{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,4]],"date-time":"2025-10-04T01:39:12Z","timestamp":1759541952207,"version":"3.40.3"},"publisher-location":"New York, NY","reference-count":18,"publisher":"Springer US","isbn-type":[{"type":"print","value":"9781071604298"},{"type":"electronic","value":"9781071604304"}],"license":[{"start":{"date-parts":[[2020,1,1]],"date-time":"2020-01-01T00:00:00Z","timestamp":1577836800000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/www.springer.com\/tdm"}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2020]]},"DOI":"10.1007\/978-1-0716-0430-4_20","type":"book-chapter","created":{"date-parts":[[2020,4,18]],"date-time":"2020-04-18T06:02:37Z","timestamp":1587189757000},"page":"191-200","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":5,"title":["Functional Analysis of Botulinum Hemagglutinin (HA)"],"prefix":"10.1007","author":[{"given":"Takuhiro","family":"Matsumura","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Yukako","family":"Fujinaga","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"297","published-online":{"date-parts":[[2020,4,19]]},"reference":[{"key":"20_CR1","doi-asserted-by":"publisher","first-page":"717","DOI":"10.1152\/physrev.2000.80.2.717","volume":"80","author":"G Schiavo","year":"2000","unstructured":"Schiavo G, Matteoli M, Montecucco C (2000) Neurotoxins affecting neuroexocytosis. Physiol Rev 80:717\u2013766","journal-title":"Physiol Rev"},{"key":"20_CR2","doi-asserted-by":"publisher","first-page":"535","DOI":"10.1038\/nrmicro3295","volume":"12","author":"O Rossetto","year":"2014","unstructured":"Rossetto O, Pirazzini M, Montecucco C (2014) Botulinum neurotoxins: genetic, structural and mechanistic insights. Nat Rev Microbial 12:535\u2013549","journal-title":"Nat Rev Microbial"},{"key":"20_CR3","doi-asserted-by":"publisher","first-page":"165","DOI":"10.1016\/0163-7258(82)90061-4","volume":"19","author":"G Sakaguchi","year":"1982","unstructured":"Sakaguchi G (1982) Clostridium botulinum toxins. Pharmacol Ther 19:165\u2013194","journal-title":"Pharmacol Ther"},{"key":"20_CR4","first-page":"45","volume":"364","author":"Y Fujinaga","year":"2013","unstructured":"Fujinaga Y, Sugawara Y, Matsumura T (2013) Uptake of botulinum neurotoxin in the intestine. Curr Top Microbiol Immunol 364:45\u201359","journal-title":"Curr Top Microbiol Immunol"},{"key":"20_CR5","doi-asserted-by":"publisher","first-page":"977","DOI":"10.1126\/science.1214270","volume":"335","author":"S Gu","year":"2012","unstructured":"Gu S, Rumpel S, Zhou J, Strotmeier J, Bigalke H et al (2012) Botulinum neurotoxin is shielded by NTNHA in an interlocked complex. Science 335:977\u2013981","journal-title":"Science"},{"key":"20_CR6","doi-asserted-by":"publisher","first-page":"5630","DOI":"10.1073\/pnas.1222139110","volume":"110","author":"DA Benefield","year":"2013","unstructured":"Benefield DA, Dessain SK, Shine N, Ohi MD, Lacy DB (2013) Molecular assembly of botulinum neurotoxin progenitor complexes. Proc Natl Acad Sci U S A 110:5630\u20135635","journal-title":"Proc Natl Acad Sci U S A"},{"key":"20_CR7","doi-asserted-by":"publisher","first-page":"e1003690","DOI":"10.1371\/journal.ppat.1003690","volume":"9","author":"K Lee","year":"2013","unstructured":"Lee K, Gu S, Jin L, Le TT CLW et al (2013) Structure of a bimodular botulinum neurotoxin complex provides insights into its oral toxicity. PLoS Pathog 9:e1003690","journal-title":"PLoS Pathog"},{"key":"20_CR8","doi-asserted-by":"publisher","first-page":"35617","DOI":"10.1074\/jbc.M113.521179","volume":"288","author":"S Amatsu","year":"2013","unstructured":"Amatsu S, Sugawara Y, Matsumura T, Kitadokoro K, Fujinaga Y (2013) Crystal structure of Clostridium botulinum whole hemagglutinin reveals a huge triskelion-shaped molecular complex. J Biol Chem 288:35617\u201335625","journal-title":"J Biol Chem"},{"key":"20_CR9","doi-asserted-by":"publisher","first-page":"3841","DOI":"10.1099\/00221287-143-12-3841","volume":"143","author":"Y Fujinaga","year":"1997","unstructured":"Fujinaga Y, Inoue K, Watanabe S et al (1997) The haemagglutinin of Clostridium botulinum type C progenitor toxin plays an essential role in binding of toxin to the epithelial cells of Guinea pig small intestine, leading to the efficient absorption of the toxin. Microbiology 