Xeroderma pigmentosum group C sensor: unprecedented recognition strategy and tight spatiotemporal regulation - Wikidata - awgldk - TriplyDB

Xeroderma pigmentosum group C sensor: unprecedented recognition strategy and tight spatiotemporal regulation

Xeroderma pigmentosum group C sensor: unprecedented recognition strategy and tight spatiotemporal regulation

http://www.wikidata.org/entity/Q26777633

about

Global-genome Nucleotide Excision Repair Controlled by Ubiquitin/Sumo Modifiers Transcriptional and Posttranslational Regulation of Nucleotide Excision Repair: The Guardian of the Genome against Ultraviolet Radiation Nucleotide Excision Repair Lesion-Recognition Protein Rad4 Captures a Pre-Flipped Partner Base in a Benzo[a]pyrene-Derived DNA Lesion: How Structure Impacts the Binding Pathway The Nucleotide Excision Repair Pathway Limits L1 Retrotransposition Deficient Nucleotide Excision Repair in Squamous Cell Carcinoma Cells.A unique chromosomal in-frame deletion identified among seven XP-C patients.Poly(ADP-ribose) polymerase 1 escorts XPC to UV-induced DNA lesions during nucleotide excision repair.Enhanced spontaneous DNA twisting/bending fluctuations unveiled by fluorescence lifetime distributions promote mismatch recognition by the Rad4 nucleotide excision repair complex.

P2860

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P2860

Xeroderma pigmentosum group C sensor: unprecedented recognition strategy and tight spatiotemporal regulation

http://www.wikidata.org/entity/Q26777633

description

2016 nî lūn-bûn

@nan

2016 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2016 թվականի փետրվարին հրատարակված գիտական հոդված

@hy

2016年の論文

@ja

2016年論文

@yue

2016年論文

@zh-hant

2016年論文

@zh-hk

2016年論文

@zh-mo

2016年論文

@zh-tw

2016年论文

@wuu

name

Xeroderma pigmentosum group C ...... ight spatiotemporal regulation

@ast

Xeroderma pigmentosum group C ...... ight spatiotemporal regulation

@en

Xeroderma pigmentosum group C ...... ight spatiotemporal regulation

@nl

type

label

Xeroderma pigmentosum group C ...... ight spatiotemporal regulation

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Xeroderma pigmentosum group C ...... ight spatiotemporal regulation

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Xeroderma pigmentosum group C ...... ight spatiotemporal regulation

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prefLabel

Xeroderma pigmentosum group C ...... ight spatiotemporal regulation

@ast

Xeroderma pigmentosum group C ...... ight spatiotemporal regulation

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Xeroderma pigmentosum group C ...... ight spatiotemporal regulation

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S00018-015-2075-Z

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Cellular and Molecular Life Sciences

P1476

Xeroderma pigmentosum group C ...... ight spatiotemporal regulation

@en

P2093

Hanspeter Naegeli

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

Jun-Hyun Min

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

Marjo-Riitta Puumalainen

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P275

Creative Commons Attribution 4.0 International

P2860

The xeroderma pigmentosum group C protein complex XPC-HR23B plays an important role in the recruitment of transcription factor IIH to damaged DNA

3-Methyladenine-DNA glycosylase (MPG protein) interacts with human RAD23 proteins

Stable binding of human XPC complex to irradiated DNA confers strong discrimination for damaged sites

Centrosome protein centrin 2/caltractin 1 is part of the xeroderma pigmentosum group C complex that initiates global genome nucleotide excision repair

Human STAGA complex is a chromatin-acetylating transcription coactivator that interacts with pre-mRNA splicing and DNA damage-binding factors in vivo

The ubiquitin ligase activity in the DDB2 and CSA complexes is differentially regulated by the COP9 signalosome in response to DNA damage

Three DNA polymerases, recruited by different mechanisms, carry out NER repair synthesis in human cells

Centrin 2 stimulates nucleotide excision repair by interacting with xeroderma pigmentosum group C protein.

Function of the p97-Ufd1-Npl4 complex in retrotranslocation from the ER to the cytosol: dual recognition of nonubiquitinated polypeptide segments and polyubiquitin chains

The cullin 4B-based UV-damaged DNA-binding protein ligase binds to UV-damaged chromatin and ubiquitinates histone H2A

P2888

s00018-015-2075-z

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547-566

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scholarly article

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2005690

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10.1007/S00018-015-2075-Z

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P433

3

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73

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Peter Rüthemann

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2016-02-01T00:00:00Z

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283447246

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1045875199

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26521083

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DNA-binding protein

biomedical investigative technique

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4713717

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