Promiscuous RNA binding ensures effective encapsidation of APOBEC3 proteins by HIV-1.
The apolipoprotein B mRNA-editing enzyme catalytic polypeptide-like 3 (APOBEC3) proteins are cell-encoded cytidine deaminases, some of which, such as APOBEC3G (A3G) and APOBEC3F (A3F), act as potent human immunodeficiency virus type-1 (HIV-1) restriction factors. These proteins require packaging int...
Saved in:
| Main Authors: | Luis Apolonia, Reiner Schulz, Tomaž Curk, Paula Rocha, Chad M Swanson, Torsten Schaller, Jernej Ule, Michael H Malim |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Public Library of Science (PLoS)
2015-01-01
|
| Series: | PLoS Pathogens |
| Online Access: | https://doi.org/10.1371/journal.ppat.1004609 |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
Similar Items
-
APOBEC3G inhibits elongation of HIV-1 reverse transcripts.
by: Kate N Bishop, et al.
Published: (2008-12-01) -
RNA-dependent oligomerization of APOBEC3G is required for restriction of HIV-1.
by: Hendrik Huthoff, et al.
Published: (2009-03-01) -
The role of flexibility and conformational selection in the binding promiscuity of PDZ domains.
by: Márton Münz, et al.
Published: (2012-01-01) -
Data structures for compound promiscuity analysis: promiscuity cliffs, pathways and promiscuity hubs formed by inhibitors of the human kinome
by: Filip Miljković, et al.
Published: (2019-08-01) -
Pyranose dehydrogenase ligand promiscuity: a generalized approach to simulate monosaccharide solvation, binding, and product formation.
by: Michael M H Graf, et al.
Published: (2014-12-01)