about
The Mre11 protein interacts with both Rad50 and the HerA bipolar helicase and is recruited to DNA following gamma irradiation in the archaeon Sulfolobus acidocaldariusUnraveling DNA helicases. Motif, structure, mechanism and functionThe human Pif1 helicase, a potential Escherichia coli RecD homologue, inhibits telomerase activitySingle-molecule studies reveal dynamics of DNA unwinding by the ring-shaped T7 helicaseRecBCD enzyme and the repair of double-stranded DNA breaksRecBCD enzyme switches lead motor subunits in response to chi recognitionChi hotspot activity in Escherichia coli without RecBCD exonuclease activity: implications for the mechanism of recombinationDNA binding to RecD: role of the 1B domain in SF1B helicase activityInsights into Chi recognition from the structure of an AddAB-type helicase-nuclease complexEnd-resection at DNA double-strand breaks in the three domains of lifeCell cycle-dependent regulation of a human DNA helicase that localizes in DNA damage fociRecBCD enzyme is a DNA helicase with fast and slow motors of opposite polarityCrystal structure of RecBCD enzyme reveals a machine for processing DNA breaksDNA helicase activity of the RecD protein from Deinococcus radioduransCharacterization of the helicase activity and substrate specificity of Mycobacterium tuberculosis UvrDSingle-molecule imaging of Bacteroides fragilis AddAB reveals the highly processive translocation of a single motor helicase.Oxidative stress resistance in Deinococcus radiodurans.Novel, fluorescent, SSB protein chimeras with broad utility.Visualizing protein movement on DNA at the single-molecule level using DNA curtainsForward and reverse motion of single RecBCD molecules on DNA.Construction of recB-recD genetic fusion and functional analysis of RecBDC fusion enzyme in Escherichia coliAdnAB: a new DSB-resecting motor-nuclease from mycobacteria.All three subunits of RecBCD enzyme are essential for DNA repair and low-temperature growth in the Antarctic Pseudomonas syringae Lz4WCharacterization of the mycobacterial AdnAB DNA motor provides insights into the evolution of bacterial motor-nuclease machinesVisualizing protein-DNA interactions at the single-molecule levelKinetic mechanism for DNA unwinding by multiple molecules of Dda helicase aligned on DNA.The adnAB locus, encoding a putative helicase-nuclease activity, is essential in StreptomycesEnd resection at double-strand breaks: mechanism and regulation.Double strand break unwinding and resection by the mycobacterial helicase-nuclease AdnAB in the presence of single strand DNA-binding protein (SSB).Prokaryotic and eukaryotic DNA helicases. Essential molecular motor proteins for cellular machinery.The SOS Regulatory Network.Roles of E. coli double-strand-break-repair proteins in stress-induced mutationMechanisms of helicases.DNA unwinding and protein displacement by superfamily 1 and superfamily 2 helicases.Relationship of DNA degradation by Saccharomyces cerevisiae exonuclease 1 and its stimulation by RPA and Mre11-Rad50-Xrs2 to DNA end resectionThe AddAB helicase-nuclease catalyses rapid and processive DNA unwinding using a single Superfamily 1A motor domain.The conserved C-terminus of the PcrA/UvrD helicase interacts directly with RNA polymerase.Structure-specific DNA binding and bipolar helicase activities of PcrA.Agrobacterium rhizogenes GALLS protein contains domains for ATP binding, nuclear localization, and type IV secretion.Molecular and Functional Characterization of RecD, a Novel Member of the SF1 Family of Helicases, from Mycobacterium tuberculosis.
