TY  - JOUR
A1  - Lang, R.
A1  - Herzog, C.
A1  - Stangl, R.
A1  - Brunn, E.
A1  - Braun, M.
A1  - Christl, Manfred
A1  - Peters, K.
A1  - Peters, E.-M.
A1  - Schnering, H. G. von
T1  - Reaktionen von Homobenzvalenen mit 4-Phenyl-3H-1,2,4-triazol-3,5(4H)-dion, Tetracyanethylen, Chlorsulfonylisocyanat und Schwefeldioxid. Einige konzertierte 1,4-Additionen an eine Vinylcyclopropan-Einheit
T1  - Reactions of Homobenzvalenes wlth 4-Phenyl-3H-1,2,4-trlazole-3,5(4H)-dione, Tetracyanoethylene, Chlorosulfonyl  Isocyanate, and Sulfur Dioxide. Several Concerted 1,4-Additions to a Vinylcyclopropane Subunit
N2  - No abstract available
KW  - Organische Chemie
KW  - 6-Thiatricyclo[3.2.1.o 2.7 ]oct-3-ene 6
KW  - 6-dioxide
KW  - Homo Diels-Alder reactions
KW  - Cyclopropanetetracarbonitrile derivatives
KW  - Barbaralane derivatives
KW  - Urazoles
KW  - polycyclic
Y1  - 1990
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-58527
ER  - 
TY  - JOUR
A1  - Gimpl, G.
A1  - Gerstberger, R.
A1  - Mauss, U.
A1  - Klotz, Karl-Norbert
A1  - Lang, R. E.
T1  - Solubilization and characterization of active neuropeptide-Y receptors from rabbit kidney
N2  - Active neuropeptide Y receptors were solubilized from rabbit kidney membranes using the zwitterionic detergent 3-[ (3-cholamidopropy l)dimethylammonio ]- 1-propanesulfonic acid (CHAPS). In membrane fragmentsandsoluble extracts neuropeptide Y bindingwas time dependent, saturable, reversible, and of high affinity. Scatchard analysis of equilibrium binding data indicated a single class of binding sites with respective Kn and Bmax values of 0.09 nM and 530 fmol/mg of protein for the membrane-bound receptors and 0.10 nM and 1585 fmol/mg of protein for the soluble receptors. Neuropeptide Y bindingwas specifically inhibited by the nonhydrolyzable GTP analog guanosine 5' -0- (3-thiotripbosphate) in a concentration-dependent manner, with IC\(_{50}\) values of 28 and 0.14 \(\mu\)M for membrane- bound and soluble receptors, respectively, suggesting that neuropeptide Y receptors are functionally coupled to GTP-binding regulatory proteins. CrossHoking studies were performed with the heterobifunctional N-hydroxysuccinimidyl-4-azidobenzoate and the monofunctional neuropeptide Y derivative, azidobenzoyl and led to the identification of a 100 kDa peptide that should represent the covalently labeled neuropeptide Y receptor.
KW  - Toxikologie
Y1  - 1990
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-60375
ER  - 
TY  - JOUR
A1  - Schwan, Carsten
A1  - Lang, Alexander E.
A1  - Schlosser, Andreas
A1  - Fujita-Becker, Setsuko
A1  - AlHaj, Abdulatif
A1  - Schröder, Rasmus R.
A1  - Faix, Jan
A1  - Aktories, Klaus
A1  - Mannherz, Hans Georg
T1  - Inhibition of Arp2/3 complex after ADP-ribosylation of Arp2 by binary Clostridioides toxins
JF  - Cells
N2  - Clostridioides bacteria are responsible for life threatening infections. Here, we show that in addition to actin, the binary toxins CDT, C2I, and Iota from Clostridioides difficile, botulinum, and perfrigens, respectively, ADP-ribosylate the actin-related protein Arp2 of Arp2/3 complex and its additional components ArpC1, ArpC2, and ArpC4/5. The Arp2/3 complex is composed of seven subunits and stimulates the formation of branched actin filament networks. This activity is inhibited after ADP-ribosylation of Arp2. Translocation of the ADP-ribosyltransferase component of CDT toxin into human colon carcinoma Caco2 cells led to ADP-ribosylation of cellular Arp2 and actin followed by a collapse of the lamellipodial extensions and F-actin network. Exposure of isolated mouse colon pieces to CDT toxin induced the dissolution of the enterocytes leading to luminal aggregation of cellular debris and the collapse of the mucosal organization. Thus, we identify the Arp2/3 complex as hitherto unknown target of clostridial ADP-ribosyltransferases.
KW  - actin
KW  - ADP-ribosyltransferases
KW  - Arp2/3 complex
KW  - Clostridioides binary toxins
Y1  - 2022
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-297454
SN  - 2073-4409
VL  - 11
IS  - 22
ER  -