Teleocidin B inhibits binding of epidermal growth factor to cellular receptors probably by the same mechanism as phorbol esters
ISSN: |
0006-291X
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Source: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
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Topics: |
Biology
Chemistry and Pharmacology
Physics
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Type of Medium: |
Electronic Resource
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URL: |
_version_ | 1798292252740550656 |
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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 fhp |
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 U |
uid | nat_lic_papers_NLZ18423154X |