Site-specific DNA transesterification catalyzed by a restriction enzyme. - Wikidata - awgldk - TriplyDB

Site-specific DNA transesterification catalyzed by a restriction enzyme.

Site-specific DNA transesterification catalyzed by a restriction enzyme.

http://www.wikidata.org/entity/Q35616738

about

Expression and purification of BmrI restriction endonuclease and its N-terminal cleavage domain variants The other face of restriction: modification-dependent enzymes Hpy188I-DNA pre- and post-cleavage complexes--snapshots of the GIY-YIG nuclease mediated catalysis Template-directed addition of nucleosides to DNA by the BfiI restriction enzyme The DNA binding and 3'-end preferential activity of human tyrosyl-DNA phosphodiesterase.Type II restriction endonucleases--a historical perspective and more Natural and engineered nicking endonucleases--from cleavage mechanism to engineering of strand-specificity Restriction-modification system with methyl-inhibited base excision and abasic-site cleavage activities Enzymatic mechanism of human apurinic/apyrimidinic endonuclease against a THF AP site model substrate.Nucleases: diversity of structure, function and mechanism.Highlights of the DNA cutters: a short history of the restriction enzymes A novel mechanism for the scission of double-stranded DNA: BfiI cuts both 3'-5' and 5'-3' strands by rotating a single active site A switch in the mechanism of communication between the two DNA-binding sites in the SfiI restriction endonuclease.The monomeric GIY-YIG homing endonuclease I-BmoI uses a molecular anchor and a flexible tether to sequentially nick DNA.Automated solid-phase synthesis of RNA oligonucleotides containing a nonbridging phosphorodithioate linkage via phosphorothioamidites.Tetrameric restriction enzymes: expansion to the GIY-YIG nuclease family.Entirely enzymatic nanofabrication of DNA-protein conjugates.Dispersed phantom scatterer technique reveals subtle differences in substrate recognition by phospholipase D inactive mutants.

P2860

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P2860

Site-specific DNA transesterification catalyzed by a restriction enzyme.

http://www.wikidata.org/entity/Q35616738

description

2007 nî lūn-bûn

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2007年の論文

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2007年論文

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2007年論文

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2007年論文

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2007年論文

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2007年論文

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2007年论文

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2007年论文

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2007年论文

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name

Site-specific DNA transesterification catalyzed by a restriction enzyme.

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Site-specific DNA transesterification catalyzed by a restriction enzyme.

@en

type

label

Site-specific DNA transesterification catalyzed by a restriction enzyme.

@ast

Site-specific DNA transesterification catalyzed by a restriction enzyme.

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prefLabel

Site-specific DNA transesterification catalyzed by a restriction enzyme.

@ast

Site-specific DNA transesterification catalyzed by a restriction enzyme.

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P1433

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P356

PNAS.0608689104

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

Site-specific DNA transesterification catalyzed by a restriction enzyme.

@en

P2093

Bernard A Connolly

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

Giedrius Sasnauskas

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

Stephen E Halford

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

Virginijus Siksnys

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

P2860

Enzyme-Catalyzed Phosphoryl Transfer Reactions

Structure of the metal-independent restriction enzyme BfiI reveals fusion of a specific DNA-binding domain with a nonspecific nuclease

The tyrosyl-DNA phosphodiesterase Tdp1 is a member of the phospholipase D superfamily

A novel family of phospholipase D homologues that includes phospholipid synthases and putative endonucleases: identification of duplicated repeats and potential active site residues

Crystal structure of a phospholipase D family member

Two-metal active site binding of a Tn5 transposase synaptic complex

Structural principles for the inhibition of the 3'-5' exonuclease activity of Escherichia coli DNA polymerase I by phosphorothioates

A new method for determining the stereochemistry of DNA cleavage reactions: application to the SfiI and HpaII restriction endonucleases and to the MuA transposase.

The PLD superfamily: insights into catalysis.

Human Tdp1 cleaves a broad spectrum of substrates, including phosphoamide linkages.

P304

2115-2120

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scholarly article

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10.1073/PNAS.0608689104

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7

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104

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1785359

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