Time-Resolved Fluorescence Anisotropy Study of the Interaction Between DNA and a Peptide Truncated from the p53 Protein Core Domain.

about

Time-Resolved Fluorescence Anisotropy Study of the Interaction Between DNA and a Peptide Truncated from the p53 Protein Core Domain.

Item

http://www.wikidata.org/entity/Q45094683

description

2013 nî lūn-bûn

@nan

2013年の論文

@ja

2013年学术文章

@wuu

2013年学术文章

@zh

2013年学术文章

@zh-cn

2013年学术文章

@zh-hans

2013年学术文章

@zh-my

2013年学术文章

@zh-sg

2013年學術文章

@yue

2013年學術文章

@zh-hant

name

Time-Resolved Fluorescence Ani ...... m the p53 Protein Core Domain.

@en

Time-Resolved Fluorescence Ani ...... m the p53 Protein Core Domain.

@nl

type

Item

label

Time-Resolved Fluorescence Ani ...... m the p53 Protein Core Domain.

@en

Time-Resolved Fluorescence Ani ...... m the p53 Protein Core Domain.

@nl

prefLabel

Time-Resolved Fluorescence Ani ...... m the p53 Protein Core Domain.

@en

Time-Resolved Fluorescence Ani ...... m the p53 Protein Core Domain.

@nl

P1476

Time-Resolved Fluorescence Ani ...... m the p53 Protein Core Domain.

@en

P2093

Chengxuan Liu

http://www.w3.org/2001/XMLSchema#string

Gaiting Liang

http://www.w3.org/2001/XMLSchema#string

Lily Zu

http://www.w3.org/2001/XMLSchema#string

Zhen Liu

http://www.w3.org/2001/XMLSchema#string

P2860

Crystal structure of a superstable mutant of human p53 core domain. Insights into the mechanism of rescuing oncogenic mutations

Crystal Structure of the p53 Core Domain Bound to a Full Consensus Site as a Self-Assembled Tetramer

Crystal structure of a p53 tumor suppressor-DNA complex: understanding tumorigenic mutations

Definition of a consensus binding site for p53

Amino acid-base interactions: a three-dimensional analysis of protein-DNA interactions at an atomic level

p53 contains large unstructured regions in its native state.

Orientational dynamics and dye-DNA interactions in a dye-labeled DNA aptamer.

Ethanol and aloe emodin alter the p53 mutational spectrum in ultraviolet radiation-induced murine skin tumors.

Structure-function-rescue: the diverse nature of common p53 cancer mutants.

Functional four-base A/T gap core sequence CATTAG of P53 response elements specifically bound tetrameric P53 differently than two-base A/T gap core sequence CATG bound both dimeric and tetrameric P53

P2888

s10895-013-1322-7

P304

533-539

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1007/S10895-013-1322-7

http://www.w3.org/2001/XMLSchema#string

P433

http://www.w3.org/2001/XMLSchema#string

P478

http://www.w3.org/2001/XMLSchema#string

P577

2013-11-19T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P6179

1029894143

http://www.w3.org/2001/XMLSchema#string

P698

24249420

http://www.w3.org/2001/XMLSchema#string