{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,26]],"date-time":"2026-07-26T13:14:09Z","timestamp":1785071649837,"version":"3.55.0"},"reference-count":17,"publisher":"American Association for the Advancement of Science (AAAS)","issue":"4195","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Science"],"published-print":{"date-parts":[[1975,6,27]]},"abstract":"<jats:p>\n            Magnesium adenosine triphosphate (Mg\n            <jats:sup>2+<\/jats:sup>\n            -ATP) is known to produce dissociation of muscle actin and myosin in vitro, while its hydrolysis leads to reassociation. The interaction of purified actin and myosin from human muscle, in the presence of Mg\n            <jats:sup>2+<\/jats:sup>\n            -ATP, was stimulated by minute amounts of adenosine diphosphate (ADP), a product of ATP hydrolysis. By contrast, the dissociation of the actomyosin complex was inhibited by ADP. These data suggest that ADP serves to modulate muscle contraction. Ethanol and its primary metabolite, acetaldehyde, inhibited these effects of ADP. The inhibition was reversible when the preparations were freed of these compounds. The effects of ethanol and acetaldehyde on the response of actomyosin to ADP may play a role in the pathogenesis of alcoholic myopathy and cardiomyopathy.\n          <\/jats:p>","DOI":"10.1126\/science.124949","type":"journal-article","created":{"date-parts":[[2006,10,5]],"date-time":"2006-10-05T15:11:22Z","timestamp":1160061082000},"page":"1319-1320","source":"Crossref","is-referenced-by-count":57,"title":["Adenosine Diphosphate Effect on Contractility of Human Muscle Actomyosin: Inhibition by Ethanol and Acetaldehyde"],"prefix":"10.1126","volume":"188","author":[{"given":"Saul","family":"Puszkin","sequence":"first","affiliation":[{"name":"Department of Pathology, Mount Sinai School of Medicine, New York 10029"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Emanuel","family":"Rubin","sequence":"additional","affiliation":[{"name":"Department of Pathology, Mount Sinai School of Medicine, New York 10029"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"221","reference":[{"key":"e_1_2_1_1_1","doi-asserted-by":"crossref","first-page":"197","DOI":"10.1085\/jgp.50.6.197","volume":"50","year":"1967","unstructured":"BARANY, M, ATPASE ACTIVITY OF MYOSIN CORRELATED WITH SPEED OF MUSCLE SHORTENING, JOURNAL OF GENERAL PHYSIOLOGY 50: 197 (1967).","journal-title":"JOURNAL OF GENERAL PHYSIOLOGY"},{"key":"e_1_2_1_2_1","doi-asserted-by":"crossref","first-page":"200","DOI":"10.1001\/archneur.1969.00480140100010","volume":"21","year":"1969","unstructured":"GERGELY, J, ARCH NEUROL 21: 200 (1969).","journal-title":"ARCH NEUROL"},{"key":"e_1_2_1_3_1","doi-asserted-by":"crossref","first-page":"3304","DOI":"10.1016\/S0021-9258(18)97720-3","volume":"239","year":"1964","unstructured":"KATZ, A.M., INFLUENCE OF TROPOMYOSIN UPON REACTIONS OF ACTOMYOSIN AT LOW IONIC STRENGTH, JOURNAL OF BIOLOGICAL CHEMISTRY 239: 3304 (1964).","journal-title":"JOURNAL OF BIOLOGICAL CHEMISTRY"},{"key":"e_1_2_1_4_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(19)52451-6"},{"key":"e_1_2_1_5_1","doi-asserted-by":"crossref","first-page":"357","DOI":"10.1016\/0006-3002(59)90607-9","volume":"32","year":"1959","unstructured":"MARSH, B.B., THE ESTIMATION OF INORGANIC PHOSPHATE IN THE PRESENCE OF ADENOSINE TRIPHOSPHATE, BIOCHIMICA ET BIOPHYSICA ACTA 32: 357 (1959).","journal-title":"BIOCHIMICA ET BIOPHYSICA ACTA"},{"key":"e_1_2_1_6_1","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.me.22.020171.001013"},{"key":"e_1_2_1_7_1","doi-asserted-by":"crossref","first-page":"695","DOI":"10.1016\/0005-2728(72)90204-6","volume":"256","year":"1972","unstructured":"PUSZKIN, S, ACTOMYOSIN-LIKE PROTEIN FROM BRAIN - 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