Xrcc3 is required for assembly of Rad51 complexes in vivo. - Wikidata - awgldk - TriplyDB

Xrcc3 is required for assembly of Rad51 complexes in vivo.

Xrcc3 is required for assembly of Rad51 complexes in vivo.

http://www.wikidata.org/entity/Q41016235

about

The RAD51 family member, RAD51L3, is a DNA-stimulated ATPase that forms a complex with XRCC2 Identification and purification of two distinct complexes containing the five RAD51 paralogs Homologous pairing and ring and filament structure formation activities of the human Xrcc2*Rad51D complex Interplay between human DNA repair proteins at a unique double-strand break in vivo Ring-shaped Rad51 paralog protein complexes bind Holliday junctions and replication forks as visualized by electron microscopy Functional interaction between the Bloom's syndrome helicase and the RAD51 paralog, RAD51L3 (RAD51D)PARP1-dependent recruitment of KDM4D histone demethylase to DNA damage sites promotes double-strand break repair The Arabidopsis homologue of Xrcc3 plays an essential role in meiosis Haploinsufficiency of the Mus81-Eme1 endonuclease activates the intra-S-phase and G2/M checkpoints and promotes rereplication in human cells The Rad51 paralog Rad51B promotes homologous recombinational repair Disruption of mouse SNM1 causes increased sensitivity to the DNA interstrand cross-linking agent mitomycin C The BRCA2-interacting protein BCCIP functions in RAD51 and BRCA2 focus formation and homologous recombinational repair XRCC3 promotes homology-directed repair of DNA damage in mammalian cells Homologous-pairing activity of the human DNA-repair proteins Xrcc3.Rad51C Complex formation by the human RAD51C and XRCC3 recombination repair proteins XRCC2 is Required for the Formation of Rad51 Foci Induced by Ionizing Radiation and DNA Cross-Linking Agent Mitomycin C Distinct roles for two RAD51-related genes in Trypanosoma brucei antigenic variation.Functional characterization of polymorphisms in DNA repair genes using cytogenetic challenge assays Double-strand break repair-adox: Restoration of suppressed double-strand break repair during mitosis induces genomic instability Repair of strand breaks by homologous recombination Sapacitabine for cancer Rad52 associates with RPA and functions with rad55 and rad57 to assemble meiotic recombination complexes Interactions between Mcm10p and other replication factors are required for proper initiation and elongation of chromosomal DNA replication in Saccharomyces cerevisiae.Saccharomyces cerevisiae Dmc1 protein promotes renaturation of single-strand DNA (ssDNA) and assimilation of ssDNA into homologous super-coiled duplex DNA.Assembly of RecA-like recombinases: distinct roles for mediator proteins in mitosis and meiosis Homologous recombination and human health: the roles of BRCA1, BRCA2, and associated proteins RAD51C interacts with RAD51B and is central to a larger protein complex in vivo exclusive of RAD51 XRCC2 is a nuclear RAD51-like protein required for damage-dependent RAD51 focus formation without the need for ATP binding Impaired DNA damage-induced nuclear Rad51 foci formation uniquely characterizes Fanconi anemia group D1 The Polycomb group protein EZH2 impairs DNA repair in breast epithelial cells Chromosome instability and defective recombinational repair in knockout mutants of the five Rad51 paralogs Rad52 partially substitutes for the Rad51 paralog XRCC3 in maintaining chromosomal integrity in vertebrate cells.XRCC3 deficiency results in a defect in recombination and increased endoreduplication in human cells The interplay of RecA-related proteins and the MND1-HOP2 complex during meiosis in Arabidopsis thaliana.Phase II studies of gemcitabine and cisplatin in heavily and minimally pretreated metastatic breast cancer.Gemcitabine and cisplatin combination regimen in patients with anthracycline- and taxane-pretreated metastatic breast cancer.The homologous recombination protein RAD51D protects the genome from large deletions Arabidopsis RAD51, RAD51C and XRCC3 proteins form a complex and facilitate RAD51 localization on chromosomes for meiotic recombination.DNA repair polymorphisms modify bladder cancer risk: a multi-factor analytic strategy.The effect of a DNA repair gene on cellular invasiveness: XRCC3 over-expression in breast cancer cells

