High thermostability and lack of cooperative DNA binding distinguish the p63 core domain from the homologous tumor suppressor p53.
about
Crystal structure of a p53 core tetramer bound to DNAStabilising the DNA-binding domain of p53 by rational design of its hydrophobic coreStructures of p63 DNA binding domain in complexes with half-site and with spacer-containing full response elementsPliable DNA Conformation of Response Elements Bound to Transcription Factor p63deltaNp63alpha functions as both a positive and a negative transcriptional regulator and blocks in vitro differentiation of murine keratinocytesSolution structure and binding specificity of the p63 DNA binding domainStability of the core domain of p53: insights from computer simulations.Cooperativity dominates the genomic organization of p53-response elements: a mechanistic viewThe p53 core domain is a molten globule at low pH: functional implications of a partially unfolded structure.SCH529074, a small molecule activator of mutant p53, which binds p53 DNA binding domain (DBD), restores growth-suppressive function to mutant p53 and interrupts HDM2-mediated ubiquitination of wild type p53Stability of p53 homologsPreferential binding of hot spot mutant p53 proteins to supercoiled DNA in vitro and in cells.BEclear: Batch Effect Detection and Adjustment in DNA Methylation Data.Diffusion NMR spectroscopy: folding and aggregation of domains in p53.The functional domains in p53 family proteins exhibit both common and distinct properties.Quality control in oocytes by p63 is based on a spring-loaded activation mechanism on the molecular and cellular level.Structure of the p53 core domain dimer bound to DNA.Differential recognition of response elements determines target gene specificity for p53 and p63Effects of stability on the biological function of p53.A p53-type response element in the GDF15 promoter confers high specificity for p53 activation.WT p53, but not tumor-derived mutants, bind to Bcl2 via the DNA binding domain and induce mitochondrial permeabilization.p53 binding prevents phosphatase-mediated inactivation of diphosphorylated c-Jun N-terminal kinase.Azidophenyl as a click-transformable redox label of DNA suitable for electrochemical detection of DNA-protein interactions.No evidence of direct binding between ursodeoxycholic acid and the p53 DNA-binding domain.Master regulatory role of p63 in epidermal development and disease.Structural basis for p53 binding-induced DNA bending.Vinylsulfonamide and acrylamide modification of DNA for cross-linking with proteins.Intrinsic aggregation propensity of the p63 and p73 TI domains correlates with p53R175H interaction and suggests further significance of aggregation events in the p53 family.In vitro folding and characterization of the p53 DNA binding domain.
P2860
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P2860
High thermostability and lack of cooperative DNA binding distinguish the p63 core domain from the homologous tumor suppressor p53.
description
2001 nî lūn-bûn
@nan
2001年の論文
@ja
2001年学术文章
@wuu
2001年学术文章
@zh
2001年学术文章
@zh-cn
2001年学术文章
@zh-hans
2001年学术文章
@zh-my
2001年学术文章
@zh-sg
2001年學術文章
@yue
2001年學術文章
@zh-hant
name
High thermostability and lack ...... mologous tumor suppressor p53.
@en
High thermostability and lack ...... mologous tumor suppressor p53.
@nl
type
label
High thermostability and lack ...... mologous tumor suppressor p53.
@en
High thermostability and lack ...... mologous tumor suppressor p53.
@nl
prefLabel
High thermostability and lack ...... mologous tumor suppressor p53.
@en
High thermostability and lack ...... mologous tumor suppressor p53.
@nl
P2093
P2860
P356
P1476
High thermostability and lack ...... mologous tumor suppressor p53.
@en
P2093
P2860
P304
37390-37401
P356
10.1074/JBC.M103801200
P407
P577
2001-07-26T00:00:00Z