Strand- and site-specific DNA lesion demarcation by the xeroderma pigmentosum group D helicase.
about
Global-genome Nucleotide Excision Repair Controlled by Ubiquitin/Sumo ModifiersXeroderma pigmentosum group C sensor: unprecedented recognition strategy and tight spatiotemporal regulationClose encounters for the first time: Helicase interactions with DNA damageNucleotide excision repair in eukaryotesFunctional and structural studies of the nucleotide excision repair helicase XPD suggest a polarity for DNA translocationStructural Basis for Bulky-Adduct DNA-Lesion Recognition by the Nucleotide Excision Repair Protein Rad14Single-molecule analysis reveals human UV-damaged DNA-binding protein (UV-DDB) dimerizes on DNA via multiple kinetic intermediates.Lack of association between the XPD Lys751Gln polymorphism and colorectal cancer risk: a meta-analysis.Slowly progressing nucleotide excision repair in trichothiodystrophy group A patient fibroblasts.XPB and XPD helicases in TFIIH orchestrate DNA duplex opening and damage verification to coordinate repair with transcription and cell cycle via CAK kinase.Impact of age-associated cyclopurine lesions on DNA repair helicases.DNA repair mechanisms in dividing and non-dividing cells.Structure-function analysis of the EF-hand protein centrin-2 for its intracellular localization and nucleotide excision repairFunctional regulation of the DNA damage-recognition factor DDB2 by ubiquitination and interaction with xeroderma pigmentosum group C protein.Structural insights into the recognition of cisplatin and AAF-dG lesion by Rad14 (XPA)Tripartite DNA Lesion Recognition and Verification by XPC, TFIIH, and XPA in Nucleotide Excision Repair.DNA helicase and helicase-nuclease enzymes with a conserved iron-sulfur cluster.Molecular mechanisms of xeroderma pigmentosum (XP) proteins.The efficiencies of damage recognition and excision correlate with duplex destabilization induced by acetylaminofluorene adducts in human nucleotide excision repair.Sequence-dependent base pair stepping dynamics in XPD helicase unwinding.G-quadruplex recognition and remodeling by the FANCJ helicaseTrypanosoma brucei harbours a divergent XPB helicase paralogue that is specialized in nucleotide excision repair and conserved among kinetoplastid organisms.Strand-specific recognition of DNA damages by XPD provides insights into nucleotide excision repair substrate versatility.Archaeal genome guardians give insights into eukaryotic DNA replication and damage response proteins.Regulation of endonuclease activity in human nucleotide excision repair.Xeroderma pigmentosum group C protein interacts with histones: regulation by acetylated states of histone H3.PostExcision Events in Human Nucleotide Excision Repair.Molecular mechanism of global genome nucleotide excision repair.Mechanistic and biological considerations of oxidatively damaged DNA for helicase-dependent pathways of nucleic acid metabolism.A unique chromosomal in-frame deletion identified among seven XP-C patients.Regulation of translocation polarity by helicase domain 1 in SF2B helicases.Conservation and Divergence in Nucleotide Excision Repair Lesion Recognition.Repair-Resistant DNA Lesions.Direct correlation of DNA binding and single protein domain motion via dual illumination fluorescence microscopy.Common TFIIH recruitment mechanism in global genome and transcription-coupled repair subpathways.ERCC2 and ERCC3 DNA helicases form an open bubble structure in damaged DNAGenetic instability associated with loop or stem-loop structures within transcription units can be independent of nucleotide excision repair.
