Zobrazeno 1 - 10
of 18
pro vyhledávání: '"Tânia F Oliveira"'
Publikováno v:
PLoS ONE, Vol 10, Iss 9, p e0137705 (2015)
In many territorial species androgen hormones are known to increase in response to territorial intrusions as a way to adjust the expression of androgen-dependent behaviour to social challenges. The dear enemy effect has also been described in territo
Externí odkaz:
https://doaj.org/article/539ea9c894f84f0eb0c53c3a11148ea7
Autor:
Benjamin F. Cravatt, Tânia F. Oliveira, José A. Brito, Rui Moreira, Kenneth M. Lum, Luís A. R. Carvalho, Vanessa T. Almeida, Susana D. Lucas, Lídia Gonçalves, Margarida Archer, Rita C. Guedes
Publikováno v:
ACS chemical biology. 15(4)
3-Oxo-β-sultams are four-membered ring ambident electrophiles that can react with nucleophiles either at the carbonyl carbon or at the sulfonyl sulfur atoms, and that have been reported to inhibit serine hydrolases via acylation of the active-site s
Publikováno v:
FEBS Journal. 280:4681-4692
Glutamate dehydrogenases (EC 1.4.1.2–4) catalyse the oxidative deamination of l-glutamate to α-ketoglutarate using NAD+ and/or NADP+ as a cofactor. Subunits of homo-hexameric bacterial enzymes comprise a substrate-binding Domain I followed by a nu
Publikováno v:
Acta crystallographica. Section F, Structural biology communications. 72(Pt 6)
Glutamate dehydrogenases (EC 1.4.1.2–4) catalyse the oxidative deamination of L-glutamate to α-ketoglutarate using NAD(P)+as a cofactor. The bacterial enzymes are hexameric, arranged with 32 symmetry, and each polypeptide consists of an N-terminal
Autor:
Muaawia A. Hamza, John B. Carrigan, Michael A. Sharkey, Amir R. Khan, Santosh Panjikar, Tânia F. Oliveira, Paul C. Engel
Publikováno v:
Journal of Structural Biology. 177:543-552
Glutamate dehydrogenases (EC 1.4.1.2-4) catalyse the oxidative deamination of l-glutamate to α-ketoglutarate using NAD(P) as a cofactor. The bacterial enzymes are hexamers and each polypeptide consists of an N-terminal substrate-binding (Domain I) f
Autor:
Inês A. C. Pereira, Tânia F. Oliveira, Margarida Archer, Pedro M. Matias, Sofia S. Venceslau, Clemens Vonrhein
Publikováno v:
Journal of Structural Biology. 164:236-239
Dissimilatory sulfite reductase (dSiR, DsrAB) is a key protein in dissimilatory sulfur metabolism, one of the earliest types of energy metabolism to be traced on earth. dSirs are large oligomeric proteins around 200 kDa forming an α 2 β 2 arrangeme
Autor:
Margarida Archer, Diogo Athayde, Ana Lúcia Rosário, Ana P. Batista, Manuela M. Pereira, Tânia F. Oliveira, Filipa V. Sena, José A. Brito
Publikováno v:
Acta crystallographica. Section F, Structural biology communications. 71(Pt 4)
In recent years, type II NADH dehydrogenases (NDH-IIs) have emerged as potential drug targets for a wide range of human disease causative agents. In this work, the NDH-II enzyme from the Gram-positive human pathogenStaphylococcus aureuswas recombinan
Publikováno v:
The EMBO Journal. 25:5951-5960
Oxidation of membrane-bound quinol molecules is a central step in the respiratory electron transport chains used by biological cells to generate ATP by oxidative phosphorylation. A novel family of cytochrome c quinol dehydrogenases that play an impor
Autor:
Przemyslaw Nogly, Ana Lúcia Rosário, Filipa Varela, Arnulf Kletzin, Malgorzata Magoch, Pikyee Ma, Meike Stelter, Peter J. F. Henderson, Margarida Archer, Miguel Pessanha, José A. Brito, Ana Rita Silva, Tânia F. Oliveira
Publikováno v:
PLoS ONE, Vol 8, Iss 11 (2013)
PLoS ONE
PLoS ONE
Autor:
Miguel Pessanha, Filipa Varela, Meike Stelter, Margarida Archer, Peter J. F. Henderson, Tânia F. Oliveira, Arnulf Kletzin, Przemyslaw Nogly, Pikyee Ma, José A. Brito, Ana Rita Silva, Ana Lúcia Rosário, Malgorzata Magoch
Publikováno v:
PLoS ONE
PLoS ONE, Public Library of Science, 2013, 8 (10), pp.e76913
PLoS ONE, Vol 8, Iss 10, p e76913 (2013)
PLoS ONE, 2013, 8 (10), pp.e76913
PLoS ONE; Vol 8
PLoS ONE, 8 (10)
PLoS ONE, Public Library of Science, 2013, 8 (10), pp.e76913
PLoS ONE, Vol 8, Iss 10, p e76913 (2013)
PLoS ONE, 2013, 8 (10), pp.e76913
PLoS ONE; Vol 8
PLoS ONE, 8 (10)
Membrane proteins play a key role in many fundamental cellular processes such as transport of nutrients, sensing of environmental signals and energy transduction, and account for over 50% of all known drug targets. Despite their importance, structura
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::18bad1f3c65842924f7ce9d12929069d
https://hal.univ-grenoble-alpes.fr/hal-01322381
https://hal.univ-grenoble-alpes.fr/hal-01322381