Résumé
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 changing landscape, researchers in biochemistry and molecular biology must re-think their priorities in terms of scientific output dissemination. The evaluation processes and institutional funding for scientific publications should also be revised accordingly. This article presents the results of discussions within the Department of Biochemistry, University of São Paulo, on this subject.
Sujets)
Humains , Périodiques comme sujet/statistiques et données numériques , Édition/tendances , Recherche , Biochimie , Biologie moléculaire , Périodiques comme sujet/normes , Périodiques comme sujet/tendances , BrésilRésumé
The bindings of 125I-laminin to trypomastigotes is specific and 2-5 x 10**3 laminin-binding sites were calculated to be presented on the surface of a live trypomastigote. Anti-laminin antibodies were able to inhibit the invasion of cultured cells by trypomastigotes (62-75 per cent), suggesting that laminin may be involved in the adhesion of the parasite to host cells. By affinity chromatography, an 85-KDa glycoprotein was isolated (laminin-bindign glycoprotein, LBG) from trypomastigote lysates, but not from epimastigote lysates. It is suggested that at least fragment E8 (but not E1) from laminin could be involbed in the reaction which is independent of the carbohydrate moieties from both ligand and recepto. It is also shown that LBG is member of the Tc-85 family, previously shown to be related to the invasion process of the parasite