Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Charles Steven Schasteen"'
Publikováno v:
Journal of Controlled Release. 21:49-62
A major obstacle in the development of many new pharmaceuticals, particularly proteins and peptides, is their absorption across the small intestine mucosal barrier. We have developed a cell culture screen to discover novel compounds that increase the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::eb1a934646d3a8cec6acf854e7a4f8c5
https://doi.org/10.1016/0168-3659(92)90007-e
https://doi.org/10.1016/0168-3659(92)90007-e
Publikováno v:
Pharmacology. 42:156-168
The human intestinal cell line, Caco-2, and the Ca2+ ionophores, A23187 and ionomycin, were used to determine the interrelationships of 45Ca2+ efflux, transepithelial
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f912f93ea7bde8326b6bb9b1c8991201
https://doi.org/10.1159/000138793
https://doi.org/10.1159/000138793
Autor:
Janet C. Mayden, Charles Steven Schasteen, Rory F. Finn, George Irvin Glover, Sharon A. McLafferty, Lea D. Bullock, R. Paul Levine
Publikováno v:
Molecular Immunology. 28:17-26
Synthetic peptides based on functionally equivalent (as defined by similar patterns of chemically equivalent amino acids) serine protease inhibitor (serpin) C-terminal sequences inhibit both classical and alternative pathways of complement activation
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a782ce7d7c4f9ce28b1e8aa5210b368b
https://doi.org/10.1016/0161-5890(91)90082-u
https://doi.org/10.1016/0161-5890(91)90082-u
Publikováno v:
Pharmaceutical Research. :210-216
The Caco-2 cell culture model of human small intestinal absorptive cells was used to investigate transepithelial transport. Transport of permeability markers such as mannitol demonstrated that Caco-2 monolayers became less permeable with increasing a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1375cf24f59b9507baf8c4917ebbb15e
https://doi.org/10.1023/a:1015844104539
https://doi.org/10.1023/a:1015844104539
Publikováno v:
Journal of Controlled Release. 13:314-315
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::35d575ae76502d47628fb986d296b8c9
https://doi.org/10.1016/0168-3659(90)90034-q
https://doi.org/10.1016/0168-3659(90)90034-q
Publikováno v:
Molecular Immunology. 25:1261-1267
Sequence homology comparisons between serum serine protease inhibitors led to the prediction that the C-terminal sequences are functionally equivalent and represent an essential protease binding domain. Inhibition of complement serine protease D clea
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::116095984b770e50093cb847cad7da84
https://doi.org/10.1016/0161-5890(88)90040-5
https://doi.org/10.1016/0161-5890(88)90040-5
Autor:
Charles Steven Schasteen, George Irvin Glover, Janet C. Mayden, Sharon A. McLafferty, R. Paul Levine, Wu-Schyong Liu, C.Y. Han
Publikováno v:
Molecular immunology. 25(12)
Synthetic peptides based on the amino acid sequence at the site of cleavage of C3 by classical and alternative pathway convertases were found to be poor inhibitors of hemolysis except at concns of 1 m M and higher. Synthetic peptides of a second type
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::239373f12894783a2dce00907a7b0ed9
https://pubmed.ncbi.nlm.nih.gov/3266292
https://pubmed.ncbi.nlm.nih.gov/3266292