Quantitative proteome and phosphoproteome analyses highlight the adherent population during Trypanosoma cruzi metacyclogenesis
Trypanosoma cruzi metacyclogenesis is a natural process that occurs inside the triatomine vector and corresponds to the differentiation of non-infective epimastigotes into infective metacyclic trypomastigotes. The biochemical alterations necessary for the differentiation process have been widely stu...
Gespeichert in:
| Veröffentlicht in: | Scientific reports 2017-08, Vol.7 (1), p.9899-12, Article 9899 |
|---|---|
| Hauptverfasser: | , , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 12 |
|---|---|
| container_issue | 1 |
| container_start_page | 9899 |
| container_title | Scientific reports |
| container_volume | 7 |
| creator | Amorim, Juliana C. Batista, Michel da Cunha, Elizabeth S. Lucena, Aline C. R. Lima, Carla V. de Paula Sousa, Karla Krieger, Marco A. Marchini, Fabricio K. |
| description | Trypanosoma cruzi
metacyclogenesis is a natural process that occurs inside the triatomine vector and corresponds to the differentiation of non-infective epimastigotes into infective metacyclic trypomastigotes. The biochemical alterations necessary for the differentiation process have been widely studied with a focus on adhesion and nutritional stress. Here, using a mass spectrometry approach, a large-scale phospho(proteome) study was performed with the aim of understanding the metacyclogenesis processes in a quantitative manner. The results indicate that major modulations in the phospho(proteome) occur under nutritional stress and after 12 and 24 h of adhesion. Significant changes involve key cellular processes, such as translation, oxidative stress, and the metabolism of macromolecules, including proteins, lipids, and carbohydrates. Analysis of the signalling triggered by kinases and phosphatases from 7,336 identified phosphorylation sites demonstrates that 260 of these sites are modulated throughout the differentiation process, and some of these modulated proteins have previously been identified as drug targets in trypanosomiasis treatment. To the best of our knowledge, this study provides the first quantitative results highlighting the modulation of phosphorylation sites during metacyclogenesis and the greater coverage of the proteome to the parasite during this process. The data are available via ProteomeXchange with identifier number PXD006171. |
| doi_str_mv | 10.1038/s41598-017-10292-3 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_5574995</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>1933944226</sourcerecordid><originalsourceid>FETCH-LOGICAL-c474t-44a42e6af2895d2c15c5358bc838ffd3d468a1f8463bf1c525be57f844590de83</originalsourceid><addsrcrecordid>eNp1kU1rHSEUhqW0NCHNH8iiCN10M62fM7oplNAvCJRAshavc-aOYUan6gRuF_3t9fam4bYQ4aAen_N69EXogpJ3lHD1PgsqtWoI7RpKmGYNf4ZOGRGyYZyx50frE3Se8x2pQzItqH6JTphSkhGlTtGv69WG4ost_h7wkmKBOAO2ocfLGHONo5yddhkyHv12nGoUXMaa7kdIEApe4rJOVScG3K_Jhy2-SbvFhpjjbLFL60-PZyjW7dwUtxAg-_wKvRjslOH8YT5Dt58_3Vx-ba6-f_l2-fGqcaITpRHCCgatHZjSsmeOSie5VBunuBqGnveiVZYOSrR8M1AnmdyA7OpeSE16UPwMfTjoLutmht7VfpOdzJL8bNPOROvNvyfBj2Yb742UndBaVoG3DwIp_lghFzP77GCabIC4ZkM151oIxtqKvvkPvYtrqp-3p2SnWsGkrhQ7UC7FnBMMj81QYvYOm4PDpjps_jhseC16ffyMx5K_flaAH4C87B2AdHT307K_AcWcteU</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1957864259</pqid></control><display><type>article</type><title>Quantitative proteome and phosphoproteome analyses highlight the adherent population during Trypanosoma cruzi metacyclogenesis</title><source>MEDLINE</source><source>DOAJ Directory of Open Access Journals</source><source>Springer Nature OA Free Journals</source><source>Nature Free</source><source>EZB-FREE-00999 freely available EZB journals</source><source>PubMed Central</source><source>Free Full-Text Journals in Chemistry</source><creator>Amorim, Juliana C. ; Batista, Michel ; da Cunha, Elizabeth S. ; Lucena, Aline C. R. ; Lima, Carla V. de Paula ; Sousa, Karla ; Krieger, Marco A. ; Marchini, Fabricio K.</creator><creatorcontrib>Amorim, Juliana C. ; Batista, Michel ; da Cunha, Elizabeth S. ; Lucena, Aline C. R. ; Lima, Carla V. de Paula ; Sousa, Karla ; Krieger, Marco A. ; Marchini, Fabricio K.</creatorcontrib><description>Trypanosoma cruzi
