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ChannelsDB: database of biomacromolecular tunnels and pores
L. Pravda, D. Sehnal, R. Svobodová Vareková, V. Navrátilová, D. Toušek, K. Berka, M. Otyepka, J. Koca,
Jazyk angličtina Země Anglie, Velká Británie
Typ dokumentu časopisecké články, práce podpořená grantem
NLK
Directory of Open Access Journals
od 2005
Free Medical Journals
od 1996
PubMed Central
od 1974
Europe PubMed Central
od 1974
Open Access Digital Library
od 1996-01-01 do 2030-12-31
Open Access Digital Library
od 1974-01-01
Open Access Digital Library
od 1996-01-01
Open Access Digital Library
od 1996-01-01
Medline Complete (EBSCOhost)
od 1996-01-01
Oxford Journals Open Access Collection
od 1996-01-01
ROAD: Directory of Open Access Scholarly Resources
od 1974
PubMed
29036719
DOI
10.1093/nar/gkx868
Knihovny.cz E-zdroje
- MeSH
- aminokyseliny chemie metabolismus MeSH
- cytochrom P-450 CYP2D6 chemie genetika metabolismus MeSH
- databáze proteinů * MeSH
- eukaryotické buňky cytologie enzymologie MeSH
- exprese genu MeSH
- hydrofobní a hydrofilní interakce MeSH
- iontové kanály chemie genetika metabolismus MeSH
- jaderný pór chemie genetika metabolismus MeSH
- katalytická doména MeSH
- koenzymy chemie metabolismus MeSH
- lidé MeSH
- mutace MeSH
- prokaryotické buňky cytologie enzymologie MeSH
- software * MeSH
- statická elektřina MeSH
- zvířata MeSH
- Check Tag
- lidé MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
ChannelsDB (http://ncbr.muni.cz/ChannelsDB) is a database providing information about the positions, geometry and physicochemical properties of channels (pores and tunnels) found within biomacromolecular structures deposited in the Protein Data Bank. Channels were deposited from two sources; from literature using manual deposition and from a software tool automatically detecting tunnels leading to the enzymatic active sites and selected cofactors, and transmembrane pores. The database stores information about geometrical features (e.g. length and radius profile along a channel) and physicochemical properties involving polarity, hydrophobicity, hydropathy, charge and mutability. The stored data are interlinked with available UniProt annotation data mapping known mutation effects to channel-lining residues. All structures with channels are displayed in a clear interactive manner, further facilitating data manipulation and interpretation. As such, ChannelsDB provides an invaluable resource for research related to deciphering the biological function of biomacromolecular channels.
Citace poskytuje Crossref.org
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