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Molecular and Cellular Endocrinology|January 25, 2012
C-peptide induces human renal mesangial cell proliferation in vitro, activating Src-kinase, PI-3 kinase and ERK1/2Dusica Vasic, Andreas Spyrantis, Renate Durst, et al.Human Nature (Hawthorne, N.Y.)|October 8, 2014
Impartial institutions, pathogen stress and the expanding social networkDaniel Hruschka, Charles Efferson, Ting Jiang, et al.The Journal of Biological Chemistry|August 5, 2006
The iron-sulfur cluster-free hydrogenase (Hmd) is a metalloenzyme with a novel iron binding motifMalgorzata Korbas, Sonja Vogt, Wolfram Meyer-Klaucke, et al.Journal of Molecular Biology|March 17, 2006
The crystal structure of the apoenzyme of the iron-sulphur cluster-free hydrogenaseOliver Pilak, Björn Mamat, Sonja Vogt, et al.Dalton Transactions (Cambridge, England : 2003)|March 12, 2010
The iron-site structure of [Fe]-hydrogenase and model systems: an X-ray absorption near edge spectroscopy studyMarco Salomone-Stagni, Francesco Stellato, C Matthew Whaley, et al.Science (New York, N.Y.)|July 26, 2008
The crystal structure of [Fe]-hydrogenase reveals the geometry of the active siteSeigo Shima, Oliver Pilak, Sonja Vogt, et al.Psychological Science in the Public Interest : a Journal of the American Psychological Society|October 13, 2022
Scaling Up Change: A Critical Review and Practical Guide to Harnessing Social Norms for Climate ActionSara M Constantino, Gregg Sparkman, Gordon T Kraft-Todd, et al.FEBS Letters|January 24, 2009
The crystal structure of C176A mutated [Fe]-hydrogenase suggests an acyl-iron ligation in the active site iron complexTakeshi Hiromoto, Kenichi Ataka, Oliver Pilak, et al.Inorganic Chemistry|April 15, 2008
Characterization of the Fe site in iron-sulfur cluster-free hydrogenase (Hmd) and of a model compound via nuclear resonance vibrational spectroscopy (NRVS)Yisong Guo, Hongxin Wang, Yuming Xiao, et al.Pageof 4