Structural basis for reactivating the mutant TERT promoter by cooperative binding of p52 and ETS1

10.1038/s41467-018-05644-0

Saved in:
Bibliographic Details
Main Authors: Xu, X, Li, Y, Bharath, S.R, Ozturk, M.B, Bowler, M.W, Loo, B.Z.L, Tergaonkar, V, Song, H
Other Authors: BIOCHEMISTRY
Format: Article
Published: Nature Publishing Group 2020
Subjects:
DNA
Online Access:https://scholarbank.nus.edu.sg/handle/10635/174210
Tags: Add Tag
No Tags, Be the first to tag this record!
Institution: National University of Singapore
id sg-nus-scholar.10635-174210
record_format dspace
spelling sg-nus-scholar.10635-1742102024-04-22T03:11:05Z Structural basis for reactivating the mutant TERT promoter by cooperative binding of p52 and ETS1 Xu, X Li, Y Bharath, S.R Ozturk, M.B Bowler, M.W Loo, B.Z.L Tergaonkar, V Song, H BIOCHEMISTRY DNA fragment immunoglobulin enhancer binding protein protein p52 transcription factor Ets 1 disulfide DNA ETS1 protein, human immunoglobulin enhancer binding protein protein binding telomerase TERT protein, human transcription factor Ets 1 cancer chemical binding complexity crystal structure DNA inhibition mutation reactivation Article binding affinity crystal structure DNA binding ETS domain gene activation HEK293T cell line human human cell immunoprecipitation multiple cancer promoter region protein protein interaction signal transduction TERT gene transactivation binding site chemistry enzyme activation Escherichia coli genetics HEK293 cell line metabolism protein multimerization X ray crystallography Binding Sites Crystallography, X-Ray Disulfides DNA Enzyme Activation Escherichia coli HEK293 Cells Humans NF-kappa B NF-kappa B p52 Subunit Promoter Regions, Genetic Protein Binding Protein Multimerization Proto-Oncogene Protein c-ets-1 Signal Transduction Telomerase 10.1038/s41467-018-05644-0 Nature Communications 9 1 3183 2020-09-04T01:46:49Z 2020-09-04T01:46:49Z 2018 Article Xu, X, Li, Y, Bharath, S.R, Ozturk, M.B, Bowler, M.W, Loo, B.Z.L, Tergaonkar, V, Song, H (2018). Structural basis for reactivating the mutant TERT promoter by cooperative binding of p52 and ETS1. Nature Communications 9 (1) : 3183. ScholarBank@NUS Repository. https://doi.org/10.1038/s41467-018-05644-0 2041-1723 https://scholarbank.nus.edu.sg/handle/10635/174210 Nature Publishing Group Unpaywall 20200831
institution National University of Singapore
building NUS Library
continent Asia
country Singapore
Singapore
content_provider NUS Library
collection ScholarBank@NUS
topic DNA fragment
immunoglobulin enhancer binding protein
protein p52
transcription factor Ets 1
disulfide
DNA
ETS1 protein, human
immunoglobulin enhancer binding protein
protein binding
telomerase
TERT protein, human
transcription factor Ets 1
cancer
chemical binding
complexity
crystal structure
DNA
inhibition
mutation
reactivation
Article
binding affinity
crystal structure
DNA binding
ETS domain
gene activation
HEK293T cell line
human
human cell
immunoprecipitation
multiple cancer
promoter region
protein protein interaction
signal transduction
TERT gene
transactivation
binding site
chemistry
enzyme activation
Escherichia coli
genetics
HEK293 cell line
metabolism
protein multimerization
X ray crystallography
Binding Sites
Crystallography, X-Ray
Disulfides
DNA
Enzyme Activation
Escherichia coli
HEK293 Cells
Humans
NF-kappa B
NF-kappa B p52 Subunit
Promoter Regions, Genetic
Protein Binding
Protein Multimerization
Proto-Oncogene Protein c-ets-1
Signal Transduction
Telomerase
spellingShingle DNA fragment
immunoglobulin enhancer binding protein
protein p52
transcription factor Ets 1
disulfide
DNA
ETS1 protein, human
immunoglobulin enhancer binding protein
protein binding
telomerase
TERT protein, human
transcription factor Ets 1
cancer
chemical binding
complexity
crystal structure
DNA
inhibition
mutation
reactivation
Article
binding affinity
crystal structure
DNA binding
ETS domain
gene activation
HEK293T cell line
human
human cell
immunoprecipitation
multiple cancer
promoter region
protein protein interaction
signal transduction
TERT gene
transactivation
binding site
chemistry
enzyme activation
Escherichia coli
genetics
HEK293 cell line
metabolism
protein multimerization
X ray crystallography
Binding Sites
Crystallography, X-Ray
Disulfides
DNA
Enzyme Activation
Escherichia coli
HEK293 Cells
Humans
NF-kappa B
NF-kappa B p52 Subunit
Promoter Regions, Genetic
Protein Binding
Protein Multimerization
Proto-Oncogene Protein c-ets-1
Signal Transduction
Telomerase
Xu, X
Li, Y
Bharath, S.R
Ozturk, M.B
Bowler, M.W
Loo, B.Z.L
Tergaonkar, V
Song, H
Structural basis for reactivating the mutant TERT promoter by cooperative binding of p52 and ETS1
description 10.1038/s41467-018-05644-0
author2 BIOCHEMISTRY
author_facet BIOCHEMISTRY
Xu, X
Li, Y
Bharath, S.R
Ozturk, M.B
Bowler, M.W
Loo, B.Z.L
Tergaonkar, V
Song, H
format Article
author Xu, X
Li, Y
Bharath, S.R
Ozturk, M.B
Bowler, M.W
Loo, B.Z.L
Tergaonkar, V
Song, H
author_sort Xu, X
title Structural basis for reactivating the mutant TERT promoter by cooperative binding of p52 and ETS1
title_short Structural basis for reactivating the mutant TERT promoter by cooperative binding of p52 and ETS1
title_full Structural basis for reactivating the mutant TERT promoter by cooperative binding of p52 and ETS1
title_fullStr Structural basis for reactivating the mutant TERT promoter by cooperative binding of p52 and ETS1
title_full_unstemmed Structural basis for reactivating the mutant TERT promoter by cooperative binding of p52 and ETS1
title_sort structural basis for reactivating the mutant tert promoter by cooperative binding of p52 and ets1
publisher Nature Publishing Group
publishDate 2020
url https://scholarbank.nus.edu.sg/handle/10635/174210
_version_ 1800914223407038464