Zobrazeno 1 - 10
of 18
pro vyhledávání: '"Boris C. Dunkov"'
Publikováno v:
Journal of Insect Science, Vol 2, p 7 (2002)
Secreted ferritin in the mosquito, Aedes aegypti, has several subunits that are the products of at least two genes, one encoding a homologue of the vertebrate heavy chain (HCH) and the other the light chain homologue (LCH). Here we report the develop
Externí odkaz:
https://doaj.org/article/86ff26db69f24891ac83ef1fbaf7edea
Autor:
Boris C. Dunkov, Octavio A. C. Talyuli, Gabriela O. Paiva-Silva, Gabriel A. Silva, Luiza de Oliveira Ramos Pereira, Pedro L. Oliveira, Vanessa Bottino-Rojas
Publikováno v:
Scientific Reports
Scientific Reports, Vol 9, Iss 1, Pp 1-12 (2019)
Scientific Reports, Vol 9, Iss 1, Pp 1-12 (2019)
Heme oxygenase (HO) is a ubiquitous enzyme responsible for heme breakdown, which yields carbon monoxide (CO), biliverdin (BV) and ferrous ion. Here we show that the Aedes aegypti heme oxygenase gene (AeHO – AAEL008136) is expressed in different dev
Autor:
Teodora Georgieva, Boris C. Dunkov
Publikováno v:
Insect Biochemistry and Molecular Biology. 36:300-309
Sequencing of the genomes of Drosophila melanogaster, Anopheles gambiae, Apis mellifera, and Bombyx mori provided an opportunity to examine the diversity and organization of genes encoding insect transferrins (Tsf) and ferritins. Information obtained
Publikováno v:
Insect Biochemistry and Molecular Biology. 32:295-302
Drosophila melanogaster secreted ferritin like the cytosolic ferritins of other organisms is composed of two subunits, a heavy chain homologue (HCH) and a light chain homologue (LCH). We report the cloning of a cDNA encoding the ferritin LCH of this
Autor:
Teodora Georgieva, Toyoshi Yoshiga, Nedjalka Harizanova, Kiril H. Ralchev, Boris C. Dunkov, John H. Law
Publikováno v:
European Journal of Biochemistry. 260:414-420
Drosophila melanogaster transferrin cDNA was cloned from an ovarian cDNA library by using a PCR fragment amplified by two primers designed from other dipteran transferrin sequences. The clone (2035 bp) encodes a protein of 641 amino acids containing
Publikováno v:
Proceedings of the National Academy of Sciences. 96:2716-2721
Insect ferritins have subunits homologous to the heavy and light chains of vertebrate ferritins. Cloning and sequence of the heavy chain homologue (HCH) of Drosophila melanogaster ferritin subunit have been reported earlier. When Northern blots of D.
Autor:
Richard H. ffrench-Constant, René Feyereisen, Frank Shotkoski, Giovanni Mocelin, Boris C. Dunkov, Victor M. Guzov, Alexandra Brun, Marcel Amichot
Publikováno v:
DNA and Cell Biology. 16:1345-1356
The cytochrome P450 gene Cyp6a2 from Drosophila melanogaster is located on the right arm of chromosome 2 at position 43A1-2 and comprises two exons separated by a 69-bp intron. Phenobarbital treatment of flies leads to a rapid increase in the level o
Publikováno v:
Archives of Insect Biochemistry and Physiology. 29:293-307
Ferritin, an iron storage protein, was isolated from larvae and pupae of Aedes aegypti grown in an iron-rich medium. Mosquito ferritin is a high molecular weight protein composed of several different, relatively small, subunits. Subunits of molecular
Autor:
Igor C. Almeida, Hatisaburo Masuda, Clarissa M. Maya-Monteiro, Pedro L. Oliveira, Gabriela O. Paiva-Silva, Boris C. Dunkov, Christine Cruz-Oliveira, Ernesto S. Nakayasu
Hematophagous insects are vectors of diseases that affect hundreds of millions of people worldwide. A common physiological event in the life of these insects is the hydrolysis of host hemoglobin in the digestive tract, leading to a massive release of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::368c25f29d31335d75e7bc118ae9d8cb
https://europepmc.org/articles/PMC1472424/
https://europepmc.org/articles/PMC1472424/
Autor:
Sara Holmberg, Fanis Missirlis, T. Georgieva, Boris C. Dunkov, Tracey A. Rouault, John H. Law
Mitochondrial function depends on iron-containing enzymes and proteins, whose maturation requires available iron for biosynthesis of iron–sulfur clusters and heme. Little is known about how mitochondrial iron homeostasis is maintained, although the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2b99aefe8fd3e500430a48ccba35dc5b
https://europepmc.org/articles/PMC1458669/
https://europepmc.org/articles/PMC1458669/