| Abstract | Recent studies indicate that the protein affected in spinal muscular atrophy, SMN, plays a role in the assembly of a number of macromolecular complexes that function in the nucleus, interacting with its partner proteins via their arginine- and glycine-rich domains. |
| Authors | M P Terns, R M Terns
(Affiliation: Department of Biochemistry and Molecular Biology, University of Georgia, Life Sciences Building, Athens, Georgia 30602, USA. mterns at bmb.uga.edu)
|
| Journal | Current biology : CB
(Curr Biol)
Vol. 11
Issue 21
Pg. R862-4
(Oct 30 2001)
ISSN: 0960-9822 England |
| PMID | 11696342
(Publication Type: Journal Article, Research Support, Non-U.S. Gov't, Research Support, U.S. Gov't, Non-P.H.S., Research Support, U.S. Gov't, P.H.S., Review)
|
| Chemical References |
- Cyclic AMP Response Element-Binding Protein
- Nerve Tissue Proteins
- RNA-Binding Proteins
- Ribonucleoproteins, Small Nuclear
- SMN Complex Proteins
|
| Topics |
- Coiled Bodies
(metabolism)
- Cyclic AMP Response Element-Binding Protein
- Muscular Atrophy, Spinal
(etiology)
- Nerve Tissue Proteins
(metabolism)
- Protein Binding
- RNA Splicing
- RNA-Binding Proteins
- Ribonucleoproteins, Small Nuclear
(metabolism)
- Ribosomes
(metabolism)
- SMN Complex Proteins
- Spliceosomes
(metabolism)
- Transcription, Genetic
|
