In situ analysis of repair processes for oxidative DNA damage in mammalian cells. - Wikidata - wikimedia - TriplyDB

In situ analysis of repair processes for oxidative DNA damage in mammalian cells.

In situ analysis of repair processes for oxidative DNA damage in mammalian cells.

http://www.wikidata.org/entity/Q31111805

about

XRCC1 polymorphisms and breast cancer risk from the New York Site of the Breast Cancer Family Registry: A family-based case-control study HMGB1 is a cofactor in mammalian base excision repair APLF (C2orf13) is a novel human protein involved in the cellular response to chromosomal DNA strand breaks A novel human AP endonuclease with conserved zinc-finger-like motifs involved in DNA strand break responses Human DNA polymerase iota protects cells against oxidative stress Translocation of XRCC1 and DNA ligase IIIalpha from centrosomes to chromosomes in response to DNA damage in mitotic human cells Partial complementation of a DNA ligase I deficiency by DNA ligase III and its impact on cell survival and telomere stability in mammalian cells Coordination of steps in single-nucleotide base excision repair mediated by apurinic/apyrimidinic endonuclease 1 and DNA polymerase beta A polycomb group protein, PHF1, is involved in the response to DNA double-strand breaks in human cell Early steps in the DNA base excision/single-strand interruption repair pathway in mammalian cells Regulation of poly(ADP-ribose) polymerase 1 activity by the phosphorylation state of the nuclear NAD biosynthetic enzyme NMN adenylyl transferase 1 Human base excision repair enzymes apurinic/apyrimidinic endonuclease1 (APE1), DNA polymerase beta and poly(ADP-ribose) polymerase 1: interplay between strand-displacement DNA synthesis and proofreading exonuclease activity XRCC1 is required for DNA single-strand break repair in human cells.Microirradiation techniques in radiobiological research Femtosecond near-infrared laser microirradiation reveals a crucial role for PARP signaling on factor assemblies at DNA damage sites.Real-time imaging of DNA damage in yeast cells using ultra-short near-infrared pulsed laser irradiation Discovery and Structure–Activity Relationship of Novel 2,3-Dihydrobenzofuran-7-carboxamide and 2,3-Dihydrobenzofuran-3(2 H )-one-7-carboxamide Derivatives as Poly(ADP-ribose)polymerase-1 Inhibitors DNA damage during the G0/G1 phase triggers RNA-templated, Cockayne syndrome B-dependent homologous recombination Bisphenol a promotes cell survival following oxidative DNA damage in mouse fibroblasts Riboflavin activated by ultraviolet A1 irradiation induces oxidative DNA damage-mediated mutations inhibited by vitamin C Comparative analysis of different laser systems to study cellular responses to DNA damage in mammalian cells Two-stage dynamic DNA quality check by xeroderma pigmentosum group C protein.Recruitment of DNA repair synthesis machinery to sites of DNA damage/repair in living human cells.X-ray repair cross-complementing group 1 (XRCC1) genetic polymorphisms and risk of childhood acute lymphoblastic leukemia: a meta-analysis.Differential recruitment of DNA Ligase I and III to DNA repair sites.Replication-dependent and -independent responses of RAD18 to DNA damage in human cells.Autophosphorylation of DNA-PKCS regulates its dynamics at DNA double-strand breaks.XRCC1 and PCNA are loading platforms with distinct kinetic properties and different capacities to respond to multiple DNA lesions.Feedback-regulated poly(ADP-ribosyl)ation by PARP-1 is required for rapid response to DNA damage in living cells Rapid recruitment of BRCA1 to DNA double-strand breaks is dependent on its association with Ku80 Repair of laser-localized DNA interstrand cross-links in G1 phase mammalian cells Functional capacity of XRCC1 protein variants identified in DNA repair-deficient Chinese hamster ovary cell lines and the human population A novel and simple micro-irradiation technique for creating localized DNA double-strand breaks.WRN is recruited to damaged telomeres via its RQC domain and tankyrase1-mediated poly-ADP-ribosylation of TRF1.DNA polymerase β uses its lyase domain in a processive search for DNA damage.Tankyrase1-mediated poly(ADP-ribosyl)ation of TRF1 maintains cell survival after telomeric DNA damage.HMGB1: roles in base excision repair and related function.DNA interstrand crosslink repair in mammalian cells: step by step.The DNA repair complex Ku70/86 modulates Apaf1 expression upon DNA damage Creating localized DNA double-strand breaks with microirradiation.

