The interaction of phomopsin A with bovine brain tubulin
| ISSN: |
0003-9861
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|---|---|
| Source: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
|
| Topics: |
Biology
Chemistry and Pharmacology
Physics
|
| Type of Medium: |
Electronic Resource
|
| URL: |
| _version_ | 1798292191997591553 |
|---|---|
| autor | Luduena, R.F. Prasad, V. Roach, M.C. Lacey, E. |
| autorsonst | Luduena, R.F. Prasad, V. Roach, M.C. Lacey, E. |
| book_url | http://dx.doi.org/10.1016/0003-9861(89)90191-4 |
| datenlieferant | nat_lic_papers |
| fussnote | Phomopsin A is an anti-mitotic compound from the fungus Phomopsis leptostromiformis which is a potent inhibitor of microtubule assembly in vitro; like maytansine, it is known to compete with vinblastine for binding to tubulin . A major difference between the effects of maytansine and vinblastine is that vinblastine is a potent inhibitor of tubulin decay, whereas maytansine has little or no effect on decay. Since phomopsin A is structurally distinct from either maytansine or vinblastine, tubulin decay may be measured by either the time-dependent loss of the ability to bind to [^3H]colchicine or the time-dependent increase in the binding of bis(8-anilinonaphthalene 1-sulfonate) (BisANS) to tubulin. By either method, phomopsin A was found to be a much stronger inhibitor of tubulin decay than is vinblastine or any other drug yet tested, and, in fact, when decay is measured by the increase of BisANS binding, phomopsin A appears to stop the process entirely. This may prove to be useful in the determination of the higherorder structure of the tubulin molecule. |
| hauptsatz | hsatz_simple |
| identnr | NLZ183403932 |
| issn | 0003-9861 |
| journal_name | Archives of Biochemistry and Biophysics |
| materialart | 1 |
| package_name | Elsevier |
| publikationsort | Amsterdam |
| publisher | Elsevier |
| reference | 272 (1989), S. 32-38 |
| search_space | articles |
| shingle_author_1 | Luduena, R.F. Prasad, V. Roach, M.C. Lacey, E. |
| shingle_author_2 | Luduena, R.F. Prasad, V. Roach, M.C. Lacey, E. |
| shingle_author_3 | Luduena, R.F. Prasad, V. Roach, M.C. Lacey, E. |
| shingle_author_4 | Luduena, R.F. Prasad, V. Roach, M.C. Lacey, E. |
| shingle_catch_all_1 | Luduena, R.F. Prasad, V. Roach, M.C. Lacey, E. The interaction of phomopsin A with bovine brain tubulin 0003-9861 00039861 Elsevier |
| shingle_catch_all_2 | Luduena, R.F. Prasad, V. Roach, M.C. Lacey, E. The interaction of phomopsin A with bovine brain tubulin 0003-9861 00039861 Elsevier |
| shingle_catch_all_3 | Luduena, R.F. Prasad, V. Roach, M.C. Lacey, E. The interaction of phomopsin A with bovine brain tubulin 0003-9861 00039861 Elsevier |
| shingle_catch_all_4 | Luduena, R.F. Prasad, V. Roach, M.C. Lacey, E. The interaction of phomopsin A with bovine brain tubulin 0003-9861 00039861 Elsevier |
| shingle_title_1 | The interaction of phomopsin A with bovine brain tubulin |
| shingle_title_2 | The interaction of phomopsin A with bovine brain tubulin |
| shingle_title_3 | The interaction of phomopsin A with bovine brain tubulin |
| shingle_title_4 | The interaction of phomopsin A with bovine brain tubulin |
| sigel_instance_filter | dkfz geomar wilbert ipn albert fhp |
| source_archive | Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
| timestamp | 2024-05-06T08:44:36.704Z |
| titel | The interaction of phomopsin A with bovine brain tubulin |
| titel_suche | The interaction of phomopsin A with bovine brain tubulin Phomopsin A is an anti-mitotic compound from the fungus Phomopsis leptostromiformis which is a potent inhibitor of microtubule assembly in vitro; like maytansine, it is known to compete with vinblastine for binding to tubulin . A major difference between the effects of maytansine and vinblastine is that vinblastine is a potent inhibitor of tubulin decay, whereas maytansine has little or no effect on decay. Since phomopsin A is structurally distinct from either maytansine or vinblastine, tubulin decay may be measured by either the time-dependent loss of the ability to bind to [^3H]colchicine or the time-dependent increase in the binding of bis(8-anilinonaphthalene 1-sulfonate) (BisANS) to tubulin. By either method, phomopsin A was found to be a much stronger inhibitor of tubulin decay than is vinblastine or any other drug yet tested, and, in fact, when decay is measured by the increase of BisANS binding, phomopsin A appears to stop the process entirely. This may prove to be useful in the determination of the higherorder structure of the tubulin molecule. |
| topic | W V U |
| uid | nat_lic_papers_NLZ183403932 |