Zobrazeno 1 - 10
of 12
pro vyhledávání: '"João P. L. Guerra"'
Publikováno v:
International Journal of Molecular Sciences, Vol 24, Iss 12, p 10256 (2023)
Dps proteins (DNA-binding proteins from starved cells) are multifunctional stress defense proteins from the Ferritin family expressed in Prokarya during starvation and/or acute oxidative stress. Besides shielding bacterial DNA through binding and con
Externí odkaz:
https://doaj.org/article/11367d3f2c4c4d7f916ca00350524eb6
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, Vol 23, Iss 9, p 4871 (2022)
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
Externí odkaz:
https://doaj.org/article/8af7ee7082a14e9d855ee0648422a0d0
Publikováno v:
International Journal of Molecular Sciences; Volume 24; Issue 12; Pages: 10256
Dps proteins (DNA-binding proteins from starved cells) are multifunctional stress defense proteins from the Ferritin family expressed in Prokarya during starvation and/or acute oxidative stress. Besides shielding bacterial DNA through binding and con
Autor:
João P. L. Guerra, Clement E. Blanchet, Bruno J. C. Vieira, João C. Waerenborgh, Nykola C. Jones, Søren Vrønning Hoffmann, Alice S. Pereira, Pedro Tavares
Publikováno v:
Guerra, J P L, Blanchet, C E, Vieira, B J C, Waerenborgh, J C, Jones, N C, Hoffmann, S V, Pereira, A S & Tavares, P 2023, ' Controlled modulation of the dynamics of the Deinococcus grandis Dps N-terminal tails by divalent metals ', Protein Science, vol. 32, no. 2, e4567 . https://doi.org/10.1002/pro.4567
Protein science 32(2), e4567 (2023). doi:10.1002/pro.4567
Protein science 32(2), e4567 (2023). doi:10.1002/pro.4567
Protein science 32(2), e4567 (2023). doi:10.1002/pro.4567
DNA-binding proteins from starved cells (Dps) are small multifunctional nanocages expressed by prokaryotes in acute oxidative stress conditions or during the starvation-induced stationary
DNA-binding proteins from starved cells (Dps) are small multifunctional nanocages expressed by prokaryotes in acute oxidative stress conditions or during the starvation-induced stationary
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:
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
Publikováno v:
Proc Natl Acad Sci U S A
bis-(3′,5′)-cyclic diadenosine monophosphate (c-di-AMP) is a second messenger with roles in virulence, cell wall and biofilm formation, and surveillance of DNA integrity in many bacterial species, including pathogens. Strikingly, it has also been
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:
Coordination Chemistry Reviews. 449:214187
The subject of this review article was first reported approximately three decades ago upon the discovery of a starvation-inducible protein found tightly bound to chromosomal DNA in 3-day-old starved cultures of Escherichia coli. As a result, they wer