A myristoyl switch regulates membrane binding of HIV-1 Gag
- 5 January 2004
- journal article
- editorial
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 101 (2) , 417-418
- https://doi.org/10.1073/pnas.0308043101
Abstract
No abstract availableThis publication has 37 references indexed in Scilit:
- N-terminal N -myristoylation of proteins: prediction of substrate proteins from amino acid sequence 1 1Edited by J. ThorntonJournal of Molecular Biology, 2002
- Multimerization of Human Immunodeficiency Virus Type 1 Gag Promotes Its Localization to Barges, Raft-Like Membrane MicrodomainsJournal of Virology, 2001
- HIV-1 Gag Proteins: Diverse Functions in the Virus Life CycleVirology, 1998
- Structural Basis for Activation of ARF GTPaseCell, 1998
- Crystal structures of the trimeric human immunodeficiency virus type 1 matrix protein: implications for membrane association and assembly.Proceedings of the National Academy of Sciences, 1996
- Three-dimensional Structure of the Human Immunodeficiency Virus Type 1 Matrix ProteinJournal of Molecular Biology, 1994
- Structural similarity between the p17 matrix protein of HIV-1 and interferon-γNature, 1994
- Myristylation and palmitylation of Src family members: The fats of the matterCell, 1994
- Binding of acylated peptides and fatty acids to phospholipid vesicles: Pertinence to myristoylated proteinsBiochemistry, 1993
- Role of capsid precursor processing and myristoylation in morphogenesis and infectivity of human immunodeficiency virus type 1.Proceedings of the National Academy of Sciences, 1989