metacyclogenesis is a natural process that occurs inside the triatomine vector and corresponds to the differentiation of non-infective epimastigotes into infective metacyclic trypomastigotes. The biochemical alterations necessary for the differentiation process have been widely studied with a focus on adhesion and nutritional stress. Here, using a mass spectrometry approach, a large-scale phospho(proteome) study was performed with the aim of understanding the metacyclogenesis processes in a quantitative manner. The results indicate that major modulations in the phospho(proteome) occur under nutritional stress and after 12 and 24 h of adhesion. Significant changes involve key cellular processes, such as translation, oxidative stress, and the metabolism of macromolecules, including proteins, lipids, and carbohydrates. Analysis of the signalling triggered by kinases and phosphatases from 7,336 identified phosphorylation sites demonstrates that 260 of these sites are modulated throughout the differentiation process, and some of these modulated proteins have previously been identified as drug targets in trypanosomiasis treatment. To the best of our knowledge, this study provides the first quantitative results highlighting the modulation of phosphorylation sites during metacyclogenesis and the greater coverage of the proteome to the parasite during this process. The data are available via ProteomeXchange with identifier number PXD006171.</description><identifier>ISSN: 2045-2322</identifier><identifier>EISSN: 2045-2322</identifier><identifier>DOI: 10.1038/s41598-017-10292-3</identifier><identifier>PMID: 28852088</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>101/58 ; 631/1647/296 ; 631/337/475 ; 631/337/475/2290 ; Adhesion ; Carbohydrates ; Cytoskeleton - metabolism ; Epimastigotes ; Humanities and Social Sciences ; Kinases ; Life Cycle Stages ; Lipid metabolism ; Lipids ; Macromolecules ; Mass spectrometry ; Mass spectroscopy ; multidisciplinary ; Nutrient deficiency ; Oxidative metabolism ; Oxidative stress ; Parasites ; Phosphoproteins - chemistry ; Phosphoproteins - metabolism ; Phosphorylation ; Protein Biosynthesis ; Proteome ; Proteomes ; Protozoa ; Protozoan Proteins - chemistry ; Protozoan Proteins - metabolism ; Science ; Science (multidisciplinary) ; Trypanosoma cruzi ; Trypanosoma cruzi - physiology ; Trypanosomiasis ; Trypomastigotes ; Vector-borne diseases</subject><ispartof>Scientific reports, 2017-08, Vol.7 (1), p.9899-12, Article 9899</ispartof><rights>The Author(s) 2017</rights><rights>2017. This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c474t-44a42e6af2895d2c15c5358bc838ffd3d468a1f8463bf1c525be57f844590de83</citedby><cites>FETCH-LOGICAL-c474t-44a42e6af2895d2c15c5358bc838ffd3d468a1f8463bf1c525be57f844590de83</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5574995/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5574995/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,864,885,27924,27925,41120,42189,51576,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/28852088$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Amorim, Juliana C.</creatorcontrib><creatorcontrib>Batista, Michel</creatorcontrib><creatorcontrib>da Cunha, Elizabeth S.</creatorcontrib><creatorcontrib>Lucena, Aline C. R.</creatorcontrib><creatorcontrib>Lima, Carla V. de Paula</creatorcontrib><creatorcontrib>Sousa, Karla</creatorcontrib><creatorcontrib>Krieger, Marco A.</creatorcontrib><creatorcontrib>Marchini, Fabricio K.</creatorcontrib><title>Quantitative proteome and phosphoproteome analyses highlight the adherent population during Trypanosoma cruzi metacyclogenesis</title><title>Scientific reports</title><addtitle>Sci Rep</addtitle><addtitle>Sci Rep</addtitle><description>Trypanosoma cruzi
