{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,29]],"date-time":"2025-10-29T12:45:19Z","timestamp":1761741919949},"reference-count":58,"publisher":"Elsevier BV","issue":"4","license":[{"start":{"date-parts":[[2000,3,1]],"date-time":"2000-03-01T00:00:00Z","timestamp":951868800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Journal of Molecular Biology"],"published-print":{"date-parts":[[2000,3]]},"DOI":"10.1006\/jmbi.2000.3537","type":"journal-article","created":{"date-parts":[[2002,10,7]],"date-time":"2002-10-07T11:12:52Z","timestamp":1033989172000},"page":"1117-1126","source":"Crossref","is-referenced-by-count":16,"title":["Three-dimensional structure of a presynaptic neurotoxic phospholipase A2 from Daboia russelli pulchella at 2.4 \u00c5 resolution 1 1Edited by D. Rees"],"prefix":"10.1006","volume":"296","author":[{"given":"Vikas","family":"Chandra","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Punit","family":"Kaur","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Alagiri","family":"Srinivasan","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Tej P","family":"Singh","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1006\/jmbi.2000.3537_BIB1","doi-asserted-by":"crossref","first-page":"827","DOI":"10.1016\/0041-0101(96)00036-0","article-title":"Phospholipase A2 - a structural review","volume":"34","author":"Arni","year":"1996","journal-title":"Toxicon"},{"key":"10.1006\/jmbi.2000.3537_BIB2","doi-asserted-by":"crossref","first-page":"311","DOI":"10.1107\/S0907444994011455","article-title":"Structure of calcium-independent phospholipase like myotoxic proteins from Bothrops asper venom","volume":"51","author":"Arni","year":"1995","journal-title":"Acta Crystallog. sect. D"},{"key":"10.1006\/jmbi.2000.3537_BIB3","doi-asserted-by":"crossref","first-page":"177","DOI":"10.1006\/abbi.1999.1210","article-title":"Crystal structure of myotoxin II, a monomeric Lys49-phospholipase A2 homologue isolated from the venom of Cerrophidion (Bothrops) Godmani","volume":"366","author":"Arni","year":"1999","journal-title":"Arch. Biochem. Biophys"},{"key":"10.1006\/jmbi.2000.3537_BIB4","doi-asserted-by":"crossref","first-page":"384","DOI":"10.1007\/s000180050440","article-title":"Review","volume":"56","author":"Betzel","year":"1999","journal-title":"Cell. Mol. Life Sci"},{"key":"10.1006\/jmbi.2000.3537_BIB5","doi-asserted-by":"crossref","first-page":"828","DOI":"10.1016\/0005-2744(76)90329-6","article-title":"A phospholipase A2 with anticoagulant activity. I. Isolation from Vipera berus venom and properties","volume":"429","author":"Boffa","year":"1976","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1006\/jmbi.2000.3537_BIB6","doi-asserted-by":"crossref","first-page":"839","DOI":"10.1016\/0005-2744(76)90330-2","article-title":"A Phospholipase A2 with anticoagulant activity. II. Inhibition of the phospholipid activity in coagulation","volume":"429","author":"Boffa","year":"1976","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1006\/jmbi.2000.3537_BIB7","doi-asserted-by":"crossref","first-page":"471","DOI":"10.1111\/j.1432-1033.1979.tb13278.x","article-title":"Post-synaptic effects of Crotoxin and its isolated subunits","volume":"99","author":"Bon","year":"1979","journal-title":"Eur. J. Biochem"},{"key":"10.1006\/jmbi.2000.3537_BIB8","series-title":"A System for X-ray Crystallography and NMR","article-title":"X-PLOR v3.1 User\u2019s Guide","author":"Br\u00fcnger","year":"1992"},{"key":"10.1006\/jmbi.2000.3537_BIB9","doi-asserted-by":"crossref","first-page":"472","DOI":"10.1038\/355472a0","article-title":"The free R-value","volume":"355","author":"Br\u00fcnger","year":"1992","journal-title":"Nature"},{"key":"10.1006\/jmbi.2000.3537_BIB10","doi-asserted-by":"crossref","first-page":"458","DOI":"10.1126\/science.235.4787.458","article-title":"Crystallographic R factor refinement by molecular