Full-length archaeal Rad51 structure and mutants: mechanisms for RAD51 assembly and control by BRCA2 - Wikidata - awgldk - TriplyDB

Full-length archaeal Rad51 structure and mutants: mechanisms for RAD51 assembly and control by BRCA2

Full-length archaeal Rad51 structure and mutants: mechanisms for RAD51 assembly and control by BRCA2

http://www.wikidata.org/entity/Q27641910

about

Valine 1532 of human BRC repeat 4 plays an important role in the interaction between BRCA2 and RAD51 Interaction with the BRCA2 C terminus protects RAD51-DNA filaments from disassembly by BRC repeats The BRC repeats of BRCA2 modulate the DNA-binding selectivity of RAD51 Rec2 interplay with both Brh2 and Rad51 balances recombinational repair in Ustilago maydis Domain mapping of the Rad51 paralog protein complexes Trypanosoma brucei BRCA2 acts in antigenic variation and has undergone a recent expansion in BRC repeat number that is important during homologous recombination Stimulation of Dmc1-mediated DNA strand exchange by the human Rad54B protein Conformational flexibility revealed by the crystal structure of a crenarchaeal RadA Human Rad51 filaments on double- and single-stranded DNA: correlating regular and irregular forms with recombination function.Structure of RadB recombinase from a hyperthermophilic archaeon, Thermococcus kodakaraensis KOD1: an implication for the formation of a near-7-fold helical assembly.Distinct roles for two RAD51-related genes in Trypanosoma brucei antigenic variation.Hexameric structures of the archaeal secretion ATPase GspE and implications for a universal secretion mechanism The C-terminal domain of yeast PCNA is required for physical and functional interactions with Cdc9 DNA ligase Crystal structure of the left-handed archaeal RadA helical filament: identification of a functional motif for controlling quaternary structures and enzymatic functions of RecA family proteins Structural and Functional Analyses of Five Conserved Positively Charged Residues in the L1 and N-Terminal DNA Binding Motifs of Archaeal RadA Protein Structural and functional analyses of the DMC1-M200V polymorphism found in the human population Superoxide dismutase from the eukaryotic thermophile Alvinella pompejana: structures, stability, mechanism, and insights into amyotrophic lateral sclerosis Three New Structures of Left-Handed RadA Helical Filaments: Structural Flexibility of N-Terminal Domain Is Critical for Recombinase Activity Structural and Functional Characterisation of a Conserved Archaeal RadA Paralog with Antirecombinase Activity p38α MAP Kinase C-Terminal Domain Binding Pocket Characterized by Crystallographic and Computational Analyses Nbs1 Flexibly Tethers Ctp1 and Mre11-Rad50 to Coordinate DNA Double-Strand Break Processing and Repair Crystal structure of the phage T4 recombinase UvsX and its functional interaction with the T4 SF2 helicase UvsW Human Flap Endonuclease Structures, DNA Double-Base Flipping, and a Unified Understanding of the FEN1 Superfamily Using a Fragment-Based Approach To Target Protein-Protein Interactions Insights into FlaI Functions in Archaeal Motor Assembly and Motility from Structures, Conformations, and Genetics Structure of a filament of stacked octamers of human DMC1 recombinase A new protein complex promoting the assembly of Rad51 filaments Structural Analysis of Shu Proteins Reveals a DNA Binding Role Essential for Resisting Damage Structure of a hexameric form of RadA recombinase fromMethanococcus voltae Structural and SAXS analysis of the budding yeast SHU-complex proteins High-resolution structure of the presynaptic RAD51 filament on single-stranded DNA by electron cryo-microscopy.Engineering archeal surrogate systems for the development of protein-protein interaction inhibitors against human RAD51 Homologous recombination and human health: the roles of BRCA1, BRCA2, and associated proteins An archaeal Rad54 protein remodels DNA and stimulates DNA strand exchange by RadA Genetic steps of mammalian homologous repair with distinct mutagenic consequences Developing advanced X-ray scattering methods combined with crystallography and computation X-ray solution scattering (SAXS) combined with crystallography and computation: defining accurate macromolecular structures, conformations and assemblies in solution The RecB nuclease domain binds to RecA-DNA filaments: implications for filament loading.BRCA2 BRC motifs bind RAD51-DNA filaments.Structure of human Rad51 protein filament from molecular modeling and site-specific linear dichroism spectroscopy.

