Teleocidin B inhibits binding of epidermal growth factor to cellular receptors probably by the same mechanism as phorbol esters

Imai, Y. ; Kaneko, Y. ; Matsuzaki, F. ; Endo, Y. ; Oda, T.

Amsterdam : Elsevier
ISSN:
0006-291X
Source:
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
Topics:
Biology
Chemistry and Pharmacology
Physics
Type of Medium:
Electronic Resource
URL:
_version_ 1798292252740550656
autor Imai, Y.
Kaneko, Y.
Matsuzaki, F.
Endo, Y.
Oda, T.
autorsonst Imai, Y.
Kaneko, Y.
Matsuzaki, F.
Endo, Y.
Oda, T.
book_url http://dx.doi.org/10.1016/0006-291X(80)91465-5
datenlieferant nat_lic_papers
fussnote Teleocidin B purified from Streptomyces inhibited the binding of epidermal growth factor(EGF) to rat AH66 hepatoma cells by reducing the receptor affinity. A prolonged treatment of AH66 cells with teleocidin B caused these cells to escape from and to become refractory to teleocidin B-inhibition of EGF binding as seen in TPA-treatment. In addition, those cells refractory to teleocidin B were refractory to a phorbol ester as well, indicating these two compounds with different molecular structure brought similar perturbation of surface structure of AH66 cells.
hauptsatz hsatz_simple
identnr NLZ18423154X
issn 0006-291X
journal_name Biochemical and Biophysical Research Communications
materialart 1
package_name Elsevier
publikationsort Amsterdam
publisher Elsevier
reference 97 (1980), S. 926-931
search_space articles
shingle_author_1 Imai, Y.
Kaneko, Y.
Matsuzaki, F.
Endo, Y.
Oda, T.
shingle_author_2 Imai, Y.
Kaneko, Y.
Matsuzaki, F.
Endo, Y.
Oda, T.
shingle_author_3 Imai, Y.
Kaneko, Y.
Matsuzaki, F.
Endo, Y.
Oda, T.
shingle_author_4 Imai, Y.
Kaneko, Y.
Matsuzaki, F.
Endo, Y.
Oda, T.
shingle_catch_all_1 Imai, Y.
Kaneko, Y.
Matsuzaki, F.
Endo, Y.
Oda, T.
Teleocidin B inhibits binding of epidermal growth factor to cellular receptors probably by the same mechanism as phorbol esters
0006-291X
0006291X
Elsevier
shingle_catch_all_2 Imai, Y.
Kaneko, Y.
Matsuzaki, F.
Endo, Y.
Oda, T.
Teleocidin B inhibits binding of epidermal growth factor to cellular receptors probably by the same mechanism as phorbol esters
0006-291X
0006291X
Elsevier
shingle_catch_all_3 Imai, Y.
Kaneko, Y.
Matsuzaki, F.
Endo, Y.
Oda, T.
Teleocidin B inhibits binding of epidermal growth factor to cellular receptors probably by the same mechanism as phorbol esters
0006-291X
0006291X
Elsevier
shingle_catch_all_4 Imai, Y.
Kaneko, Y.
Matsuzaki, F.
Endo, Y.
Oda, T.
Teleocidin B inhibits binding of epidermal growth factor to cellular receptors probably by the same mechanism as phorbol esters
0006-291X
0006291X
Elsevier
shingle_title_1 Teleocidin B inhibits binding of epidermal growth factor to cellular receptors probably by the same mechanism as phorbol esters
shingle_title_2 Teleocidin B inhibits binding of epidermal growth factor to cellular receptors probably by the same mechanism as phorbol esters
shingle_title_3 Teleocidin B inhibits binding of epidermal growth factor to cellular receptors probably by the same mechanism as phorbol esters
shingle_title_4 Teleocidin B inhibits binding of epidermal growth factor to cellular receptors probably by the same mechanism as phorbol esters
sigel_instance_filter dkfz
geomar
wilbert
ipn
albert
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source_archive Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
timestamp 2024-05-06T08:45:34.474Z
titel Teleocidin B inhibits binding of epidermal growth factor to cellular receptors probably by the same mechanism as phorbol esters
titel_suche Teleocidin B inhibits binding of epidermal growth factor to cellular receptors probably by the same mechanism as phorbol esters
Teleocidin B purified from Streptomyces inhibited the binding of epidermal growth factor(EGF) to rat AH66 hepatoma cells by reducing the receptor affinity. A prolonged treatment of AH66 cells with teleocidin B caused these cells to escape from and to become refractory to teleocidin B-inhibition of EGF binding as seen in TPA-treatment. In addition, those cells refractory to teleocidin B were refractory to a phorbol ester as well, indicating these two compounds with different molecular structure brought similar perturbation of surface structure of AH66 cells.
topic W
V
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uid nat_lic_papers_NLZ18423154X