dynamics","volume":"235","author":"Br\u00fcnger","year":"1987","journal-title":"Science"},{"key":"10.1006\/jmbi.2000.3537_BIB11","doi-asserted-by":"crossref","first-page":"585","DOI":"10.1107\/S0108767390002355","article-title":"Slow-cooling protocols for crystallographic refinement by simulated annealing","volume":"46","author":"Br\u00fcnger","year":"1990","journal-title":"Acta Crystallog. sect. A"},{"key":"10.1006\/jmbi.2000.3537_BIB12","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1016\/S0041-0101(97)00051-2","article-title":"The three-dimensional structures of two toxins from snake venom throw light on the anticoagulant and neurotoxic sites of phospholipase A2","volume":"36","author":"Carredano","year":"1998","journal-title":"Toxicon"},{"key":"10.1006\/jmbi.2000.3537_BIB13","first-page":"760","article-title":"The CCP4 sulte","volume":"50","year":"1994","journal-title":"Acta Crystallog. sect. D"},{"key":"10.1006\/jmbi.2000.3537_BIB14","doi-asserted-by":"crossref","first-page":"23018","DOI":"10.1016\/S0021-9258(17)31613-7","article-title":"Cloning and characterization of novel rat and mouse low molecular weight Ca(2+)-dependent phospholipase A2 s containing 16 cysteines","volume":"269","author":"Chen","year":"1994","journal-title":"J. Biol. Chem"},{"key":"10.1006\/jmbi.2000.3537_BIB15","series-title":"Venom Phospholipase A2 Enzymes. Structure, Function and Mechanism","first-page":"29","article-title":"Molecular biology of snake venom phospholipases A2","author":"Danse","year":"1997"},{"key":"10.1006\/jmbi.2000.3537_BIB16","series-title":"The Enzymes","doi-asserted-by":"crossref","first-page":"307","DOI":"10.1016\/S1874-6047(08)60307-8","author":"Dennis","year":"1983"},{"key":"10.1006\/jmbi.2000.3537_BIB17","doi-asserted-by":"crossref","first-page":"604","DOI":"10.1038\/289604a0","article-title":"Active site and catalytic mechanism of phospholipase A2","volume":"289","author":"Dijkstra","year":"1981","journal-title":"Nature"},{"key":"10.1006\/jmbi.2000.3537_BIB18","doi-asserted-by":"crossref","first-page":"97","DOI":"10.1016\/0022-2836(81)90081-4","article-title":"Structure of bovine pancreatic phospholipase A2 at 1.7 \u00c5 resolution","volume":"147","author":"Dijkstra","year":"1981","journal-title":"J. Mol. Biol"},{"key":"10.1006\/jmbi.2000.3537_BIB19","doi-asserted-by":"crossref","first-page":"163","DOI":"10.1016\/S0022-2836(83)80328-3","article-title":"Structure of porcine pancreatic phospholipase A2 at 2.6 \u00c5 resolution and comparison with bovine phospholipase A2","volume":"168","author":"Dijkstra","year":"1983","journal-title":"J. Mol. Biol"},{"key":"10.1006\/jmbi.2000.3537_BIB20","doi-asserted-by":"crossref","first-page":"545","DOI":"10.1111\/j.1432-1033.1983.tb07860.x","article-title":"Classification of phospholipases A2 according to sequence. Evolutionary and pharmacological implications","volume":"137","author":"Dufton","year":"1983","journal-title":"Eur. J. Biochem"},{"key":"10.1006\/jmbi.2000.3537_BIB21","doi-asserted-by":"crossref","first-page":"392","DOI":"10.1107\/S0108767391001071","article-title":"Accurate bond and angle parameters for X-ray protein structure refinement","volume":"47","author":"Engh","year":"1991","journal-title":"Acta Crystallog. sect. A"},{"key":"10.1006\/jmbi.2000.3537_BIB22","doi-asserted-by":"crossref","first-page":"342","DOI":"10.1073\/pnas.90.1.342","article-title":"Crystal structure of phospholipase A2 from Indian cobra reveals a trimeric association","volume":"90","author":"Fremont","year":"1993","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"10.1006\/jmbi.2000.3537_BIB23","doi-asserted-by":"crossref","first-page":"665","DOI":"10.1016\/0041-0101(94)90336-0","article-title":"Primary sequence determination of the most basic myonecrotic phospholipase A2 from venom of Vipera russelli","volume":"32","author":"Godwa","year":"1994","journal-title":"Toxicon"},{"key":"10.1006\/jmbi.2000.3537_BIB24","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1111\/j.1432-1033.1989.tb15172.x","article-title":"Purification