Zobrazeno 1 - 10
of 36
pro vyhledávání: '"Jürgen U. Linder"'
Autor:
Jürgen U. Linder
Publikováno v:
Molecular and Cellular Biochemistry. 334:215-219
Production of cGMP in bacteria has been studied since the early 1970s. From the beginning on it proved to be a challenging topic. In Escherichia coli the cGMP levels were two orders of magnitude lower than the corresponding cAMP levels. Furthermore,
Publikováno v:
FEBS Journal. 274:1514-1523
The C-terminal catalytic domains of the 11 mammalian phosphodiesterase families (PDEs) are important drug targets. Five of the 11 PDE families contain less well-characterized N-terminal GAF domains. cGMP is the ligand for the GAF domains in PDEs 2, 5
Autor:
Markus Gruber, Michael Hulko, Joachim E. Schultz, Franziska Berndt, Jürgen U. Linder, Anita Schultz, Andrei N. Lupas, Vincent Truffault, Jörg Martin, Murray Coles
Publikováno v:
Cell. 126(5):929-940
SummaryHAMP domains connect extracellular sensory with intracellular signaling domains in over 7500 proteins, including histidine kinases, adenylyl cyclases, chemotaxis receptors, and phosphatases. The solution structure of an archaeal HAMP domain sh
Autor:
Joachim E. Schultz, Anita Schultz, Peter Sander, Jürgen U. Linder, Ying Lan Guo, Stefan Ehlers, Christine Keller, Dorothea Dittrich, Ursula Kurz
Publikováno v:
Molecular Microbiology. 57:667-677
The adenylyl cyclase Rv1625c from Mycobacterium tuberculosis codes for a protein with six transmembrane spans and a catalytic domain, i.e. it corresponds to one half of the pseudoheterodimeric mammalian adenylyl cyclases (ACs). Rv1625c is active as a
Publikováno v:
FEBS Journal. 272:3085-3092
Class III adenylyl cyclases usually possess six highly conserved catalytic residues. Deviations in these canonical amino acids are observed in several putative adenylyl cyclase genes as apparent in several bacterial genomes. This suggests that a vari
Autor:
Ivo Tews, Jürgen U. Linder, Anita Schultz, Joachim E. Schultz, Irmgard Sinning, Felix Findeisen
Publikováno v:
Science. 308:1020-1023
Class III adenylyl cyclases contain catalytic and regulatory domains, yet structural insight into their interactions is missing. We show that the mycobacterial adenylyl cyclase Rv1264 is rendered a pH sensor by its N-terminal domain. In the structure
Publikováno v:
The EMBO Journal. 24:663-673
Rv1900c, a Mycobacterium tuberculosis adenylyl cyclase, is composed of an N-terminal alpha/beta-hydrolase domain and a C-terminal cyclase homology domain. It has an unusual 7% guanylyl cyclase side-activity. A canonical substrate-defining lysine and
Autor:
Jost H. Weber, Jürgen U. Linder, Anita Schultz, Andrey E. Vishnyakov, Kristina Hambach, Joachim E. Schultz
Publikováno v:
Cellular Signalling. 16:115-125
In Paramecium, cAMP formation is stimulated by a potassium conductance, which is an intrinsic property of the adenylyl cyclase. We cloned a full-length cDNA and several gDNA fragments from Paramecium and Tetrahymena coding for adenylyl cyclases with
Publikováno v:
The EMBO Journal. 20:3667-3675
The gene Rv1625c from Mycobacterium tuberculosis encodes a membrane-anchored adenylyl cyclase corresponding to exactly one-half of a mammalian adenylyl cyclase. An engineered, soluble form of Rv1625c was expressed in Escherichia coli. It formed a hom
Publikováno v:
European Journal of Biochemistry. 268:105-110
The nine membrane-bound mammalian adenylyl cyclases (ACs) contain two highly diverged membrane anchors, M1 and M2, with six transmembrane spans each and two conserved cytosolic domains which coalesce into a pseudoheterodimeric catalytic unit. Previou