49 research outputs found
AMYPdb: A database dedicated to amyloid precursor proteins
<p>Abstract</p> <p>Background</p> <p>Misfolding and aggregation of proteins into ordered fibrillar structures is associated with a number of severe pathologies, including Alzheimer's disease, prion diseases, and type II diabetes. The rapid accumulation of knowledge about the sequences and structures of these proteins allows using of <it>in silico </it>methods to investigate the molecular mechanisms of their abnormal conformational changes and assembly. However, such an approach requires the collection of accurate data, which are inconveniently dispersed among several generalist databases.</p> <p>Results</p> <p>We therefore created a free online knowledge database (AMYPdb) dedicated to amyloid precursor proteins and we have performed large scale sequence analysis of the included data. Currently, AMYPdb integrates data on 31 families, including 1,705 proteins from nearly 600 organisms. It displays links to more than 2,300 bibliographic references and 1,200 3D-structures. A Wiki system is available to insert data into the database, providing a sharing and collaboration environment. We generated and analyzed 3,621 amino acid sequence patterns, reporting highly specific patterns for each amyloid family, along with patterns likely to be involved in protein misfolding and aggregation.</p> <p>Conclusion</p> <p>AMYPdb is a comprehensive online database aiming at the centralization of bioinformatic data regarding all amyloid proteins and their precursors. Our sequence pattern discovery and analysis approach unveiled protein regions of significant interest. AMYPdb is freely accessible <abbrgrp><abbr bid="B1">1</abbr></abbrgrp>.</p
Suivi rhéologique du processus d'agrégation de la protéine tau
International audienceAlzheimer's disease is one of thirty pathology called conformational disease that are characterized by errors folding and assembly of protein. In Alzheimer's disease, tau protein and amyloid beta peptide are responsible of the neuronal degeneration. Understanding these mechanisms and diagnosis are closely linked to the availability of an efficient analytical concept for monitoring ex vivo self-assembly of proteins. To understand the aggregation's mechanism, a microsystem is developed for the detection of protein tau based on the micro-rheological followed by high frequency ultrasonic waves. The sensor used is a TSM (Thickness Shear Mode) resonator operating in shear mode at a fundamental frequency of 5MHz. In contact with the fluid to be characterized, the sensor generate shear waves, which are measured in reflection through instrumentation developed in the laboratory. From the measurement of the complex impedance of quartz with a network analyzer, the extraction of G' (elastic modulus) and G'' (viscous modulus) is possible. Initial results indicate that our sensor can quantify, by viscosity, concentration variations of a peptide sequence of tau protein, and can differentiate, by plasticity, the conformational state. </p
La maladie d'Alzheimer. Contribution a la recherche de marqueurs biologiques
SIGLEINIST T 71182 / INIST-CNRS - Institut de l'Information Scientifique et TechniqueFRFranc
Etude du mecanisme de lecture du codon non-sens UGA, par le tRNATrp suppresseur, chez E. coli
SIGLET 54389 / INIST-CNRS - Institut de l'Information Scientifique et TechniqueFRFranc
Color and Graphic Display (CGD): Programs for Multiple Sequence Alignment Analysis in Spreadsheet Software
Interpretation of multiple sequence alignments is of major interest for the prediction of functional and structural domains in proteins or for the organization of related sequences in families and subfamilies. However, a necessity for the bench scientist is the use of outstanding programs in a friendly computing environment. This paper describes Color and Graphic Display (CGD), a set of modules that runs as part of the Microsoft® Excel® spreadsheet to color and analyze multiple sequence alignments. Discussed here are the main functions of CGD and the use of the program to highlight residues of importance in a water channel family. Although CGD was created for protein sequences, most of the modules are compatible with DNA sequences
Function, structural properties and molecular model of a bacterial aquaglyceroporin
International audienc
APPROCHE PREDICTIVE ET CARACTERISATION FONCTIONNELLE DE CANAUX DE LA FAMILLE MIP
RENNES1-BU Sciences Philo (352382102) / SudocSudocFranceF