and characterization of five variants of phospholipase A2 and complete primary structure of the main phospholipase A2 variant in Heloderma suspectum (Gila monster) venom","volume":"186","author":"Gomez","year":"1989","journal-title":"Eur. J. Biochem"},{"key":"10.1006\/jmbi.2000.3537_BIB25","doi-asserted-by":"crossref","first-page":"3573","DOI":"10.1074\/jbc.272.6.3573","article-title":"Structural aspects of interfacial adsorption. A crystallographic and site-directed mutagenesis study of the phospholipase A2 from the venom of Agkistrodon piscivorus piscivorus","volume":"272","author":"Han","year":"1997","journal-title":"J. Biol. Chem"},{"key":"10.1006\/jmbi.2000.3537_BIB26","series-title":"Snake Toxins","first-page":"91","article-title":"Phospholipases in snake venoms and their effects on nerve and muscle","author":"Harris","year":"1991"},{"key":"10.1006\/jmbi.2000.3537_BIB27","doi-asserted-by":"crossref","first-page":"201","DOI":"10.1016\/0076-6879(91)97146-P","article-title":"Dissection and sequence analysis of phospholipase A2","volume":"197","author":"Heinrikson","year":"1991","journal-title":"Methods Enzymol"},{"key":"10.1006\/jmbi.2000.3537_BIB28","doi-asserted-by":"crossref","first-page":"4913","DOI":"10.1016\/S0021-9258(17)40140-2","article-title":"Amino acid sequence of phospholipase A2-alpha from the venom of Crotalus adamanteus. A new classification of phospholipases A2 based upon structural determinants","volume":"252","author":"Heinrikson","year":"1977","journal-title":"J. Biol. Chem"},{"key":"10.1006\/jmbi.2000.3537_BIB29","doi-asserted-by":"crossref","first-page":"17649","DOI":"10.1016\/S0021-9258(18)38213-9","article-title":"The crystal structure of a lysine 49 phospholipase A2 from the venom of the cottonmouth snake at 2.0 \u00c5 resolution","volume":"265","author":"Holland","year":"1990","journal-title":"J. Biol. Chem"},{"key":"10.1006\/jmbi.2000.3537_BIB30","doi-asserted-by":"crossref","first-page":"110","DOI":"10.1107\/S0108767390010224","article-title":"Improved methods for building models in electron density maps and the location of errors in these models","volume":"47","author":"Jones","year":"1991","journal-title":"Acta Crystallog. sect. A"},{"key":"10.1006\/jmbi.2000.3537_BIB31","doi-asserted-by":"crossref","first-page":"916","DOI":"10.1107\/S0021889888007903","article-title":"Evaluation of a single-crystal X-ray diffraction data from a position-sensitive detector","volume":"21","author":"Kabsch","year":"1988","journal-title":"J. Appl. Crystallog"},{"key":"10.1006\/jmbi.2000.3537_BIB32","doi-asserted-by":"crossref","first-page":"8602","DOI":"10.1016\/S0021-9258(19)68887-3","article-title":"The 2.5 \u00c5 crystal structure of a dimeric phospholipase A2 from the venom of Crotalus atrox","volume":"256","author":"Keith","year":"1981","journal-title":"J. Biol. Chem"},{"key":"10.1006\/jmbi.2000.3537_BIB33","series-title":"Venom Phospholipase A2 Enzymes. Structure, Function and Mechanism","first-page":"7","article-title":"Phospholipase A2 - A complex multifunctional protein puzzle","author":"Kini","year":"1997"},{"key":"10.1006\/jmbi.2000.3537_BIB34","doi-asserted-by":"crossref","first-page":"14402","DOI":"10.1016\/S0021-9258(18)47808-8","article-title":"Structure-function relationships of phospholipases. The anticoagulant region of phospholipase A2","volume":"262","author":"Kini","year":"1987","journal-title":"J. Biol. Chem"},{"key":"10.1006\/jmbi.2000.3537_BIB35","doi-asserted-by":"crossref","first-page":"613","DOI":"10.1016\/0041-0101(89)90013-5","article-title":"A model to explain the pharmacological effects of snake venom phospholipase A2","volume":"27","author":"Kini","year":"1989","journal-title":"Toxicon"},{"key":"10.1006\/jmbi.2000.3537_BIB36","doi-asserted-by":"crossref","first-page":"826","DOI":"10.1107\/S0907444995014983","article-title":"xdlMAPMAN