Publications related to Directed evolution of O6-alkylguanine-DNA alkyltransferase for applications in protein labeling

Labeling of fusion proteins with small molecular in vivo

Kai Johnsson, Alexandre Juillerat, Thomas Gronemeyer, Antje Keppler

A general method for covalent labeling of fusion proteins in vivo that complements the existing methods for protein labeling in vivo and in vitro is presented. This new method might lead to new ways of studying and manipulating proteins in living cells. Co ...

Wiley2004

Scope and limitations of the double [4+3]-cycloadditions of 2-oxyallyl cations to 2,2 '-methylenedifuran and derivatives

Pierre Vogel, Marc-Etienne Schwenter, Kai Torsten Meilert

The reactivity of various 2-oxyallyl cations toward 2,2'-methylenedifuran (1b), 2,2'-(hydroxymethyl)difuran (1c), 2,2'-(trimethylsilylmethylene)difuran (1d), and di(2-furyl)methanone (1e) has been explored. Difuryl derivatives 1c, 1d, and le refused to und ...

2003

Metabolism of atrazine and derivatives in vetiver plants

Jean-Paul Schwitzguebel, Sylvie Vullioud-Marcacci

Metabolism of atrazine and derivatives in vetiver plants ...

2003

Directed Evolution of O6-Alkylguanine-DNA Alkyltransferase for Efficient Labeling of Fusion Proteins with Small Molecules In Vivo

Horst Vogel, Kai Johnsson, Horst Pick, Alexandre Juillerat, Thomas Gronemeyer, Antje Keppler

We report here the generation of mutants of the human O6-alkylguanine-DNA alkyltransferase (hAGT) for the efficient in vivo labeling of fusion proteins with synthetic reporter mols. Libraries of hAGT were displayed on phage, and mutants capable of efficien ...

2003

Asymmetric synthesis of 1-aminopentadecane-3,5,7,9,11,13,15-heptols and of 1,15-diaminopentadecane-3,5,7,9,11,13-hexols and derivatives

Pierre Vogel, Sandrine Gerber

Starting from 2,2'-methylenedifuran, enantiomerically enriched (98%) (3R,5S,7R,9S,11R,13R)- and (3R,5S,7S,9R,11R,13R)-15-amino-5,7,9,11-tetrahydroxy-3,13-bis(4-methoxyb enzoyloxy)pentadec-1-yl) pivalate were prepared as well as (3R,5R,7R,9R,11S,13S)-1,15-d ...

2002

$ l _{ p } $ -Multiresolution Analysis: How to Reduce Ringing and Sparsify the Error

Michaël Unser, Thierry Blu

We propose to design the reduction operator of an image pyramid so as to minimize the approximation error in the

l _{ p }

-sense (not restricted to the usual p=2), where p can take non-integer values. The underlying image model is specified using shift- ...

IEEE2002

Derivatives of (2R,3R,4S)-2-Aminomethylpyrrolidine-3,4-diol are Selective alpha-Mannosidase Inhibitors

Pierre Vogel, Sandrine Gerber, Inmaculada Robina, Eliazar Rodriguez Garcia, Raynald Demange

A collection of (2R,3R,4S)-3,4-dihydroxypyrrolidin-2-yl derivatives have been tested for their inhibitory activities toward 25 glycosidases. Competitive (K-i=7.4 VM) and selective inhibition of alpha -mannosidase from jack bean has been found for (2R,3R,4S ...

2001

Changing the substrate specificity of cytochrome c peroxidase using directed evolution

Kai Johnsson, Petra Tafelmeyer

Cytochrome c peroxidase (I) from Saccharomyces cerevisiae was subjected to directed mol. evolution to generate mutants with increased activity against ABTS [2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)]. Using a combination of DNA shuffling and s ...

2001

Evolutionary approaches to study cytochrome c peroxidase

Kai Johnsson, Petra Tafelmeyer

A review with 15 refs. Directed mol. evolution of enzymes and proteins has emerged as an extremely powerful method to create proteins with novel properties, both for practical applications as well as for mechanistic studies. To demonstrate the underlying p ...

2001

Directed molecular evolution of cytochrome c peroxidase

Kai Johnsson, Petra Tafelmeyer

Cytochrome c peroxidase (CCP) from Saccharomyces cerevisiae was subjected to directed mol. evolution to generate mutants with increased activity against the classical peroxidase substrate, guaiacol, thus changing the substrate specificity of CCP from the p ...

2000

Directed evolution of O6-alkylguanine-DNA alkyltransferase for applications in protein labeling

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Labeling of fusion proteins with small molecular in vivo

Scope and limitations of the double [4+3]-cycloadditions of 2-oxyallyl cations to 2,2 '-methylenedifuran and derivatives

Metabolism of atrazine and derivatives in vetiver plants

Directed Evolution of O6-Alkylguanine-DNA Alkyltransferase for Efficient Labeling of Fusion Proteins with Small Molecules In Vivo

Asymmetric synthesis of 1-aminopentadecane-3,5,7,9,11,13,15-heptols and of 1,15-diaminopentadecane-3,5,7,9,11,13-hexols and derivatives

$ l _{ p } $ -Multiresolution Analysis: How to Reduce Ringing and Sparsify the Error

Derivatives of (2R,3R,4S)-2-Aminomethylpyrrolidine-3,4-diol are Selective alpha-Mannosidase Inhibitors

Changing the substrate specificity of cytochrome c peroxidase using directed evolution

Evolutionary approaches to study cytochrome c peroxidase

Directed molecular evolution of cytochrome c peroxidase

Metabolism of atrazine and derivatives in vetiver plants

$ l _{ p } $ -Multiresolution Analysis: How to Reduce Ringing and Sparsify the Error

Directed molecular evolution of cytochrome c peroxidase

Labeling of fusion proteins with small molecular in vivo

Asymmetric synthesis of 1-aminopentadecane-3,5,7,9,11,13,15-heptols and of 1,15-diaminopentadecane-3,5,7,9,11,13-hexols and derivatives

Scope and limitations of the double [4+3]-cycloadditions of 2-oxyallyl cations to 2,2 '-methylenedifuran and derivatives

Directed Evolution of O6-Alkylguanine-DNA Alkyltransferase for Efficient Labeling of Fusion Proteins with Small Molecules In Vivo

Derivatives of (2R,3R,4S)-2-Aminomethylpyrrolidine-3,4-diol are Selective alpha-Mannosidase Inhibitors

Evolutionary approaches to study cytochrome c peroxidase

Changing the substrate specificity of cytochrome c peroxidase using directed evolution