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Genome features of Leptospira interrogans serovar Copenhageni BJMBR
Nascimento,A.L.T.O.; Verjovski-Almeida,S.; Van Sluys,M.A.; Monteiro-Vitorello,C.B.; Camargo,L.E.A.; Digiampietri,L.A.; Harstkeerl,R.A.; Ho,P.L.; Marques,M.V.; Oliveira,M.C.; Setubal,J.C.; Haake,D.A.; Martins,E.A.L..
We report novel features of the genome sequence of Leptospira interrogans serovar Copenhageni, a highly invasive spirochete. Leptospira species colonize a significant proportion of rodent populations worldwide and produce life-threatening infections in mammals. Genomic sequence analysis reveals the presence of a competent transport system with 13 families of genes encoding for major transporters including a three-member component efflux system compatible with the long-term survival of this organism. The leptospiral genome contains a broad array of genes encoding regulatory system, signal transduction and methyl-accepting chemotaxis proteins, reflecting the organism's ability to respond to diverse environmental stimuli. The identification of a complete set...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Leptospira interrogans; Outer membrane proteins; Lipopolysaccharides; Transport; Regulatory systems.
Ano: 2004 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2004000400003
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Probing the SERCA1a sarcoplasmic reticulum Ca2+-ATPase phosphorylation-site mutant D351E with inorganic phosphate BJMBR
Carreira,A.C.O.; Bastos,C.M.V.; Verjovski-Almeida,S..
The expression of sarcoplasmic reticulum SERCA1a Ca2+-ATPase wild-type and D351E mutants was optimized in yeast under the control of a galactose promoter. Fully active wild-type enzyme was recovered in yeast microsomal membrane fractions in sufficient amounts to permit a rapid and practical assay of ATP hydrolysis and phosphoenzyme formation from ATP or Pi. Mutant and wild-type Ca2+-ATPase were assayed for phosphorylation by Pi under conditions that are known to facilitate this reaction in the wild-type enzyme, including pH 6.0 or 7.0 at 25ºC in the presence of dimethylsulfoxide. Although glutamyl (E) and aspartyl (D) residue side chains differ by only one methylene group, no phosphoenzyme could be detected in the D351E mutant, even upon the addition of...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Phosphorylation site mutant; Catalytic site; Yeast expression system; Saccharomyces cerevisiae; P-type ATPase.
Ano: 2007 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2007001000004
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Where do we aspire to publish? A position paper on scientific communication in biochemistry and molecular biology BJMBR
Baptista,M.S.; Alves,M.J.M.; Arantes,G.M.; Armelin,H.A.; Augusto,O.; Baldini,R.L.; Basseres,D.S.; Bechara,E.J.H.; Bruni-Cardoso,A.; Chaimovich,H.; Colepicolo Neto,P.; Colli,W.; Cuccovia,I.M.; Da-Silva,A.M.; Di Mascio,P.; Farah,S.C.; Ferreira,C.; Forti,F.L.; Giordano,R.J.; Gomes,S.L.; Gueiros Filho,F.J.; Hoch,N.C.; Hotta,C.T.; Labriola,L.; Lameu,C.; Machini,M.T.; Malnic,B.; Marana,S.R.; Medeiros,M.H.G.; Meotti,F.C.; Miyamoto,S.; Oliveira,C.C.; Souza-Pinto,N.C.; Reis,E.M.; Ronsein,G.E.; Salinas,R.K.; Schechtman,D.; Schreier,S.; Setubal,J.C.; Sogayar,M.C.; Souza,G.M.; Terra,W.R.; Truzzi,D.R.; Ulrich,H.; Verjovski-Almeida,S.; Winck,F.V.; Zingales,B.; Kowaltowski,A.J..
The scientific publication landscape is changing quickly, with an enormous increase in options and models. Articles can be published in a complex variety of journals that differ in their presentation format (online-only or in-print), editorial organizations that maintain them (commercial and/or society-based), editorial handling (academic or professional editors), editorial board composition (academic or professional), payment options to cover editorial costs (open access or pay-to-read), indexation, visibility, branding, and other aspects. Additionally, online submissions of non-revised versions of manuscripts prior to seeking publication in a peer-reviewed journal (a practice known as pre-printing) are a growing trend in biological sciences. In this...
Tipo: Info:eu-repo/semantics/other Palavras-chave: Scientific journals; Scientific editing; Pre-prints; Open access; Peer review.
Ano: 2019 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2019000900401
Registros recuperados: 3
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