and xdlDATAMAN programs for reformatting, analysis and manipulating of biomacromolecular electron density maps and reflection data sets","volume":"52","author":"Kleywegt","year":"1996","journal-title":"Acta Crystallog. sect. D"},{"key":"10.1006\/jmbi.2000.3537_BIB37","doi-asserted-by":"crossref","first-page":"249","DOI":"10.1111\/j.1432-1033.1989.tb15014.x","article-title":"Analysis of the cDNA for phospholipase A2 from honeybee venom glands. The deduced amino acid sequence reveals homology to the corresponding vertebrate enzymes","volume":"184","author":"Kuchler","year":"1989","journal-title":"Eur. J. Biochem"},{"key":"10.1006\/jmbi.2000.3537_BIB38","doi-asserted-by":"crossref","first-page":"1109","DOI":"10.1016\/S0969-2126(01)00246-5","article-title":"Structure of beta 2-bungarotoxin","volume":"3","author":"Kwong","year":"1995","journal-title":"Structure"},{"key":"10.1006\/jmbi.2000.3537_BIB39","doi-asserted-by":"crossref","first-page":"283","DOI":"10.1107\/S0021889892009944","article-title":"PROCHECK","volume":"26","author":"Laskowski","year":"1993","journal-title":"J. Appl. Crystallog"},{"key":"10.1006\/jmbi.2000.3537_BIB40","doi-asserted-by":"crossref","first-page":"802","DOI":"10.1107\/S0365110X52002161","article-title":"Traitment Statistique des Errius dans la Determination des Structures Cristallinis","volume":"5","author":"Luzzati","year":"1952","journal-title":"Acta Crystallog"},{"key":"10.1006\/jmbi.2000.3537_BIB41","doi-asserted-by":"crossref","first-page":"3518","DOI":"10.1074\/jbc.270.8.3518","article-title":"Conodipine-M, a novel phospholipase A2 isolated from the venom of the marine snail Conus magus","volume":"270","author":"McIntosh","year":"1995","journal-title":"J. Biol. Chem"},{"key":"10.1006\/jmbi.2000.3537_BIB42","doi-asserted-by":"crossref","first-page":"157","DOI":"10.1107\/S0108767393007597","article-title":"AmoRe","volume":"50","author":"Navaza","year":"1994","journal-title":"Acta Crystallog"},{"key":"10.1006\/jmbi.2000.3537_BIB43","series-title":"Proceedings of the CCP4 Study Weekened","first-page":"56","article-title":"Oscillation data reduction program","author":"Otwinowski","year":"1993"},{"key":"10.1006\/jmbi.2000.3537_BIB44","doi-asserted-by":"crossref","first-page":"223","DOI":"10.1016\/0167-4838(93)90217-F","article-title":"Studies on the sub-unit structure of textilotoxin, a potent pre-synaptic neurotoxin from the venom of the Australian commom brown snake (Pseudonaja textilis). 3. The complete amino-acid sequence of all the subunits","volume":"1161","author":"Pearson","year":"1993","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1006\/jmbi.2000.3537_BIB45","doi-asserted-by":"crossref","first-page":"573","DOI":"10.1016\/S0014-5793(97)00853-3","article-title":"Crystal structure of vipoxin at 2.0 \u00c5","volume":"412","author":"Perbandt","year":"1997","journal-title":"FEBS Letters"},{"key":"10.1006\/jmbi.2000.3537_BIB46","doi-asserted-by":"crossref","first-page":"283","DOI":"10.1016\/S0065-3233(08)60402-7","article-title":"Conformation of polypeptides and proteins","volume":"23","author":"Ramachandran","year":"1968","journal-title":"Advan. Protein Chem"},{"key":"10.1006\/jmbi.2000.3537_BIB47","doi-asserted-by":"crossref","first-page":"11627","DOI":"10.1016\/S0021-9258(17)39077-4","article-title":"A comparison of the crystal structures of phospholipase A2 from bovine pancreas and Crotalus atrox venom","volume":"260","author":"Renetseder","year":"1985","journal-title":"J. Biol. Chem"},{"key":"10.1006\/jmbi.2000.3537_BIB48","doi-asserted-by":"crossref","first-page":"1541","DOI":"10.1126\/science.2274785","article-title":"Interfacial catalysis","volume":"250","author":"Scott","year":"1990","journal-title":"Science"},{"key":"10.1006\/jmbi.2000.3537_BIB49","doi-asserted-by":"crossref","first-page":"22645","DOI":"10.1016\/S0021-9258(18)41721-8","article-title":"Crystallographical