1A proposed signaling motif for nuclear import in mRNA processing via the formation of arginine claw.Phosphorylation Increases Persistence Length and End-to-End Distance of a Segment of Tau Protein.Phosphorylation of prion protein at serine 43 induces prion protein conformational changeOGlcNAcylation 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 Basis for Phosphorylation-dependent SUMO Recognition by the DNA Repair Protein RAP80.Structure of the 1-36 N-terminal fragment of human phospholamban phosphorylated at Ser-16 and Thr-17.Phosphorylation of JAK2 at serine 523: a negative regulator of JAK2 that is stimulated by growth hormone and epidermal growth factor.Detecting the site of phosphorylation in phosphopeptides without loss of phosphate group using MALDI TOF mass spectrometry.Phosphorylation disrupts the central helix in Op18/stathmin and suppresses binding to tubulin.Phosphorylation of serine residues affects the conformation of the calmodulin binding domain of human protein 4.1.Synthesis and conformational analysis of stevastelin C3 analogues and their activity against the dual-specific vaccina H1-related phosphatase.CDK4/6 Inhibition Augments Anti-Tumor Immunity by Enhancing T Cell Activation.Phosphorylated α-Synuclein-Copper Complex Formation in the Pathogenesis of Parkinson's Disease.Loss of intramolecular electrostatic interactions and limited conformational ensemble may promote self-association of cis-tau peptide.Phosphorylation alters backbone conformational preferences of serine and threonine peptides.Dynamical role of phosphorylation on serine/threonine-proline Pin1 substrates from constant force molecular dynamics simulations.Control of intrinsically disordered stathmin by multisite phosphorylation.
P2860
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P2860
Direct effects of phosphorylation on the preferred backbone conformation of peptides: a nuclear magnetic resonance study.
description
1999 nî lūn-bûn
@nan
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
1999年论文
@zh
1999年论文
@zh-cn
name
Direct effects of phosphorylat ...... lear magnetic resonance study.
@en
type
label
Direct effects of phosphorylat ...... lear magnetic resonance study.
@en
prefLabel
Direct effects of phosphorylat ...... lear magnetic resonance study.
@en
P2093
P2860
P1433
P1476
Direct effects of phosphorylat ...... lear magnetic resonance study.
@en
P2093
P2860
P356
10.1016/S0006-3495(99)77179-1
P407
P433
P577
1999-01-01T00:00:00Z