{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2023,9,6]],"date-time":"2023-09-06T05:20:33Z","timestamp":1693977633017},"reference-count":33,"publisher":"Oxford University Press (OUP)","issue":"5","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2014,3,1]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:p>Summary:\u2003Plasmodium falciparum (Pf)-mediated malaria is one of the most devastating diseases in the world, and the search for suitable antimalarial drugs remains an extraordinary challenge for scientists working in this area. Novel unconventional approaches could reveal new potential targets that may be useful for the treatment of malaria. We used a bioinformatics approach to analyze the entire genome of the Pf3D7 strain. Because the carbon (C-) content is a pivotal parameter that determines the hydrophobicity of a protein, which in turn controls protein folding and function, we analyzed the entire Pf3D7 proteome based on the gene\u2019s thymine (T)-controlled amino acid expression. Our data disclose a total of 14 proteins encoded by chromosome-4 and chromosome-9 that have an outstanding T-encoded and C-controlled hydrophobic character. The identification of these proteins could open new pivotal drug-targeting avenues.<\/jats:p>\n               <jats:p>Contact:\u2003klaus@hanyang.ac.kr<\/jats:p>\n               <jats:p>Supplementary information: \u00a0Supplementary data are available at Bioinformatics online.<\/jats:p>","DOI":"10.1093\/bioinformatics\/btt587","type":"journal-article","created":{"date-parts":[[2013,10,17]],"date-time":"2013-10-17T01:33:55Z","timestamp":1381973635000},"page":"597-600","source":"Crossref","is-referenced-by-count":2,"title":["Thymine distribution in genes provides novel insight into the functional significance of the proteome of the malaria parasite <i>Plasmodium falciparum<\/i> 3D7"],"prefix":"10.1093","volume":"30","author":[{"given":"Balamurugan","family":"Palanisamy","sequence":"first","affiliation":[{"name":"1 School of Biotechnology and Health Sciences, Karunya University, Karunya Nagar, Coimbatore 641114, Tamil Nadu, India and 2Graduate School of Biomedical Science and Engineering, Hanyang University, 222 Wangsimni-ro, Seongdong-gu, Seoul 133-791, Republic of Korea"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Rajasekaran","family":"Ekambaram","sequence":"additional","affiliation":[{"name":"1 School of Biotechnology and Health Sciences, Karunya University, Karunya Nagar, Coimbatore 641114, Tamil Nadu, India and 2Graduate School of Biomedical Science and Engineering, Hanyang University, 222 Wangsimni-ro, Seongdong-gu, Seoul 133-791, Republic of Korea"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Klaus","family":"Heese","sequence":"additional","affiliation":[{"name":"1 School of Biotechnology and Health Sciences, Karunya University, Karunya Nagar, Coimbatore 641114, Tamil Nadu, India and 2Graduate School of Biomedical Science and Engineering, Hanyang University, 222 Wangsimni-ro, Seongdong-gu, Seoul 133-791, Republic of Korea"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"286","published-online":{"date-parts":[[2013,10,15]]},"reference":[{"key":"2023012710430059300_btt587-B1","doi-asserted-by":"crossref","first-page":"225","DOI":"10.1529\/biophysj.106.098004","article-title":"Hydrophobic, hydrophilic, and charged amino acid networks within protein","volume":"93","author":"Aftabuddin","year":"2007","journal-title":"Biophys. 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