Analysis of human immunodeficiency virus type 1 matrix binding to membranes and nucleic acids

Alfadhli, Ayna; Still, Amelia; Barklis, Eric

doi:10.1128/jvi.01197-09

Cited by 145HIV Research and TreatmentLipid Membrane Structure and BehaviorCellular transport and secretion

Analysis of human immunodeficiency virus type 1 matrix binding to membranes and nucleic acids

Open access

Alfadhli, Ayna, Still, Amelia, Barklis, Eric·2009·Journal of Virology

DOI 10.1128/jvi.01197-09PMC PMC2786731

Open this paper in CoChat — free account

Abstract

The human immunodeficiency virus type 1 (HIV-1) matrix (MA) protein targets HIV-1 precursor Gag (PrGag) proteins to assembly sites at plasma membrane (PM) sites that are enriched in cholesterol and phosphatidylinositol-(4,5)-bisphosphate [PI(4,5)P 2 ]. MA is myristoylated, which enhances membrane binding, and specifically binds PI(4,5)P 2 through headgroup and 2′ acyl chain contacts. MA also binds nucleic acids, although the significance of this association with regard to the viral life cycle is unclear. We have devised a novel MA binding assay and used it to examine MA interactions with membranes and nucleic acids. Our results indicate that cholesterol increases the selectivity of MA for PI(4,5)P 2 -containing membranes, that PI(4,5)P 2 binding tolerates 2′ acyl chain variation, and that the MA myristate enhances membrane binding efficiency but not selectivity. We also observed that soluble PI(4,5)P 2 analogues do not compete effectively with PI(4,5)P 2 -containing liposomes for MA binding but surprisingly do increase nonspecific binding to liposomes. Finally, we have demonstrated that PI(4,5)P 2 -containing liposomes successfully outcompete nucleic acids for MA binding, whereas other liposomes do not. These results support a model in which RNA binding protects MA from associating with inappropriate cellular membranes prior to PrGag delivery to PM assembly sites.

Integrity signals

Registry

Crossref · 10.1128/jvi.01197-09

Cites

58 of 58 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

We couldn’t retrieve this paper’s full text, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

PI(4,5)P2 outcompetes RNA for MA interaction.
“and that PI(4,5)P 2 outcompetes RNA for MA interaction (80).”
From Role of host tRNAs and aminoacyl-tRNA synthetases in retroviral replication (2019) · cites this paper as [80]

