Name
Abstract | ||
|---|---|---|
Histone proteins are often noted for their high degree of sequence conservation. It is less often recognized that the histones are a heterogeneous protein family. Furthermore, several classes of non-histone proteins containing the histone fold motif exist. Novel histone and histone fold protein sequences continue to be added to public databases every year. The Histone Database (http://genome.nhgri.nih.gov/histones/) is a searchable, periodically updated collection of histone fold-containing sequences derived from sequence-similarity searches of public databases. Sequence sets are presented in redundant and non-redundant FASTA form, hotlinked to GenBank sequence files. Partial sequences are also now included in the database, which has considerably augmented its taxonomic coverage. Annotated alignments of full-length non-redundant sets of sequences are now available in both web-viewable (HTML) and downloadable (PDF) formats. The database also provides summaries of current information on solved histone fold structures, post-translational modifications of histones, and the human histone gene complement. |
Year | DOI | Venue |
|---|---|---|
2002 | 10.1093/nar/30.1.341 | NUCLEIC ACIDS RESEARCH |
Keywords | Field | DocType |
sequence alignment,internet,histones,protein conformation,genetic variation | Genome,Sequence alignment,Protein family,Sequence database,Histone,Biology,Histone fold,Genetics,Molecular biology,GenBank,Database,Protein structure | Journal |
Volume | Issue | ISSN |
30 | 1 | 0305-1048 |
Citations | PageRank | References |
2 | 0.50 | 1 |
Authors | ||
7 | ||
Name | Order | Citations | PageRank |
|---|---|---|---|
| Steven Sullivan | 1 | 5 | 1.69 |
| Daniel W Sink | 2 | 4 | 1.17 |
| Kenneth L Trout | 3 | 3 | 0.86 |
| Izabela Makalowska | 4 | 47 | 7.26 |
| Patrick M Taylor | 5 | 2 | 0.50 |
| Andreas D Baxevanis | 6 | 67 | 15.48 |
| David Landsman | 7 | 618 | 78.83 |