Title |
NMR backbone resonance assignment and solution secondary structure determination of human NSD1 and NSD2
|
---|---|
Published in |
Biomolecular NMR Assignments, June 2016
|
DOI | 10.1007/s12104-016-9691-x |
Pubmed ID | |
Authors |
Nader Amin, Daniel Nietlispach, Seema Qamar, Joe Coyle, Elisabetta Chiarparin, Glyn Williams |
Abstract |
Proteins of the NSD family are histone-methyl transferases with critical functions in the regulation of chromatin structure and function. NSD1 and NSD2 are homologous proteins that function as epigenetic regulators of transcription through their abilities to catalyse histone methylation. Misregulation of NSD1 and NSD2 expression or mutations in their genes are linked to a number of human diseases such as Sotos syndrome, and cancers including acute myeloid leukemia, multiple myeloma, and lung cancer. The catalytic domain of both proteins contains a conserved SET domain which is involved in histone methylation. Here we report the backbone resonance assignments and secondary structure information of the catalytic domains of human NSD1 and NSD2. |
X Demographics
Geographical breakdown
Country | Count | As % |
---|---|---|
United States | 1 | 50% |
France | 1 | 50% |
Demographic breakdown
Type | Count | As % |
---|---|---|
Scientists | 1 | 50% |
Members of the public | 1 | 50% |
Mendeley readers
Geographical breakdown
Country | Count | As % |
---|---|---|
Unknown | 20 | 100% |
Demographic breakdown
Readers by professional status | Count | As % |
---|---|---|
Researcher | 5 | 25% |
Other | 4 | 20% |
Student > Master | 3 | 15% |
Student > Bachelor | 2 | 10% |
Student > Ph. D. Student | 1 | 5% |
Other | 3 | 15% |
Unknown | 2 | 10% |
Readers by discipline | Count | As % |
---|---|---|
Biochemistry, Genetics and Molecular Biology | 6 | 30% |
Medicine and Dentistry | 5 | 25% |
Agricultural and Biological Sciences | 2 | 10% |
Pharmacology, Toxicology and Pharmaceutical Science | 1 | 5% |
Sports and Recreations | 1 | 5% |
Other | 1 | 5% |
Unknown | 4 | 20% |