The Escherichia coli RuvB branch migration protein forms double hexameric rings around DNA.

scientific article published on August 1994

The Escherichia coli RuvB branch migration protein forms double hexameric rings around DNA. is …
instance of (P31):
scholarly articleQ13442814

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P819ADS bibcode1994PNAS...91.7618S
P356DOI10.1073/PNAS.91.16.7618
P932PMC publication ID44453
P698PubMed publication ID8052630
P5875ResearchGate publication ID15145878

P50authorStephen C. WestQ7608844
Edward H EgelmanQ44068749
P2093author name stringX Yu
C J Benson
A Stasiak
I R Tsaneva
P2860cites workTwo related superfamilies of putative helicases involved in replication, recombination, repair and expression of DNA and RNA genomesQ24635818
Bidirectional RNA helicase activity of eucaryotic translation initiation factors 4A and 4FQ29620295
Functional interactions of ligand cofactors with Escherichia coli transcription termination factor rho. II. Binding of RNAQ31148744
Mass mapping with the scanning transmission electron microscopeQ34181977
Escherichia coli DNA helicases: mechanisms of DNA unwindingQ35225286
RuvA and RuvB proteins of Escherichia coli exhibit DNA helicase activity in vitroQ36101351
Structure and regulation of the Escherichia coli ruv operon involved in DNA repair and recombination.Q36216012
Classification of images of biomolecular assemblies: a study of ribosomes and ribosomal subunits of Escherichia coliQ36427603
Interaction of Escherichia coli RuvA and RuvB proteins with synthetic Holliday junctionsQ37060462
Association of DNA helicase and primase activities with a subassembly of the herpes simplex virus 1 helicase-primase composed of the UL5 and UL52 gene productsQ37395148
SOS-inducible DNA repair proteins, RuvA and RuvB, of Escherichia coli: functional interactions between RuvA and RuvB for ATP hydrolysis and renaturation of the cruciform structure in supercoiled DNAQ37597566
Resolution of Holliday junctions by RuvC resolvase: cleavage specificity and DNA distortion.Q38315860
The herpes simplex virus type-1 origin binding protein. DNA helicase activityQ38322424
Physical properties of the Escherichia coli transcription termination factor rho. 1. Association states and geometry of the rho hexamerQ38331083
Formation and resolution of recombination intermediates by E. coli RecA and RuvC proteins.Q38331746
The dnaB gene product of Escherichia coli. I. Purification, homogeneity, and physical propertiesQ40146044
Processing of recombination intermediates by the RecG and RuvAB proteins of Escherichia coliQ40406462
Nucleotide sequencing of the ruv region of Escherichia coli K-12 reveals a LexA regulated operon encoding two genesQ40544468
The processing of recombination intermediates: mechanistic insights from studies of bacterial proteinsQ40804112
Escherichia coli RuvC protein is an endonuclease that resolves the Holliday structureQ41083963
Molecular and functional analysis of the ruv region of Escherichia coli K-12 reveals three genes involved in DNA repair and recombinationQ41866318
Purification and properties of the RuvA and RuvB proteins of Escherichia coliQ44131194
Structure and assembly of the Escherichia coli transcription termination factor rho and its interactions with RNA I. Cryoelectron microscopic studiesQ44870020
Three-dimensional reconstruction of single particles embedded in iceQ52430878
Branch migration of Holliday junctions promoted by the Escherichia coli RuvA and RuvB proteins. II. Interaction of RuvB with DNA.Q54652795
Branch migration of Holliday junctions promoted by the Escherichia coli RuvA and RuvB proteins. I. Comparison of RuvAB- and RuvB-mediated reactions.Q54652800
ATP-dependent branch migration of Holliday junctions promoted by the RuvA and RuvB proteins of E. coli.Q54677225
Physical properties of the Escherichia coli transcription termination factor rho. 2. Quaternary structure of the rho hexamer.Q54684599
Characterization of the helicase activity of the Escherichia coli UvrAB protein complex.Q54734902
Escherichia coli DNA helicase I catalyzes a unidirectional and highly processive unwinding reaction.Q54751630
Formation of a RuvAB-Holliday Junction Complex in VitroQ58028630
ATP-dependent assembly of double hexamers of SV40 T antigen at the viral origin of DNA replicationQ59098660
P433issue16
P407language of work or nameEnglishQ1860
P921main subjectEscherichia coliQ25419
P304page(s)7618-7622
P577publication date1994-08-01
P1433published inProceedings of the National Academy of Sciences of the United States of AmericaQ1146531
P1476titleThe Escherichia coli RuvB branch migration protein forms double hexameric rings around DNA
P478volume91