J
Joachim E. Schultz
Researcher at University of Tübingen
Publications - 159
Citations - 7153
Joachim E. Schultz is an academic researcher from University of Tübingen. The author has contributed to research in topics: Adenylyl cyclase & Cyclase. The author has an hindex of 47, co-authored 156 publications receiving 6882 citations. Previous affiliations of Joachim E. Schultz include Weizmann Institute of Science & National Institutes of Health.
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Journal ArticleDOI
Identification of the carbohydrate receptor for Shiga toxin produced by Shigella dysenteriae type 1.
Alf A. Lindberg,J E Brown,Nicklas Strömberg,M Westling-Ryd,Joachim E. Schultz,Karl-Anders Karlsson +5 more
TL;DR: Glycolipid-bound, bilayer-close galabiose is proposed as the functional receptor for membrane penetration of the toxin, while galabioses bound in glycoproteins affords binding sites but is not able to mediate penetration.
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The HAMP Domain Structure Implies Helix Rotation in Transmembrane Signaling
Michael Hulko,Franziska Berndt,Markus Gruber,Jürgen U. Linder,Vincent Truffault,Anita Schultz,Jörg Martin,Joachim E. Schultz,Andrei N. Lupas,Murray Coles +9 more
TL;DR: The solution structure of an archaeal HAMP domain shows a homodimeric, four-helical, parallel coiled coil with unusual interhelical packing, related to the canonical packing by rotation of the helices, which suggests a model for the mechanism of signal transduction.
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Point mutations in the aromatic/arginine region in aquaporin 1 allow passage of urea, glycerol, ammonia, and protons
TL;DR: It is shown that ammonia passes through all four AQP1 mutants, and that the exquisite electrostatic proton barrier in AQPs comprises both the NPA constriction as well as the ar/R constriction.
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The class III adenylyl cyclases: multi-purpose signalling modules.
TL;DR: Inspection of amino acid sequence profiles suggests a division of the class III adenylyl cyclases in to four subclasses, class IIIa-IIId, suggesting a plasticity of the catalytic mechanisms.
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A single, bi-functional aquaglyceroporin in blood-stage Plasmodium falciparum malaria parasites.
TL;DR: PfAQP is expressed in blood-stage parasites throughout the development from rings via trophozoites to schizonts and is localized to the parasite but not to the erythrocyte cytoplasm or membrane, and efficiently provides access to the serum glycerol pool for the use in ATP generation and primarily in the phospholipid synthesis.