ArticleJournal of the American Chemical Society2010
Solid-state NMR studies of HIV-1 capsid protein assemblies.
Article in Journal of the American Chemical Society, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.
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Who cites it
62 citing papers in PubMed.
- Synthesis ofMagnetic resonance in chemistry : MRC · 2026Article
- Selective detection of a key region in chemotaxis signaling protein complexes by solid-state NMR.Biophysical journal · 2025Article
- Advances in HIV-1 Assembly.Viruses · 2022Review
- Virus Structures and Dynamics by Magic-Angle Spinning NMR.Annual review of virology · 2021Review
- Curvature of the Retroviral Capsid Assembly Is Modulated by a Molecular Switch.The journal of physical chemistry letters · 2021Article
- Review
- Strategies for identifying dynamic regions in protein complexes: Flexibility changes accompany methylation in chemotaxis receptor signaling states.Biochimica et biophysica acta. Biomembranes · 2020Article
- Atomic-resolution structure of HIV-1 capsid tubes by magic-angle spinning NMR.Nature structural & molecular biology · 2020Article
- In Situ Detection of Endogenous HIV Activation by Dynamic Nuclear Polarization NMR and Flow Cytometry.International journal of molecular sciences · 2020Article
- Carbon-nitrogen REDOR to identify ms-timescale mobility in proteins.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2019Article
- Accuracy and precision of protein structures determined by magic angle spinning NMR spectroscopy: for some 'with a little help from a friend'.Journal of biomolecular NMR · 2019Article
- Dynamic Nuclear Polarization Magic-Angle Spinning Nuclear Magnetic Resonance Combined with Molecular Dynamics Simulations Permits Detection of Order and Disorder in Viral Assemblies.The journal of physical chemistry. B · 2019Article
- Analytical Techniques to Characterize the Structure, Properties, and Assembly of Virus Capsids.Analytical chemistry · 2019Review
- 100 kHz MAS Proton-Detected NMR Spectroscopy of Hepatitis B Virus Capsids.Frontiers in molecular biosciences · 2019Article
- Combining Cell-Free Protein Synthesis and NMR Into a Tool to Study Capsid Assembly Modulation.Frontiers in molecular biosciences · 2019Article
- Dynamic regulation of HIV-1 capsid interaction with the restriction factor TRIM5α identified by magic-angle spinning NMR and molecular dynamics simulations.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Segmental isotopic labeling of HIV-1 capsid protein assemblies for solid state NMR.Journal of biomolecular NMR · 2018Article
- Expanding the horizons for structural analysis of fully protonated protein assemblies by NMR spectroscopy at MAS frequencies above 100 kHz.Solid state nuclear magnetic resonance · 2017Article
- In vitro assembly of the Rous Sarcoma Virus capsid protein into hexamer tubes at physiological temperature.Scientific reports · 2017Article
- On the use of ultracentrifugal devices for routine sample preparation in biomolecular magic-angle-spinning NMR.Journal of biomolecular NMR · 2017Article
2 more citing papers are in PubMed but not listed here.
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7 authors.
Funding
Abstract
In mature HIV-1 virions, the 26.6 kDa CA protein is assembled into a characteristic cone-shaped core (capsid) that encloses the RNA viral genome. The assembled capsid structure is best described by a fullerene cone model that is made up from a hexameric lattice containing a variable number of CA pentamers, thus allowing for closure of tubular or conical structures. In this paper, we present a solid-state NMR analysis of the wild-type HIV-1 CA protein, prepared as conical and spherical assemblies that are stable and are not affected by magic angle spinning of the samples at frequencies between 10 and 25 kHz. Multidimensional homo- and heteronuclear correlation spectra of CA assemblies of uniformly (13)C,(15)N-labeled CA exhibit narrow lines, indicative of the conformational homogeneity of the protein in these assemblies. For the conical assemblies, partial residue-specific resonance assignments were obtained. Analysis of the NMR spectra recorded for the conical and spherical assemblies indicates that the CA protein structure is not significantly different in the different morphologies. The present results demonstrate that the assemblies of CA protein are amenable to detailed structural analysis by solid-state NMR spectroscopy.
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