Zobrazeno 1 - 10
of 57
pro vyhledávání: '"Vittorio Moret"'
Publikováno v:
Biochemical and Biophysical Research Communications. 213:249-257
The Tyr-phosphorylation of the cytoplasmic domain of the major membrane-spanning band 3, rather than the Ser/Thr-phosphorylation of the membrane proteins (spectrin and band 3 itself), might be functionally related to certain morphological changes of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6d97eb6a9d0e9c3c19697cdd8c7c17a3
https://doi.org/10.1006/bbrc.1995.2123
https://doi.org/10.1006/bbrc.1995.2123
Publikováno v:
Biochemical and Biophysical Research Communications. 187:853-858
In human erythrocytes Ser/Thr- and Tyr-phosphorylations of cytoplasmic domain of band 3 are catalyzed by casein kinase I and Tyr-protein kinase respectively, both distributed between cytosol and membrane structures. The results reported here show tha
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::45e6106d9f029c8546c5c33cabed853b
https://doi.org/10.1016/0006-291x(92)91275-u
https://doi.org/10.1016/0006-291x(92)91275-u
Publikováno v:
Biochemical and Biophysical Research Communications. 178:1021-1027
The pH-dependence of the distribution of Tyr- and Ser/Thr-protein kinases between cytosol and membrane in human erythrocytes was investigated. When the internal pH of human erythrocytes is decreased from 8 to 7.3 the membrane-associated Tyr-protein k
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c18d12a52653e2f2fe366165901e636d
https://doi.org/10.1016/0006-291x(91)90994-i
https://doi.org/10.1016/0006-291x(91)90994-i
Publikováno v:
Biochemical and Biophysical Research Communications. 166:1378-1383
Some cytosolic proteins of human erythrocytes can be phosphorylated on tyrosine residues by endogenous Tyr-protein kinase(s). Their phosphorylation is enhanced by addition of Tyr-protein kinase, purified from human erythrocyte cytosol. The most phosp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c2d249113d8c7df22d67e67dfb79a191
https://doi.org/10.1016/0006-291x(90)91019-o
https://doi.org/10.1016/0006-291x(90)91019-o
Publikováno v:
Scopus-Elsevier
Band-3 protein (approximately 95 kDa), the major and multifunctional transmembrane protein of human erythrocytes, has been shown to be phosphorylated by endogenous Tyr-protein kinases on different Tyr residues at its N and C cytoplasmic domains. Both
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d0387605cd914d8e6f5234ad400e615a
http://hdl.handle.net/11577/111958
http://hdl.handle.net/11577/111958
Autor:
Luciana Bordin, D. Piccinelli-Siliprandi, Giulio Clari, Vittorio Moret, Antonio Toninello, F. Cattapan
The results indicated here, together with those previously reported, show that spermine, ubiquitous polyamine, while promoting the transmembrane translocation of casein kinase II (CKII) across the outer membrane to more internal compartments of rat l
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9870f1e48a98dc93b5158cc8a69fb815
http://hdl.handle.net/11577/2506478
http://hdl.handle.net/11577/2506478
The present paper shows that an increased phosphorylation of the membrane proteins, promoted by the okadaic acid (strong inhibitor of P-Ser/Thr-protein phosphatase(s)), is accompanied by a release of casein kinase from the membrane into cytosol. Such
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fb53af8dac48ddae6e6ae2c1df883a67
http://hdl.handle.net/11562/998745
http://hdl.handle.net/11562/998745
Autor:
Vittorio Moret, Noris Siliprandi, Giulio Clari, Federica Cattapan, Luciana Bordin, Antonio Toninello
Spermine, ubiquitous intracellular polyamine, is able to promote the transmembrane translocation of casein kinase CKII through the outer membrane of rat liver mitochondria and its binding to more internal mitochondrial structures. These findings sugg
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::efecf72b0688bd92f1c13d7808c603c1
http://hdl.handle.net/11577/2506481
http://hdl.handle.net/11577/2506481
Publikováno v:
Biochimica et biophysica acta. 1148(1)
In human erythrocytes, okadaic acid, a potent inhibitor of certain protein phosphatases, promotes a marked increase of Ser/Thr-phosphorylation of membrane proteins, including band-3 protein. Moreover, okadaic acid also increases the band-3-mediated o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fc019498d2e9c7178fe4ee447043c9af
https://pubmed.ncbi.nlm.nih.gov/8388726
https://pubmed.ncbi.nlm.nih.gov/8388726