Mutually compensatory mutations during evolution of the tetramerization domain of tumor suppressor p53 lead to impaired hetero-oligomerization
about
p73 and p63 are homotetramers capable of weak heterotypic interactions with each other but not with p53Accommodation of a highly symmetric core within a symmetric protein superfoldStructural evolution of C-terminal domains in the p53 familyStructural evolution of p53, p63, and p73: Implication for heterotetramer formationProtein sequence signatures support the African clade of mammalsPervasive cryptic epistasis in molecular evolutionThe nature of protein domain evolution: shaping the interaction networkCRASP: a program for analysis of coordinated substitutions in multiple alignments of protein sequences.Epistatic interactions modulate the evolution of mammalian mitochondrial respiratory complex components.Evolution of transcription factor binding sites in Mammalian gene regulatory regions: conservation and turnover.The role of tetramerization in p53 function.Dobzhansky-Muller incompatibilities in protein evolution.Missense meanderings in sequence space: a biophysical view of protein evolution.The origins of the evolutionary signal used to predict protein-protein interactions.Accelerated evolution and coevolution drove the evolutionary history of AGPase sub-units during angiosperm radiation.Disruption of an intermonomer salt bridge in the p53 tetramerization domain results in an increased propensity to form amyloid fibrils.Force-clamp spectroscopy detects residue co-evolution in enzyme catalysis.Protein co-evolution, co-adaptation and interactions.Co-evolution and co-adaptation in protein networks.Using experimental evolution to probe molecular mechanisms of protein function.The novel p53 isoform "delta p53" is a misfolded protein and does not bind the p21 promoter site.Deterministic, compensatory mutational events in the capsid of foot-and-mouth disease virus in response to the introduction of mutations found in viruses from persistent infections.Mechanism of rescue of common p53 cancer mutations by second-site suppressor mutations.Conformational detection of p53's oligomeric state by FlAsH Fluorescence.Fifty years of co-evolution and beyond: integrating co-evolution from molecules to species.Cotranslational protein assembly imposes evolutionary constraints on homomeric proteins.Functional trade-offs and environmental variation shaped ancient trajectories in the evolution of dim-light vision
P2860
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P2860
Mutually compensatory mutations during evolution of the tetramerization domain of tumor suppressor p53 lead to impaired hetero-oligomerization
description
1999 nî lūn-bûn
@nan
1999年の論文
@ja
1999年学术文章
@wuu
1999年学术文章
@zh-cn
1999年学术文章
@zh-hans
1999年学术文章
@zh-my
1999年学术文章
@zh-sg
1999年學術文章
@yue
1999年學術文章
@zh
1999年學術文章
@zh-hant
name
Mutually compensatory mutation ...... mpaired hetero-oligomerization
@ast
Mutually compensatory mutation ...... mpaired hetero-oligomerization
@en
type
label
Mutually compensatory mutation ...... mpaired hetero-oligomerization
@ast
Mutually compensatory mutation ...... mpaired hetero-oligomerization
@en
prefLabel
Mutually compensatory mutation ...... mpaired hetero-oligomerization
@ast
Mutually compensatory mutation ...... mpaired hetero-oligomerization
@en
P2860
P356
P1476
Mutually compensatory mutation ...... mpaired hetero-oligomerization
@en
P2093
P2860
P304
P356
10.1073/PNAS.96.7.3595
P407
P50
P577
1999-03-01T00:00:00Z