The Hydrophobic Effect: Formation of Micelles and Biological Membranes
Tanford, C. (1991) · Medical Entomology and Zoology · Cited by 3,331 · see citing works
Cholesterol interactions with phospholipids in membranes
Ohvo-Rekilä, H. (2002) · Progress in Lipid Research · doi:10.1016/s0163-7827(01)00020-0 · Cited by 1,099 · see citing works
Evidence for Budding of Human Immunodeficiency Virus Type 1 Selectively from Glycolipid-Enriched Membrane Lipid Rafts
Nguyen, D., & Hildreth, J. E. K. (2000) · Journal of Virology · doi:10.1128/jvi.74.7.3264-3272.2000 · Cited by 788 · see citing works
The HIV lipidome: A raft with an unusual composition
Brügger, B., Glass, B., Haberkant, P., Leibrecht, I., Wieland, F., & Kräusslich, H. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0511136103 · Cited by 708 · see citing works
Plasma membrane rafts play a critical role in HIV-1 assembly and release
Ono, A., & Freed, E. O. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.241320298 · Cited by 705 · see citing works
Myristoylation-dependent replication and assembly of human immunodeficiency virus 1.
Bryant, M. L., & Ratner, L. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.2.523 · Cited by 624 · see citing works
Phosphatidylinositol (4,5) bisphosphate regulates HIV-1 Gag targeting to the plasma membrane
Ono, A., Ablan, S. D., Lockett, S. J., Nagashima, K., & Freed, E. O. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0405596101 · Cited by 553 · see citing works
Structural basis for targeting HIV-1 Gag proteins to the plasma membrane for virus assembly
Saad, J. S., Miller, J., Tai, J., Kim, A., Ghanam, R. H., & Summers, M. F. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0602818103 · Cited by 545 · see citing works
Identification of a membrane-binding domain within the amino-terminal region of human immunodeficiency virus type 1 Gag protein which interacts with acidic phospholipids
Zhou, W., Parent, L. J., Wills, J. W., & Resh, M. D. (1994) · Journal of Virology · doi:10.1128/jvi.68.4.2556-2569.1994 · Cited by 529 · see citing works
Synthesis, Assembly, and Processing of Viral Proteins
Swanstrom, R. I., & Wills, J. (1997) · Europe PMC (PubMed Central) · Cited by 513 · see citing works
Crystal structures of the trimeric human immunodeficiency virus type 1 matrix protein: implications for membrane association and assembly
Hill, C. P., Worthylake, D., Bancroft, D. P., Christensen, A. M., & Sundquist, W. I. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.7.3099 · Cited by 473 · see citing works
Lipid composition and fluidity of the human immunodeficiency virus envelope and host cell plasma membranes.
Aloia, R. C., Tian, H., & Jensen, F. C. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.11.5181 · Cited by 443 · see citing works
Domains of the human immunodeficiency virus type 1 matrix and gp41 cytoplasmic tail required for envelope incorporation into virions
Freed, E., & Martin, M. (1996) · Journal of Virology · doi:10.1128/jvi.70.1.341-351.1996 · Cited by 382 · see citing works
Plasma Membrane Is the Site of Productive HIV-1 Particle Assembly
Jouvenet, N., Neil, S. J. D., Bess, C., Johnson, M. C., Virgen, C. A., Simon, S. M., & Bieniasz, P. D. (2006) · PLoS Biology · doi:10.1371/journal.pbio.0040435 · Cited by 358 · see citing works
Virion incorporation of envelope glycoproteins with long but not short cytoplasmic tails is blocked by specific, single amino acid substitutions in the human immunodeficiency virus type 1 matrix
Freed, E., & Martin, M. (1995) · Journal of Virology · doi:10.1128/jvi.69.3.1984-1989.1995 · Cited by 344 · see citing works
Entropic switch regulates myristate exposure in the HIV-1 matrix protein
Tang, C., Loeliger, E., Luncsford, P. J., Kinde, I., Beckett, D., & Summers, M. F. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0305665101 · Cited by 320 · see citing works
The matrix protein of human immunodeficiency virus type 1 is required for incorporation of viral envelope protein into mature virions
Yu, X., Yuan, X., Matsuda, Z., Lee, T. H., & Essex, M. (1992) · Journal of Virology · doi:10.1128/jvi.66.8.4966-4971.1992 · Cited by 319 · see citing works
Role of the matrix protein in the virion association of the human immunodeficiency virus type 1 envelope glycoprotein
Dorfman, T., Mammano, F., Haseltine, W. A., & Göttlinger, H. G. (1994) · Journal of Virology · doi:10.1128/jvi.68.3.1689-1696.1994 · Cited by 288 · see citing works
