{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,10]],"date-time":"2026-06-10T14:49:23Z","timestamp":1781102963152,"version":"3.54.1"},"reference-count":31,"publisher":"National Academy of Sciences","issue":"21","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[1998,10,13]]},"abstract":"<jats:p>\n                    Sequence analysis of a heat-stable protein necessary for the activation of ADP ribosylation factor-dependent phospholipase D (PLD) reveals that this protein has a structure highly homologous to the previously known G\n                    <jats:sub>M2<\/jats:sub>\n                    ganglioside activator whose deficiency results in the AB-variant of G\n                    <jats:sub>M2<\/jats:sub>\n                    gangliosidosis. The heat-stable activator protein indeed has the capacity to enhance enzymatic conversion of G\n                    <jats:sub>M2<\/jats:sub>\n                    to G\n                    <jats:sub>M3<\/jats:sub>\n                    ganglioside that is catalyzed by \u03b2-hexosaminidase A. Inversely, G\n                    <jats:sub>M2<\/jats:sub>\n                    ganglioside activator purified separately from tissues as described earlier [Conzelmann, E. &amp; Sandhoff, K. (1987)\n                    <jats:italic>Methods Enzymol.<\/jats:italic>\n                    138, 792\u2013815] stimulates ADP ribosylation factor-dependent PLD in a dose-dependent manner. At higher concentrations of ammonium sulfate, the PLD activator protein apparently substitutes for protein kinase C and phosphatidylinositol 4,5-bisphosphate, both of which are known as effective stimulators of the PLD reaction. The mechanism of action of the heat-stable PLD activator protein remains unknown.\n                  <\/jats:p>","DOI":"10.1073\/pnas.95.21.12249","type":"journal-article","created":{"date-parts":[[2002,7,26]],"date-time":"2002-07-26T10:42:40Z","timestamp":1027680160000},"page":"12249-12253","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":15,"title":["Requirement of G\n                    <sub>M2<\/sub>\n                    ganglioside activator for phospholipase D activation"],"prefix":"10.1073","volume":"95","author":[{"given":"Shun-ichi","family":"Nakamura","sequence":"first","affiliation":[{"name":"Department of Biochemistry, Kobe University School of Medicine, Kobe 650-0017, Japan; and Biosignal Research Center, Kobe University, Kobe 657-8501, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Toshihiro","family":"Akisue","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, Kobe University School of Medicine, Kobe 650-0017, Japan; 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and Biosignal Research Center, Kobe University, Kobe 657-8501, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Taro","family":"Okada","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, Kobe University School of Medicine, Kobe 650-0017, Japan; and Biosignal Research Center, Kobe University, Kobe 657-8501, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kimihisa","family":"Yoshida","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, Kobe University School of Medicine, Kobe 650-0017, Japan; and Biosignal Research Center, Kobe University, Kobe 657-8501, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shun\u2019ichi","family":"Kuroda","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, Kobe University School of Medicine, Kobe 650-0017, Japan; and Biosignal Research Center, Kobe University, Kobe 657-8501, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ushio","family":"Kikkawa","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, Kobe University School of Medicine, Kobe 650-0017, Japan; 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