Zobrazeno 1 - 10
of 173
pro vyhledávání: '"Joachim E Schultz"'
Publikováno v:
eLife, Vol 5 (2016)
Adenylate cyclases convert intra- and extracellular stimuli into a second messenger cAMP signal. Many bacterial and most eukaryotic ACs possess membrane anchors with six transmembrane spans. We replaced the anchor of the AC Rv1625c by the quorum-sens
Externí odkaz:
https://doaj.org/article/02eadf442ac946158275d0613548e9b6
Autor:
Joachim E. Schultz
Publikováno v:
Frontiers in Pharmacology, Vol 13 (2022)
The nine membrane-delimited eukaryotic adenylyl cyclases are pseudoheterodimers with an identical domain order of seven (nine) distinct subdomains. Bioinformatics show that the protein evolved from a monomeric bacterial progenitor by gene duplication
Externí odkaz:
https://doaj.org/article/a30b2eb36df04ff299eb310de5bd1a70
Publikováno v:
Cellular Signalling. 103:110568
Acidic lipid extracts from mouse liver, kidney, heart, brain, and lung inhibited human pseudoheterodimeric adenylyl cyclases (hACs) expressed in HEK293 cells. Using an acidic lipid extract from bovine lung, a combined MS- and bioassay-guided fraction
Autor:
Anubha Seth, Marius Landau, Andrej Shevchenko, Sofia Traikov, Anita Schultz, Sherif Elsabbagh, Joachim E. Schultz
Nine mammalian adenylyl cyclases (AC) are pseudoheterodimers with two hexahelical membrane domains which are isoform-specifically conserved. Previously we proposed that these membrane domains are orphan receptors (10.7554/eLife.13098; 10.1016/j.cells
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2577d2e252cadf8dfca668f7790c82d0
https://doi.org/10.1101/2022.02.23.481604
https://doi.org/10.1101/2022.02.23.481604
Autor:
Anita Schultz, Stephanie Beltz, Jens Bassler, Andrei N. Lupas, Joachim E. Schultz, Miriam Ziegler
Publikováno v:
The FEBS Journal. 284:1204-1217
Adenylate cyclases (ACs) are signaling proteins that produce the second messenger cAMP. Class III ACs comprise four groups (class IIIa-d) of which class IIIa and IIIb ACs have been identified in bacteria and eukaryotes. Many class IIIa ACs are anchor
Autor:
Joachim E. Schultz, Thorsten Friedrich, Gottfried Unden, Juliane Wissig, Jens Bassler, Heike Bähre, Christopher Schubert, Julia Grischin
Publikováno v:
Molecular microbiology. 112(1)
The nucleotide cyclase CyaC of Sinorhizobium meliloti is a member of class III adenylate cyclases (AC), a diverse group present in all forms of life. CyaC is membrane-integral by a hexahelical membrane domain (6TM) with the basic topology of mammalia
Publikováno v:
International journal of medical microbiology : IJMM. 309(3-4)
Nine pseudoheterodimeric mammalian adenylate cyclases possess two dissimilar hexahelical membrane domains (TM1 and TM2), two dissimilar cyclase-transducing-elements (CTEs) and two complementary catalytic domains forming a catalytic dimer (often terme
Publikováno v:
Cellular Signalling. 68:109538
Nine mammalian adenylate cyclase (mAC) isoforms are pseudoheterodimers with two dissimilar hexahelical membrane-anchors, isoform-specifically conserved for more than half a billion years. In the past, we have postulated a receptor function for these
Publikováno v:
Cellular signalling. 46
Class III adenylate cyclases (ACs) are widespread signaling proteins, which translate diverse intracellular and extracellular stimuli into a uniform intracellular signal. They are typically composed of an N-terminal array of input domains and transdu