P2860

Q22254407-9D70E8C0-8B21-4FB9-B348-117AB81515D7 Q24292055-F6EDA5F4-24D2-4DB4-8A27-ACCE69876BF6 Q24292270-D32058AC-8F24-4B74-87B2-42ED9BAD84E6 Q24300377-9F84E948-1B0D-4982-8E40-C782C52374E8 Q24301827-A03030F1-9AD1-4967-9C13-4C7317BDC0A9 Q24323327-18E42DBF-9640-4249-A88F-960BB5E99A66 Q24337719-09AACD2F-2442-4C21-ABC0-E38178999627 Q24535915-5B5739F0-3F05-4198-9042-1B44D3BA91CA Q24537482-2B6A4A65-8403-4437-9889-FF66895901B4 Q24551864-2AE236B7-66B4-44F4-99E2-9B741A7ED7C7 Q24554173-2FAECA59-C276-498F-B5AE-24532E7003A0 Q24556631-5266BBB9-E3CA-43EE-B599-B9E8953C226A Q24597771-B921E4BC-92B3-4705-8152-7FCD75D37BB5 Q24598025-A8DC353B-3627-41BF-B7B1-CBE370E4BCD6 Q24630873-3F92A43E-AFD1-40B4-BED8-2ABBF008EFE3 Q24793741-008F4C66-C3A9-40C9-A4F3-BF1183A6BE64 Q24815002-9FFECCA6-912D-41F7-82C5-082BB10A33E1 Q24816878-DA5303B3-F8BF-4200-B1F3-975CD31F5B7E Q26991670-8593800A-2309-4E37-ACFE-DB81D0B08E9E Q27012688-2B9A2784-AA68-4633-8565-82F1CA174AAC Q27024675-8CA89807-A4E6-4B9D-92B7-26B26E8DE8AD Q27931495-F6DA1305-547F-44CE-A24C-2E6E641E68E7 Q27934471-A1E5FB04-7527-4826-8AAD-A0E92D31BC9D Q27935123-76F22CC2-0D9A-4C0F-ACD4-BD15EA292937 Q27936545-0378815B-1377-484A-8C5F-0FBB1F1A04BD Q28085364-00F9BB4B-DF89-45B9-9925-D15CA17C11C4 Q28211319-272F22BD-0924-43AB-8D35-5AF77AAFFC05 Q28212328-B3A46CBD-CD4F-4BB9-B349-5A60371F9A18 Q28214715-56102A8E-B29D-4208-AC74-CEDE4477197A Q28285316-259D8C3F-924E-452A-B165-4021A500BBAB Q29622881-C98C8A9C-F1D2-42C6-8106-B99A48D296B8 Q30453366-DE8D217A-5FC4-4823-9D85-2B176FF1DD9B Q31038985-AF1B520F-CDED-4427-8475-DD61C5A553E8 Q33302679-54BB6D64-4F3B-4E65-A171-D0D2C8C68EE2 Q33383830-F3773AAA-1B9A-4FA6-9D72-968DC9AB9DA7 Q33393809-74E49667-A233-4B02-9D31-F8C2BFD05690 Q33558155-13507CE7-0E00-4D95-A9E8-BEB4729FDC49 Q33797608-674380C1-02D1-49EE-82AC-D2CC3E737A49 Q33802272-0B68E02D-CAA3-4135-B4CF-5CCAD8F7FEB2 Q33808978-8937A398-45CC-486B-B261-5A2779285201

P2860

Xrcc3 is required for assembly of Rad51 complexes in vivo.

http://www.wikidata.org/entity/Q41016235

description

1998 nî lūn-bûn

@nan

1998年の論文

@ja

1998年論文

@yue

1998年論文

@zh-hant

1998年論文

@zh-hk

1998年論文

@zh-mo

1998年論文

@zh-tw

1998年论文

@wuu

1998年论文

@zh

1998年论文

@zh-cn

name

Xrcc3 is required for assembly of Rad51 complexes in vivo.

@en

type

label

Xrcc3 is required for assembly of Rad51 complexes in vivo.

@en

prefLabel

Xrcc3 is required for assembly of Rad51 complexes in vivo.