P2860

Q23920041-9CB831E6-8BD7-4556-8A46-79C9F623CD63 Q24292806-61C28AC3-918F-4A80-BD3A-B2BBE8AA9118 Q24299831-FA36C213-F0F8-4026-BC24-3F299EA0F17D Q24301368-7916A0E1-0BDF-47ED-A8B2-E46F4B32211F Q24323561-42E27DF9-1E94-4CA9-BF22-0074EFCDA36C Q24557436-7E4E5428-B3D3-4B55-B810-EF268EF06725 Q24619372-B6F2D7D5-E3E4-451F-B507-F693598A91FE Q24647277-89589CC9-6A0A-4681-9EE0-0EA47072D0A2 Q24649958-7957CA3D-489B-4B3F-939C-B3DE075E2076 Q24650179-682E489D-4F18-4608-B169-A381EA46657B Q24681295-B203CD70-173D-4240-BF8D-3CEDCE0B4B79 Q24793931-7CA90750-9FF1-4C2D-9CBF-21CD24CD33B1 Q24796404-CEDAC292-CB05-4B65-A249-9F1E87DE4038 Q26786419-273BCBAC-BAC4-4F1F-AD75-B1E2536B60FD Q27324256-3A7A2419-73EB-497D-ACE6-BF9AC38C16A4 Q27324389-C0793DC2-840F-4DD8-822E-5FEF7DE210BE Q27684311-5A675AE4-0289-4475-8FD4-C148BD7D52D7 Q28263882-296079E6-B3AF-41C2-BC9E-3755D33957AE Q28543514-836BE5BA-4EC1-48BF-9828-CCD1E5432D9D Q30479266-60B12666-86BF-4F35-BD95-BAD7866E2EDD Q30487741-E2BA5AE9-3C60-4A3D-B77B-313270B044F1 Q30489886-461441F0-A847-499A-8491-320016167015 Q30831106-CD082825-9FBB-4CC5-9DA1-B3E1953E6F4A Q31057165-E2F5463A-6238-4BC0-B699-B902F5F11500 Q33251083-6260414E-8D1B-4016-BCC3-705E73F41B27 Q33257837-B29243B5-5004-4C59-A386-BA263171F112 Q33282240-9D472A88-E2EA-4A14-BCC6-399EA613BA51 Q33299607-41031B62-3120-4FF0-B679-4EC3B68004A1 Q33304975-A1E05F37-8158-4543-A55A-B7DA8D62157B Q33378036-56C075F6-49AB-434F-842B-C336C04D420F Q33493863-2F7EC358-2C56-48F2-8582-AAE320CBE755 Q33552989-C11DE323-86CD-4AB8-BD23-4B0D5DDFF825 Q33553010-935F0EA2-7F9D-4B5E-BCE6-95EB0EBD2171 Q33580323-1E32C336-FBF7-40A1-848C-E728397245BA Q33580434-925FC2B9-296A-4207-A76A-A0E51EDF745B Q33580476-1832500B-D9A9-4162-AC6D-AD512F2F61B1 Q33638180-1A7ADECC-01F7-4203-BBCB-BDE4A887BA7F Q33669915-61A2B581-38AC-46DC-8009-4A8B85AFAC40 Q33725241-6DEC8BB9-D572-4998-88B4-DB094265E793 Q33811685-C2CAC2A8-9D78-47AF-B447-11F801B7C8FB

P2860

In situ analysis of repair processes for oxidative DNA damage in mammalian cells.

http://www.wikidata.org/entity/Q31111805

description

2004 nî lūn-bûn

@nan

2004 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2004 թվականի սեպտեմբերին հրատարակված գիտական հոդված

@hy

2004年の論文

@ja

2004年論文

@yue

2004年論文

@zh-hant

2004年論文

@zh-hk

2004年論文

@zh-mo

2004年論文

@zh-tw

2004年论文

@wuu

name

In situ analysis of repair processes for oxidative DNA damage in mammalian cells.

@ast

In situ analysis of repair processes for oxidative DNA damage in mammalian cells.

@en

type

label

In situ analysis of repair processes for oxidative DNA damage in mammalian cells.

@ast

In situ analysis of repair processes for oxidative DNA damage in mammalian cells.

@en

prefLabel

In situ analysis of repair processes for oxidative DNA damage in mammalian cells.

@ast

In situ analysis of repair processes for oxidative DNA damage in mammalian cells.

