{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2024,7,12]],"date-time":"2024-07-12T00:04:47Z","timestamp":1720742687906},"reference-count":16,"publisher":"Springer Science and Business Media LLC","issue":"2","license":[{"start":{"date-parts":[[2016,10,27]],"date-time":"2016-10-27T00:00:00Z","timestamp":1477526400000},"content-version":"unspecified","delay-in-days":0,"URL":"http:\/\/www.springer.com\/tdm"}],"funder":[{"name":"None"}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["J Thromb Thrombolysis"],"published-print":{"date-parts":[[2017,2]]},"DOI":"10.1007\/s11239-016-1442-4","type":"journal-article","created":{"date-parts":[[2016,10,27]],"date-time":"2016-10-27T11:04:06Z","timestamp":1477566246000},"page":"203-208","update-policy":"http:\/\/dx.doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":18,"title":["Carbon monoxide releasing molecule-2 inhibition of snake venom thrombin-like activity: novel biochemical \u201cbrake\u201d?"],"prefix":"10.1007","volume":"43","author":[{"given":"Vance G.","family":"Nielsen","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Charles M.","family":"Bazzell","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"297","published-online":{"date-parts":[[2016,10,27]]},"reference":[{"key":"1442_CR1","doi-asserted-by":"crossref","first-page":"262","DOI":"10.1016\/0167-4838(92)90086-S","volume":"1160","author":"TF Huang","year":"1992","unstructured":"Huang TF, Chang MC, Peng HC, Teng CM (1992) A novel alpha-type fibrinogenase from Agkistrodon rhodostoma snake venom. Biochim Biophys Acta 1160:262\u2013268","journal-title":"Biochim Biophys Acta"},{"key":"1442_CR2","doi-asserted-by":"crossref","first-page":"288","DOI":"10.1007\/s11239-016-1343-6","volume":"42","author":"VG Nielsen","year":"2016","unstructured":"Nielsen VG (2016) Ancrod revisited: viscoelastic analyses of the effects of Calloselasma rhodostoma venom on plasma coagulation and fibrinolysis. J Thromb Thrombolysis 42:288\u2013293","journal-title":"J Thromb Thrombolysis"},{"key":"1442_CR3","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1111\/j.1432-1033.1974.tb03317.x","volume":"42","author":"JP Collins","year":"1974","unstructured":"Collins JP, Jones JG (1974) Identification of serine and histidine as essential amino-acid residues in the coagulant enzyme ancrod. Eur J Biochem 42:81\u201387","journal-title":"Eur J Biochem"},{"key":"1442_CR4","doi-asserted-by":"crossref","first-page":"474","DOI":"10.1177\/15353702-0322805-09","volume":"228","author":"R Wang","year":"2003","unstructured":"Wang R, Wu L (2003) Interaction of selective amino acid residues of K(ca) channels with carbon monoxide. Exp Biol Med 228:474\u2013480","journal-title":"Exp Biol Med"},{"key":"1442_CR5","doi-asserted-by":"crossref","first-page":"665","DOI":"10.1007\/s00424-011-0924-7","volume":"461","author":"V Telezhkin","year":"2011","unstructured":"Telezhkin V, Brazier SP, Mears R, M\u00fcller CT, Riccardi D, Kemp PJ (2011) Cysteine residue 911 in C-terminal tail of human BK(Ca)\u03b1 channel subunit is crucial for its activation by carbon monoxide. Pflug Arch 461:665\u2013675","journal-title":"Pflug Arch"},{"key":"1442_CR6","doi-asserted-by":"crossref","first-page":"639","DOI":"10.1165\/rcmb.2008-0458OC","volume":"41","author":"M Althaus","year":"2009","unstructured":"Althaus M, Fronius M, Buch\u00e4ckert Y, Vad\u00e1sz I, Clauss WG, Seeger W, Motterlini R, Morty RE (2009) Carbon monoxide rapidly impairs alveolar fluid clearance by inhibiting epithelial sodium channels. Am J Respir Cell Mol Biol 41:639\u2013650","journal-title":"Am J Respir Cell Mol Biol"},{"key":"1442_CR7","doi-asserted-by":"crossref","first-page":"6460","DOI":"10.1016\/S0021-9258(19)34138-9","volume":"246","author":"FS Markland","year":"1971","unstructured":"Markland FS, Damus PS (1971) Purification and properties of a thrombin-like enzyme from the venom of Crotalus adamanteus (Eastern diamondback rattlesnake). J Biol Chem 246:6460\u20136473","journal-title":"J Biol Chem"},{"key":"1442_CR8","doi-asserted-by":"crossref","first-page":"151","DOI":"10.1016\/0049-3848(75)90020-1","volume":"6","author":"CA Bonilla","year":"1975","unstructured":"Bonilla CA (1975) Defibrinating enzyme from timber rattlesnake (Crotalus h. horridus) venom: a potential agent for therapeutic defibrination. I. Purification and properties. Thromb Res 