Oligomerization of the tetramerization domain of p53 probed by two- and three-color single-molecule FRET.
about
Theory of FRET "Spectroscopic Ruler" for Short Distances: Application to Polyproline.Protein folding transition path times from single molecule FRET.Mapping the energy landscapes of supramolecular assembly by thermal hysteresisDiffusion-limited association of disordered protein by non-native electrostatic interactionsWild-type p53 oligomerizes more efficiently than p53 hot-spot mutants and overcomes mutant p53 gain-of-function via a "dominant-positive" mechanism
P2860
Oligomerization of the tetramerization domain of p53 probed by two- and three-color single-molecule FRET.
description
2017 nî lūn-bûn
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2017年の論文
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2017年学术文章
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2017年学术文章
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name
Oligomerization of the tetrame ...... ee-color single-molecule FRET.
@en
Oligomerization of the tetrame ...... ee-color single-molecule FRET.
@nl
type
label
Oligomerization of the tetrame ...... ee-color single-molecule FRET.
@en
Oligomerization of the tetrame ...... ee-color single-molecule FRET.
@nl
prefLabel
Oligomerization of the tetrame ...... ee-color single-molecule FRET.
@en
Oligomerization of the tetrame ...... ee-color single-molecule FRET.
@nl
P2093
P2860
P356
P1476
Oligomerization of the tetrame ...... ee-color single-molecule FRET.
@en
P2093
Fanjie Meng
Irina V Gopich
Jae-Yeol Kim
John M Louis
Kevin McHale
P2860
P304
E6812-E6821
P356
10.1073/PNAS.1700357114
P407
P577
2017-07-31T00:00:00Z