Retroviruses human immunodeficiency virus and murine leukemia virus are enriched in phosphoinositides
Chan, R., Uchil, P. D., Jin, J., Shui, G., Ott, D. E., Mothes, W., & Wenk, M. R. (2008) · Journal of Virology · doi:10.1128/jvi.00981-08 · Cited by 282 · see citing works
Interaction between the human immunodeficiency virus Type 1 Gag matrix domain and phosphatidylinositol-(4,5)-bisphosphate is essential for efficient Gag membrane binding
Chukkapalli, V., Hogue, I. B., Boyko, V., Hu, W.-S., & Ono, A. (2008) · Journal of Virology · doi:10.1128/jvi.01614-07 · Cited by 268 · see citing works
Identification of human immunodeficiency virus type 1 Gag protein domains essential to membrane binding and particle assembly
Spearman, P. W., Wang, J. J., Heyden, N. V., & Ratner, L. (1994) · Journal of Virology · doi:10.1128/jvi.68.5.3232-3242.1994 · Cited by 245 · see citing works
Multimerization of Human Immunodeficiency Virus Type 1 Gag Promotes Its Localization to Barges, Raft-Like Membrane Microdomains
Lindwasser, O. W., & Resh, M. D. (2001) · Journal of Virology · doi:10.1128/jvi.75.17.7913-7924.2001 · Cited by 244 · see citing works
Mutations in the N-terminal region of human immunodeficiency virus type 1 matrix protein block intracellular transport of the Gag precursor
Yuan, X., Yu, X., Lee, T. H., & Essex, M. (1993) · Journal of Virology · doi:10.1128/jvi.67.11.6387-6394.1993 · Cited by 240 · see citing works
Role of the Gag Matrix Domain in Targeting Human Immunodeficiency Virus Type 1 Assembly
Ono, A., Orenstein, J. M., & Freed, E. O. (2000) · Journal of Virology · doi:10.1128/jvi.74.6.2855-2866.2000 · Cited by 239 · see citing works
Binding of Human Immunodeficiency Virus Type 1 Gag to Membrane: Role of the Matrix Amino Terminus
Ono, A., & Freed, E. O. (1999) · Journal of Virology · doi:10.1128/jvi.73.5.4136-4144.1999 · Cited by 238 · see citing works
Differential membrane binding of the human immunodeficiency virus type 1 matrix protein
Zhou, W., & Resh, M. D. (1996) · Journal of Virology · doi:10.1128/jvi.70.12.8540-8548.1996 · Cited by 226 · see citing works
Cholesterol Depletion of Human Immunodeficiency Virus Type 1 and Simian Immunodeficiency Virus with β-Cyclodextrin Inactivates and Permeabilizes the Virions: Evidence for Virion-Associated Lipid Rafts
Graham, D. R. M., Chertova, E. N., Hilburn, J. M., Arthur, L. O., & Hildreth, J. E. K. (2003) · Journal of Virology · doi:10.1128/jvi.77.15.8237-8248.2003 · Cited by 205 · see citing works
Membrane binding of human immunodeficiency virus type 1 matrix protein in vivo supports a conformational myristyl switch mechanism
Spearman, P. W., Horton, R., Ratner, L., & Kuli-zade, I. (1997) · Journal of Virology · doi:10.1128/jvi.71.9.6582-6592.1997 · Cited by 204 · see citing works
Assembly, processing, and infectivity of human immunodeficiency virus type 1 gag mutants
Wang, C. T., & Barklis, E. (1993) · Journal of Virology · doi:10.1128/jvi.67.7.4264-4273.1993 · Cited by 184 · see citing works
Self-citation
Evidence for a Stable Interaction of gp41 with Pr55Gag in Immature Human Immunodeficiency Virus Type 1 Particles
Wyma, D. J., Kotov, A., & Aiken, C. (2000) · Journal of Virology · doi:10.1128/jvi.74.20.9381-9387.2000 · Cited by 182 · see citing works
Rescue of human immunodeficiency virus type 1 matrix protein mutants by envelope glycoproteins with short cytoplasmic domains
Mammano, F., Kondo, E., Sodroski, J., Bukovský, A., & Göttlinger, H. G. (1995) · Journal of Virology · doi:10.1128/jvi.69.6.3824-3830.1995 · Cited by 157 · see citing works
Opposing Effects of Human Immunodeficiency Virus Type 1 Matrix Mutations Support a Myristyl Switch Model of Gag Membrane Targeting
Paillart, J., & Göttlinger, H. G. (1999) · Journal of Virology · doi:10.1128/jvi.73.4.2604-2612.1999 · Cited by 151 · see citing works
Conformation of the HIV-1 Gag Protein in Solution
Datta, S. A. K., Curtis, J. E., Ratcliff, W., Clark, P. K., Crist, R. M., Lebowitz, J., Krueger, S., & Rein, A. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.10.073 · Cited by 145 · see citing works
Interactions between HIV-1 Gag Molecules in Solution: An Inositol Phosphate-mediated Switch
Datta, S. A. K., Zhao, Z., Clark, P. K., Tarasov, S. G., Alexandratos, J. N., Campbell, S. J., Kvaratskhelia, M., Lebowitz, J., & Rein, A. R. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.10.072 · Cited by 132 · see citing works