and biochemical studies of the (inactive) Lys49 phospholipase A2 from the venom of Agkistrodon piscivorus piscivorus","volume":"267","author":"Scott","year":"1992","journal-title":"J. Biol. Chem"},{"key":"10.1006\/jmbi.2000.3537_BIB50","doi-asserted-by":"crossref","first-page":"2927","DOI":"10.1021\/bi00358a029","article-title":"Biochemical characterization of the phospholipase A2 purified from the venom of the Mexican beaded lizard (Heloderma horridum horridumWiegmann)","volume":"25","author":"Sosa","year":"1986","journal-title":"Biochemistry"},{"key":"10.1006\/jmbi.2000.3537_BIB51","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1006\/jmbi.1998.1987","article-title":"Crystal structure of Agkistrodotoxin, a phospholipase A2-type presynaptic neurotoxin from Agkistrodon halys pallas","volume":"282","author":"Tang","year":"1998","journal-title":"J. Mol. Biol"},{"key":"10.1006\/jmbi.2000.3537_BIB52","doi-asserted-by":"crossref","first-page":"99","DOI":"10.1016\/0041-0101(95)00114-X","article-title":"Two types of Russell\u2019s viper revealed by variation in phospholipases A2 from venom of the subspecies","volume":"34","author":"Tsai","year":"1996","journal-title":"Toxicon"},{"key":"10.1006\/jmbi.2000.3537_BIB53","doi-asserted-by":"crossref","first-page":"669","DOI":"10.1006\/jmbi.1996.0054","article-title":"Crystal structure of an acidic phospholipase A2 from the venom of Agkistrodon halys pallas at 2.0 \u00c5 resolution","volume":"255","author":"Wang","year":"1996","journal-title":"J. Mol. Biol"},{"key":"10.1006\/jmbi.2000.3537_BIB54","doi-asserted-by":"crossref","first-page":"159","DOI":"10.1016\/0014-5793(92)81238-H","article-title":"The three-dimensional structure of notexin, a presynaptic neurotoxic phospholipase A2 at 2.0 \u00c5 resolution","volume":"301","author":"Westerlund","year":"1992","journal-title":"FEBS Letters"},{"key":"10.1006\/jmbi.2000.3537_BIB55","doi-asserted-by":"crossref","first-page":"125","DOI":"10.3109\/15569549409089958","article-title":"Structure-function relationship of phospholipase A2 from snake venoms","volume":"13","author":"Yang","year":"1994","journal-title":"J. Toxicol. Toxin Rev"},{"key":"10.1006\/jmbi.2000.3537_BIB56","doi-asserted-by":"crossref","first-page":"6082","DOI":"10.1021\/bi00477a028","article-title":"Kinetic and inhibition studies of phospholipase A2 with short-chain substrates and inhibitors","volume":"29","author":"Yuan","year":"1990","journal-title":"Biochemistry"},{"key":"10.1006\/jmbi.2000.3537_BIB57","doi-asserted-by":"crossref","first-page":"510","DOI":"10.1107\/S0907444997013644","article-title":"Structure of a basic phospholipase A2 from Agkistrodon halys Pallas at 2.13 \u00c5 resolution","volume":"54","author":"Zhao","year":"1998","journal-title":"Acta Crystallog. sect. D"},{"key":"10.1006\/jmbi.2000.3537_BIB58","doi-asserted-by":"crossref","first-page":"12","DOI":"10.1002\/(SICI)1097-0134(199605)25:1<12::AID-PROT2>3.0.CO;2-M","article-title":"Molecular dynamics study of phospholipase A2 on a membrane surface","volume":"25","author":"Zhou","year":"1996","journal-title":"Proteins: Struct. Funct. Genet"}],"container-title":["Journal of Molecular Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S002228360093537X?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S002228360093537X?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2021,5,3]],"date-time":"2021-05-03T10:04:03Z","timestamp":1620036243000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S002228360093537X"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2000,3]]},"references-count":58,"journal-issue":{"issue":"4","published-print":{"date-parts":[[2000,3]]}},"alternative-id":["S002228360093537X"],"URL":"https:\/\/doi.org\/10.1006\/jmbi.2000.3537","relation":{},"ISSN":["0022-2836"],"issn-type":[{"value":"0022-2836","type":"print"}],"subject":[],"published":{"date-parts":[[2000,3]]}}}