Zobrazeno 1 - 10
of 51
pro vyhledávání: '"Ronald Adamik"'
Autor:
Philip Ian Padilla, Joel Moss, Martha Vaughan, Gustavo Pacheco-Rodriguez, Ronald Adamik, Min-ju Chang
Publikováno v:
Proceedings of the National Academy of Sciences. 100:2322-2327
BIG1 and BIG2 are brefeldin A-inhibited guanine nucleotide-exchange proteins that activate ADP-ribosylation factors (ARFs), critical components of vesicular trafficking pathways. These proteins can exist in macromolecular complexes and move between G
Autor:
Victor J. Ferrans, Joel Moss, Kazuyo Takeda, Sei-Chang Kim, Akira Togawa, Martha Kirby, Martha Vaughan, Ronald Adamik, Masahito Ogasawara
Publikováno v:
Journal of Biological Chemistry. 275:3221-3230
Activation of ADP-ribosylation factors (ARFs), approximately 20-kDa GTPases that are inactive in the GDP-bound form, depends on guanine nucleotide-exchange proteins (GEPs) to accelerate GTP binding. A novel ARF GEP, designated cytohesin-4, was cloned
Publikováno v:
Journal of Biological Chemistry. 274:17417-17423
A brefeldin A (BFA)-inhibited guanine nucleotide-exchange protein (GEP) for ADP-ribosylation factors (ARF) was purified earlier from bovine brain cytosol. Cloning and expression of the cDNA confirmed that the recombinant protein (p200) is a BFA-sensi
Autor:
Hiroyuki Kanoh, Su-Chen Tsai, Jin-Xin Hong, Joel Moss, Martha Vaughan, John H. Exton, Ronald Adamik
Publikováno v:
Journal of Biological Chemistry. 273:20697-20701
Arfaptin 1, a approximately 39-kDa protein based on the deduced amino acid sequence, had been initially identified in a yeast two-hybrid screen using dominant active ARF3 (Q71L) as bait with an HL-60 cDNA library. It was suggested that arfaptin 1 may
Publikováno v:
Journal of Biological Chemistry. 271:24005-24009
ADP-ribosylation factors (ARFs) are ∼20-kDa guanine nucleotide-binding proteins that participate in vesicular transport in the Golgi and other intracellular compartments and stimulate cholera toxin ADP-ribosyltransferase activity. Both GTP binding
Publikováno v:
Proceedings of the National Academy of Sciences. 93:305-309
ADP-ribosylation factors (ARFs) are 20-kDa guanine nucleotide-binding proteins and are active in the GTP-bound state and inactive with GDP bound. ARF-GTP has a critical role in vesicular transport in several cellular compartments. Conversion of ARF-G
Publikováno v:
Proceedings of the National Academy of Sciences. 91:3063-3066
ADP-ribosylation factors (ARFs) are approximately 20-kDa guanine nucleotide-binding proteins that participate in vesicular transport in the Golgi and other intracellular compartments and stimulate cholera toxin ADP-ribosyltransferase activity. ARFs a
Publikováno v:
Biochemistry. 32:561-566
The effects of cholera toxin, a secretory product of Vibrio cholerae, result from ADP-ribosylation of the stimulatory guanine nucleotide-binding (Gs) protein of the adenylyl cyclase system. Cholera toxin A subunit (CTA) also uses agmatine, a simple g
Publikováno v:
Proceedings of the National Academy of Sciences. 89:9272-9276
Six mammalian ADP-ribosylation factors (ARFs) identified by cDNA cloning were expressed as recombinant proteins (rARFs) that stimulated cholera toxin ADP-ribosyltransferase activity. Microsequencing of soluble ARFs I and II (sARFs I and II), purified
Publikováno v:
Journal of Biological Chemistry. 266:8213-8219
Cholera toxin exerts its effects on cells in large part through the ADP-ribosylation of guanine nucleotide-binding proteins. Toxin-catalyzed ADP-ribosylation is enhanced by approximately 20-kDa guanine nucleotide-binding proteins termed ADP-ribosylat