metacyclogenesis is a natural process that occurs inside the triatomine vector and corresponds to the differentiation of non-infective epimastigotes into infective metacyclic trypomastigotes. The biochemical alterations necessary for the differentiation process have been widely studied with a focus on adhesion and nutritional stress. Here, using a mass spectrometry approach, a large-scale phospho(proteome) study was performed with the aim of understanding the metacyclogenesis processes in a quantitative manner. The results indicate that major modulations in the phospho(proteome) occur under nutritional stress and after 12 and 24 h of adhesion. Significant changes involve key cellular processes, such as translation, oxidative stress, and the metabolism of macromolecules, including proteins, lipids, and carbohydrates. Analysis of the signalling triggered by kinases and phosphatases from 7,336 identified phosphorylation sites demonstrates that 260 of these sites are modulated throughout the differentiation process, and some of these modulated proteins have previously been identified as drug targets in trypanosomiasis treatment. To the best of our knowledge, this study provides the first quantitative results highlighting the modulation of phosphorylation sites during metacyclogenesis and the greater coverage of the proteome to the parasite during this process. The data are available via ProteomeXchange with identifier number PXD006171.</description><subject>101/58</subject><subject>631/1647/296</subject><subject>631/337/475</subject><subject>631/337/475/2290</subject><subject>Adhesion</subject><subject>Carbohydrates</subject><subject>Cytoskeleton - metabolism</subject><subject>Epimastigotes</subject><subject>Humanities and Social Sciences</subject><subject>Kinases</subject><subject>Life Cycle Stages</subject><subject>Lipid metabolism</subject><subject>Lipids</subject><subject>Macromolecules</subject><subject>Mass spectrometry</subject><subject>Mass spectroscopy</subject><subject>multidisciplinary</subject><subject>Nutrient deficiency</subject><subject>Oxidative metabolism</subject><subject>Oxidative stress</subject><subject>Parasites</subject><subject>Phosphoproteins - chemistry</subject><subject>Phosphoproteins - metabolism</subject><subject>Phosphorylation</subject><subject>Protein Biosynthesis</subject><subject>Proteome</subject><subject>Proteomes</subject><subject>Protozoa</subject><subject>Protozoan Proteins - chemistry</subject><subject>Protozoan Proteins - metabolism</subject><subject>Science</subject><subject>Science (multidisciplinary)</subject><subject>Trypanosoma cruzi</subject><subject>Trypanosoma cruzi - physiology</subject><subject>Trypanosomiasis</subject><subject>Trypomastigotes</subject><subject>Vector-borne diseases</subject><issn>2045-2322</issn><issn>2045-2322</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><sourceid>C6C</sourceid><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNp1kU1rHSEUhqW0NCHNH8iiCN10M62fM7oplNAvCJRAshavc-aOYUan6gRuF_3t9fam4bYQ4aAen_N69EXogpJ3lHD1PgsqtWoI7RpKmGYNf4ZOGRGyYZyx50frE3Se8x2pQzItqH6JTphSkhGlTtGv69WG4ost_h7wkmKBOAO2ocfLGHONo5yddhkyHv12nGoUXMaa7kdIEApe4rJOVScG3K_Jhy2-SbvFhpjjbLFL60-PZyjW7dwUtxAg-_wKvRjslOH8YT5Dt58_3Vx-ba6-f_l2-fGqcaITpRHCCgatHZjSsmeOSie5VBunuBqGnveiVZYOSrR8M1AnmdyA7OpeSE16UPwMfTjoLutmht7VfpOdzJL8bNPOROvNvyfBj2Yb742UndBaVoG3DwIp_lghFzP77GCabIC4ZkM151oIxtqKvvkPvYtrqp-3p2SnWsGkrhQ7UC7FnBMMj81QYvYOm4PDpjps_jhseC16ffyMx5K_flaAH4C87B2AdHT307K_AcWcteU</recordid><startdate>20170829</startdate><enddate>20170829</enddate><creator>Amorim, Juliana C.