Recognition and cleavage of DNA by type-II restriction endonucleases. - Wikidata - awgldk - TriplyDB

Recognition and cleavage of DNA by type-II restriction endonucleases.

Recognition and cleavage of DNA by type-II restriction endonucleases.

http://www.wikidata.org/entity/Q34431350

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Homing endonucleases: keeping the house in order Nucleoside triphosphate-dependent restriction enzymes Structure and function of type II restriction endonucleases Characterization of BseMII, a new type IV restriction-modification system, which recognizes the pentanucleotide sequence 5'-CTCAG(N)(10/8)/Metal ion-mediated substrate-assisted catalysis in type II restriction endonucleases Substrate-assisted catalysis: molecular basis and biological significance Topology of Type II REases revisited; structural classes and the common conserved core Exonuclease III protection assay with FRET probe for detecting DNA-binding proteins On the DNA cleavage mechanism of Type I restriction enzymes Crystal structure of NaeI--an evolutionary bridge between DNA endonuclease and topoisomerase Metal ions and phosphate binding in the H-N-H motif: Crystal structures of the nuclease domain of ColE7/Im7 in complex with a phosphate ion and different divalent metal ions Allosteric Regulation of DNA Cleavage and Sequence-Specificity through Run-On Oligomerization How is modification of the DNA substrate recognized by the PvuII restriction endonuclease?Recognition of flanking DNA sequences by EcoRV endonuclease involves alternative patterns of water-mediated contacts The role of metals in catalysis by the restriction endonuclease BamHI Mutational analyses of restriction endonuclease-HindIII mutant E86K with higher activity and altered specificity Mutations of acidic residues in RAG1 define the active site of the V(D)J recombinase Homing endonucleases: structural and functional insight into the catalysts of intron/intein mobility Unusual evolutionary history of the tRNA splicing endonuclease EndA: relationship to the LAGLIDADG and PD-(D/E)XK deoxyribonucleases Protein stability indicates divergent evolution of PD-(D/E)XK type II restriction endonucleases.An integrated model of transcription factor diffusion shows the importance of intersegmental transfer and quaternary protein structure for target site finding.Use of plasmon coupling to reveal the dynamics of DNA bending and cleavage by single EcoRV restriction enzymes.FARE, a new family of foldback transposons in Arabidopsis.Mutational analysis of the MutH protein from Escherichia coli.Specificity changes in the evolution of type II restriction endonucleases: a biochemical and bioinformatic analysis of restriction enzymes that recognize unrelated sequences.A genetic dissection of the LlaJI restriction cassette reveals insights on a novel bacteriophage resistance system A rapid and efficient method for cloning genes of type II restriction-modification systems by use of a killer plasmid.Type II restriction endonuclease R.Eco29kI is a member of the GIY-YIG nuclease superfamily.Interfacial water as a "hydration fingerprint" in the noncognate complex of BamHI.Phasevarions mediate random switching of gene expression in pathogenic Neisseria.The zinc ion in the HNH motif of the endonuclease domain of colicin E7 is not required for DNA binding but is essential for DNA hydrolysis.Recognition of native DNA methylation by the PvuII restriction endonuclease.Type II restriction endonucleases--a historical perspective and more Boosting the prediction and understanding of DNA-binding domains from sequence Binding of SeqA protein to DNA requires interaction between two or more complexes bound to separate hemimethylated GATC sequences.Imaging DNA loops induced by restriction endonuclease EcoRII. A single amino acid substitution uncouples target recognition from cooperative DNA interaction and cleavage.The structural basis of damaged DNA recognition and endonucleolytic cleavage for very short patch repair endonuclease.Diffusion of MMPs on the surface of collagen fibrils: the mobile cell surface-collagen substratum interface.Energetic and structural considerations for the mechanism of protein sliding along DNA in the nonspecific BamHI-DNA complex.Differences between EcoRI nonspecific and "star" sequence complexes revealed by osmotic stress.

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Recognition and cleavage of DNA by type-II restriction endonucleases.

http://www.wikidata.org/entity/Q34431350

description

1997 nî lūn-bûn

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1997 թուականի Մայիսին հրատարակուած գիտական յօդուած

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1997 թվականի մայիսին հրատարակված գիտական հոդված

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1997年の論文

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1997年論文

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1997年論文

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1997年論文

@zh-hk

1997年論文

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1997年論文

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1997年论文

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name

Recognition and cleavage of DNA by type-II restriction endonucleases.

@ast

Recognition and cleavage of DNA by type-II restriction endonucleases.

@en

Recognition and cleavage of DNA by type-II restriction endonucleases.

@nl

type

label

Recognition and cleavage of DNA by type-II restriction endonucleases.

@ast

Recognition and cleavage of DNA by type-II restriction endonucleases.

@en

Recognition and cleavage of DNA by type-II restriction endonucleases.

@nl

prefLabel

Recognition and cleavage of DNA by type-II restriction endonucleases.

@ast

Recognition and cleavage of DNA by type-II restriction endonucleases.

@en

Recognition and cleavage of DNA by type-II restriction endonucleases.

@nl

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Recognition and cleavage of DNA by type-II restriction endonucleases.

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A Pingoud

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P2860

BaeI, another unusual BcgI-like restriction endonuclease

Crystal structure of trp repressor/operator complex at atomic resolution

Crystal structure of Citrobacter freundii restriction endonuclease Cfr10I at 2.15 A resolution

Crystallographic identification of metal-binding sites in Escherichia coli inorganic pyrophosphatase

Specificity of restriction endonucleases and DNA modification methyltransferases a review (Edition 3)

Molecular recognition mediated by bound water. A mechanism for star activity of the restriction endonuclease EcoRI

Metal ion catalysis in the Tetrahymena ribozyme reaction

Direct atomic force microscope imaging of EcoRI endonuclease site specifically bound to plasmid DNA molecules

On the catalytic mechanism of EcoRI and EcoRV. A detailed proposal based on biochemical results, structural data and molecular modelling.

Combinatorial mutagenesis of three major groove-contacting residues of EcoRI: single and double amino acid replacements retaining methyltransferase-sensitive activities.

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