Christoph W. Turck
Max Planck Society
260 Papers
4K Citations
Christoph W. Turck is an academic researcher from Max Planck Society. The author has contributed to research in topics: Proteome & Biology. The author has an hindex of 67, co-authored 247 publications. Previous affiliations of Christoph W. Turck include University of California, Los Angeles & University of California, San Francisco.
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Papers
Identification and Cloning of Centaurin-α A NOVEL PHOSPHATIDYLINOSITOL 3,4,5-TRISPHOSPHATE-BINDING PROTEIN FROM RAT BRAIN
Latanya Hammonds-Odie,T R Jackson,Adam A. Profit,Ira J. Blader,Christoph W. Turck,Glenn D. Prestwich,Anne B. Theibert +6 more
TL;DR: Given the specificity of binding and enrichment in brain, centaurin-α is a candidate PtdInsP3 receptor that may link the activation of phosphoinositide 3-kinase to downstream responses in the brain.
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•Journal Article
Membrane Ig cross-linking regulates phosphatidylinositol 3-kinase in B lymphocytes.
TL;DR: In this paper, it was shown that mIg cross-linking also regulates PtdIns 3-kinase, an enzyme that phosphorylates inositol phospholipids and plays a key role in mediating the effects of tyrosine kinases on growth control in fibroblasts.
137
Purification, identification, and characterization of an osmotic response element binding protein.
TL;DR: The osmotic response element binding protein (OREBP) is a transcription factor of approximately 200 kDa in size, characterized by a Rel-like DNA binding domain and a glutamine-rich transactivation domain that significantly diminished hyperosmotic AR gene induction.
136
Mechanisms of Thrombin Receptor Agonist Specificity CHIMERIC RECEPTORS AND COMPLEMENTARY MUTATIONS IDENTIFY AN AGONIST RECOGNITION SITE
Tania Nanevicz,Maki Ishii,Ling Wang,Mian Chen,Ji Chen,Christoph W. Turck,Fred E. Cohen,Shaun R. Coughlin +7 more
TL;DR: Two independent approaches, chimeric receptors and arginine scanning for complementary mutations, identified the Glu region and to a lesser degree Phe as important determinants of agonist specificity.
134
Characterization of growth factor-induced serine phosphorylation of tumor necrosis factor-α converting enzyme and of an alternatively translated polypeptide
TL;DR: In this article, the authors showed that the cytoplasmic domain of tumor necrosis factor-alpha converting enzyme (TACE) is phosphorylated in response to growth factor stimulation only on serine and not on threonine or tyrosine.
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