</creator><creator>Batista, Michel</creator><creator>da Cunha, Elizabeth S.</creator><creator>Lucena, Aline C. R.</creator><creator>Lima, Carla V. de Paula</creator><creator>Sousa, Karla</creator><creator>Krieger, Marco A.</creator><creator>Marchini, Fabricio K.</creator><general>Nature Publishing Group UK</general><general>Nature Publishing Group</general><scope>C6C</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7P</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20170829</creationdate><title>Quantitative proteome and phosphoproteome analyses highlight the adherent population during Trypanosoma cruzi metacyclogenesis</title><author>Amorim, Juliana C. ; Batista, Michel ; da Cunha, Elizabeth S. ; Lucena, Aline C. R. ; Lima, Carla V. de Paula ; Sousa, Karla ; Krieger, Marco A. ; Marchini, Fabricio K.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c474t-44a42e6af2895d2c15c5358bc838ffd3d468a1f8463bf1c525be57f844590de83</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2017</creationdate><topic>101/58</topic><topic>631/1647/296</topic><topic>631/337/475</topic><topic>631/337/475/2290</topic><topic>Adhesion</topic><topic>Carbohydrates</topic><topic>Cytoskeleton - metabolism</topic><topic>Epimastigotes</topic><topic>Humanities and Social Sciences</topic><topic>Kinases</topic><topic>Life Cycle Stages</topic><topic>Lipid metabolism</topic><topic>Lipids</topic><topic>Macromolecules</topic><topic>Mass spectrometry</topic><topic>Mass spectroscopy</topic><topic>multidisciplinary</topic><topic>Nutrient deficiency</topic><topic>Oxidative metabolism</topic><topic>Oxidative stress</topic><topic>Parasites</topic><topic>Phosphoproteins - chemistry</topic><topic>Phosphoproteins - metabolism</topic><topic>Phosphorylation</topic><topic>Protein Biosynthesis</topic><topic>Proteome</topic><topic>Proteomes</topic><topic>Protozoa</topic><topic>Protozoan Proteins - chemistry</topic><topic>Protozoan Proteins - metabolism</topic><topic>Science</topic><topic>Science (multidisciplinary)</topic><topic>Trypanosoma cruzi</topic><topic>Trypanosoma cruzi - physiology</topic><topic>Trypanosomiasis</topic><topic>Trypomastigotes</topic><topic>Vector-borne diseases</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Amorim, Juliana C.</creatorcontrib><creatorcontrib>Batista, Michel</creatorcontrib><creatorcontrib>da Cunha, Elizabeth S.</creatorcontrib><creatorcontrib>Lucena, Aline C. R.</creatorcontrib><creatorcontrib>Lima, Carla V. de Paula</creatorcontrib><creatorcontrib>Sousa, Karla</creatorcontrib><creatorcontrib>Krieger, Marco A.</creatorcontrib><creatorcontrib>Marchini, Fabricio K.</creatorcontrib><collection>Springer Nature OA Free Journals</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Science Database</collection><collection>Biological Science Database</collection><collection>Publicly Available Content Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Scientific reports</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Amorim, Juliana C.</au><au>Batista, Michel</au><au>da Cunha, Elizabeth S.</au><au>Lucena, Aline C. R.</au><au>Lima, Carla V. de Paula</au><au>Sousa, Karla</au><au>Krieger, Marco A.</au><au>Marchini, Fabricio K.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Quantitative proteome and phosphoproteome analyses highlight the adherent population during Trypanosoma cruzi metacyclogenesis</atitle><jtitle>Scientific reports</jtitle><stitle>Sci Rep</stitle><addtitle>Sci Rep</addtitle><date>2017-08-29</date><risdate>2017</risdate><volume>7</volume><issue>1</issue><spage>9899</spage><epage>12</epage><pages>9899-12</pages><artnum>9899</artnum><issn>2045-2322</issn><eissn>2045-2322</eissn><abstract>Trypanosoma cruzi
