Results 31 to 40 of about 23,918 (199)

Anthrax edema factor toxicity is strongly mediated by the N-end rule. [PDF]

PLoS ONE, 2013
Anthrax edema factor (EF) is a calmodulin-dependent adenylate cyclase that converts adenosine triphosphate (ATP) into 3'-5'-cyclic adenosine monophosphate (cAMP), contributing to the establishment of Bacillus anthracis infections and the resulting ...
Clinton E Leysath, Damilola D Phillips, Devorah Crown, Rasem J Fattah, Mahtab Moayeri, Stephen H Leppla   +5 more
doaj   +1 more source

Differential regulation of actin-activated nucleotidyl cyclase virulence factors by filamentous and globular actin. [PDF]

PLoS ONE, 2018
Several bacterial pathogens produce nucleotidyl cyclase toxins to manipulate eukaryotic host cells. Inside host cells they are activated by endogenous cofactors to produce high levels of cyclic nucleotides (cNMPs).
Dorothée Raoux-Barbot, Alexander Belyy, Lina Worpenberg, Sabrina Montluc, Celia Deville, Véronique Henriot, Christophe Velours, Daniel Ladant, Louis Renault, Undine Mechold   +9 more
doaj   +1 more source

Bacillus anthracis edema factor substrate specificity: evidence for new modes of action [PDF]

, 2012
Since the isolation of Bacillus anthracis exotoxins in the 1960s, the detrimental activity of edema factor (EF) was considered as adenylyl cyclase activity only.
Agrawal, Altaweel, Basler, Bauche, Bell, Benson, Beste, Bock, Bond, Boyd, Bradley, Brown, Burhenne, Carbonetti, Carbonetti, Carson-Walter, Casteel, Christensen, Christensen, Confer, Copsel, Crawford, Crowe, Cunningham, Dalkas, Defer, Deuquet, Ding, Drum, Duesbery, Feld, Firoved, Friedlander, Fu, Fukuhara, Gaion, Gille, Gordon, Göttle, Hammerschmidt, He, Helfman, Hong, Ivarsson, Jernigan, Johnson, Katayama, Katayama, Kaupp, Kintzer, Klimpel, Laine, Larabee, Larabee, Leppla, Liu, Martin Göttle, McDonough, Milne, Mogridge, Mogridge, Newton, Newton, Newton, Newton, Newton, Oncu, O´Brien, Park, Petosa, Pezard, Postea, Puhar, Roland Seifert, Santelli, Scobie, Scobie, Scorpio, Shapiro, Shen, Shirshev, Soelaiman, Stefan Dove, Sun, Tamayo, Taylor, Taylor, Tesmer, Thomas, Tournier, Vitale, Vitale, Vojtova, Yeager, Zong   +94 more
core   +2 more sources

Hemolytic activity of adenylate cyclase toxin fromBordetella pertussis [PDF]

FEBS Letters, 1991
Adenylate cyclase (AC) toxin fromB. pertussis enters eukaryotic cells where it produces supraphysiologie levels of cAMP. Purification of AC toxin activity [(1989) J. Biol. Chem. 264, 19279] results in increasing potency of hemolytic activity and electroelution of the 216‐kDA holotoxin yields a single protein with AC enzymatic, toxin and hemolytic ...
Ehrmann, Ingrid E., Gray, Mary C., Gordon, Valery M., Gray, Lloyd S., Hewlett, Erik L.   +4 more
openaire   +2 more sources

Bordetella Dermonecrotic Toxin Is a Neurotropic Virulence Factor That Uses Ca_V3.1 as the Cell Surface Receptor

mBio, 2020
Dermonecrotic toxin (DNT) is one of the representative toxins produced by Bordetella pertussis, but its role in pertussis, B. pertussis infection, remains unknown.
Shihono Teruya, Yukihiro Hiramatsu, Keiji Nakamura, Aya Fukui-Miyazaki, Kentaro Tsukamoto, Noriko Shinoda, Daisuke Motooka, Shota Nakamura, Keisuke Ishigaki, Naoaki Shinzawa, Takashi Nishida, Fuminori Sugihara, Yusuke Maeda, Yasuhiko Horiguchi   +13 more
doaj   +1 more source

