RESUMEN
Human Protein Reference Database (HPRD) (http://www.hprd.org) was developed to serve as a comprehensive collection of protein features, post-translational modifications (PTMs) and protein-protein interactions. Since the original report, this database has increased to >20 000 proteins entries and has become the largest database for literature-derived protein-protein interactions (>30 000) and PTMs (>8000) for human proteins. We have also introduced several new features in HPRD including: (i) protein isoforms, (ii) enhanced search options, (iii) linking of pathway annotations and (iv) integration of a novel browser, GenProt Viewer (http://www.genprot.org), developed by us that allows integration of genomic and proteomic information. With the continued support and active participation by the biomedical community, we expect HPRD to become a unique source of curated information for the human proteome and spur biomedical discoveries based on integration of genomic, transcriptomic and proteomic data.
Asunto(s)
Bases de Datos de Proteínas , Proteoma/genética , Proteoma/fisiología , Bases de Datos de Proteínas/estadística & datos numéricos , Genómica , Humanos , Internet , Mapeo de Interacción de Proteínas , Isoformas de Proteínas/análisis , Isoformas de Proteínas/genética , Isoformas de Proteínas/fisiología , Procesamiento Proteico-Postraduccional , Proteínas/análisis , Proteínas/genética , Proteínas/fisiología , Proteoma/química , Proteómica , Transducción de Señal , Integración de Sistemas , Interfaz Usuario-ComputadorRESUMEN
Inflammatory bowel disease (IBD) is an inflammatory disorder of the digestive tract reported to be primarily caused by oxidative stress. In this study, alginate encapsulated nanoceramic carriers were designed to deliver acid labile antioxidant enzyme catalase orally. Complete system was characterized for size, loading efficiency, in vitro antioxidant assay and in vitro release. The prepared nanoceramic system was found to be spherical with diameter of 925 ± 6.81 nm. The in vitro release data followed the Higuchi model in acidic buffer whereas in alkaline pH sustained and almost first order release of enzyme was observed up to 6 h.
Asunto(s)
Catalasa/química , Catalasa/uso terapéutico , Cerámica/química , Portadores de Fármacos/química , Enfermedades Inflamatorias del Intestino/tratamiento farmacológico , Nanoestructuras/química , Biocatálisis , Disponibilidad Biológica , Catalasa/metabolismo , Catalasa/farmacocinética , Liberación de Fármacos , Estabilidad de Enzimas , Concentración de Iones de Hidrógeno , Conformación ProteicaRESUMEN
Two point sets {pi} and {p'i}; i = 1, 2,..., N are related by p'i = Rpi + T + Ni, where R is a rotation matrix, T a translation vector, and Ni a noise vector. Given {pi} and {p'i}, we present an algorithm for finding the least-squares solution of R and T, which is based on the singular value decomposition (SVD) of a 3 × 3 matrix. This new algorithm is compared to two earlier algorithms with respect to computer time requirements.
RESUMEN
Plasma is one of the best studied compartments in the human body and serves as an ideal body fluid for the diagnosis of diseases. This report provides a detailed functional annotation of all the plasma proteins identified to date. In all, gene products encoded by 3778 distinct genes were annotated based on proteins previously published in the literature as plasma proteins and the identification of multiple peptides from proteins under HUPO's Plasma Proteome Project. Our analysis revealed that 51% of these genes encoded more than one protein isoform. All single nucleotide polymorphisms involving protein-coding regions were mapped onto the protein sequences. We found a number of examples of isoform-specific subcellular localization as well as tissue expression. This database is an attempt at comprehensive annotation of a complex subproteome and is available on the web at http://www.plasmaproteomedatabase.org.