metacyclogenesis is a natural process that occurs inside the triatomine vector and corresponds to the differentiation of non-infective epimastigotes into infective metacyclic trypomastigotes. The biochemical alterations necessary for the differentiation process have been widely studied with a focus on adhesion and nutritional stress. Here, using a mass spectrometry approach, a large-scale phospho(proteome) study was performed with the aim of understanding the metacyclogenesis processes in a quantitative manner. The results indicate that major modulations in the phospho(proteome) occur under nutritional stress and after 12 and 24 h of adhesion. Significant changes involve key cellular processes, such as translation, oxidative stress, and the metabolism of macromolecules, including proteins, lipids, and carbohydrates. Analysis of the signalling triggered by kinases and phosphatases from 7,336 identified phosphorylation sites demonstrates that 260 of these sites are modulated throughout the differentiation process, and some of these modulated proteins have previously been identified as drug targets in trypanosomiasis treatment. To the best of our knowledge, this study provides the first quantitative results highlighting the modulation of phosphorylation sites during metacyclogenesis and the greater coverage of the proteome to the parasite during this process. The data are available via ProteomeXchange with identifier number PXD006171.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>28852088</pmid><doi>10.1038/s41598-017-10292-3</doi><tpages>12</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 2045-2322 |
| ispartof | Scientific reports, 2017-08, Vol.7 (1), p.9899-12, Article 9899 |
| issn | 2045-2322 2045-2322 |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_5574995 |
| source | MEDLINE; DOAJ Directory of Open Access Journals; Springer Nature OA Free Journals; Nature Free; EZB-FREE-00999 freely available EZB journals; PubMed Central; Free Full-Text Journals in Chemistry |
| subjects | 101/58 631/1647/296 631/337/475 631/337/475/2290 Adhesion Carbohydrates Cytoskeleton - metabolism Epimastigotes Humanities and Social Sciences Kinases Life Cycle Stages Lipid metabolism Lipids Macromolecules Mass spectrometry Mass spectroscopy multidisciplinary Nutrient deficiency Oxidative metabolism Oxidative stress Parasites Phosphoproteins - chemistry Phosphoproteins - metabolism Phosphorylation Protein Biosynthesis Proteome Proteomes Protozoa Protozoan Proteins - chemistry Protozoan Proteins - metabolism Science Science (multidisciplinary) Trypanosoma cruzi Trypanosoma cruzi - physiology Trypanosomiasis Trypomastigotes Vector-borne diseases |
| title | Quantitative proteome and phosphoproteome analyses highlight the adherent population during Trypanosoma cruzi metacyclogenesis |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-24T19%3A18%3A12IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Quantitative%20proteome%20and%20phosphoproteome%20analyses%20highlight%20the%20adherent%20population%20during%20Trypanosoma%20cruzi%20metacyclogenesis&rft.jtitle=Scientific%20reports&rft.au=Amorim,%20Juliana%20C.&rft.date=2017-08-29&rft.volume=7&rft.issue=1&rft.spage=9899&rft.epage=12&rft.pages=9899-12&rft.artnum=9899&rft.issn=2045-2322&rft.eissn=2045-2322&rft_id=info:doi/10.1038/s41598-017-10292-3&rft_dat=%3Cproquest_pubme%3E1933944226%3C/proquest_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1957864259&rft_id=info:pmid/28852088&rfr_iscdi=true |