W. Waas

发表

Purification of a model substrate for transcription factor phosphorylation by ERK2.

K. Dalby, W. Waas, 2001, Protein expression and purification.

Adenosine inhibits exocytotic release of endogenous noradrenaline in rat heart: a protective mechanism in early myocardial ischemia.

A. Schömig, W. Waas, G. Richardt, 1987, Circulation research.

Chemiluminescent determination of adenosine, inosine, and hypoxanthine/xanthine.

W. Waas, H. Kather, E. Wieland, 1987, Analytical biochemistry.

Interaction between the release of adenosine and noradrenaline during sympathetic stimulation: a feed-back mechanism in rat heart.

A. Schömig, M. Lohse, W. Waas, 1989, Journal of molecular and cellular cardiology.

The Kinetic Mechanism of the Dual Phosphorylation of the ATF2 Transcription Factor by p38 MAP kinase a : Implications for Signal/Response profiles of MAP Kinase pathways.

K. Dalby, W. Waas, H. Lo, 2000 .

The kinetic mechanism of the serine-threonine specific protein kinase ERK2

K. Dalby, W. Waas, A. Szafranska, 2003 .

The expression and purification of the N-terminal activation domain of the transcription factor c-Myc: a model substrate for exploring ERK2 docking interactions.

K. Dalby, W. Waas, 2007, Protein expression and purification.

Discovery of a Gene Family Critical to Wyosine Base Formation in a Subset of Phenylalanine-specific Transfer RNAs*

V. de Crécy-Lagard, P. Schimmel, W. Waas, 2005, Journal of Biological Chemistry.

Role of a tRNA Base Modification and Its Precursors in Frameshifting in Eukaryotes*

P. Schimmel, W. Waas, Z. Druzina, 2007, Journal of Biological Chemistry.

Artificially ambiguous genetic code confers growth yield advantage.

P. Marlière, D. Metzgar, V. de Crécy-Lagard, 2004, Proceedings of the National Academy of Sciences of the United States of America.

Crystal Structure of a Human Peptidyl-tRNA Hydrolase Reveals a New Fold and Suggests Basis for a Bifunctional Activity*

E. Ruoslahti, J. M. de Pereda, W. Waas, 2004, Journal of Biological Chemistry.

A universal plate format for increased throughput of assays that monitor multiple aminoacyl transfer RNA synthetase activities.

P. Schimmel, W. Waas, K. Beebe, 2007, Analytical biochemistry.

A universal plate format for increased throughput of assays that monitor multiple aminoacyl-tRNA synthetase activities

W. Waas, K. Beebe, P. Schimmel, 2013 .

A kinetic approach towards understanding substrate interactions and the catalytic mechanism of the serine/threonine protein kinase ERK2: identifying a potential regulatory role for divalent magnesium.

K. Dalby, W. Waas, A. Szafranska, 2004, Biochimica et biophysica acta.

The Kinetic Mechanism of the Dual Phosphorylation of the ATF2 Transcription Factor by p38 Mitogen-activated Protein (MAP) Kinase α

Kevin N. Dalby, K. Dalby, W. Waas, 2001, The Journal of Biological Chemistry.

Transient Protein-Protein Interactions and a Random-ordered Kinetic Mechanism for the Phosphorylation of a Transcription Factor by Extracellular-regulated Protein Kinase 2*

K. Dalby, W. Waas, 2002, The Journal of Biological Chemistry.

Physiological concentrations of divalent magnesium ion activate the serine/threonine specific protein kinase ERK2.

K. Dalby, W. Waas, 2003, Biochemistry.

Phosphorylation of the transcription factor Ets-1 by ERK2: rapid dissociation of ADP and phospho-Ets-1.

Pengyu Y. Ren, K. Dalby, W. Waas, 2010, Biochemistry.

Two rate-limiting steps in the kinetic mechanism of the serine/threonine specific protein kinase ERK2: a case of fast phosphorylation followed by fast product release.

K. Dalby, W. Waas, A. Szafranska, 2003, Biochemistry.

Evidence that tRNA synthetase-directed proton transfer stops mistranslation.

P. Schimmel, W. Waas, 2007, Biochemistry.

Genetic Code Ambiguity Confers a Selective Advantage on Acinetobacter baylyi

D. Metzgar, V. de Crécy-Lagard, P. Schimmel, 2007, Journal of bacteriology.