@en

P1433

Q31111805-CB57C7E7-6CFD-4FAB-A3C9-2659E63198CF

P1476

Q31111805-1BE30CC4-E7DD-4157-AF23-80986FD5B6E7

P2093

Q31111805-1F45FB0C-D2BF-4458-8C74-A6CCB494B158

Q31111805-4F9BA621-15A8-432D-B624-A911C8EABC73

Q31111805-8B0F6528-FDE7-4E20-AD8C-704E90DE9EEE

Q31111805-A8AC65A2-A33C-450D-8001-AACBF77E81B7

Q31111805-ABC62C6F-19BE-48F1-8FA1-074DA0AFCF5A

Q31111805-E6E431EC-266A-45FC-B147-EDA6ED8660B3

Q31111805-F2E5BB7B-516B-44A6-826F-B70BCFFB0CD6

P2860

Q31111805-0B470FE4-8C26-4D79-B4B1-0E8894ACF471

Q31111805-0BA107E7-3283-47A5-9BB2-6161154346AA

Q31111805-135CBF86-A628-411B-9E3B-43C1A41D455F

Q31111805-17DB8D8D-A90F-4869-9F01-F21AD0194910

Q31111805-1BC231A7-B9DE-4EAF-BB30-3C46C105E94A

Q31111805-2CC0421E-9CE1-44F3-90D6-8BC7AC9E081F

Q31111805-2D5A4996-5831-4287-A84B-53450A52D910

Q31111805-31E60CC0-46D3-4182-9455-804478351D28

Q31111805-3485253C-C73E-4BA8-9611-A7697FE39408

Q31111805-38D29D28-76A3-4841-B543-40F22A39DF4A

P304

Q31111805-4122179D-5BB3-4E04-B50A-89F303FC2C4A

P31

Q31111805-E0BBD21A-7454-4212-981A-CFE011A02047

P356

Q31111805-88B36FBB-237A-4938-9990-831D57BC0956

P407

Q31111805-FC2F3CC8-C29D-4F26-8525-6937AC123A92

P433

Q31111805-465311B2-4F51-400A-89E1-5BC241B2DCFE

P478

Q31111805-34325C4C-9BD4-43AD-B5B6-EEFDC6ECF44A

P50

Q31111805-9B991B47-2792-4CA3-8B84-193B859C2675

P577

Q31111805-0461D403-08AB-4BBB-8AEE-67A59B1B3F13

P5875

Q31111805-E03FF148-70B3-4852-ACEC-3E21B8AF839F

P698

Q31111805-D3C1459C-5B3C-4292-872A-23AA48B2EDF4

P921

Q31111805-F85E2ADF-2190-4859-8540-A1B623C0780C

P932

Q31111805-90A506E3-B683-4D44-93D5-87F4F0D917C9

P356

PNAS.0406048101

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

In situ analysis of repair processes for oxidative DNA damage in mammalian cells

@en

P2093

Akira Yasui

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

Li Lan

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

Masashi Takao

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

Mitsuko Masutani

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

Satoshi Nakajima

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

Satoshi Okano

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

Yoshitsugu Oohata

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

P2860

Functional and physical interactions between ERCC1 and MSH2 complexes for resistance to cis-diamminedichloroplatinum(II) in mammalian cells

Nucleosome assembly by a complex of CAF-1 and acetylated histones H3/H4

Domain specific interaction in the XRCC1-DNA polymerase beta complex

A CAF-1-PCNA-mediated chromatin assembly pathway triggered by sensing DNA damage

XRCC1 co-localizes and physically interacts with PCNA

Quantitative determination of expression of the prostate cancer protein alpha-methylacyl-CoA racemase using automated quantitative analysis (AQUA): a novel paradigm for automated and continuous biomarker measurements

Role of XRCC1 in the coordination and stimulation of oxidative DNA damage repair initiated by the DNA glycosylase hOGG1

Identification and characterization of a novel human DNA glycosylase for repair of cytosine-derived lesions

Poly(ADP-ribose) polymerase-2 (PARP-2) is required for efficient base excision DNA repair in association with PARP-1 and XRCC1

A back-up glycosylase in Nth1 knock-out mice is a functional Nei (endonuclease VIII) homologue

P304

13738-13743

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

P31

scholarly article

P356

10.1073/PNAS.0406048101

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

P407

P433

38

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

P478

101

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

P50

Samuel H. Wilson

P577

2004-09-13T00:00:00Z

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

P5875

8349896

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

P698

15365186

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

P921

P932

518826

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