P2860
Q26747331-20BA5267-74BE-4B24-AF6F-0ED1A2FA1D22Q26777633-659E07EE-EAA7-4650-BB73-CBA0BF67F673Q26828639-E03D8999-7409-486A-ACDD-5159C379D3C3Q26850656-E2DF5B80-53BF-4AD8-9ABE-D5130917F861Q27675554-E2782352-8632-45E1-89C7-71F95EBA1131Q27705197-CB0245F0-9844-4F0B-B70F-43A84A7BF984Q30577983-7985A4EE-80D1-4755-AE21-7990D75883EDQ33921771-D2F56C8B-3295-4568-9025-B15FE327DC7FQ33951430-A0613D4B-8209-4E14-B458-8E00A5B9B5BBQ34184951-26D5C84D-907B-4D43-95B9-2EF0E42F20E0Q34542484-F0EE0E19-FC49-4B30-8251-5C32037AEDE2Q34727858-88D7DD40-7AB1-4EAE-804C-55E761E9ABCCQ34743642-EC5EE726-43A7-4D31-ABA8-99930A79D0C0Q35089083-7EA18EFE-DE69-4135-9B2C-17C20657697EQ35671448-87A89EF3-B19D-4806-A87B-EDCE8A5E32A2Q35780735-DD0BEFFA-88AA-443D-90CD-1246BFCDD469Q36044809-16C2BACD-A51D-4EE7-9971-457656F319BCQ36142135-B8B52A86-0929-4E6D-90B1-7614D12857E5Q36413249-D1B43E86-FBB6-4C32-ABD0-FC3266EF008CQ36889452-04A7E638-0C74-4B02-B446-C12CE362773AQ37336936-D832457C-CFE4-40E3-AD27-E8FC69D048CEQ37395890-A6278D12-AAC5-4DEC-8C2A-71E46EB45EEAQ37563531-E0C99D80-089D-4934-ADBA-662B402317CBQ37631446-6688D0BD-B83F-4488-B861-B4D9CF5F2DA8Q37877050-0F83FED3-CCFB-4EFA-8025-8B55C9218372Q38715086-7F1EAEBF-247B-48F6-8761-CBD83FF8DF7EQ38958950-F23F899D-AEB8-4831-927B-E92E7AA8BDE9Q38962638-1CE10D02-5C2A-4FB4-9A8C-BC703D906AC5Q39019092-84CC036E-889B-4A59-8891-0D64759EBA67Q39624671-1B2DBC9B-8A49-4A38-BA30-A7014E069E6CQ40514758-25832DB6-DD3E-45C0-8E5B-5C8C2760A168Q41002702-D734B14D-6A1A-476F-8392-06201DD0EC43Q41508281-28563783-7833-4F27-A98C-F69E220A4428Q42935113-46CCA40A-02E9-4C0B-94F3-7638C5F8C5C4Q47122825-8D13403E-6A1F-495E-809F-42C4027666E5Q50287420-2CEC58A2-C5B5-49BB-BB77-F9504D5D4465Q52688242-50F1E1D0-BFAF-4374-A39B-F7E32D40EAB7
P2860
Strand- and site-specific DNA lesion demarcation by the xeroderma pigmentosum group D helicase.
description
2010 nî lūn-bûn
@nan
2010 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Strand- and site-specific DNA ...... pigmentosum group D helicase.
@ast
Strand- and site-specific DNA ...... pigmentosum group D helicase.
@en
Strand- and site-specific DNA ...... pigmentosum group D helicase.
@nl
type
label
Strand- and site-specific DNA ...... pigmentosum group D helicase.
@ast
Strand- and site-specific DNA ...... pigmentosum group D helicase.
@en
Strand- and site-specific DNA ...... pigmentosum group D helicase.
@nl
prefLabel
Strand- and site-specific DNA ...... pigmentosum group D helicase.
@ast
Strand- and site-specific DNA ...... pigmentosum group D helicase.
@en
Strand- and site-specific DNA ...... pigmentosum group D helicase.
@nl
P2093
P2860
P356
P1476
Strand- and site-specific DNA ...... pigmentosum group D helicase.
@en
P2093
Hanspeter Naegeli
Nadine Mathieu
Nina Kaczmarek
P2860
P304
17545-17550
P356
10.1073/PNAS.1004339107
P407
P577
2010-09-27T00:00:00Z