scispace - formally typeset
S

Shuang Yong Xu

Researcher at New England Biolabs

Publications -  10
Citations -  918

Shuang Yong Xu is an academic researcher from New England Biolabs. The author has contributed to research in topics: Restriction enzyme & DNA. The author has an hindex of 8, co-authored 10 publications receiving 846 citations. Previous affiliations of Shuang Yong Xu include Icahn School of Medicine at Mount Sinai.

Papers
More filters
Journal ArticleDOI

A nomenclature for restriction enzymes, DNA methyltransferases, homing endonucleases and their genes

Richard J. Roberts, +46 more
TL;DR: In this article, a nomenclature for restriction endonucleases, DNA methyltransferases, homing endon nucleases and related genes and gene products is described.
Journal ArticleDOI

Structural basis of asymmetric DNA methylation and ATP-triggered long-range diffusion by EcoP15I

TL;DR: The structure of a Type III R–M system, consisting of the entire EcoP15I complex (Mod2Res1) bound to DNA, is reported, which suggests how ATP hydrolysis is coupled to long-range diffusion of a helicase on DNA, and how a dimeric methyltransferase functions to methylate only one of the two DNA strands.
Journal ArticleDOI

Cloning of CviPII nicking and modification system from chlorella virus NYs-1 and application of Nt.CviPII in random DNA amplification

TL;DR: The cloning and expression of the CviPII DNA nicking and modification system encoded by chlorella virus NYs-1 is described and can be used to generate single-stranded DNAs for isothermal strand-displacement amplification.
Journal ArticleDOI

Natural zinc ribbon HNH endonucleases and engineered zinc finger nicking endonuclease

TL;DR: The identification of a large pool of previously unknown natural NEases and engineered NEases provides more ‘tools’ for DNA manipulation and molecular diagnostics and the small modular HNH nicking domain can be used to generate rare NEases applicable to targeted genome editing.
Journal ArticleDOI

Structure Determination and Biochemical Characterization of a Putative HNH Endonuclease from Geobacter metallireducens GS-15

TL;DR: The crystal structure of a putative HNH endonuclease, Gmet_0936 protein from Geobacter metallireducens GS-15, has been determined at 2.6 Å resolution using single-wavelength anomalous dispersion method, and shows a weak DNA binding activity in a DNA mobility shift assay and a weak Mn2+-dependent nicking activity on supercoiled plasmids in low pH buffers.