{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,28]],"date-time":"2025-10-28T00:25:03Z","timestamp":1761611103561},"reference-count":33,"publisher":"Wiley","issue":"23","license":[{"start":{"date-parts":[[2002,12,2]],"date-time":"2002-12-02T00:00:00Z","timestamp":1038787200000},"content-version":"vor","delay-in-days":1,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["European Journal of Biochemistry"],"published-print":{"date-parts":[[2002,12]]},"abstract":"<jats:p>Ammodytoxins (Atxs) are presynaptically acting snake venom phospholipase A<jats:sub>2<\/jats:sub> (PLA<jats:sub>2<\/jats:sub>) toxins the molecular mechanism of whose neurotoxicity is not completely understood. Two chimeric PLA<jats:sub>2<\/jats:sub>s were prepared by replacing the C\u2010terminal part of a nontoxic venom PLA<jats:sub>2<\/jats:sub>, ammodytin I<jats:sub>2<\/jats:sub>, with that of AtxA(K108N). The chimeras were not toxic, but were able to bind strongly to an Atxs\u2010specific neuronal receptor, R25. They also showed an increased affinity for calmodulin, a recently identified high\u2010affinity binding protein for Atxs, whereas affinity for a neuronal M\u2010type PLA<jats:sub>2<\/jats:sub> receptor remained largely unchanged. The results show that the C\u2010terminal region of Atxs, which is known to be involved in neurotoxicity, is critical for their interaction with specific binding proteins, but that some other part of the molecule also contributes to toxicity.<\/jats:p>","DOI":"10.1046\/j.1432-1033.2002.03301.x","type":"journal-article","created":{"date-parts":[[2003,3,11]],"date-time":"2003-03-11T18:36:42Z","timestamp":1047407802000},"page":"5759-5764","source":"Crossref","is-referenced-by-count":23,"title":["The C\u2010terminal region of ammodytoxins is important but not sufficient for neurotoxicity"],"prefix":"10.1111","volume":"269","author":[{"given":"Petra","family":"Prijatelj","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Igor","family":"Kri\u017eaj","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Bogdan","family":"Kralj","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Franc","family":"Guben\u0161ek","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jo\u017ee","family":"Punger\u010dar","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2002,12,2]]},"reference":[{"key":"e_1_2_17_2_2","doi-asserted-by":"publisher","DOI":"10.1016\/S1388-1981(00)00105-0"},{"key":"e_1_2_17_3_2","doi-asserted-by":"publisher","DOI":"10.1021\/cr990139w"},{"key":"e_1_2_17_4_2","first-page":"97","volume-title":"Venom Phospholipase A2 Enzymes: Structure, Function and Mechanism","author":"Scott D.L.","year":"1997"},{"key":"e_1_2_17_5_2","first-page":"1","volume-title":"Venom Phospholipase A2 Enzymes: Structure, Function and Mechanism","author":"Kini R.M.","year":"1997"},{"key":"e_1_2_17_6_2","first-page":"245","volume-title":"Venom Phospholipase A2 Enzymes: Structure, Function and Mechanism","author":"Guben\u0161ek F.","year":"1997"},{"key":"e_1_2_17_7_2","doi-asserted-by":"publisher","DOI":"10.1016\/0041-0101(80)90092-6"},{"key":"e_1_2_17_8_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0300-9084(00)01172-X"},{"key":"e_1_2_17_9_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0968-0004(00)01556-5"},{"key":"e_1_2_17_10_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(18)60492-2"},{"key":"e_1_2_17_11_2","first-page":"126","article-title":"Neurotoxins with phospholipase A2 activity in snake venoms","volume":"9","author":"Chang C.C.","year":"1985","journal-title":"Proc. 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