The N-terminus of IntDOT forms hydrophobic interactions during Holliday Junction resolution.

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The N-terminus of IntDOT forms hydrophobic interactions during Holliday Junction resolution.

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2016 nî lūn-bûn

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2016年の論文

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2016年論文

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2016年論文

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2016年論文

@zh-hk

2016年論文

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2016年論文

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2016年论文

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2016年论文

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2016年论文

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The N-terminus of IntDOT forms ...... Holliday Junction resolution.

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The N-terminus of IntDOT forms ...... Holliday Junction resolution.

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The N-terminus of IntDOT forms ...... Holliday Junction resolution.

@en

The N-terminus of IntDOT forms ...... Holliday Junction resolution.

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The N-terminus of IntDOT forms ...... Holliday Junction resolution.

@en

The N-terminus of IntDOT forms ...... Holliday Junction resolution.

@nl

P1476

The N-terminus of IntDOT forms ...... Holliday Junction resolution.

@en

P2093

Adam J Kolakowski

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Jeffrey F Gardner

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P2860

Human intestinal bacteria as reservoirs for antibiotic resistance genes

Structure-function analysis of IntDOT.

Homology-dependent interactions determine the order of strand exchange by IntDOT recombinase.

Evidence for extensive resistance gene transfer among Bacteroides spp. and among Bacteroides and other genera in the human colon.

Development of an in vitro integration assay for the Bacteroides conjugative transposon CTnDOT.

JPred4: a protein secondary structure prediction server.

The Bacteroides thetaiotaomicron protein Bacteroides host factor A participates in integration of the integrative conjugative element CTnDOT into the chromosome.

Mutations in the amino-terminal domain of lambda-integrase have differential effects on integrative and excisive recombination.

A structural basis for allosteric control of DNA recombination by lambda integrase.

P304

10-16

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P31

scholarly article

P356

10.1016/J.PLASMID.2016.07.003

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P478

87-88

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P577

2016-07-12T00:00:00Z

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P698

27422335

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P921

hydrophobicity

P932

5121019

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