dc.creator | Fogaca, AC | |
dc.creator | Almeida, IC | |
dc.creator | Eberlin, MN | |
dc.creator | Tanaka, AS | |
dc.creator | Bulet, P | |
dc.creator | Daffre, S | |
dc.date | 2006 | |
dc.date | APR | |
dc.date | 2014-11-17T11:55:03Z | |
dc.date | 2015-11-26T16:42:45Z | |
dc.date | 2014-11-17T11:55:03Z | |
dc.date | 2015-11-26T16:42:45Z | |
dc.date.accessioned | 2018-03-28T23:27:27Z | |
dc.date.available | 2018-03-28T23:27:27Z | |
dc.identifier | Peptides. Elsevier Science Inc, v. 27, n. 4, n. 667, n. 674, 2006. | |
dc.identifier | 0196-9781 | |
dc.identifier | WOS:000237047000009 | |
dc.identifier | 10.1016/j.peptides.2005.07.013 | |
dc.identifier | http://www.repositorio.unicamp.br/jspui/handle/REPOSIP/60888 | |
dc.identifier | http://www.repositorio.unicamp.br/handle/REPOSIP/60888 | |
dc.identifier | http://repositorio.unicamp.br/jspui/handle/REPOSIP/60888 | |
dc.identifier.uri | http://repositorioslatinoamericanos.uchile.cl/handle/2250/1273369 | |
dc.description | The presence of an effective immune response in the hemocoel of arthropods is essential for survival as it prevents the invasion of pathogens throughout the animal body. Antimicrobial peptides (AMPs) play an important role in this response by rapidly killing invading microorganisms. In this study, a novel cysteine-rich AMP has been isolated and characterized from the hemocytes of the cattle tick, Boophilus microplus. In addition to growth inhibition of Escherichia coli and Micrococcus luteus, the newly described AMP, designated ixodidin (derived from the Family Ixodidae), was found to exert proteolytic inhibitory activity against two exogenous serine proteinases, elastase and chymotrypsin. This is the first report of a molecule of an arachnid that has been shown to inhibit bacterial growth and proteinase activity. (c) 2005 Elsevier Inc. All rights reserved. | |
dc.description | 27 | |
dc.description | 4 | |
dc.description | 667 | |
dc.description | 674 | |
dc.language | en | |
dc.publisher | Elsevier Science Inc | |
dc.publisher | New York | |
dc.publisher | EUA | |
dc.relation | Peptides | |
dc.relation | Peptides | |
dc.rights | fechado | |
dc.rights | http://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy | |
dc.source | Web of Science | |
dc.subject | antimicrobial peptide | |
dc.subject | serine proteinase inhibitor | |
dc.subject | immune system | |
dc.subject | hemocyte | |
dc.subject | tick | |
dc.subject | Spider Acanthoscurria-gomesiana | |
dc.subject | Horseshoe-crab | |
dc.subject | Cellular-localization | |
dc.subject | Chymotrypsin Elastase | |
dc.subject | Insect Defensin | |
dc.subject | Innate Immunity | |
dc.subject | Cdna Cloning | |
dc.subject | Drosophila | |
dc.subject | Expression | |
dc.subject | Binding | |
dc.title | Ixodidin, a novel antimicrobial peptide from the hemocytes of the cattle tick Boophilus microplus with inhibitory activity against serine proteinases | |
dc.type | Artículos de revistas | |