Zobrazeno 1 - 10
of 41
pro vyhledávání: '"J. L. Maller"'
Autor:
S I, Reed, J L, Maller
Publikováno v:
Current Opinion in Cell Biology. 8:763-766
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cf7e766138533897172f9df0e37d837e
https://doi.org/10.1016/s0955-0674(96)80075-5
https://doi.org/10.1016/s0955-0674(96)80075-5
Publikováno v:
Journal of Biological Chemistry. 268:9564-9569
Mitogen-activated protein (MAP) kinases are members of a 40-45-kDa family of serine/threonine protein kinases that phosphorylate several substrates including microtubule-associated protein-2, S6 kinase, and myelin basic protein. Activity of MAP kinas
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::374a9dc1a3bb364b74b47f198a12f856
https://doi.org/10.1016/s0021-9258(18)98388-2
https://doi.org/10.1016/s0021-9258(18)98388-2
Publikováno v:
Journal of Biological Chemistry. 267:9021-9027
Phosphorylated ribosomal proteins were isolated from Xenopus 40 S ribosomal subunits by reversed-phase high performance liquid chromatography (HPLC) to enable direct analysis of the phosphorylation sites in ribosomal protein S6. Xenopus S6 closely re
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9e54cffd752e8d1f366ded6cd2cff6fd
https://doi.org/10.1016/s0021-9258(19)50382-9
https://doi.org/10.1016/s0021-9258(19)50382-9
Autor:
J L, Maller
Publikováno v:
Biology of the cell. 90(6-7)
I am pleased to contribute to this special issue of Biology of the Cell in honor of Yoshio Masui. Oocyte maturation remains a small enough and young enough field that the authors assembled for this issue can trace the entire development of the field
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::0d551918f27408a766ac9fc17bc68871
https://pubmed.ncbi.nlm.nih.gov/9923070
https://pubmed.ncbi.nlm.nih.gov/9923070
Publikováno v:
The Journal of biological chemistry. 269(40)
Previously pp60v-src, cyclin A, p39mos, and maturation-promoting factor (composed of Cdc2 and cyclin B) have been shown to activate mitogen-activated protein kinase (MAPK) and MAPK kinase (MEK) in cell-free extracts of Xenopus oocytes. The pp60v-src
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::2d7d53c4bc1fd6bd661c521a3008f9da
https://pubmed.ncbi.nlm.nih.gov/7929138
https://pubmed.ncbi.nlm.nih.gov/7929138
Publikováno v:
The Journal of biological chemistry. 268(33)
The mitogen-activated protein (MAP) kinases are serine-threonine protein kinases that are activated by tyrosine and threonine phosphorylation by the dual specificity protein kinase MEK (MAP kinase/ERK kinase). The present report describes the purific
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::b7d384fa535ae5ab1c6f64d6f426f887
https://pubmed.ncbi.nlm.nih.gov/8227071
https://pubmed.ncbi.nlm.nih.gov/8227071
Publikováno v:
The Journal of biological chemistry. 268(27)
In Xenopus oocytes, mitogen-activated protein (MAP) kinase can be activated by progesterone treatment or by microinjection of cyclin A, both of which lead to activation of the cdc2 protein kinase. The tyrosine kinase pp60v-src has previously been sho
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::a7993c74fa1589defcabeac0328fafec
https://pubmed.ncbi.nlm.nih.gov/8397192
https://pubmed.ncbi.nlm.nih.gov/8397192
Publikováno v:
The Journal of biological chemistry. 268(13)
Mitogen-activated protein (MAP) kinases are members of a 40-45-kDa family of serine/threonine protein kinases that phosphorylate several substrates including microtubule-associated protein-2, S6 kinase, and myelin basic protein. Activity of MAP kinas
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::3e3a32a17c1eb1f0ffa85e91626e78d2
https://pubmed.ncbi.nlm.nih.gov/8387499
https://pubmed.ncbi.nlm.nih.gov/8387499
Publikováno v:
The Journal of biological chemistry. 267(13)
Phosphorylated ribosomal proteins were isolated from Xenopus 40 S ribosomal subunits by reversed-phase high performance liquid chromatography (HPLC) to enable direct analysis of the phosphorylation sites in ribosomal protein S6. Xenopus S6 closely re
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::7e77b09037ec1affcd90d8a76d392bf0
https://pubmed.ncbi.nlm.nih.gov/1577739
https://pubmed.ncbi.nlm.nih.gov/1577739
Publikováno v:
The Journal of biological chemistry. 267(7)
S6 kinases I and II have been purified previously from Xenopus eggs and shown to be activated by phosphorylation on serine and threonine residues. An S6 kinase clone, closely related to S6 kinase II, was subsequently identified and the protein produc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::366e7c616609d5095c7c02ae936cff7c
https://pubmed.ncbi.nlm.nih.gov/1311309
https://pubmed.ncbi.nlm.nih.gov/1311309