143:3841\u20133847","journal-title":"Microbiology"},{"key":"20_CR10","doi-asserted-by":"crossref","unstructured":"Fujinaga Y, Inoue K, Nomura T et al (2000) Identification and characterization of functional subunits of Clostridium botulinum type A progenitor toxin involved in binding to intestinal microvilli and erythrocytes. FEBS Lett 467, 179:\u201383","DOI":"10.1016\/S0014-5793(00)01147-9"},{"key":"20_CR11","doi-asserted-by":"publisher","first-page":"1529","DOI":"10.1099\/mic.0.26805-0","volume":"150","author":"Y Fujinaga","year":"2004","unstructured":"Fujinaga Y, Inoue K, Watarai S et al (2004) Molecular characterization of binding subcomponents of Clostridium botulinum type C progenitor toxin for intestinal epithelial cells and erythrocytes. Microbiology 150:1529\u20131538","journal-title":"Microbiology"},{"key":"20_CR12","first-page":"355","volume":"10","author":"T Matsumura","year":"2008","unstructured":"Matsumura T, Jin Y, Kabumoto Y et al (2008) The HA proteins of botulinum toxin disrupt intestinal epithelial intercellular junctions to increase toxin absorption. Cell Microbiol 10:355\u2013364","journal-title":"Cell Microbiol"},{"key":"20_CR13","doi-asserted-by":"publisher","first-page":"35","DOI":"10.1099\/mic.0.021246-0","volume":"155","author":"Y Jin","year":"2009","unstructured":"Jin Y, Takegahara Y, Sugawara Y et al (2009) Disruption of the epithelial barrier by botulinum haemagglutinin (HA) proteins - differences in cell tropism and the mechanism of action between HA proteins of types A or B, and HA proteins of type C. Microbiology 155:35\u201345","journal-title":"Microbiology"},{"key":"20_CR14","doi-asserted-by":"publisher","first-page":"691","DOI":"10.1083\/jcb.200910119","volume":"189","author":"Y Sugawara","year":"2010","unstructured":"Sugawara Y, Matsumura T, Takegahara Y et al (2010) Botulinum hemagglutinin disrupts the intercellular epithelial barrier by directly binding E-cadherin. J Cell Biol 189:691\u2013700","journal-title":"J Cell Biol"},{"key":"20_CR15","doi-asserted-by":"publisher","first-page":"e111170","DOI":"10.1371\/journal.pone.0111170","volume":"9","author":"Y Sugawara","year":"2014","unstructured":"Sugawara Y, Yutani M, Amatsu S et al (2014) Functional dissection of the Clostridium botulinum type B hemagglutinin complex: identification of the carbohydrate and E-cadherin binding sites. PLoS One 9:e111170","journal-title":"PLoS One"},{"key":"20_CR16","doi-asserted-by":"publisher","first-page":"1405","DOI":"10.1126\/science.1253823","volume":"344","author":"K Lee","year":"2014","unstructured":"Lee K, Zhong X, Gu S, Kruel AM, Dorner MB et al (2014) Molecular basis for disruption of E-cadherin adhesion by botulinum neurotoxin a complex. Science 344:1405\u20131410","journal-title":"Science"},{"key":"20_CR17","doi-asserted-by":"crossref","unstructured":"Matsumura T, Sugawara Y, Yutani M, Amatsu S, Yagita H et al (2015) Botulinum toxin a complex exploits intestinal M cells to enter the host and exert neurotoxicity. Nat Commun \\: 6255","DOI":"10.1038\/ncomms7255"},{"key":"20_CR18","doi-asserted-by":"publisher","first-page":"80","DOI":"10.1111\/1348-0421.12565","volume":"62","author":"S Amatsu","year":"2018","unstructured":"Amatsu S, Matsumura T, Yutani M, Fujinaga Y (2018) Multivalency effects of hemagglutinin component of type B botulinum neurotoxin complex on epithelial barrier disruption. Microbiol Immunol 62:80\u201389","journal-title":"Microbiol Immunol"}],"container-title":["Methods in Molecular Biology","Lectin Purification and Analysis"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/link.springer.com\/content\/pdf\/10.1007\/978-1-0716-0430-4_20","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,9,30]],"date-time":"2023-09-30T02:45:25Z","timestamp":1696041925000},"score":1,"resource":{"primary":{"URL":"http:\/\/link.springer.com\/10.1007\/978-1-0716-0430-4_20"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2020]]},"ISBN":["9781071604298","9781071604304"],"references-count":18,"URL":"https:\/\/doi.org\/10.1007\/978-1-0716-0430-4_20","relation":{},"ISSN":["1064-3745","1940-6029"],"issn-type":[{"type":"print","value":"1064-3745"},{"type":"electronic","value":"1940-6029"}],"subject":[],"published":{"date-parts":[[2020]]},"assertion":[{"value":"19 April 2020","order":1,"name":"first_online","label":"First Online","group":{"name":"ChapterHistory","label":"Chapter History"}}]}}