Interactions between UvrA and UvrB: the role of UvrB's domain 2 in nucleotide excision repair - Wikidata - wikimedia - TriplyDB

Interactions between UvrA and UvrB: the role of UvrB's domain 2 in nucleotide excision repair

Interactions between UvrA and UvrB: the role of UvrB's domain 2 in nucleotide excision repair

http://www.wikidata.org/entity/Q35836058

about

Crystal Structure of Bacillus stearothermophilus UvrA Provides Insight into ATP-Modulated Dimerization, UvrB Interaction, and DNA Binding A Structural Model for the Damage-sensing Complex in Bacterial Nucleotide Excision Repair Crystal structure of the membrane-bound bifunctional transglycosylase PBP1b from Escherichia coli.An N-terminal clamp restrains the motor domains of the bacterial transcription-repair coupling factor Mfd Minor Groove Orientation of the KWKK Peptide Tethered via the N-Terminal Amine to the Acrolein-Derived 1, N 2 -γ-Hydroxypropanodeoxyguanosine Lesion with a Trimethylene Linkage,Structure and mechanism of the UvrA-UvrB DNA damage sensor Nucleotide excision repair (NER) machinery recruitment by the transcription-repair coupling factor involves unmasking of a conserved intramolecular interface Nucleotide excision repair of a DNA interstrand cross-link produces single- and double-strand breaks.Controlled degradation by ClpXP protease tunes the levels of the excision repair protein UvrA to the extent of DNA damage.γ-Hydroxy-1,N2-propano-2'-deoxyguanosine DNA adduct conjugates the N-terminal amine of the KWKK peptide via a carbinolamine linkage.Structure-based DNA-targeting strategies with small molecule ligands for drug discovery.Prokaryotic nucleotide excision repair.The C-terminal zinc finger of UvrA does not bind DNA directly but regulates damage-specific DNA binding.Cooperative damage recognition by UvrA and UvrB: identification of UvrA residues that mediate DNA binding The bacterial transcription repair coupling factor.Efficient processing of TFO-directed psoralen DNA interstrand crosslinks by the UvrABC nuclease NMR analysis of [methyl-13C]methionine UvrB from Bacillus caldotenax reveals UvrB-domain 4 heterodimer formation in solution Homologous recombination but not nucleotide excision repair plays a pivotal role in tolerance of DNA-protein cross-links in mammalian cells.Interplay of DNA repair with transcription: from structures to mechanisms.Identification of residues within UvrB that are important for efficient DNA binding and damage processing.Analyzing the handoff of DNA from UvrA to UvrB utilizing DNA-protein photoaffinity labeling.The unstructured C-terminal extension of UvrD interacts with UvrB, but is dispensable for nucleotide excision repair.Prioritizing the repair of DNA damage that is encountered by RNA polymerase.Mechanistic insights into transcription coupled DNA repair.Regulation and rate enhancement during transcription-coupled DNA repair.Small-angle X-ray scattering reveals architecture and A₂B₂ stoichiometry of the UvrA-UvrB DNA damage sensor.UvrB domain 4, an autoinhibitory gate for regulation of DNA binding and ATPase activity.

P2860

Q27649421-C3C61F99-EA4C-4EF2-808C-9BBF4DE6A4BE Q27654123-C996B1FE-F65A-49A0-B25C-9FA1B7E03EC1 Q27655550-A970C7AA-044C-45E8-B0CA-16C42B7AED73 Q27657130-A611BC5D-BB26-4F4D-8A6E-D01C61D24212 Q27663148-AA354687-292A-4C5E-AE8B-3D5556AF3EAB Q27677070-697682B9-4703-4B0A-9A4D-D3F40AE5105E Q27677257-7192A131-92C0-4B8E-86C6-61120DD35391 Q33580793-EA5F1D06-2D79-4849-9581-3EDD3A841B14 Q33841737-B71073A2-8922-4ECB-9A66-B99BCCC4D167 Q33895640-1196A302-A039-4963-98FF-8BE239305EA1 Q34697484-FA36AD60-3208-4D7D-8207-E44E8261B576 Q36626668-9608B4DE-8851-4D8C-A4EF-194F509AF002 Q36675936-BE8D9A37-2348-441C-A4C0-7E5DB0631E93 Q36675940-F82C70D4-95A2-4861-91A4-063BCA733DF5 Q36713668-3A4B83BE-9B3B-4F0E-8B6F-9297F5556C0B Q37014694-4BB1A6D8-74FC-4A3B-8412-CBC0F19451E6 Q37060815-10EBC806-52BA-4969-A6C4-885DF1199771 Q37447887-8CF59C04-24E0-4DA1-AC87-0A52DEA12281 Q38053651-08CA1989-6866-4AB9-8FA1-C334957C4B9E Q38335962-908C1E0E-462A-4CB1-9DD6-2ADF31562FF9 Q38337796-E3FB0508-2FDC-4643-A417-9D580B88654B Q38350448-CF4BC8A3-4C3B-411F-A9F1-3B5243045637 Q38438044-B2FB842B-0B59-4E92-BBD6-F1640642BFA9 Q39384000-448E8B4E-8B48-4334-8BA5-BB60081D66C5 Q41816603-9CF8603B-C3B8-4090-ABCE-A1312CEF5DA0 Q44536579-C77FB4F9-0748-490D-BB46-0495E9D36B53 Q53600241-452AFB52-AEB9-4BBF-9A10-0D9C84A599E1

