Structure of UvrA nucleotide excision repair protein in complex with modified DNA - Test2 - elhamkhani - TriplyDB

Structure of UvrA nucleotide excision repair protein in complex with modified DNA

Structure of UvrA nucleotide excision repair protein in complex with modified DNA

http://www.wikidata.org/entity/Q27666597

about

Directly interrogating single quantum dot labelled UvrA2 molecules on DNA tightropes using an optically trapped nanoprobe.Investigation of bacterial nucleotide excision repair using single-molecule techniques.The biological and structural characterization of Mycobacterium tuberculosis UvrA provides novel insights into its mechanism of action Crystal structure of the UvrB dimer: insights into the nature and functioning of the UvrAB damage engagement and UvrB-DNA complexes Structure and mechanism of the UvrA-UvrB DNA damage sensor The ABC-F protein EttA gates ribosome entry into the translation elongation cycle A Decade of Biochemical and Structural Studies of the DNA Repair Machinery of Deinococcus radiodurans: Major Findings, Functional and Mechanistic Insight and Challenges Ribonucleotides as nucleotide excision repair substrates.Structural and thermodynamic insight into Escherichia coli UvrABC-mediated incision of cluster diacetylaminofluorene adducts on the NarI sequence.Probing for DNA damage with β-hairpins: similarities in incision efficiencies of bulky DNA adducts by prokaryotic and human nucleotide excision repair systems in vitro Surviving the sun: repair and bypass of DNA UV lesions.Conformational and thermodynamic properties modulate the nucleotide excision repair of 2-aminofluorene and 2-acetylaminofluorene dG adducts in the NarI sequence.Dissociation Dynamics of XPC-RAD23B from Damaged DNA Is a Determining Factor of NER Efficiency.Metabolite toxicity determines the pace of molecular evolution within microbial populations Unusual sequence effects on nucleotide excision repair of arylamine lesions: DNA bending/distortion as a primary recognition factor Prokaryotic nucleotide excision repair.Single-molecule imaging of UvrA and UvrB recruitment to DNA lesions in living Escherichia coli.Exploratory Investigation of Bacteroides fragilis Transcriptional Response during In vitro Exposure to Subinhibitory Concentration of Metronidazole.A tale of two cities: A tribute to Aziz Sancar's Nobel Prize in Chemistry for his molecular characterization of NER.Dynamics of lesion processing by bacterial nucleotide excision repair proteins Strand-specific recognition of DNA damages by XPD provides insights into nucleotide excision repair substrate versatility.Stalled transcription complexes promote DNA repair at a distance.Interplay of DNA repair with transcription: from structures to mechanisms.Prioritizing the repair of DNA damage that is encountered by RNA polymerase.Invited review: Architectures and mechanisms of ATP binding cassette proteins.Conservation and Divergence in Nucleotide Excision Repair Lesion Recognition.Single-Molecule Imaging Reveals that Rad4 Employs a Dynamic DNA Damage Recognition Process Small-angle X-ray scattering reveals architecture and A₂B₂ stoichiometry of the UvrA-UvrB DNA damage sensor.Recruitment of UvrBC complexes to UV-induced damage in the absence of UvrA increases cell survival.Mycobacterium tuberculosis UvrB forms dimers in solution and interacts with UvrA in the absence of ligands.Novel Sequence Features of DNA Repair Genes/Proteins from Deinococcus Species Implicated in Protection from Oxidatively Generated Damage.

P2860

Q27303421-DE739698-2981-4D64-8299-87D07605DB3E Q27312710-77999A04-9DA0-4E89-BAA9-07EC0D3AFEE3 Q27668076-A7BC5991-B872-46AC-A6A1-D3E0A517A7CC Q27670608-AFE7EB1F-4AF9-4008-8346-4A2A810074D7 Q27677070-07E5B621-8483-4737-951D-D4B076A25BD2 Q27681176-C7A753B3-7155-4932-8E64-39FDD9F16DC1 Q28072374-9231592E-9544-40DD-85DB-2DDD7BC4EF69 Q28544926-9D84B626-4B51-424B-B7EE-E5A6E3097EAB Q34809636-08A0C99E-2E68-4AA8-A442-A54F6C015ACA Q35540743-28B7774E-E1EB-4F8E-AFD3-2E3CBF4F4C12 Q35706169-35D61F07-F0DB-464F-AFA1-3B0C435DAE4E Q35956020-EFAE90B7-8AF6-45DA-B697-465AA3502E1E Q36057983-3D7D2FA1-CAF7-4838-BAF7-14DE56F6F14A Q36280245-6A385326-7DEE-40F3-BE3A-4414D94D9667 Q36559300-B40715DC-EBCD-47FD-A988-BC28E4732F93 Q36626668-D652B862-019C-4E07-8507-433D4576F2E2 Q37223266-CAC50B83-9AC9-41CB-B581-C6E25D7769C2 Q37266199-861862C9-A406-44AD-9543-A76F095A6A4B Q37347233-5009B747-E8E5-493D-AEC0-6B4308B6257D Q37382348-C3D94993-C4BF-4D54-9D99-8AE4F0CF75EF Q37563531-F2F1A267-8AA3-4399-A8B3-B89F3453A0FC Q37659952-83485C63-D569-42D1-80AB-9FCEB1B12568 Q38053651-3E7C2431-9006-4C8F-A436-69E1700ED06D Q38438044-E1FDB6F0-CFA3-4892-A90A-6B3A190B339A Q38796195-F3EC4D10-3D89-499A-B578-393640FAF589 Q41002702-D44AE5D1-CE3C-4156-8C9B-6773ADDE4697 Q42363341-8F6D785B-8EA7-44AB-9062-73073630988D Q44536579-6633AEAC-E66D-4B3A-A448-574238C96A8F Q47293875-017C0495-46D6-4286-8FD0-012D362555DE Q47589435-EB588553-F40F-4287-AC61-DD81DB6442A0 Q51742882-EA149A43-B7AE-4909-831B-8A3839031BFF

