Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Ursula Kurz"'
Publikováno v:
Cellular Signalling. 24:1479-1484
Human phosphodiesterase 1 is regulated by a tandem of N-terminal calmodulin/Ca(2+)-binding domains. We grafted the tandems from hPDE1A3 and -B1 onto the cyanobacterial adenylyl cyclase CyaB1 thus replacing an intrinsic tandem GAF-domain. Cyclase acti
Autor:
Markus O. Zimmermann, Ursula Kurz, Joachim E. Schultz, Ana Banjac, Frank M. Boeckler, Anita Schultz
Publikováno v:
Cellular Signalling. 24:629-634
The dimeric mammalian phosphodiesterases (PDEs) are regulated by N-terminal domains. In PDE5, the GAF-A subdomain of a GAF-tandem (GAF-A and -B) binds the activator cGMP and in PDE10 GAF-B binds cAMP. GAF-tandem chimeras of PDE5 and 10 in which the 3
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:
The FEBS journal. 281(14)
Available structures of HAMP domains suggest rotation as one potential mechanism in intraprotein signal transduction. It has been proposed that in poly-HAMP modules the signal sign is inverted with each additional HAMP. We examined signal transductio
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:
Journal of Biological Chemistry. 275:11235-11240
Paramecium has a 280-kDa guanylyl cyclase. The N terminus resembles a P-type ATPase, and the C terminus is a guanylyl cyclase with the membrane topology of canonical mammalian adenylyl cyclases, yet with the cytosolic loops, C1 and C2, inverted compa
Autor:
Klaus Schilling, Ying Lan Guo, Joachim E. Schultz, B Wiederanders, Ursula Kurz, Chin Chia Lim
Publikováno v:
FEBS Letters. 469:203-207
Proregions of papain-like cysteine proteases are potent and often highly selective inhibitors of their parental enzymes. The molecular basis of their selectivity is poorly understood. For two closely related members of the cathepsin L-like subfamily
Autor:
Günther Jung, Ursula Kurz, Susanne Klumpp, H. Völkel, Joachim E. Schultz, Jürgen Under, Volker Gnau
Publikováno v:
European Journal of Biochemistry. 238:198-206
The ciliate Paramecium tetraurelia secretes large amounts of a cysteine protease into the growth medium, presumably for extracellular food digestion. Two endoprotease isozymes (30 and 33 kDa on SDS/PAGE, respectively), both present in cell homogenate
Autor:
Ying Lan, Guo, Ursula, Kurz, Anita, Schultz, Jürgen U, Linder, Dorothea, Dittrich, Christine, Keller, Stefan, Ehlers, Peter, Sander, Joachim E, Schultz
Publikováno v:
Molecular microbiology. 57(3)
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