يعرض 1 - 10 نتائج من 252 نتيجة بحث عن '"Nardone A."', وقت الاستعلام: 0.71s تنقيح النتائج
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    دورية أكاديمية

    الوصف: In arthropods, hemolymph carries immune cells and solubilizes and transports nutrients, hormones, and other molecules that are involved in diverse physiological processes including immunity, metabolism, and reproduction. However, despite such physiological importance, little is known about its composition. We applied mass spectrometry-based label-free quantification approaches to study the proteome of hemolymph perfused from sugar-fed female and male Aedes aegypti mosquitoes. A total of 1403 proteins were identified, out of which 447 of them were predicted to be extracellular. In both sexes, almost half of these extracellular proteins were predicted to be involved in defense/immune response, and their relative abundances (based on their intensity-based absolute quantification, iBAQ) were 37.9 and 33.2%, respectively. Interestingly, among them, 102 serine proteases/serine protease-homologues were identified, with almost half of them containing CLIP regulatory domains. Moreover, proteins belonging to families classically described as chemoreceptors, such as odorant-binding proteins (OBPs) and chemosensory proteins (CSPs), were also highly abundant in the hemolymph of both sexes. Our data provide a comprehensive catalogue of A. aegypti hemolymph basal protein content, revealing numerous unexplored targets for future research on mosquito physiology and disease transmission. It also provides a reference for future studies on the effect of blood meal and infection on hemolymph composition.

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    دورية أكاديمية
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    دورية أكاديمية

    المساهمون: National Institute of Allergy and Infectious Diseases

    المصدر: Journal of Proteome Research ; volume 23, issue 4, page 1471-1487 ; ISSN 1535-3893 1535-3907

    مصطلحات موضوعية: General Chemistry, Biochemistry

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    دورية أكاديمية

    المساهمون: Institute of Biotechnology, Department of Food and Nutrition, Department of Microbiology, Faculty of Agriculture and Forestry, Cyanobacteria research, Helsinki Institute of Sustainability Science (HELSUS), Microbial Natural Products

    الوصف: Cyanobactins are linear and cyclic post-translationally modified peptides. Here we show that the prenyl-D-Arg-containing autum-nalamide A is a member of the cyanobactin family. Biochemical assays demonstrate that the AutF prenyltransferase targets the guanidinium moiety in arginine and homoarginine and is a useful tool for biotechnological applications. ; Peer reviewed

    وصف الملف: application/pdf

    العلاقة: This project was supported by a fellowship grant from the EPSRC (No. EP/S027246/1, W.E.H.), a training grant from the BBSRC (BB/V509206/1, W. E. H. and S. D.), the Novo Nordisk Foundation (18OC0034838, D. P. F.) and the NordForsk NCoE program ``NordAqua'' (Project Number 82845, D. P. F.). C. C. is funded by a PhD studentship from University of Aberdeen. N. J. is funded by the IBioIC CTP PhD programme. R. V. P. was funded by the Doctoral Programme in Microbiology and Biotechnology of the University of Helsinki. X. O. was funded by the China Scholarship Council (Grant 201906150148). We are grateful to Professor James Naismith (University of Oxford) for sharing the construct used to express the macrocyclase PCY1. We thank Dr Huanting Liu (University of St Andrews) for sharing the pEHISTEV-SUMO vector.; Clemente , C , Johnson , N , Ouyang , X , Popin , R , Dall'Angelo , S , Wahlsten , M , Jokela , J , Colombano , A , Nardone , B , Fewer , D P & Houssen , W E 2022 , ' Biochemical characterization of a cyanobactin arginine-N-prenylase from the autumnalamide biosynthetic pathway ' , Chemical Communications , vol. 58 , no. 86 , pp. 12054-12057 . https://doi.org/10.1039/d2cc01799gTest; ORCID: /0000-0003-3978-4845/work/123135547; ORCID: /0000-0001-5096-3575/work/123136680; ORCID: /0000-0002-4107-1695/work/123138419; ORCID: /0000-0003-0427-0326/work/123143232; http://hdl.handle.net/10138/350678Test; 3b58f94b-ecb7-4af4-af19-d4b0750e3f24; 000863636300001

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    دورية أكاديمية
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    دورية أكاديمية
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    دورية أكاديمية

    المساهمون: National Institute of Allergy and Infectious Diseases, Division of Intramural Research, National Institute of Allergy and Infectious Diseases, National Institutes of Health

    المصدر: Journal of Biological Chemistry ; volume 297, issue 5, page 101322 ; ISSN 0021-9258

    مصطلحات موضوعية: Cell Biology, Molecular Biology, Biochemistry

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    دورية أكاديمية