about
The conserved CPH domains of Cul7 and PARC are protein-protein interaction modules that bind the tetramerization domain of p53An induced fit mechanism regulates p53 DNA binding kinetics to confer sequence specificityMolecular basis of Pirh2-mediated p53 ubiquitylationDNA damage in oocytes induces a switch of the quality control factor TAp63α from dimer to tetramerMechanism of TAp73 inhibition by ΔNp63 and structural basis of p63/p73 hetero-tetramerizationTwo p53 tetramers bind one consensus DNA response elementVolume exclusion and soft interaction effects on protein stability under crowded conditions.The C-terminus of p63 contains multiple regulatory elements with different functions.Constant rate of p53 tetramerization in response to DNA damage controls the p53 response.Regulation of p53 localization and activity by Ubc13.Utilizing NMR to study the structure of growth-inhibitory proteins.Dominant-negative mechanism of leukemogenic PAX5 fusions.Cellular Synthesis of Protein Catenanes.Disruption of an intermonomer salt bridge in the p53 tetramerization domain results in an increased propensity to form amyloid fibrils.Analysis of the oligomeric state and transactivation potential of TAp73α.Cyclic olefin homopolymer-based microfluidics for protein crystallization and in situ X-ray diffraction.Cosolutes, Crowding, and Protein Folding Kinetics.p53 oligomerization status modulates cell fate decisions between growth, arrest and apoptosis.Single-Molecule characterization of oligomerization kinetics and equilibria of the tumor suppressor p53.Intracellular pH modulates quinary structure.Threading a peptide through a peptide: protein loops, rotaxanes, and knots.A novel member of the YchN-like fold: solution structure of the hypothetical protein Tm0979 from Thermotoga maritima.An osmolyte mitigates the destabilizing effect of protein crowding.Insight into the structural basis of pro- and antiapoptotic p53 modulation by ASPP proteins.Oligomerization of the tetramerization domain of p53 probed by two- and three-color single-molecule FRET.Protein Catenation Enhances Both the Stability and Activity of Folded Structural Domains.
P2860
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P2860
description
2001 nî lūn-bûn
@nan
2001 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի մարտին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Structure and functionality of a designed p53 dimer
@ast
Structure and functionality of a designed p53 dimer
@en
Structure and functionality of a designed p53 dimer
@nl
type
label
Structure and functionality of a designed p53 dimer
@ast
Structure and functionality of a designed p53 dimer
@en
Structure and functionality of a designed p53 dimer
@nl
prefLabel
Structure and functionality of a designed p53 dimer
@ast
Structure and functionality of a designed p53 dimer
@en
Structure and functionality of a designed p53 dimer
@nl
P2093
P3181
P356
P1476
Structure and functionality of a designed p53 dimer
@en
P2093
P304
P3181
P356
10.1006/JMBI.2001.4450
P407
P577
2001-03-01T00:00:00Z