Zobrazeno 1 - 10
of 21
pro vyhledávání: '"Nathan Moskowitz"'
Autor:
Donlin M. Long, Nathan Moskowitz
Publikováno v:
Neurosurgery Quarterly. 1:2-18
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9d14046e79a891c79e602025e57947cf
https://doi.org/10.1097/00013414-199101010-00002
https://doi.org/10.1097/00013414-199101010-00002
Autor:
Nathan Moskowitz
Publikováno v:
Spine. 34:i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2a4b988bfbdbb212240faffbe3233895
https://doi.org/10.1097/01.brs.0000344819.46900.ac
https://doi.org/10.1097/01.brs.0000344819.46900.ac
Autor:
Nathan Moskowitz
Publikováno v:
Spine. 32:i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4370fcac8c50168836ccbbf3947ad8a0
https://doi.org/10.1097/01.brs.0000294106.41399.9f
https://doi.org/10.1097/01.brs.0000294106.41399.9f
Autor:
Lawrence Shapiro, Saul Puszkin, Michael P. Lisanti, Elaine L. Hua, William Schook, Nathan Moskowitz
Publikováno v:
European Journal of Biochemistry. 125:463-470
Clathrin-associated proteins were separated from clathrin under various clathrin-denaturing conditions, i.e. heating, freezing and isoelectric precipitation. The proteins retained biological activity; they were purified further by affinity chromatogr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6786a4f8c06988b94d77610bf66ee7ce
https://doi.org/10.1111/j.1432-1033.1982.tb06706.x
https://doi.org/10.1111/j.1432-1033.1982.tb06706.x
Publikováno v:
Biochemical and Biophysical Research Communications. 115:94-99
Phospholipase A2 in the presence of Ca2+ was stimulated by calmodulin and by prostaglandin F2α. Prostaglandin E2, cyclic-AMP and cyclic-GMP inhibited phospholipase A2 in the presence or absence of calmodulin. Dimethylsuberimidate cross-linking of ph
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dbf491a301cecb87e0b85f80a524c74b
https://doi.org/10.1016/0006-291x(83)90973-7
https://doi.org/10.1016/0006-291x(83)90973-7
Publikováno v:
Journal of Neurochemistry. 38:1742-1747
A systematic characterization of the affinity of calmodulin for brain coated vesicles was undertaken. Binding of 125I-labeled calmodulin to coated vesicles was saturable and competed with unlabeled calmodulin, but not with troponin-C. Scatchard analy
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4109ddaacc8bbeda04c37f6d7d567d3a
https://doi.org/10.1111/j.1471-4159.1982.tb06657.x
https://doi.org/10.1111/j.1471-4159.1982.tb06657.x
Publikováno v:
Journal of Neurochemistry. 41:1576-1586
Brain synaptic vesicle phospholipase A2 (PLA2) activity was characterized. It is Ca2+-dependent and has a pH optimum of 9.0. The enzyme has a Km of 60 microM and a Vmax of 2.0 nmol/mg/h. Calmodulin, prostaglandin F2 alpha, and cAMP, and ATP all incre
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e26a0c74f6ba6887a947de5298743b33
https://doi.org/10.1111/j.1471-4159.1983.tb00867.x
https://doi.org/10.1111/j.1471-4159.1983.tb00867.x
Autor:
Nathan Moskowitz, Kenan Haver, E L Hua, William Schook, Michael P. Lisanti, W S Bloom, Saul Puszkin
Publikováno v:
Journal of Histochemistry & Cytochemistry. 30:497-503
The interaction of clathrin with cytoskeletal proteins was studied cytochemically by immunofluorescent staining and biochemically by the binding of actin to clathrin on the surfaces of polystyrene particles. Using a cytoskeletal-disrupting agent, the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::267e7434e7dd92df6ad2d92e7282a561
https://doi.org/10.1177/30.6.6808054
https://doi.org/10.1177/30.6.6808054
Publikováno v:
Journal - American Water Works Association. 50:821-826
suming and, as will be shown, is not always accurate or precise in the hands of some chemists. For these reasons, an attempt was made to find a method which would overcome some of these limitations. The use of the alkaloids, brucine and strychnine, a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1557daced116efbf5b369bc4b2de48cf
https://doi.org/10.1002/j.1551-8833.1958.tb16213.x
https://doi.org/10.1002/j.1551-8833.1958.tb16213.x