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Structure of Ocr from bacteriophage T7, a protein that mimics B-form DNA
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title
Structure of Ocr from bacteriophage T7, a protein that mimics B-form DNA
(English)
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main subject
protein structure
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bacteriophage
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based on heuristic
inferred from title
author
Malcolm Walkinshaw
series ordinal
1
object named as
M D Walkinshaw
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author name string
P Taylor
series ordinal
2
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S S Sturrock
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3
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C Atanasiu
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4
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T Berge
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5
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R M Henderson
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6
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J M Edwardson
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7
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D T F Dryden
series ordinal
8
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publication date
January 2002
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published in
Molecular Cell
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volume
9
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page(s)
187-94
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issue
1
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cites work
Characterisation of the structure of ocr, the gene 0.3 protein of bacteriophage T7.
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Inhibition of the type I restriction-modification enzymes EcoB and EcoK by the gene 0.3 protein of bacteriophage T7
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A motif conserved among the type I restriction-modification enzymes and antirestriction proteins: a possible basis for mechanism of action of plasmid-encoded antirestriction functions
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Translocation-independent dimerization of the EcoKI endonuclease visualized by atomic force microscopy
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Shape of Ocr, the gene 0.3 protein of bacteriophage T7: modeling based on light scattering experiments.
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Deoxyribonucleic acid restriction and modification systems in Salmonella: chromosomally located systems of different serotypes
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Solvent-accessible surfaces of proteins and nucleic acids
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Structure of a B-DNA dodecamer: conformation and dynamics
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Direct observation of DNA translocation and cleavage by the EcoKI endonuclease using atomic force microscopy
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EcoA and EcoE: alternatives to the EcoK family of type I restriction and modification systems of Escherichia coli.
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The alternate expression of two restriction and modification systems
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R124, an fi+ R Factor of a New Compatibility Class
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Dali/FSSP classification of three-dimensional protein folds
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Complementation analysis of temperature-sensitive host specificity mutations in Escherichia coli
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The DNA recognition subunit of the type IB restriction-modification enzyme EcoAI tolerates circular permutions of its polypeptide chain
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Analysis of the subunit assembly of the typeIC restriction-modification enzyme EcoR124I
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Protein-protein interactions: a review of protein dimer structures
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MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures
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Active protection by bacteriophages T3 and T7 againstE. coli B-and K-specific restriction of their DNA
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DNA methylation of bacterial viruses T3 and T7 by different DNA methylases in Escherichia coli K12 cells
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Regulation of endonuclease activity by proteolysis prevents breakage of unmodified bacterial chromosomes by type I restriction enzymes
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Protein-protein and protein-DNA interactions in the type I restriction endonuclease R.EcoR124I.
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Type I restriction systems: sophisticated molecular machines (a legacy of Bertani and Weigle)
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The DNA binding characteristics of the trimeric EcoKI methyltransferase and its partially assembled dimeric form determined by fluorescence polarisation and DNA footprinting
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Sequence-specific DNA binding by EcoKI, a type IA DNA restriction enzyme
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Protein mimicry of DNA from crystal structures of the uracil-DNA glycosylase inhibitor protein and its complex with Escherichia coli uracil-DNA glycosylase
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Solution structure of DinI provides insight into its mode of RecA inactivation
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Scanning force microscopy of DNA deposited onto mica: equilibration versus kinetic trapping studied by statistical polymer chain analysis.
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A novel bacteriophage defence mechanism: the anti-restriction protein
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Gene 0.3 of bacteriophage T7 acts to overcome the DNA restriction system of the host
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Genetic and physical mapping in the early region of bacteriophage T7 DNA
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Crystallization and preliminary X-ray analysis of ocr, the product of gene 0.3 of bacteriophage T7
1 reference
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Crossref
reference URL
https://api.crossref.org/works/10.1016%2FS1097-2765%2802%2900435-5
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EcoA: the first member of a new family of type I restriction modification systems. Gene organization and enzymatic activities
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A third family of allelic hsd genes in Salmonella enterica: sequence comparisons with related proteins identify conserved regions implicated in restriction of DNA.
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Families of restriction enzymes: an analysis prompted by molecular and genetic data for type ID restriction and modification systems
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DNA bending by photolyase in specific and non-specific complexes studied by atomic force microscopy.
1 reference
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A model for the abrogation of the SOS response by an SOS protein: a negatively charged helix in DinI mimics DNA in its interaction with RecA.
1 reference
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1 reference
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Crossref
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Identifiers
DOI
10.1016/S1097-2765(02)00435-5
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
2224967
OpenCitations bibliographic resource ID
2224967
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
2224967
PubMed ID
11804597
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
2224967
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