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Molecular & Cellular Proteomics : MCP|November 23, 2013
Quantitative phosphoproteomics reveals the role of protein arginine phosphorylation in the bacterial stress responseAndreas Schmidt, Débora Broch Trentini, Silvia Spiess, et al.
Journal of Molecular Biology|August 8, 2009
Structural basis of substrate specificity of plant 12-oxophytodienoate reductasesConstanze Breithaupt, Robert Kurzbauer, Florian Schaller, et al.
Nature Plants|November 29, 2017
The crystal structure of Deg9 reveals a novel octameric-type HtrA proteaseMin Ouyang, Xiaoyi Li, Shun Zhao, et al.
Nature|November 4, 2016
Arginine phosphorylation marks proteins for degradation by a Clp proteaseDébora Broch Trentini, Marcin Józef Suskiewicz, Alexander Heuck, et al.
Nature Structural & Molecular Biology|February 8, 2011
Substrate-induced remodeling of the active site regulates human HTRA1 activityLinda Truebestein, Annette Tennstaedt, Timon Mönig, et al.
Molecular Biosystems|August 12, 2009
Peptidic small molecule activators of the stress sensor DegSPatrick Hauske, Nicolette Mamant, Sonja Hasenbein, et al.
Proceedings of the National Academy of Sciences of the United States of America|September 20, 2006
Crystal structure of 12-oxophytodienoate reductase 3 from tomato: self-inhibition by dimerizationConstanze Breithaupt, Robert Kurzbauer, Hauke Lilie, et al.
Science (New York, N.Y.)|June 6, 2009
McsB is a protein arginine kinase that phosphorylates and inhibits the heat-shock regulator CtsRJakob Fuhrmann, Andreas Schmidt, Silvia Spiess, et al.
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