Reference - Detail
| RRC ID | 36129 |
|---|---|
| Author | Mevius DE, Shen Y, Morishita M, di Luccio E. |
| Title | Cloning, expression, purification and crystallization of Schizosaccharomyces pombe Set7, a putative histone methyltransferase. |
| Journal | Acta Crystallogr F Struct Biol Commun |
| Abstract |
Dysfunction of histone-modifying enzymes affects chromatin regulation and is involved in carcinogenesis, tumour progression and other diseases. Histone methyltransferases are a family of key histone-modifying enzymes, but their structures, functions and mechanisms are incompletely understood, thus constraining drug-design efforts. Here, preliminary steps towards structure-function studies of Schizosaccharomyces pombe Set7, a putative histone methyltransferase and the first yeast full-length SET-domain-containing protein to be studied using X-ray crystallography, are reported. The methods from cloning to X-ray diffraction and phasing are discussed and the results will aid in prospective studies of histone-modifying enzymes. |
| Volume | 72(Pt 4) |
| Pages | 263-8 |
| Published | 2016-4-1 |
| DOI | 10.1107/S2053230X16003794 |
| PII | S2053230X16003794 |
| PMID | 27050258 |
| PMC | PMC4822981 |
| MeSH | Amino Acid Sequence Base Sequence Cloning, Molecular Crystallization Histone Methyltransferases Histone-Lysine N-Methyltransferase Schizosaccharomyces / chemistry* Schizosaccharomyces pombe Proteins / chemistry Schizosaccharomyces pombe Proteins / genetics* Schizosaccharomyces pombe Proteins / isolation & purification* |
| IF | 0.968 |
| Times Cited | 1 |
| WOS Category | BIOCHEMICAL RESEARCH METHODS BIOCHEMISTRY & MOLECULAR BIOLOGY BIOPHYSICS CRYSTALLOGRAPHY |
| Altmetric score |
オルトメトリクス指標項目
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| The most frequently cited source | X(Twitter) |
| Total number of mentions | 4 |
| Altmetric score changes over past 6months | 0.0 |
| Resource | |
| Yeast | cDNA library |