Weixin Tang

CylA is a sequence-specific protease involved in toxin biosynthesis.
CylA is a sequence-specific protease involved in toxin biosynthesis. J Ind Microbiol Biotechnol. 2019 Mar; 46(3-4):537-549.
PMID: 30484123

Evolved Cas9 variants with broad PAM compatibility and high DNA specificity.
Evolved Cas9 variants with broad PAM compatibility and high DNA specificity. Nature. 2018 04 05; 556(7699):57-63.
PMID: 29512652

Rewritable multi-event analog recording in bacterial and mammalian cells.
Rewritable multi-event analog recording in bacterial and mammalian cells. Science. 2018 Apr 13; 360(6385).
PMID: 29449507

Aptazyme-embedded guide RNAs enable ligand-responsive genome editing and transcriptional activation.
Aptazyme-embedded guide RNAs enable ligand-responsive genome editing and transcriptional activation. Nat Commun. 2017 Jun 28; 8:15939.
PMID: 28656978

The Enterococcal Cytolysin Synthetase Coevolves with Substrate for Stereoselective Lanthionine Synthesis.
The Enterococcal Cytolysin Synthetase Coevolves with Substrate for Stereoselective Lanthionine Synthesis. ACS Chem Biol. 2016 09 16; 11(9):2438-46.
PMID: 27348535

Applications of the class II lanthipeptide protease LicP for sequence-specific, traceless peptide bond cleavage.
Applications of the class II lanthipeptide protease LicP for sequence-specific, traceless peptide bond cleavage. Chem Sci. 2015 Nov 01; 6(11):6270-6279.
PMID: 30090246

The enterococcal cytolysin synthetase has an unanticipated lipid kinase fold.
The enterococcal cytolysin synthetase has an unanticipated lipid kinase fold. Elife. 2015 Jul 30; 4.
PMID: 26226635

Substrate control in stereoselective lanthionine biosynthesis.
Substrate control in stereoselective lanthionine biosynthesis. Nat Chem. 2015 Jan; 7(1):57-64.
PMID: 25515891

The sequence of the enterococcal cytolysin imparts unusual lanthionine stereochemistry.
The sequence of the enterococcal cytolysin imparts unusual lanthionine stereochemistry. Nat Chem Biol. 2013 Mar; 9(3):157-9.
PMID: 23314913

Structural characterization of four prochlorosins: a novel class of lantipeptides produced by planktonic marine cyanobacteria.
Structural characterization of four prochlorosins: a novel class of lantipeptides produced by planktonic marine cyanobacteria. Biochemistry. 2012 May 29; 51(21):4271-9.
PMID: 22574919

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