Primary cilia elongation in response to interleukin-1 mediates the inflammatory response [PDF]

, 2012
Primary cilia are singular, cytoskeletal organelles present in the majority of mammalian cell types where they function as coordinating centres for mechanotransduction, Wnt and hedgehog signalling. The length of the primary cilium is proposed to modulate
A. K. T. Wann, AC Lin, AJ Espanol, AM Malone, BD Engel, BK Yoder, CA Dinarello, CG Jensen, CM Asleson, D Qian, DA Lee, E Verghese, E Verghese, EJ Michaud, EM Mokrzan, GJ Pazour, H Tukachinsky, I Memon, J Kim, JA Deane, JL Rosenbaum, JM Neugebauer, K Gardner, KJ Palmer, L Schneider, M Barzi, M Cao, M. M. Knight, MA Lancaster, MB Hovater, N Sharma, P Tummala, PA Lefebvre, PV Tran, RY Kwon, S Abdul-Majeed, S Agarwal, S Kim, S Massinen, S Mukhopadhyay, S Pritchard, S Toffoli, SC Goetz, SM Nauli, SR McGlashan, SR McGlashan, SR McGlashan, TT Chowdhury, TY Besschetnova, Y Chen, Y Ou, YH Choi   +51 more
core   +2 more sources

Cell Propagation of Cholera Toxin CTA ADP-Ribosylating Factor by Exosome Mediated Transfer [PDF]

, 2018
In this study, we report how the cholera toxin (CT) A subunit (CTA), the enzyme moiety responsible for signaling alteration in host cells, enters the exosomal pathway, secretes extracellularly, transmits itself to a cell population.
Boussadia, Zaira, Carollo, Maria, Fabbri, Alessia, Falchi, Mario, Fecchi, Katia, Fiani, Maria Luisa, Gallina, Angelo, Palermo, Angela, Parisi, Sofia, Pasquini, Luca, Sargiacomo, Massimo, Zanetti, Cristiana   +11 more
core   +1 more source

Reconstitution of cholera toxin-activated adenylate cyclase. [PDF]

Proceedings of the National Academy of Sciences, 1978
Reconstitution of adenylate cyclase activity responsive to stimulation by guanylyl-5'imidodiphosphate or NaF may be achieved by mixing dilute Lubrol 12A9-solubilized extracts of wild-type S49 membranes with membranes of an adenylate cyclase-deficient variant.
G L, Johnson, H R, Kaslow, H R, Bourne
openaire   +2 more sources

Are guanine nucleotide binding proteins a distinct class of regulatory proteins? [PDF]

, 1983
Proteins which bind guanine nucleotides are found in a diverse set of key regulatory positions. They are involved in hormone action, visual transduction, protein synthesis and microtubule assembly. In addition to their ability to bind guanine nucleotides
Kleinzeller, Cassel, Martin, Pfeuffer, Hanski, Northup, Northup, Rodbell, Cooper, Houslay, Manning, Johnson, Bokoch, Zahniser, Stryer, Kuhn, Fung, Baehr, Hurley, Hughes, Yamazaki, Abood, Bitensky, Kawamura, Kawamura, Emeis, Swarup, Maitra, Schreier, Safer, Safer, Fakunding, Brot, Hachmann, Uchida, Collier, Montanaro, Beaudet, Laursen, Velenzuela, Spiegelman, Carlier, Zackroff, Weisenberg, Heyworth, Heyworth, Goodhardt, Shih, Capon, Willingham   +49 more
core   +1 more source

Homologous and unique G protein alpha subunits in the nematode Caenorhabditis elegans [PDF]

, 1991
A cDNA corresponding to a known G protein alpha subunit, the alpha subunit of Go (Go alpha), was isolated and sequenced. The predicted amino acid sequence of C. elegans Go alpha is 80-87% identical to other Go alpha sequences.
Lochrie, Michael A., Mendel, Jane E., Simon, Melvin I., Sternberg, Paul W.   +3 more
core   +1 more source