Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Anne L. Frattali"'
Autor:
Jeffrey E. Pessin, Anne L. Frattali
Publikováno v:
Journal of Biological Chemistry. 268:7393-7400
Insulin receptor beta subunit autophosphorylation occurs in an intramolecular trans-reaction in which one beta subunit phosphorylates the adjacent beta subunit within an alpha 2 beta 2 holoreceptor complex (Frattali, A. L., Treadway, J. L., and Pessi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3e489849280b5cc2a96d3397c42d4ff2
https://doi.org/10.1016/s0021-9258(18)53187-2
https://doi.org/10.1016/s0021-9258(18)53187-2
Publikováno v:
Biochemistry. 31:11801-11805
We have previously demonstrated that isolated insulin and IGF-1 alpha beta half-receptors can be reconstituted into a functional alpha 2 beta 2 hybrid receptor complex [Treadway et al. (1989) J. Biol. Chem. 264, 21450-21453]. In the present study, we
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::47253499583b4c5b34e0c9669d37e4d8
https://doi.org/10.1021/bi00162a018
https://doi.org/10.1021/bi00162a018
Publikováno v:
Journal of Biological Chemistry. 267:19521-19528
To examine the role of intramolecular beta subunit trans- and cis-autophosphorylation in signal transduction, the vaccinia virus/bacteriophage T7 expression system was used to generate insulin holoreceptors composed of a kinase-defective half-recepto
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e366325e77f61059ca0808c2a0460d35
https://doi.org/10.1016/s0021-9258(18)41806-6
https://doi.org/10.1016/s0021-9258(18)41806-6
Publikováno v:
Journal of Cellular Biochemistry. 48:43-50
Classical insulin and IGF-1 receptors are alpha 2 beta 2 heterotetrameric complexes synthesized from two identical alpha beta half-receptor precursors. Recent data strongly suggests, however, that nonidentical alpha beta half-receptor precursors can
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6119bbf10a34bc23bde8227fa1423f86
https://doi.org/10.1002/jcb.240480108
https://doi.org/10.1002/jcb.240480108
Publikováno v:
Journal of Biological Chemistry. 266:9829-9834
We previously have demonstrated that intramolecular interactions between alpha beta-alpha beta subunits are necessary for insulin-dependent activation of the protein kinase domain within a single alpha 2 beta 2 heterotetrameric insulin-receptor compl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ce393d8713a90ff1098de6f9bcd57163
https://doi.org/10.1016/s0021-9258(18)92894-2
https://doi.org/10.1016/s0021-9258(18)92894-2
Autor:
Jeffrey M. Weinberg, Anne L. Frattali, Victoria P. Werth, Elizabeth M. Spiers, Jonathan T. Wolfe, Stanley J. Naides
Publikováno v:
Journal of clinical rheumatology : practical reports on rheumaticmusculoskeletal diseases. 2(2)
Human parvovirus B19 is responsible for a wide variety of clinical syndromes, including erythema infectiosum, or fifth disease, polyarthritis, aplastic crisis in patients with hemolytic anemia, and chronic anemia in immunocompromised persons. Liver e
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a3a6575842d380157e6eb755b6f096a8
https://pubmed.ncbi.nlm.nih.gov/19078035
https://pubmed.ncbi.nlm.nih.gov/19078035
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression. 1050:27-33
Four different mutations were produced at position 912 of Escherichia coli 16S rRNA in the multicopy plasmid pKK3535. Cells transformed with the mutant plasmids were assayed for growth in steptomycin. The U912 mutant conferred low level streptomycin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ea76e0532a29610d6e093e02c13464f5
https://doi.org/10.1016/0167-4781(90)90136-p
https://doi.org/10.1016/0167-4781(90)90136-p
Autor:
Jeffrey E. Pessin, Anne L. Frattali
Publikováno v:
Annals of the New York Academy of Sciences. 687
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bf6948bccaf28c06b656b85c2776a8e6
https://pubmed.ncbi.nlm.nih.gov/8323192
https://pubmed.ncbi.nlm.nih.gov/8323192