P2860

Q24304116-403460B6-C546-44D2-97AE-CCDEBEF1CFF6 Q24306511-213CEF67-2DA7-493B-9A66-3D143444340C Q24323065-9E451F4A-75C7-4166-942A-11EC673970E2 Q24537592-D4DE98F9-4C42-43C1-91E7-CE20B91659EC Q24634177-FF8D13F3-38AE-4593-9EF2-4A0098933EF2 Q24646998-C8C06A0C-988B-4891-92C4-545E7830CC31 Q24672957-DE777682-BF89-4B73-8B91-AED1EA1CC779 Q24795616-5C291680-D33F-45B2-9A5C-37A7E1EDBA0F Q24810357-E5C0CAA9-4BC4-4FA5-AC83-69C960ADE1A9 Q24810392-A87BC9C9-AA0F-4481-83CA-85D2B9E18BC2 Q24815002-9F851789-6AED-4B07-A90A-4FE4EA37540E Q27643662-E8DD98F0-E8C5-43EE-B96C-D952E2B0C8BC Q27643859-B43A54EE-B139-44AB-9FA0-1051BBEE571A Q27643938-C5AE780B-952B-4DE4-9509-C8A481834F02 Q27648064-40E3EB5C-C4C2-4363-9362-622FD6A8CE6A Q27650895-AF2E02DF-7541-45F4-A3A5-02FD875498D7 Q27653085-A5E6E7ED-5C6A-4108-A3FF-E9A2419C8FF5 Q27654195-7EB84C7B-C793-4E23-BC9E-69A46456E8EA Q27655359-308D0DB2-5979-4DA2-B82A-BFFE4B659611 Q27655779-444F2D4B-CB0B-4EC0-9F04-6A3415FCBA1A Q27657670-ECA3845F-2A63-464B-8F98-60BE9D151274 Q27665450-77D09F22-D31D-42A9-A647-B7BA61CE565B Q27667524-A383EB68-75F3-4BCC-9190-4449EA8B148E Q27675981-15E7EFFA-3B1B-4959-A898-2B24D508801F Q27676405-755CAF6D-CFFF-4F41-8913-50FB1131A61B Q27677167-03AA8BDA-1157-468A-BD4E-E2CB765AF5A0 Q27677299-D4DF1894-3ED2-4E84-88B9-C46BA72B0939 Q27678277-11C953A8-ADE5-4799-8C28-C90E01CE5372 Q27681132-A9556563-29F5-41E4-ACC2-6810B2DFF40C Q27681654-E7AA84CC-59F9-4D74-A502-5E1B93291575 Q27728002-F9AA0F52-4306-41BD-B8AA-8DE17C93C8DE Q27728438-62FDFF96-E8EB-4B21-8884-2F1086294B61 Q28085364-D3C5C78D-3DC1-419F-8B86-CE5E2AE8F291 Q28238006-CEE248E7-7D05-43A2-A0D3-3B22F38497A4 Q28287955-A63698BE-03E0-4F38-B0EB-2F08A388D62E Q28681355-8C4D15AE-304A-4DCC-A010-191323820937 Q29619405-5492BF3F-03D9-4C8C-8137-DFC1F9004664 Q30435064-F18CFB29-D4EA-4CF3-963F-6D08A4250AC7 Q30437059-D1541DDD-0527-45D6-B724-3EF3761F9F8D Q30437093-B28D8131-1898-4606-B0B6-EC8CD38F64BD

P2860

Full-length archaeal Rad51 structure and mutants: mechanisms for RAD51 assembly and control by BRCA2

http://www.wikidata.org/entity/Q27641910

description

2003 nî lūn-bûn

@nan

2003 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2003 թվականի սեպտեմբերին հրատարակված գիտական հոդված

