Conformational preferences in the Ser133-phosphorylated and non-phosphorylated forms of the kinase inducible transactivation domain of CREB
about
Intrinsically disordered proteins in a physics-based worldPhysicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs)Roles of phosphorylation and helix propensity in the binding of the KIX domain of CREB-binding protein by constitutive (c-Myb) and inducible (CREB) activatorsMultiscale enhanced sampling of intrinsically disordered protein conformations.Molecular recognition of protein surfaces: high affinity ligands for the CBP KIX domain.Structural plasticity in influenza virus protein NS2 (NEP).Discrete molecular dynamics can predict helical prestructured motifs in disordered proteinsRegulation of the cystic fibrosis transmembrane conductance regulator Cl- channel by its R domain.Overexpression of post-translationally modified peptides in Escherichia coli by co-expression with modifying enzymes.Intrinsically disordered proteins display no preference for chaperone binding in vivo.Binding-induced folding of a natively unstructured transcription factor.Molecular dynamics simulation of phosphorylated KID post-translational modification.PONDR-FIT: a meta-predictor of intrinsically disordered amino acidsMalleable machines take shape in eukaryotic transcriptional regulation.Expanding the proteome: disordered and alternatively folded proteins.Protein disorder and short conserved motifs in disordered regions are enriched near the cytoplasmic side of single-pass transmembrane proteinsA transcription factor-binding domain of the coactivator CBP is essential for long-term memory and the expression of specific target genes.Conformational propensities of intrinsically disordered proteins influence the mechanism of binding and foldingRate constants and mechanisms of intrinsically disordered proteins binding to structured targetsRole of Intrinsic Protein Disorder in the Function and Interactions of the Transcriptional Coactivators CREB-binding Protein (CBP) and p300A novel method of predicting protein disordered regions based on sequence features.A functional R domain from cystic fibrosis transmembrane conductance regulator is predominantly unstructured in solutionDetailed structural characterization of unbound protein phosphatase 1 inhibitors.Residual structure within the disordered C-terminal segment of p21(Waf1/Cip1/Sdi1) and its implications for molecular recognition.Linking folding and binding.pH-induced folding of an apoptotic coiled coil.Modulation of Intrinsically Disordered Protein Function by Post-translational Modifications.Optimization of the GBMV2 implicit solvent force field for accurate simulation of protein conformational equilibria.The principle of conformational signaling.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.Enhanced sampling simulations to construct free-energy landscape of protein-partner substrate interaction.Conformational Ensembles of an Intrinsically Disordered Protein pKID with and without a KIX Domain in Explicit Solvent Investigated by All-Atom Multicanonical Molecular Dynamics.Model for stathmin/OP18 binding to tubulin.LIM kinase 1 activates cAMP-responsive element-binding protein during the neuronal differentiation of immortalized hippocampal progenitor cells.Molecular epitopes of the ankyrin-spectrin interaction.The SCHOOL of nature: II. Protein order, disorder and oligomericity in transmembrane signaling.Functional characterization and conformational analysis of the Herpesvirus saimiri Tip-C484 protein.Unusual biophysics of immune signaling-related intrinsically disordered proteins.Structural analysis of the extracellular domain of vaccinia virus envelope protein, A27L, by NMR and CD spectroscopy.
P2860
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P2860
Conformational preferences in the Ser133-phosphorylated and non-phosphorylated forms of the kinase inducible transactivation domain of CREB
description
1998 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 1998
@ast
im Juli 1998 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
wetenschappelijk artikel (gepubliceerd op 1998/07/03)
@nl
наукова стаття, опублікована в липні 1998
@uk
مقالة علمية (نشرت في 3-7-1998)
@ar
name
Conformational preferences in ...... transactivation domain of CREB
@ast
Conformational preferences in ...... transactivation domain of CREB
@en
type
label
Conformational preferences in ...... transactivation domain of CREB
@ast
Conformational preferences in ...... transactivation domain of CREB
@en
prefLabel
Conformational preferences in ...... transactivation domain of CREB
@ast
Conformational preferences in ...... transactivation domain of CREB
@en
P2860
P1433
P1476
Conformational preferences in ...... transactivation domain of CREB
@en
P2093
G C Pérez-Alvarado
I Radhakrishnan
P2860
P304
P356
10.1016/S0014-5793(98)00680-2
P407
P577
1998-07-01T00:00:00Z