PubMed Health⌕ Search

Biomedical subjects

Alex Mitchell

Publications and source records attributed to Alex Mitchell.

5 recordsLinked to original sources

New developments in the InterPro database.

InterPro is an integrated resource for protein families, domains and functional sites, which integrates the following protein signature databases: PROSITE, PRINTS, ProDom, Pfam, SMART, TIGRFAMs, PIRSF, SUPERFAMILY, Gene3D and PANTHER. The latter two new member databases have been integrated since the last publication in this journal. There have been several new developments in InterPro, including an additional reading field, new database links, extensions to the web interface and additional match XML files. InterPro has always provided matches to UniProtKB proteins on the website and in the match XML file on the FTP site. Additional matches to proteins in UniParc (UniProt archive) are now available for download in the new match XML files only. The latest InterPro release (13.0) contains more than 13 000 entries, covering over 78% of all proteins in UniProtKB. The database is available for text- and sequence-based searches via a webserver (http://www.ebi.ac.uk/interpro), and for download by anonymous FTP (ftp://ftp.ebi.ac.uk/pub/databases/interpro). The InterProScan search tool is now also available via a web service at http://www.ebi.ac.uk/Tools/webservices/WSInterProScan.html.

Databases, Protein↗

InterPro, progress and status in 2005.

InterPro, an integrated documentation resource of protein families, domains and functional sites, was created to integrate the major protein signature databases. Currently, it includes PROSITE, Pfam, PRINTS, ProDom, SMART, TIGRFAMs, PIRSF and SUPERFAMILY. Signatures are manually integrated into InterPro entries that are curated to provide biological and functional information. Annotation is provided in an abstract, Gene Ontology mapping and links to specialized databases. New features of InterPro include extended protein match views, taxonomic range information and protein 3D structure data. One of the new match views is the InterPro Domain Architecture view, which shows the domain composition of protein matches. Two new entry types were introduced to better describe InterPro entries: these are active site and binding site. PIRSF and the structure-based SUPERFAMILY are the latest member databases to join InterPro, and CATH and PANTHER are soon to be integrated. InterPro release 8.0 contains 11 007 entries, representing 2573 domains, 8166 families, 201 repeats, 26 active sites, 21 binding sites and 20 post-translational modification sites. InterPro covers over 78% of all proteins in the Swiss-Prot and TrEMBL components of UniProt. The database is available for text- and sequence-based searches via a webserver (http://www.ebi.ac.uk/interpro), and for download by anonymous FTP (ftp://ftp.ebi.ac.uk/pub/databases/interpro).

Databases, Protein↗

A review about the impact of multiple sclerosis on health-related quality of life.

PURPOSE: There is increasing recognition that the global wellbeing of patients with chronic neurological disease is an important outcome in research and clinical practice alike. Many studies involving individuals with multiple sclerosis have demonstrated that the overall wellbeing is not a simple manifestation of impairment or disability. The strongest correlations with health-related quality of life appear to be patient rated emotional adjustment to illness and patient rated handicap. In recent years, health-related quality of life questionnaires that measure the physical, social, emotional, and occupational impact of illness have been developed and validated in populations with MS. Most questionnaires are now available in a range of languages. This development is likely to lead to increasing recognition of neuropsychiatric complications of MS in clinical practice and better quantification of treatment responses in clinical trials. CONCLUSION: Further work is required to decide which scale is most suited to which purpose. Assessment of multiple sclerosis-specific health-related quality of life should be included in future clinical trials to provide a complete picture of patients' health status.

Cognition Disorders↗

CSF phosphorylated tau--does it constitute an accurate biological test for Alzheimer's disease?

INTRODUCTION: There is considerable interest in developing a diagnostic test which could differentiate between early Alzheimer's disease (AD) and other causes of memory impairment with more than 80% sensitivity and 80% specificity. OBJECTIVE: To review the studies that have examined CSF phosphorylated tau as diagnostic test of AD vs clinically representative comparison groups. METHOD: A critical review of the literature using Embase, Web of Science, Medline and Psychinfo databases supplemented by handsearching and contact with experts in the field. RESULTS: CSF phosphorylated tau is a marker of AD that improves upon the utility of CSF total tau and clinical examination alone. Studies have found high levels of tau phosphorylated at Threonine 231 and/or Serine 199 in AD but not in other causes of dementia, in depression or in healthy elderly controls. Of particular interest, the test appears equally valid in cases of early AD as in moderate or late stages and may also be of use in predicting future decline in subjects with mild cognitive impairment. CONCLUSION: CSF phosphorylated tau is a promising diagnostic test for AD but this requires replication using pathologically confirmed cases.

Aged↗