Zobrazeno 1 - 10
of 10
pro vyhledávání: '"João P. L. Guerra"'
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:
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
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
Autor:
João P. L. Guerra, Paulina Faria, Alexandre de Oliveira, Vitor Silva, Paulo C. Lemos, Alice S. Pereira
Publikováno v:
Repositório Científico de Acesso Aberto de Portugal
Repositório Científico de Acesso Aberto de Portugal (RCAAP)
instacron:RCAAP
Repositório Científico de Acesso Aberto de Portugal (RCAAP)
instacron:RCAAP
The authors acknowledge Prof. Luís Baltazar, for the support on rheological characterization of the bioproducts, and to the Portuguese Foundation for Science and Technology (FCT) for the financial support within research project PTDC/EPH-PAT/4684/20