{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,16]],"date-time":"2026-03-16T12:20:39Z","timestamp":1773663639189,"version":"3.50.1"},"reference-count":24,"publisher":"The Royal Society","issue":"1854","license":[{"start":{"date-parts":[[2017,5,3]],"date-time":"2017-05-03T00:00:00Z","timestamp":1493769600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/royalsociety.org\/journals\/ethics-policies\/data-sharing-mining\/"}],"content-domain":{"domain":["royalsocietypublishing.org"],"crossmark-restriction":true},"short-container-title":["Proc. R. Soc. B."],"published-print":{"date-parts":[[2017,5,17]]},"abstract":"<jats:p>\n            The phenylalanine\/tyrosine degradation pathway is frequently described as a catabolic pathway that funnels aromatic amino acids into citric acid cycle intermediates. Previously, we demonstrated that the accumulation of tyrosine generated during the hydrolysis of blood meal proteins in\n            <jats:italic>Rhodnius prolixus<\/jats:italic>\n            is potentially toxic, a harmful outcome that is prevented by the action of the first two enzymes in the tyrosine degradation pathway. In this work, we further evaluated the relevance of all other enzymes involved in phenylalanine\/tyrosine metabolism in the physiology of this insect. The knockdown of most of these enzymes produced a wide spectrum of distinct phenotypes associated with reproduction, development and nymph survival, demonstrating a highly pleiotropic role of tyrosine metabolism. The phenotypes obtained for two of these enzymes, homogentisate dioxygenase and fumarylacetoacetase, have never before been described in any arthropod. To our knowledge, this report is the first comprehensive gene-silencing analysis of an amino acid metabolism pathway in insects. Amino acid metabolism is exceptionally important in haematophagous arthropods due to their particular feeding behaviour.\n          <\/jats:p>","DOI":"10.1098\/rspb.2016.2607","type":"journal-article","created":{"date-parts":[[2017,5,3]],"date-time":"2017-05-03T09:10:44Z","timestamp":1493802644000},"page":"20162607","update-policy":"https:\/\/doi.org\/10.1098\/crossmark-policy","source":"Crossref","is-referenced-by-count":31,"title":["Developmental roles of tyrosine metabolism enzymes in the blood-sucking insect\n            <i>Rhodnius prolixus<\/i>"],"prefix":"10.1098","volume":"284","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-2266-9616","authenticated-orcid":false,"given":"Marcos","family":"Sterkel","sequence":"first","affiliation":[{"name":"Instituto de Bioqu\u00edmica M\u00e9dica Leopoldo de Meis, Universidade Federal do Rio de Janeiro, Rio de Janeiro 21941-902, Brazil"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Pedro L.","family":"Oliveira","sequence":"additional","affiliation":[{"name":"Instituto de Bioqu\u00edmica M\u00e9dica Leopoldo de Meis, Universidade Federal do Rio de Janeiro, Rio de Janeiro 21941-902, Brazil"},{"name":"Instituto Nacional de Ci\u00eancia e Tecnologia em Entomologia Molecular (INCT-EM), Rio de Janeiro, Brazil"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"175","published-online":{"date-parts":[[2017,5,3]]},"reference":[{"key":"e_1_3_6_2_2","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0084865"},{"key":"e_1_3_6_3_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.ibmb.2004.09.004"},{"key":"e_1_3_6_4_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.cub.2016.06.025"},{"key":"e_1_3_6_5_2","doi-asserted-by":"publisher","DOI":"10.1136\/bmj.3.5617.511-a"},{"key":"e_1_3_6_6_2","doi-asserted-by":"publisher","DOI":"10.1002\/ajmg.c.30092"},{"key":"e_1_3_6_7_2","first-page":"251","article-title":"The nature of the defect in tyrosine metabolism in alcaptonuria","volume":"230","author":"Du BN","year":"1957","journal-title":"J. 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