@en

P1433

Q41016235-9BBD7C39-3D0E-4774-829B-6E9513272430

P1476

Q41016235-19B8DCF3-D178-485D-96EE-2E72F0FFC33F

P2093

Q41016235-2C50F6D6-A233-4DB9-8B7B-870F695D1DDE

Q41016235-742F6CAA-8609-46D8-84A0-FCE4BFC62A6A

Q41016235-7B75DAE4-A73B-484C-8A1E-233AE128E8C6

Q41016235-9998FD43-CD6D-4F21-9A83-425BEFFECDF1

Q41016235-AFC204CC-CF46-4270-A03D-7530E9541228

Q41016235-B9AC6314-C8AB-45F4-A8B8-9B833988228C

Q41016235-F986FFDD-E688-46BA-8731-B3A1C4DC38AD

P2860

Q41016235-001B201D-082E-4B9B-9A14-9D569AF3D3E1

Q41016235-006FB040-3AA3-477F-9C6A-D46AAC68C614

Q41016235-046C485B-94DB-4B6D-B14B-27313C809C9A

Q41016235-0C853D66-FA60-4EB9-BF98-24BBCBEE84F0

Q41016235-1100DB78-E276-40C2-A545-CE0F98EB2B9D

Q41016235-1377A0A9-E1BD-4FA8-8D4C-A06DB6C77195

Q41016235-151BA11C-9C78-4D03-82F2-C7B58E51738D

Q41016235-1596C23C-2C66-49F8-971E-7342EFBE189F

Q41016235-1D405680-837D-4AE0-8FCD-E40684F62298

Q41016235-2101EEBF-FD76-4D07-B834-640B8CEBF037

P304

Q41016235-CBE8D970-CA22-439C-A6A5-75E6B4B318F4

P31

Q41016235-BE674AFE-188F-4347-AEF6-F392CDB1F58F

P356

Q41016235-4A9E4B96-F6EF-49A5-BF00-F47F14E49DF8

P407

Q41016235-A43D3CBF-A5BA-47E2-B154-06C2E5D041E9

P433

Q41016235-25C6943A-9CF9-4B8D-9359-F754B08DED64

P478

Q41016235-C3C1065A-3362-4EEC-9D2D-FB82BE414B2D

P577

Q41016235-2C23EDCA-EDBA-4EC3-9D27-30DBEC890756

P5875

Q41016235-634E59C7-6799-4732-BC60-DC91CF1FEF79

P698

Q41016235-58604E12-3445-4B9C-B068-77E7FA66894B

P356

JBC.273.34.21482

P1433

Journal of Biological Chemistry

P1476

Xrcc3 is required for assembly of Rad51 complexes in vivo.

@en

P2093

Beckett M

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

Bhattacharyya A

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

Bishop DK

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

Calderone C

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

Ear U

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

Shinohara A

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

Weichselbaum RR

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

P2860

Isolation and characterization of RAD51C, a new human member of the RAD51 family of related genes

Cloning of human, mouse and fission yeast recombination genes homologous to RAD51 and recA

Identification, characterization, and genetic mapping of Rad51d, a new mouse and human RAD51/RecA-related gene

XRCC2 and XRCC3, new human Rad51-family members, promote chromosome stability and protect against DNA cross-links and other damages

Correction of chromosomal instability and sensitivity to diverse mutagens by a cloned cDNA of the XRCC3 DNA repair gene

Human Rad51 protein promotes ATP-dependent homologous pairing and strand transfer reactions in vitro

Identification of a novel human RAD51 homolog, RAD51B

The mouse and human homologs of DMC1, the yeast meiosis-specific homologous recombination gene, have a common unique form of exon-skipped transcript in meiosis

Functional differences and interactions among the putative RecA homologs Rad51, Rad55, and Rad57.

Rad52 associates with RPA and functions with rad55 and rad57 to assemble meiotic recombination complexes

P304

21482-21488

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

P31

scholarly article

P356

10.1074/JBC.273.34.21482

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

P407

P433

34

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

P478

273

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

P577

1998-08-01T00:00:00Z

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

P5875

13580576

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

P698

9705276

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