@hy

2003年の論文

@ja

2003年論文

@yue

2003年論文

@zh-hant

2003年論文

@zh-hk

2003年論文

@zh-mo

2003年論文

@zh-tw

2003年论文

@wuu

name

Full-length archaeal Rad51 str ...... assembly and control by BRCA2

@ast

Full-length archaeal Rad51 str ...... assembly and control by BRCA2

@en

Full-length archaeal Rad51 str ...... assembly and control by BRCA2

@nl

type

label

Full-length archaeal Rad51 str ...... assembly and control by BRCA2

@ast

Full-length archaeal Rad51 str ...... assembly and control by BRCA2

@en

Full-length archaeal Rad51 str ...... assembly and control by BRCA2

@nl

prefLabel

Full-length archaeal Rad51 str ...... assembly and control by BRCA2

@ast

Full-length archaeal Rad51 str ...... assembly and control by BRCA2

@en

Full-length archaeal Rad51 str ...... assembly and control by BRCA2

@nl

P1433

Q27641910-F7DDC86D-173B-45D1-90E5-AED146183BB3

P1476

Q27641910-369DA5C2-C0E7-478B-9F88-B8093B19E9D9

P2093

Q27641910-3E2E772E-94BE-4002-9C65-63F21C9346CA

Q27641910-404C7A06-881F-4048-88E6-999BEE35A236

Q27641910-47563D50-3C2F-4F58-867A-B3AA7A7D47E3

Q27641910-685D5BC8-65DE-4235-87CD-19129520B0AB

Q27641910-741D1B3A-C97F-4F9B-B424-56CD38E6C5C4

Q27641910-95D74033-7D89-4B7A-9FA8-1C2ADE971F44

Q27641910-AE81400B-1428-4F07-8754-10BDC945A06F

Q27641910-AF0DB957-B71C-4801-BD46-542FDAB6D062

Q27641910-B696ADE9-8A32-4727-87E4-82AA01A69E88

Q27641910-D4C2AECB-B241-4157-9F9B-7286C325E277

P2860

Q27641910-1422A000-A9DB-4E6A-A6C6-3F9668DD4379

Q27641910-23765369-A9B7-4F9C-9EA7-EE5A4FD3525C

Q27641910-26753352-1706-4410-BCC6-540B026D4F7A

Q27641910-2A2AFACA-9C0E-403E-8AA0-DC2724DF8ABD

Q27641910-2D264B93-749B-4632-80A9-E9F478D8C99A

Q27641910-2E96187A-1BED-4B93-9008-C3D04132970A

Q27641910-2F7CA597-D747-4CAE-A10D-A65BEADB9990

Q27641910-313EB5F3-0466-4EA0-A13A-F44FDCBBB791

Q27641910-37006829-7608-4F70-9AE7-E3DCDA2E4AAE

Q27641910-38347375-856C-4CFE-A531-4ACE08EF7669

P304

Q27641910-58E9CF0F-B625-477D-B62C-05410429A16F

P31

Q27641910-B7CC4A0A-92E8-4A42-BB72-FEE05650BC0A

P3181

Q27641910-0F4BC5E9-805B-4266-ABF1-9B6BA6BD3430

P356

Q27641910-F6747532-78C7-4822-A1B4-CA6D4667D7C2

P407

Q27641910-8011FF7C-AB00-4A19-9766-291BBFD7EA3F

P433

Q27641910-288CF222-96E6-4DCF-8E4C-2F80BB13AE04

P478

Q27641910-49EDB5A6-A843-4565-AAE2-1E9231A2B056

P50

Q27641910-3B991455-A11D-4EA0-AA1B-2B55A4B1CCA8

Q27641910-8C04C6AF-BACD-479C-9118-6FBAFA17F5EC

Q27641910-9F8A7B0E-0A1D-45B1-AF9B-AC9902B1203E

Q27641910-F1F75743-2A94-48A6-9841-A371E76A6254

P577

Q27641910-869C0F03-43C0-49E9-BC44-3DBEA083CD94

P5875

Q27641910-B0D28634-FF1D-4533-B6DA-02AE182CBA81

P698

Q27641910-7474A6ED-B017-4ECB-9638-40F645F0AA99

P932

Q27641910-BE45EDAC-62F6-4BC7-9FB5-BACD608DDA3A

P3181

P356

P1433

The EMBO Journal

P1476

Full-length archaeal Rad51 str ...... assembly and control by BRCA2

@en

P2093

Andrew S Arvai

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

Ashok R Venkitaraman

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

Biana Yelent

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

Chiharu Hitomi

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

David S Shin

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

David S Yu

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

Debbie Bates

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

Hiro Tsuruta

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

Luca Pellegrini

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

Mahmud K Shivji

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

P2860

Purification and characterization of the human Rad51 protein, an analogue of E. coli RecA

Insights into DNA recombination from the structure of a RAD51-BRCA2 complex

Crystal structures of Mycobacterium tuberculosis RecA and its complex with ADP-AlF(4): implications for decreased ATPase activity and molecular aggregation

Structure of the single-strand annealing domain of human RAD52 protein

The N-terminal domain of the human Rad51 protein binds DNA: structure and a DNA binding surface as revealed by NMR

Crystal structure of the Holliday junction DNA in complex with a single RuvA tetramer

Crystal structure of T7 gene 4 ring helicase indicates a mechanism for sequential hydrolysis of nucleotides

Crystal structure of the homologous-pairing domain from the human Rad52 recombinase in the undecameric form

BRCA2 function in DNA binding and recombination from a BRCA2-DSS1-ssDNA structure

ATP-mediated conformational changes in the RecA filament

P304

4566-4576

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

P31

scholarly article

P3181

2442871

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

P356

10.1093/EMBOJ/CDG429

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

P407

P433

17

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

P478

22

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

P50

Douglas S. Daniels

P577

2003-09-01T00:00:00Z

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

P5875

10594628

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

P698

12941707

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

P932

202371

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