P2860

Structure of UvrA nucleotide excision repair protein in complex with modified DNA

http://www.wikidata.org/entity/Q27666597

description

2011 nî lūn-bûn

@nan

2011 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի փետրվարին հրատարակված գիտական հոդված

@hy

2011年の論文

@ja

2011年論文

@yue

2011年論文

@zh-hant

2011年論文

@zh-hk

2011年論文

@zh-mo

2011年論文

@zh-tw

2011年论文

@wuu

name

Structure of UvrA nucleotide excision repair protein in complex with modified DNA

@ast

Structure of UvrA nucleotide excision repair protein in complex with modified DNA

@en

Structure of UvrA nucleotide excision repair protein in complex with modified DNA

@nl

type

label

Structure of UvrA nucleotide excision repair protein in complex with modified DNA

@ast

Structure of UvrA nucleotide excision repair protein in complex with modified DNA

@en

Structure of UvrA nucleotide excision repair protein in complex with modified DNA

@nl

prefLabel

Structure of UvrA nucleotide excision repair protein in complex with modified DNA

@ast

Structure of UvrA nucleotide excision repair protein in complex with modified DNA

@en

Structure of UvrA nucleotide excision repair protein in complex with modified DNA

@nl

P1433

Q27666597-3A6A7961-F4C0-4759-89ED-D1EE0E488A64

P1476

Q27666597-BD01689A-B421-4CD5-854F-40E34E2A047E

P2093

Q27666597-21443ABE-01E7-4AD6-B732-680B85E5A012

Q27666597-848166A0-DC17-4BA1-99B1-CDF2E4103893

Q27666597-A521A246-658F-4BC7-ADD1-F29798C5686B

P2860

Q27666597-0931AF02-5AC3-43D2-80F0-1AAFDB93C0E3

Q27666597-0D66C56C-56BE-46B8-A609-C612ABB2EBCA

Q27666597-241F2D5E-A3B4-4ADF-BFA6-3A7DB3358897

Q27666597-2CABD054-15A5-4F0D-AB68-55007077E5E3

Q27666597-2F452928-8052-4C45-9711-E1A8C22FD9C5

Q27666597-34E36319-214C-495A-B4B2-BD606678B7CE

Q27666597-3ACA0E82-F455-4873-9657-6B9F07CB4C42

Q27666597-4B46AFBD-0575-47CA-A7F4-977E08647176

Q27666597-4E917461-035C-42C1-8DFB-14966BDEBD11

Q27666597-500957DC-252B-445E-9E61-43630289B3FC

P2888

Q27666597-7228E7F4-C72A-450B-A7D2-3DCCC13D5F65

P304

Q27666597-CD7C62C5-3995-448A-A396-8DF3E4C9F8CF

P31

Q27666597-2B90C2B2-DF32-4FC3-B433-875FB84CB8ED

P3181

Q27666597-BF0142FF-1940-450F-BFE3-90484CD66E24

P356

Q27666597-CCDA0648-B9EB-47A7-A720-DD2E665F873F

P433

Q27666597-876F82A5-FA1D-4A9E-AD6B-80A358FB38CC

P478

Q27666597-7DFC3F66-ED76-4D4A-AA78-FF5CE5D60ED4

P50

Q27666597-0A31B4F7-D003-4203-A56D-D99BE68A118D

Q27666597-C4775484-98AD-4E2B-858C-F6DC0F1AECBA

P577

Q27666597-4A14E0E0-D4CB-4854-AAED-BCB23662392B

P5875

Q27666597-A6EBF008-2A74-4C0D-801E-5BDD4A90E2FA

P6179

Q27666597-229F53CF-B085-4B43-A4FC-12C5085CCF62

P698

Q27666597-662FD327-A81F-4563-8E74-DC408FEF5557

P921

Q27666597-3559A92D-C164-412A-8367-4AA92553A394

Q27666597-C177BE95-B1BA-48B7-BAE9-F486AB477D30

P932

Q27666597-2101FA56-894C-47E1-BCCC-E05DA1D8EA5E

P3181

P356

P1433

Nature Structural & Molecular Biology

P1476

Structure of UvrA nucleotide excision repair protein in complex with modified DNA

@en

P2093

Anna Tańska

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

Elżbieta Nowak

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

Marcin Nowotny

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

P2860

Structural basis of UV DNA-damage recognition by the DDB1-DDB2 complex

Conserved domains in DNA repair proteins and evolution of repair systems

Electrostatics of nanosystems: application to microtubules and the ribosome

MolProbity: all-atom structure validation for macromolecular crystallography

Processing of X-ray diffraction data collected in oscillation mode

Solution conformation of the (+)-trans-anti-benzo[g]chrysene-dA adduct opposite dT in a DNA duplex

Crystal structure of the DNA nucleotide excision repair enzyme UvrB from Thermus thermophilus

Crystal structure of Thermus thermophilus HB8 UvrB protein, a key enzyme of nucleotide excision repair

Crystal structure of UvrB, a DNA helicase adapted for nucleotide excision repair.

Crystal structures of mismatch repair protein MutS and its complex with a substrate DNA

P2888

P304

191-197

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

P31

scholarly article

P3181

625571

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

P356

10.1038/NSMB.1973

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

P433

2

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

P478

18

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

P50

Krzysztof Skowronek

P577

2011-01-16T00:00:00Z

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

P5875

49760516

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

P6179

1048559817

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

P698

21240268

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

P921

protein structure

structural biology

P932

3428727

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