P2860

Interactions between UvrA and UvrB: the role of UvrB's domain 2 in nucleotide excision repair

http://www.wikidata.org/entity/Q35836058

description

2004 nî lūn-bûn

@nan

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

2004年论文

@zh

2004年论文

@zh-cn

name

Interactions between UvrA and ...... in nucleotide excision repair

@ast

Interactions between UvrA and ...... in nucleotide excision repair

@en

type

label

Interactions between UvrA and ...... in nucleotide excision repair

@ast

Interactions between UvrA and ...... in nucleotide excision repair

@en

prefLabel

Interactions between UvrA and ...... in nucleotide excision repair

@ast

Interactions between UvrA and ...... in nucleotide excision repair

@en

P1433

Q35836058-8AEFCD92-DBA5-4371-B85E-6755AB0E87C8

P1476

Q35836058-02F3BA3D-9B36-4B2A-A1F9-C48E156A3047

P2093

Q35836058-296EE12B-AB88-40DC-B30A-399A196C7B21

Q35836058-5FE7F591-702F-458F-8706-034042FD81DC

Q35836058-7582E830-BF5D-4A4B-BFB9-91228E7BF678

Q35836058-998271F5-0176-4F60-B82F-C2912A7D3EA7

Q35836058-A41ECBD5-4E22-42BF-9BCF-4CF01A4CBE4D

Q35836058-AA69B592-C3D1-433C-9918-47FDDE497B25

Q35836058-B1564271-004F-4754-BF9C-0F201610150A

P2860

Q35836058-0377667E-2993-4329-80B9-6A94C6CA5C2D

Q35836058-06FD80C7-691E-44FC-B72E-77FB8D44D549

Q35836058-11A682AB-8F80-4F6C-8DE6-FBB8120A497C

Q35836058-12F4784E-0733-4594-8261-F4EABA639919

Q35836058-14D32B34-B99C-44D8-877C-437B40B026D2

Q35836058-269ED42A-5F2B-48F1-A899-5641C3A0FCFD

Q35836058-28B3E6BC-DC28-41FA-8FA1-E341A129E33D

Q35836058-3F65AEFC-A207-4EDF-AB23-93E248B61948

Q35836058-46C67DFF-97C7-4B58-8FB7-07C58C3B3D43

Q35836058-532A4D89-F54D-4013-B950-D675445C7F41

P304

Q35836058-364A7B33-1599-4850-BD84-BBAA7BF5F0FD

P31

Q35836058-9793C0C0-7B7B-47E7-B5CA-73B5400C85B8

P356

Q35836058-75B53E85-9122-4395-9C7E-E35EA23260E1

P407

Q35836058-BC05FF7B-7D5B-4B17-BAE7-7110E7545BFA

P433

Q35836058-B9E638E1-C8A6-44FE-A20B-43106B7CC7B0

P478

Q35836058-7C02751B-8CB5-4696-B9B6-E7A7774A4B95

P50

Q35836058-B48F87AA-C9E2-44E6-8AF2-D76A52D5D0C5

P577

Q35836058-6027257C-A1F4-4D0E-AAE7-66BDA82CE969

P5875

Q35836058-22D690EE-B959-4643-A24E-936F2D1C5F2F

P698

Q35836058-C2E67B8C-DD9B-4C2E-BC4C-A490453FC8BD

P921

Q35836058-18629B6B-DE2E-414B-97AE-8EFFDC0110DD

Q35836058-FAEEF37C-3B7B-4FEF-97C9-CC45E1D0BB02

P932

Q35836058-DB7CDB47-BD40-477B-967F-C0114E487BF3

P356

SJ.EMBOJ.7600263

P1433

The EMBO Journal

P1476

Interactions between UvrA and ...... in nucleotide excision repair

@en

P2093

Bennett Van Houten

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

Bhaskar S Mandavilli

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

Deborah L Croteau

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

James J Truglio

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

Karsten Theis

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

Matthew J DellaVecchia

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

Milan Skorvaga

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

P2860

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 structure of Escherichia coli UvrB C-terminal domain, and a model for UvrB-uvrC interaction

Solution structure, hydrodynamics and thermodynamics of the UvrB C-terminal domain

Dali: a network tool for protein structure comparison

Catalytic sites for 3' and 5' incision of Escherichia coli nucleotide excision repair are both located in UvrC

The presence of two UvrB subunits in the UvrAB complex ensures damage detection in both DNA strands.

DNA excision repair

The nucleotide excision repair protein UvrB, a helicase-like enzyme with a catch.

P304

2498-2509

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

P31

scholarly article

P356

10.1038/SJ.EMBOJ.7600263

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

P407

P433

13

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

P478

23

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

P50

Caroline Kisker

P577

2004-06-10T00:00:00Z

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

P5875

8514165

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

P698

15192705

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

P921

excinuclease ABC activity

excinuclease repair complex

P932

449773

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