Zobrazeno 1 - 10
of 12
pro vyhledávání: '"B J, Lamphear"'
Publikováno v:
Journal of Biological Chemistry. 269:9445-9452
Factor VIIIa is inactivated by both factor IXa and activated protein C. The latter protease rapidly attacked a site at Arg562 (A2 subunit), whereas both proteases slowly cleaved factor VIIIa at Arg336 (A1 subunit). Cofactor inactivation catalyzed by
Autor:
B J Lamphear, Philip J. Fay
Publikováno v:
Journal of Biological Chemistry. 267:3725-3730
Heterotrimeric factor VIIIa was reconstituted from isolated A2 subunit and A1/A3-C1-C2 dimer of thrombin-activated human factor VIII in a reaction that was sensitive to pH. Maximal levels of reconstituted factor VIIIa at pH 6.0 were as much as 20-fol
Autor:
B J Lamphear, R Panniers
Publikováno v:
Journal of Biological Chemistry. 265:5333-5336
Cell-free protein-synthesizing systems derived from Ehrlich ascites tumor cells that have been exposed to elevated temperatures retain the inhibition of translation that is seen at the cellular level. A multisubunit cap binding protein complex able t
Autor:
M. Holcik, M Jr Gale, S. A. Chappell, J. Hershey, B. He, N. Standart, Robert J. Schneider, N. Nakashima, Jing Chen, J. Pelletier, T. Rouault, D. R. Morris, O. Donzé, J. B. Harford, L. E. Maquat, A. A.M. Thomas, F. Bayard, T. Skern, S. Miyamoto, T. Hohn, A. Siddiqui, Ian Mohr, S. M. Tahara, D. R. Cavener, L. S. Jefferson, R. Andino, Y. Groner, S. Lemon, S. R. Kimball, E. G. Moss, E. Goldman, W. Sossin, B. Joshi, A. Dasgupta, B. J. Lamphear, K. Igarashi, G. Sullivan Read, V. P. Mauro, R. J. Kaufman, Daniel R. Schoenberg, N. Sonenberg, M. Hatzoglou, J. D. Richter, Leslie A. Schiff, R. E. Lloyd, R. M. Krug, P. Hershey, G. Witherell, C. U.T. Hellen, G. C. Scheper, A. C. Prats, V. I. Agol, W. Filipowicz, A. Palmenberg, R. E. Rhoads, M. Kiledjian, J. L.E. Darlix, L. Gehrke, V. Racaniello, P. J. Farabaugh, R. Rivera-Pomar, M. W. Hentze, M. Wormington, O. Elroy-Stein, M. B. Mathews, M. G. Katze, B. L. Semler, T. Pe'ery, N. T. Parkin, A. Sachs, A. Kimchi, Raymond Kaempfer, S. Peltz, R. Jagus, E. V. Pilipenko, C. P. Hunter, K. Kirkegaard, M. Kozak, R. Duncan, A. E. Koromilas, R. Jackson, Encarnación Martínez-Salas, E. Wimmer, T. V. Pestova, V. Kruys, J. Wilusz, P. Sarnow, J. J. Toulmé
Three interesting ideas about the initiation of translation in eukaryotes have recently emerged in the literature. One is the possibility that internal initiation of translation might occur not only with viral but also with some cellular mRNAs. The s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b3ece8c041f3a06cd631e6d435c8bd8c
https://europepmc.org/articles/PMC86772/
https://europepmc.org/articles/PMC86772/
Publikováno v:
The Journal of biological chemistry. 270(37)
Cap-dependent binding of mRNA to the 40 S ribosomal subunit during translational initiation requires the association of eukaryotic initiation factor 4G (eIF4G; formerly eIF-4 gamma and p220) with other initiation factors, notably eIF4E, eIF4A, and eI
Autor:
B. J. Lamphear, R. E. Rhoads
Publikováno v:
Current Topics in Microbiology and Immunology ISBN: 9783642796654
An early concept in the development of the field of translational control was that mRNAs differ in their intrinsic efficiencies of binding to ribosomes (Lodish 1976). Dozens of examples of mRNAs have now been described for which differences in effici
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f17c587c6de10f7f1bb454475677f41b
https://doi.org/10.1007/978-3-642-79663-0_7
https://doi.org/10.1007/978-3-642-79663-0_7
Autor:
R E, Rhoads, B J, Lamphear
Publikováno v:
Current topics in microbiology and immunology. 203
Autor:
Dieter Blaas, Regina Kirchweger, Sommergruber W, C Hohenadl, F Sobrino, B J Lamphear, Hans-Dieter Liebig, E Ziegler, R E Rhoads, D Waters
Publikováno v:
Journal of virology. 68(9)
Many picornaviruses cause a dramatic decrease in the translation of cellular mRNAs in the infected cell, without affecting the translation of their own RNA. Specific proteolysis of protein synthesis initiation factor eIF-4 gamma occurs during infecti
Publikováno v:
The Journal of biological chemistry. 269(13)
Factor VIIIa is inactivated by both factor IXa and activated protein C. The latter protease rapidly attacked a site at Arg562 (A2 subunit), whereas both proteases slowly cleaved factor VIIIa at Arg336 (A1 subunit). Cofactor inactivation catalyzed by
Autor:
B J, Lamphear, P J, Fay
Publikováno v:
The Journal of biological chemistry. 267(6)
Heterotrimeric factor VIIIa was reconstituted from isolated A2 subunit and A1/A3-C1-C2 dimer of thrombin-activated human factor VIII in a reaction that was sensitive to pH. Maximal levels of reconstituted factor VIIIa at pH 6.0 were as much as 20-fol