| Chapter title |
PML nuclear bodies and other TRIM-defined subcellular compartments.
|
|---|---|
| Chapter number | 4 |
| Book title |
TRIM/RBCC Proteins
|
| Published in |
Advances in experimental medicine and biology, January 2012
|
| DOI | 10.1007/978-1-4614-5398-7_4 |
| Pubmed ID | |
| Book ISBNs |
978-1-4614-5397-0, 978-1-4614-5398-7
|
| Authors |
Batty, Elizabeth C, Jensen, Kirsten, Freemont, Paul S, Batty, Elizabeth C., Freemont, Paul S. |
| Abstract |
Tripartite motif (TRIM) proteins are defined by their possession of a RING, B-box and predicted coiled coil (RBCC) domain. The coiled-coil region facilitates the oligomerisation of TRIMs and contributes to the formation of high molecular weight complexes that show interesting subcellular compartmentalisations and structures. TRIM protein compartments include both nuclear and cytoplasmic filaments and aggregates (bodies), as well as diffuse subcellular distributions. TRIM 19, otherwise known as promyelocytic leukaemia (PML) protein forms nuclear aggregates termed PML nuclear bodies (PML NBs), at which a number of functionally diverse proteins transiently or covalently associate. PML NBs are therefore implicated in a wide variety of cellular functions such as transcriptional regulation, viral response, apoptosis and nuclear protein storage. |
Mendeley readers
Geographical breakdown
| Country | Count | As % |
|---|---|---|
| Unknown | 19 | 100% |
Demographic breakdown
| Readers by professional status | Count | As % |
|---|---|---|
| Student > Ph. D. Student | 3 | 16% |
| Researcher | 2 | 11% |
| Student > Postgraduate | 2 | 11% |
| Student > Doctoral Student | 1 | 5% |
| Professor | 1 | 5% |
| Other | 3 | 16% |
| Unknown | 7 | 37% |
| Readers by discipline | Count | As % |
|---|---|---|
| Agricultural and Biological Sciences | 4 | 21% |
| Biochemistry, Genetics and Molecular Biology | 3 | 16% |
| Immunology and Microbiology | 2 | 11% |
| Engineering | 1 | 5% |
| Unknown | 9 | 47% |