HHR23B, a human Rad23 homolog, stimulates XPC protein in nucleotide excision repair in vitro. - Wikidata - wikimedia - TriplyDB

HHR23B, a human Rad23 homolog, stimulates XPC protein in nucleotide excision repair in vitro.

HHR23B, a human Rad23 homolog, stimulates XPC protein in nucleotide excision repair in vitro.

http://www.wikidata.org/entity/Q40019757

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Interaction of hHR23 with S5a. The ubiquitin-like domain of hHR23 mediates interaction with S5a subunit of 26 S proteasome 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 Centrosome protein centrin 2/caltractin 1 is part of the xeroderma pigmentosum group C complex that initiates global genome nucleotide excision repair A complex between peptide:N-glycanase and two proteasome-linked proteins suggests a mechanism for the degradation of misfolded glycoproteins Centrin 2 stimulates nucleotide excision repair by interacting with xeroderma pigmentosum group C protein.Two human homologs of Rad23 are functionally interchangeable in complex formation and stimulation of XPC repair activity A DNA repair complex functions as an Oct4/Sox2 coactivator in embryonic stem cells Ubiquitin-associated (UBA) domains in Rad23 bind ubiquitin and promote inhibition of multi-ubiquitin chain assembly.Xeroderma pigmentosum group C protein interacts physically and functionally with thymine DNA glycosylase Human immunodeficiency virus type 1 Vpr interacts with HHR23A, a cellular protein implicated in nucleotide excision DNA repair A novel regulation mechanism of DNA repair by damage-induced and RAD23-dependent stabilization of xeroderma pigmentosum group C protein The comings and goings of nucleotide excision repair factors on damaged DNA Global-genome Nucleotide Excision Repair Controlled by Ubiquitin/Sumo Modifiers Xeroderma pigmentosum group C sensor: unprecedented recognition strategy and tight spatiotemporal regulation Nucleotide excision repair in eukaryotes Involvement of global genome repair, transcription coupled repair, and chromatin remodeling in UV DNA damage response changes during development Binding surface mapping of intra- and interdomain interactions among hHR23B, ubiquitin, and polyubiquitin binding site 2 of S5a A multistep damage recognition mechanism for global genomic nucleotide excision repair Developmental defects and male sterility in mice lacking the ubiquitin-like DNA repair gene mHR23B Regulation of the NEDD8 conjugation system by a splicing variant, NUB1L.Critical DNA damage recognition functions of XPC-hHR23B and XPA-RPA in nucleotide excision repair.Ordered conformational changes in damaged DNA induced by nucleotide excision repair factors.Biochemical and structural domain analysis of xeroderma pigmentosum complementation group C protein.An aromatic sensor with aversion to damaged strands confers versatility to DNA repair In vivo destabilization and functional defects of the xeroderma pigmentosum C protein caused by a pathogenic missense mutation Rad23 stabilizes Rad4 from degradation by the Ub/proteasome pathway The initiative role of XPC protein in cisplatin DNA damaging treatment-mediated cell cycle regulation.Identification of HHR23A as a substrate for E6-associated protein-mediated ubiquitination.A family of ubiquitin-like proteins binds the ATPase domain of Hsp70-like Stch.p53 and DNA damage-inducible expression of the xeroderma pigmentosum group C gene.Rad23 promotes the targeting of proteolytic substrates to the proteasome.NUB1-mediated targeting of the ubiquitin precursor UbC1 for its C-terminal hydrolysis.Structure of the mouse peptide N-glycanase-HR23 complex suggests co-evolution of the endoplasmic reticulum-associated degradation and DNA repair pathways.A novel UV-damaged DNA binding protein emerges during the chromatin-eliminating cleavage period in Ascaris suum.Structure-function analysis of the EF-hand protein centrin-2 for its intracellular localization and nucleotide excision repair New functions of XPC in the protection of human skin cells from oxidative damage Functional regulation of the DNA damage-recognition factor DDB2 by ubiquitination and interaction with xeroderma pigmentosum group C protein.Orchestral maneuvers at the damaged sites in nucleotide excision repair.Recognition of DNA damage by XPC coincides with disruption of the XPC-RAD23 complex

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P2860

HHR23B, a human Rad23 homolog, stimulates XPC protein in nucleotide excision repair in vitro.

http://www.wikidata.org/entity/Q40019757

description

1996 nî lūn-bûn

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1996年の論文

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1996年論文

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1996年論文

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1996年論文

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1996年论文

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1996年论文

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HHR23B, a human Rad23 homolog, ...... tide excision repair in vitro.

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HHR23B, a human Rad23 homolog, ...... tide excision repair in vitro.

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HHR23B, a human Rad23 homolog, ...... tide excision repair in vitro.

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HHR23B, a human Rad23 homolog, ...... tide excision repair in vitro.

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Bootsma D

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Hanaoka F

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Hoeijmakers JH

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Maekawa T

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Masutani C

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Sugasawa K

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Uchida A

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van der Spek PJ

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P2860

The role of human single-stranded DNA binding protein and its individual subunits in simian virus 40 DNA replication

A presumed DNA helicase encoded by ERCC-3 is involved in the human repair disorders xeroderma pigmentosum and Cockayne's syndrome

Purification and cloning of a nucleotide excision repair complex involving the xeroderma pigmentosum group C protein and a human homologue of yeast RAD23

XPG endonuclease makes the 3' incision in human DNA nucleotide excision repair

The ERCC2/DNA repair protein is associated with the class II BTF2/TFIIH transcription factor

Cleavage of structural proteins during the assembly of the head of bacteriophage T4

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

Rapid and efficient site-specific mutagenesis without phenotypic selection

Reconstitution of yeast nucleotide excision repair with purified Rad proteins, replication protein A, and transcription factor TFIIH.

Proliferating cell nuclear antigen is required for DNA excision repair

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