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Granjeiro,J.M.; Oliveira,R.C.; Bustos-Valenzuela,J.C.; Sogayar,M.C.; Taga,R.. |
Bone morphogenetic proteins (BMPs) are multi-functional growth factors belonging to the transforming growth factor ß superfamily. Family members are expressed during limb development, endochondral ossification, early fracture, and cartilage repair. The activity of BMPs was first identified in the 1960s but the proteins responsible for bone induction were unknown until the purification and cloning of human BMPs in the 1980s. To date, about 15 BMP family members have been identified and characterized. The signal triggered by BMPs is transduced through serine/threonine kinase receptors, type I and II subtypes. Three type I receptors have been shown to bind BMP ligands, namely: type IA and IB BMP receptors and type IA activin receptors. BMPs seem to be... |
Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Bone morphogenetic proteins; Osteogenic protein; Protein structure; Meta-analysis; Clinical trial. |
Ano: 2005 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2005001000003 |
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Barbosa,João A.R.G.; Netto,Luis E.S.; Farah,Chuck S.; Schenkman,Sergio; Meneghini,Rogério. |
This article describes the achievements of the Structural Molecular Biology Network (SMolBNet), a collaborative program of structural molecular biology, centered in the State of São Paulo, Brazil, and supported by São Paulo State Funding Agency (FAPESP). It gathers twenty scientific groups and is coordinated by the scientific staff of the Center of Structural Molecular Biology, at the National Laboratory of Synchrotron Light (LNLS), in Campinas. The SMolBNet program has been aimed at 1) solving the structure of proteins of interest related to the research projects of the groups. In some cases, the choice has been to select proteins of unknown function or of possible novel structure obtained from the sequenced genomes of the FAPESP genomic program; 2)... |
Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Structural genomics; Protein crystallography; Nuclear magnetic resonance; Protein structure. |
Ano: 2006 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0001-37652006000200006 |
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