Identification and characterization of XPC-binding domain of hHR23B. - Wikidata - wikimedia - TriplyDB

Identification and characterization of XPC-binding domain of hHR23B.

Identification and characterization of XPC-binding domain of hHR23B.

http://www.wikidata.org/entity/Q38341326

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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 Two human homologs of Rad23 are functionally interchangeable in complex formation and stimulation of XPC repair activity Role of the UBL-UBA protein KPC2 in degradation of p27 at G1 phase of the cell cycle.Xeroderma pigmentosum group C protein interacts physically and functionally with thymine DNA glycosylase Involvement of rhp23, a Schizosaccharomyces pombe homolog of the human HHR23A and Saccharomyces cerevisiae RAD23 nucleotide excision repair genes, in cell cycle control and protein ubiquitination Nucleotide excision repair of DNA with recombinant human proteins: definition of the minimal set of factors, active forms of TFIIH, and modulation by CAK A novel regulation mechanism of DNA repair by damage-induced and RAD23-dependent stabilization of xeroderma pigmentosum group C protein Structural determinants for the binding of ubiquitin-like domains to the proteasome 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 The 19S complex of the proteasome regulates nucleotide excision repair in yeast.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 Order of assembly of human DNA repair excision nuclease.Assembly, subunit composition, and footprint of human DNA repair excision nuclease.The involvement of ataxia-telangiectasia mutated protein activation in nucleotide excision repair-facilitated cell survival with cisplatin treatment.Biochemical and structural domain analysis of xeroderma pigmentosum complementation group C protein.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 Identification of HHR23A as a substrate for E6-associated protein-mediated ubiquitination.Ubiquitin-specific protease 7 regulates nucleotide excision repair through deubiquitinating XPC protein and preventing XPC protein from undergoing ultraviolet light-induced and VCP/p97 protein-regulated proteolysis.Rad23 promotes the targeting of proteolytic substrates to the proteasome.Solution structure and backbone dynamics of the XPC-binding domain of the human DNA repair protein hHR23B.Structure of a human DNA repair protein UBA domain that interacts with HIV-1 Vpr.Structure of the mouse peptide N-glycanase-HR23 complex suggests co-evolution of the endoplasmic reticulum-associated degradation and DNA repair pathways.A meta-analysis of DNA repair gene XPC polymorphisms and cancer risk.Lack of recognition by global-genome nucleotide excision repair accounts for the high mutagenicity and persistence of aristolactam-DNA adducts.The Png1-Rad23 complex regulates glycoprotein turnover.Dissection of the molecular defects caused by pathogenic mutations in the DNA repair factor XPC.Structural studies of the yeast DNA damage-inducible protein Ddi1 reveal domain architecture of this eukaryotic protein family.Xeroderma pigmentosum complementation group C protein (XPC) serves as a general sensor of damaged DNA.A human XPC protein interactome--a resource Binding of HIV-1 Vpr protein to the human homolog of the yeast DNA repair protein RAD23 (hHR23A) requires its xeroderma pigmentosum complementation group C binding (XPCB) domain as well as the ubiquitin-associated 2 (UBA2) domain.Molecular mechanisms of ultraviolet radiation-induced DNA damage and repair.Expression of a novel RAD23B mRNA splice variant in the human testis.Dosage suppressors of pds1 implicate ubiquitin-associated domains in checkpoint control Differential interaction of the E3 ligase parkin with the proteasomal subunit S5a and the endocytic protein Eps15.

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Identification and characterization of XPC-binding domain of hHR23B.

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1997 nî lūn-bûn

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1997年学术文章

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1997年学术文章

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1997年學術文章

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1997年學術文章

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1997年學術文章

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name

Identification and characterization of XPC-binding domain of hHR23B.

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type

label

Identification and characterization of XPC-binding domain of hHR23B.

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prefLabel

Identification and characterization of XPC-binding domain of hHR23B.

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Molecular and Cellular Biology

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Identification and characterization of XPC-binding domain of hHR23B.

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Araki M

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Bootsma D

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Hanaoka F

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Maekawa T

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Masutani C

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P2860

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

Two human homologs of Rad23 are functionally interchangeable in complex formation and stimulation of XPC repair activity

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

DNA repair defect in xeroderma pigmentosum group C and complementing factor from HeLa cells

XPC and human homologs of RAD23: intracellular localization and relationship to other nucleotide excision repair complexes

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

Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa

Assessing the requirements for nucleotide excision repair proteins of Saccharomyces cerevisiae in an in vitro system.

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