Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Adolph Ulfohn"'
Autor:
Adolph Ulfohn, Arnold M. Seligman, Olympia Aybar, Samuel Sass, Benjamin Witten, Samuel E. Gaby, Sheldon C. Kravitz, Jacob I. Miller, Albert Schilling, Daniel Bakal, Charles E Williamson, Stanley P. Kramer, Stanley Miller, Louis E. Goodman
Publikováno v:
Cancer. 16:727-736
Autor:
Charles E. Williamson, Arnold M. Seligman, Stanley P. Kramer, Samuel Sass, Simon Calle, Benjamin Witten, Adolph Ulfohn
Publikováno v:
Journal of Surgical Research. 8:345-359
Although circumvention of the problem of systemic toxicity during regional infusions was shown to be possible with S-182, an alkylating agent with a very short half-life, practical use of this drug was hampered by its lack of water solubility and dam
Autor:
Benjamin Witten, Charles E. Williamson, Adolph Ulfohn, Samuel Sass, Arnold M. Seligman, Louis E. Goodman, Stanley P. Kramer
Publikováno v:
Journal of Medicinal Chemistry. 8:14-17
Autor:
Samuel D. Gaby, Maria G. Ascoli, Kwan-Chung Tsou, Howard E. Dorfman, Louis E. Goodman, Stanley P. Kramer, Olimpia Aybar, Adolph Ulfohn, Daniel Bakal, Elena Cendana, Arnold M. Seligman
Publikováno v:
Cancer. 18:307-312
Autor:
Samuel Sass, Anselmo G. Mamaril, Benjamin Witten, Simon Calle, Arnold M. Seligman, Daniel Bakal, Charles E. Williamson, Louis E. Goodman, Belur S. Bhagavan, Yale H. Caplan, Adolph Ulfohn
Publikováno v:
The Journal of surgical research. 11(5)
Clinical trials of a new water-soluble short half-life alkylating agent (S-73) administered by intra-arterial infusion into 56 patients with a variety of malignant tumors, revealed only limited usefulness. The best responses were seen in a case of Ka
Autor:
Adolph Ulfohn, Louis E. Goodman, Arnold M. Seligman, Stanley P. Kramer, Charles E. Williamson, Rolando Madamba, Samuel Sass, Benjamin Witten, Simon Calle, Daniel Bakal
Publikováno v:
Cancer. 20(5)
This is a preliminary report on the experimental and clinical use of a new alkylating agent (S-73) which is water soluble, stable to hydrolysis for hours, but with esterase-susceptible linkages, which results in inactivation of the agent by esterase