P2860
Q21262981-DBFFDB67-29F6-43EE-B53A-98A9BDC95DA3Q22065679-55F9BBCE-71C3-402F-902D-DB555AE863FCQ24306780-C19DDEF6-544A-43B6-89F7-0A29B663FBC1Q24642351-B59A560E-EFC4-4BBF-BFC6-C6EFD5F65EA6Q24650931-776099EF-483D-483B-A75B-02DADD9D620CQ24684193-F85E36C6-0590-49D1-8FB8-09AC56D71B8BQ24685287-911FCDCC-70A5-4040-BEA0-548395B60150Q27651386-99FBE642-3583-48AB-A4B9-C32B100FDCB3Q27677071-E811CE69-AED4-4B87-8C00-FAB874F87730Q27694756-C8D8E65F-EFE0-475B-BFA9-3C206E3969F1Q28116217-10622F22-FC97-47BE-AA0E-689B20AC6CB1Q28180401-D3A30AD9-3954-48D2-B095-2B42D5853379Q28292707-1BBAAC87-A050-4954-9284-A0A34B5CA370Q28485666-786A5EB7-318B-43B1-81E5-C7B48177FDD3Q28487081-6307227C-ABB3-452C-B59A-7FD823F6BD20Q30494935-5670760B-067A-4468-A5AA-0EEFB8FD7874Q30499016-37B0CE4B-FCB2-4022-84F8-A4A45E892109Q30500680-BCD0C42D-A95B-45D4-9415-8CBB6F5617A7Q30585002-FEF2AE02-2940-4BF6-989E-C95443ADF0BFQ30751649-A0199667-0A01-4160-905A-4EB792524076Q33375176-48450113-CF77-42B6-9EB9-0C6C3C1DFA85Q33453070-CA81DA5F-886C-461C-98C4-967CEAADFED0Q33535942-2497962C-D89D-40F6-A5A0-553DB170C4FBQ33594007-1752994B-5F74-4D6B-9BF0-05BF205D7CA3Q33643127-23EFBF52-FA7B-4CE6-A4C6-A42F912472C6Q33876054-D536AE6A-C53A-4295-B78B-A9017EA2B8FAQ33899551-CE04A0C2-016A-42AA-9119-538A00340997Q33938581-ED78AEC3-B088-4804-85C0-26921D58C5D7Q34251039-BF07D05F-7F1F-4506-AE9A-471BE84046D3Q34318859-E7BA49EF-B2B8-4464-A9BE-46A90FF89E71Q34337115-685F23C1-3EA3-41EA-BDE5-0BABEE19971FQ34470485-73373B78-A1D5-4377-8F35-39FF687A4818Q34521150-C0CCA15D-D91E-4D4E-81D1-A6EE99B982FBQ34652749-4EECA0E5-5539-4848-AD5D-30CBDD491948Q34670029-EBD6D5A1-3697-476D-9E36-BC7E830AB835Q34723538-BA3EB2C2-CC73-4120-B770-3EB3B03074CAQ35023532-731B4BE6-4B97-43A3-9C83-1C4728403596Q35130884-DFC0F1D4-23C2-41EE-B9AF-8A32767F4A32Q35220612-7706D378-BE67-4467-8381-1AF4A59C4D03Q35583057-90E9C954-E663-49B8-8457-F613F10DB1DB
P2860
description
2003 nî lūn-bûn
@nan
2003年の論文
@ja
2003年学术文章
@wuu
2003年学术文章
@zh-cn
2003年学术文章
@zh-hans
2003年学术文章
@zh-my
2003年学术文章
@zh-sg
2003年學術文章
@yue
2003年學術文章
@zh
2003年學術文章
@zh-hant
name
RecBCD enzyme is a bipolar DNA helicase.
@en
RecBCD enzyme is a bipolar DNA helicase.
@nl
type
label
RecBCD enzyme is a bipolar DNA helicase.
@en
RecBCD enzyme is a bipolar DNA helicase.
@nl
prefLabel
RecBCD enzyme is a bipolar DNA helicase.
@en
RecBCD enzyme is a bipolar DNA helicase.
@nl
P2860
P356
P1433
P1476
RecBCD enzyme is a bipolar DNA helicase.
@en
P2093
Stephen C Kowalczykowski
P2860
P2888
P304
P356
10.1038/NATURE01673
P407
P577
2003-06-01T00:00:00Z
P6179
1052768024