Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Ana V, Almeida"'
Autor:
Kirsten Severing, Ana V. Almeida
Publikováno v:
Advanced Science, Vol 9, Iss 1, Pp n/a-n/a (2022)
Externí odkaz:
https://doaj.org/article/5d2a34a7007a41638f09d9018f7157a8
Autor:
Ana V. Almeida, Ana J. Carvalho, Tomás Calmeiro, Nykola C. Jones, Søren V. Hoffmann, Elvira Fortunato, Alice S. Pereira, Pedro Tavares
Publikováno v:
Almeida, A V, Carvalho, A J, Calmeiro, T, Jones, N C, Hoffmann, S V, Fortunato, E, Pereira, A S & Tavares, P 2022, ' Condensation and protection of DNA by the Myxococcus xan-thus encapsulin: a novel function ', International Journal of Molecular Sciences, vol. 23, no. 14, 7829 . https://doi.org/10.3390/ijms23147829
International Journal of Molecular Sciences; Volume 23; Issue 14; Pages: 7829
International Journal of Molecular Sciences; Volume 23; Issue 14; Pages: 7829
Encapsulins are protein nanocages capable of harboring smaller proteins (cargo proteins) within their cavity. The function of the encapsulin systems is related to the encapsulated cargo proteins. The Myxococcus xanthus encapsulin (EncA) naturally enc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c92f5ee3b8a875e58b4b99acf7063605
https://pure.au.dk/portal/da/publications/condensation-and-protection-of-dna-by-the-myxococcus-xanthus-encapsulin-a-novel-function(ff55577c-9533-4d7e-867b-ddb088327b7a).html
https://pure.au.dk/portal/da/publications/condensation-and-protection-of-dna-by-the-myxococcus-xanthus-encapsulin-a-novel-function(ff55577c-9533-4d7e-867b-ddb088327b7a).html
Autor:
João P. Jacinto, Nykola C. Jones, Pedro Tavares, Alice S. Pereira, João P. L. Guerra, Ana V. Almeida, Søren Vrønning Hoffmann, Daniela Penas
Publikováno v:
Jacinto, J P, Penas, D, Guerra, J P L, Almeida, A V, Jones, N C, Hoffmann, S V, Tavares, P & Pereira, A S 2021, ' Dps-DNA interaction in Marinobacter hydrocarbonoclasticus protein : effect of a single-charge alteration ', European Biophysics Journal, vol. 50, pp. 513-521 . https://doi.org/10.1007/s00249-021-01538-0
DNA-binding proteins from starved cells (Dps) are members of the ferritin family of proteins found in prokaryotes, with hollow rounded cube-like structures, composed of 12 equal subunits. These protein nanocages are bifunctional enzymes that protect
Autor:
Ana V, Almeida, Ana J, Carvalho, Tomás, Calmeiro, Nykola C, Jones, Søren V, Hoffmann, Elvira, Fortunato, Alice S, Pereira, Pedro, Tavares
Publikováno v:
International journal of molecular sciences. 23(14)
Encapsulins are protein nanocages capable of harboring smaller proteins (cargo proteins) within their cavity. The function of the encapsulin systems is related to the encapsulated cargo proteins. The
Autor:
João P L, Guerra, Clement E, Blanchet, Bruno J C, Vieira, Ana V, Almeida, João C, Waerenborgh, Nykola C, Jones, Søren V, Hoffmann, Pedro, Tavares, Alice S, Pereira
Publikováno v:
International journal of molecular sciences. 23(9)
DNA-binding proteins from starved cells (Dps) are homododecameric nanocages, with N- and C-terminal tail extensions of variable length and amino acid composition. They accumulate iron in the form of a ferrihydrite mineral core and are capable of bind
Autor:
Alice S. Pereira, João P. Jacinto, Nykola C. Jones, Pedro Tavares, Ana V. Almeida, Søren Vrønning Hoffmann, João C. Waerenborgh, João P. L. Guerra, Bruno J. C. Vieira
Publikováno v:
Almeida, A V, Jacinto, J P, Guerra, J P L, Vieira, B J C, Waerenborgh, J C, Jones, N C, Hoffmann, S V, Pereira, A S & Tavares, P 2021, ' Structural features and stability of apo-and holo-forms of a simple iron–sulfur protein ', European Biophysics Journal, vol. 50, pp. 561-570 . https://doi.org/10.1007/s00249-021-01546-0
Iron–sulfur centers are widespread in living organisms, mostly performing electron transfer functions, either in electron transfer chains or as part of multi-enzymatic complexes, while being also present in enzyme active sites, handling substrate c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ad43f24edf60c9eb37f4bfba6b4d514f
https://pure.au.dk/portal/da/publications/structural-features-and-stability-of-apo-and-holoforms-of-a-simple-ironsulfur-protein(0aa076f5-442f-48f1-a5d2-6635eed7edf5).html
https://pure.au.dk/portal/da/publications/structural-features-and-stability-of-apo-and-holoforms-of-a-simple-ironsulfur-protein(0aa076f5-442f-48f1-a5d2-6635eed7edf5).html
Autor:
João P, Jacinto, Daniela, Penas, João P L, Guerra, Ana V, Almeida, Nykola C, Jones, Søren V, Hoffmann, Pedro, Tavares, Alice S, Pereira
Publikováno v:
European biophysics journal : EBJ. 50(3-4)
DNA-binding proteins from starved cells (Dps) are members of the ferritin family of proteins found in prokaryotes, with hollow rounded cube-like structures, composed of 12 equal subunits. These protein nanocages are bifunctional enzymes that protect
Autor:
Ana V, Almeida, João P, Jacinto, João P L, Guerra, Bruno J C, Vieira, João C, Waerenborgh, Nykola C, Jones, Søren V, Hoffmann, Alice S, Pereira, Pedro, Tavares
Publikováno v:
European biophysics journal : EBJ. 50(3-4)
Iron-sulfur centers are widespread in living organisms, mostly performing electron transfer functions, either in electron transfer chains or as part of multi-enzymatic complexes, while being also present in enzyme active sites, handling substrate cat
Publikováno v:
Advanced Materials Technologies. 7:2101596
Publikováno v:
Coordination Chemistry Reviews. 448:214188
Compartmentalization is an essential process that allows cells to organize, creating controlled microenvironments for specific metabolic pathways. Therefore, this allows the increase of reaction rates and/or protection of the cell from the effect of