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Biological activity of heterologous murine interleukin-10 and preliminary studi...
Carvalho, Vera; Castanheira, Pedro; Faria, Tiago Q.; Gonçalves, Catarina; Madureira, Pedro; Faro, Carlos; Domingues, Lucília; Brito, Rui M. M.Interleukin-10 (IL-10) is an anti-inflammatory cytokine, which active form is a non-covalent homodimer with two intramolecular disulphide bonds essential for its biological activity. A mutated form of murine IL-10 was successfully expressed in E. coli, recovered and purified from inclusion bodies. Its ability to reduce tumor necrosis factor synthesis and down-regulate class II major histocompatibility complex...
Mining approximate motifs in time series
Azevedo, Paulo J.; Ferreira, Pedro Gabriel; Silva, Cândida G.; Brito, Rui M. M.The problem of discovering previously unknown frequent patterns in time series, also called motifs, has been recently introduced. A motif is a subseries pattern that appears a significant number of times. Results demonstrate that motifs may provide valuable insights about the data and have a wide range of applications in data mining tasks. The main motivation for this study was the need to mine time series data...
Comparative calorimetric study of non-amyloidogenic and amyloidogenic variants ...
Shnyrov, Valery L.; Villar, Enrique; Zhadan, Galina G.; Sanchez-Ruiz, Jose M.; Quintas, Alexandre; Saraiva, Maria João M.; Brito, Rui M. M.Familial amyloidotic polyneuropathy (FAP) is an autosomal dominant hereditary type of amyloidosis involving amino acid substitutions in transthyretin (TTR). V30M-TTR is the most frequent variant, and L55P-TTR is the variant associated with the most aggressive form of FAP. The thermal stability of the wild-type, V30M-TTR, L55P-TTR and a non-amyloidogenic variant, T119M-TTR, was studied by high-sensitivity differ...
Solution Structures of the C-Terminal Domain of Cardiac Troponin C Free and Bou...
Gasmi-Seabrook, Geneviève M. C.; Howarth, Jack W.; Finley, Natosha; Abusamhadneh, Ekram; Gaponenko, Vadim; Brito, Rui M. M.; Solaro, R. JohnThe N-terminal domain of cardiac troponin I (cTnI) comprising residues 33−80 and lacking the cardiac-specific amino terminus forms a stable binary complex with the C-terminal domain of cardiac troponin C (cTnC) comprising residues 81−161. We have utilized heteronuclear multidimensional NMR to assign the backbone and side-chain resonances of Ca2+-saturated cTnC(81−161) both free and bound to cTnI(33−80). No sign...
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