Zobrazeno 1 - 10
of 21
pro vyhledávání: '"R. L. Sabina"'
Autor:
R. Boulieu, A. Lenoir, J. F. Mornex, C. Bohman, J. Balzarini, P. Wigerinck, A. Aerschot, P. Herdewijn, Erik Clercq, S. Brosh, E. Zoref-Shani, O. Sperling, E. Danziger, Y. Sidi, Y. Bromberg, Renate Burgemeister, Elke Rötzer, Wolf Gutensohn, G. P. Connolly, P. J. Harrison, R. B. Diasio, Z. Lu, R. Zhang, U. Gresser, W. Gutensohn, R. Resta, L. F. Thompson, F. Javaux, M. F. Vincent, G. Berghe, I. Kamilli, R. Rauch, D. Hahn, C. W. Keuzenkamp-Jansen, R. A. Abreu, J. P. M. Bökkerink, M. A. H. Heijden, M. Löffler, C. Becker, E. Wegerie, M. Marcussen, K. Overgaard-Hansen, H. Klenow, A. M. Marinaki, E. H. Harley, M. B. McBride, H. A. Simmonds, F. Moro, J. S. Cameron, C. S. Ogg, D. G. Williams, S. Rigden, G. Haycock, M. E. Miranda, J. G. Puig, F. A. Mateos, J. O. Vázquez, V. W. T. Ruiz Haperen, G. Veerman, J. B. Vermorken, G. J. Peters, C. L. Wilt, P. Noordhuis, K. Smid, H. M. Pinedo, C. Salerno, A. Lomonte, O. Giardini, C. Crifo, R. T. Smolenski, M. H. Yacoub, A. M. -L. Seymour, A. P. A. Stegmann, M. W. Honders, R. Willemze, J. E. Landegent, E. H. Stet, G. M. Vogels-Mentink, L. H. J. Lambooy, J. M. F. Trijbels, R. J. Torres, M. G. Tozzi, R. Pesi, M. Turriani, S. Allegrini, M. Camici, P. L. Ipata, A. A. Berg, J. R. Meinsma, H. Lenthe, A. H. Gennip, A. B. P. Kuilenburg, N. G. G. M. Abeling, H. D. Bakker, R. J. Slingerland, F. Bergh, R. L. Sabina
Publikováno v:
Pharmacy World & Science. 15:F7-F14
Publikováno v:
Molecular and Cellular Biology. 10:5271-5278
AMP deaminase (AMPD) is a central enzyme in eucaryotic energy metabolism, and tissue-specific as well as stage-specific isoforms are found in many vertebrates. This study demonstrates the AMPD1 gene product in rat is alternatively spliced. The second
Publikováno v:
Journal of Biological Chemistry. 265:11474-11481
From a population of wild type S49 cells, a clone, DTB6, was isolated in a single step from selective medium containing thymidine and dibutyryl cyclic AMP that exhibited a 60% deficiency in AMP deaminase (AMP-D) activity. The AMP-D deficiency conferr
Autor:
R L, Sabina
Publikováno v:
Neurologic clinics. 18(1)
Myoadenylate deaminase deficiency is a clinically heterogeneous metabolic disorder that is commonly diagnosed in a variety of neurologic settings. Although the molecular basis for this purine nucleotide catabolic derangement may typically be attribut
Publikováno v:
The American journal of physiology. 270(1 Pt 1)
Dietary supplementation of the creatine analogue beta-guanidinopropionic acid (beta-GPA) decreases in vitro skeletal muscle AMP deaminase (AMP-D) activity in rats. Downregulation of AMP-D activity was progressive and greater in fast-twitch muscles (7
Publikováno v:
The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society. 42(7)
The three major isoforms of AMP-deaminase (AMPda) were localized in human skeletal muscle and cultured muscle cells by immunocytochemistry. The M isoform was mainly located in Type II muscle fibers and showed a clear cross-striation. Particularly str
Publikováno v:
The Journal of biological chemistry. 267(31)
Human AMPD2 cDNA clones have been isolated from T-lymphoblast and placental lambda gt11 libraries utilizing a previously cloned rat partial AMPD2 cDNA as the probe. Alignment analysis of all cDNA clones indicates the presence of intervening sequences
Autor:
D K, Mahnke-Zizelman, R L, Sabina
Publikováno v:
The Journal of biological chemistry. 267(29)
Higher eukaryotes express multiple isoforms of AMP deaminase (EC 3.5.4.6). In humans, four AMP deaminase variants, termed M (muscle), L (liver), E1, and E2 (erythrocyte) can be distinguished by a variety of biochemical and immunological criteria. Pre
Publikováno v:
The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society. 40(7)
The cellular distribution of AMP deaminase (AMPda) isozymes was documented for rat soleus and plantaris muscles, utilizing immunofluorescence microscopy and immunoprecipitation methods. AMPda is a ubiquitous enzyme existing as three distinct isozymes
Publikováno v:
Advances in experimental medicine and biology.