6:151\u2013169","journal-title":"Thromb Res"},{"key":"1442_CR9","doi-asserted-by":"crossref","first-page":"236","DOI":"10.1016\/0167-4838(83)90300-X","volume":"748","author":"YY Shu","year":"1983","unstructured":"Shu YY, Moran JB, Geren CR (1983) A thrombin-like enzyme from timber rattlesnake venom. Biochim Biophys Acta 748:236\u2013244","journal-title":"Biochim Biophys Acta"},{"key":"1442_CR10","doi-asserted-by":"crossref","first-page":"801","DOI":"10.1097\/MBC.0000000000000146","volume":"25","author":"VG Nielsen","year":"2014","unstructured":"Nielsen VG, Garza JI (2014) Comparison of the effects of CORM-2, CORM-3 and CORM-A1 on coagulation in human plasma. Blood Coagul Fibrinolysis 25:801\u2013805","journal-title":"Blood Coagul Fibrinolysis"},{"key":"1442_CR11","doi-asserted-by":"crossref","first-page":"1116","DOI":"10.1177\/0960327115621366","volume":"35","author":"VG Nielsen","year":"2016","unstructured":"Nielsen VG (2016) Iron and carbon monoxide prevent degradation of plasmatic coagulation by thrombin-like activity in rattlesnake venom. Hum Exp Toxicol 35:1116\u20131122","journal-title":"Hum Exp Toxicol"},{"key":"1442_CR12","doi-asserted-by":"publisher","DOI":"10.1016\/j.jacc.2016.07.729","author":"VG Nielsen","year":"2016","unstructured":"Nielsen VG, Boyer LV, Redford DT, Ford P (2016) Thrombelastographic characterization of the thrombin-like activity of Crotalus simus and Bothrops asper venoms. Blood Coagul Fibrinolysis. doi: 10.1016\/j.jacc.2016.07.729","journal-title":"Blood Coagul Fibrinolysis"},{"key":"1442_CR13","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1007\/s10534-016-9909-5","volume":"29","author":"VG Nielsen","year":"2016","unstructured":"Nielsen VG, Jacobsen WK (2016) Iron modulates the alpha chain of fibrinogen. Biometals 29:235\u2013238","journal-title":"Biometals"},{"key":"1442_CR14","doi-asserted-by":"crossref","first-page":"16414","DOI":"10.1074\/jbc.M110.198010","volume":"286","author":"A Jara-Oseguera","year":"2011","unstructured":"Jara-Oseguera A, Ishida IG, Rangel-Yescas GE, Espinosa-Jalapa N, Pe\u00b4rez-Guzma\u00b4n JA, El\u00edas-Vinas D, Le Lagadec R, Rosenbaum T, Islas LD (2011) Uncoupling charge movement from channel opening in voltage-gated potassium channels by ruthenium complexes. J Biol Chem 286:16414\u201316425","journal-title":"J Biol Chem"},{"key":"1442_CR15","doi-asserted-by":"crossref","first-page":"271","DOI":"10.1152\/japplphysiol.00726.2015","volume":"120","author":"O Pak","year":"2016","unstructured":"Pak O, Bakr AG, Gierhardt M, Albus J, Strielkov I, Kroschel F, Hoeres T, Hecker M, Ghofrani HA, Seeger W, Weissmann N, Sommer N (2016) Effects of carbon monoxide-releasing molecules on pulmonary vasoreactivity in isolated perfused lungs. J Appl Physiol 120:271\u2013281","journal-title":"J Appl Physiol"},{"key":"1442_CR16","doi-asserted-by":"crossref","first-page":"3796","DOI":"10.1161\/STROKEAHA.109.565119","volume":"40","author":"DE Levy","year":"2009","unstructured":"Levy DE, del Zoppo GJ, Demaerschalk BM, Demchuk AM, Diener HC, Howard G, Kaste M, Pancioli AM, Ringelstein EB, Spatareanu C, Wasiewski WW (2009) Ancrod in acute ischemic stroke: results of 500 subjects beginning treatment within 6\u00a0h of stroke onset in the ancrod stroke program. Stroke 40:3796\u20133803","journal-title":"Stroke"}],"container-title":["Journal of Thrombosis and Thrombolysis"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/link.springer.com\/content\/pdf\/10.1007\/s11239-016-1442-4.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/link.springer.com\/article\/10.1007\/s11239-016-1442-4\/fulltext.html","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/link.springer.com\/content\/pdf\/10.1007\/s11239-016-1442-4.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,7,11]],"date-time":"2022-07-11T16:12:28Z","timestamp":1657555948000},"score":1,"resource":{"primary":{"URL":"http:\/\/link.springer.com\/10.1007\/s11239-016-1442-4"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2016,10,27]]},"references-count":16,"journal-issue":{"issue":"2","published-print":{"date-parts":[[2017,2]]}},"alternative-id":["1442"],"URL":"https:\/\/doi.org\/10.1007\/s11239-016-1442-4","relation":{},"ISSN":["0929-5305","1573-742X"],"issn-type":[{"value":"0929-5305","type":"print"},{"value":"1573-742X","type":"electronic"}],"subject":[],"published":{"date-parts":[[2016,10,27]]}}}