Human Immunodeficiency Virus Type 1 Assembly and Lipid Rafts: Pr55 gag Associates with Membrane Domains That Are Largely Resistant to Brij98 but Sensitive to Triton X-100
Holm, K., Weclewicz, K., Hewson, R., & Suomalainen, M. (2003) · Journal of Virology · doi:10.1128/jvi.77.8.4805-4817.2003 · Cited by 132 · see citing works
HIV-1 matrix organizes as a hexamer of trimers on membranes containing phosphatidylinositol-(4,5)-bisphosphate
Alfadhli, A., Barklis, R. L., & Barklis, E. (2009) · Virology · doi:10.1016/j.virol.2009.02.048 · Cited by 125 · see citing works
Self-citation
Electrostatic interactions drive membrane association of the human immunodeficiency virus Type 1 Gag MA domain
Dalton, A. K., Ako-Adjei, D., Murray, P. S., Murray, D., & Vogt, V. M. (2007) · Journal of Virology · doi:10.1128/jvi.02757-06 · Cited by 118 · see citing works
Point Mutations in the HIV-1 Matrix Protein Turn Off the Myristyl Switch
Saad, J. S., Loeliger, E., Luncsford, P. J., Liriano, M., Tai, J., Kim, A., Miller, J. L., Joshi, A., Freed, E. O., & Summers, M. F. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.11.068 · Cited by 111 · see citing works
Depletion of cellular cholesterol inhibits membrane binding and higher-order multimerization of human immunodeficiency virus type 1 Gag
Ono, A., Waheed, A. A., & Freed, E. O. (2006) · Virology · doi:10.1016/j.virol.2006.10.011 · Cited by 106 · see citing works
Conditional infectivity of a human immunodeficiency virus matrix domain deletion mutant
Wang, C. T., Zhang, Y., McDermott, J., & Barklis, E. (1993) · Journal of Virology · doi:10.1128/jvi.67.12.7067-7076.1993 · Cited by 105 · see citing works
Self-citation
A myristoyl switch regulates membrane binding of HIV-1 Gag
Resh, M. D. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0308043101 · Cited by 103 · see citing works
Retroviral Matrix Domains Share Electrostatic Homology: Models for Membrane Binding Function throughout the Viral Life Cycle
Murray, P. S., Li, Z., Wang, J., Tang, C. L., Honig, B. H., & Murray, D. (2005) · Structure · doi:10.1016/j.str.2005.07.010 · Cited by 96 · see citing works
Human Immunodeficiency Virus Type 1 Protease Triggers a Myristoyl Switch That Modulates Membrane Binding of Pr55 gag and p17MA
Hermida-Matsumoto, L., & Resh, M. D. (1999) · Journal of Virology · doi:10.1128/jvi.73.3.1902-1908.1999 · Cited by 95 · see citing works
Redundant Roles for Nucleocapsid and Matrix RNA-Binding Sequences in Human Immunodeficiency Virus Type 1 Assembly
Ott, D. E., Coren, L. V., & Gagliardi, T. D. (2005) · Journal of Virology · doi:10.1128/jvi.79.22.13839-13847.2005 · Cited by 90 · see citing works
Roles of Matrix, p2, and N-Terminal Myristoylation in Human Immunodeficiency Virus Type 1 Gag Assembly
Morikawa, Y., HOCKLEY, D. J., Nermut, M. V., & Jones, I. M. (2000) · Journal of Virology · doi:10.1128/jvi.74.1.16-23.2000 · Cited by 80 · see citing works
Detection of a Trimeric Human Immunodeficiency Virus Type 1 Gag Intermediate Is Dependent on Sequences in the Matrix Protein, p17
Morikawa, Y., Zhang, W., HOCKLEY, D. J., Nermut, M. V., & Jones, I. M. (1998) · Journal of Virology · doi:10.1128/jvi.72.9.7659-7663.1998 · Cited by 75 · see citing works
In the beginning: genome recognition, RNA encapsidation and the initiation of complex retrovirus assembly
Jewell, N. A., & Mansky, L. M. (2000) · Journal of General Virology · doi:10.1099/0022-1317-81-8-1889 · Cited by 72 · see citing works
A Mutation in the Human Immunodeficiency Virus Type 1 Gag Protein Destabilizes the Interaction of the Envelope Protein Subunits gp120 and gp41
Davis, M., Jiang, J., Zhou, J.-J., Freed, E., & Aiken, C. (2006) · Journal of Virology · doi:10.1128/jvi.80.5.2405-2417.2006 · Cited by 71 · see citing works
Biochemical Characterization of Rous Sarcoma Virus MA Protein Interaction with Membranes
Dalton, A. K., Murray, P. S., Murray, D., & Vogt, V. M. (2005) · Journal of Virology · doi:10.1128/jvi.79.10.6227-6238.2005 · Cited by 65 · see citing works
Partitioning of HIV-1 Gag and Gag-Related Proteins to Membranes
Ehrlich, L. S., Fong, S., Scarlata, S., Zybarth, G., & Carter, C. (1996) · Biochemistry · doi:10.1021/bi952337x · Cited by 62 · see citing works
Role of Myristylation in HIV-1 Gag Assembly
Bouamr, F., Scarlata, S., & Carter, C. (2003) · Biochemistry · doi:10.1021/bi020692z · Cited by 57 · see citing works
Characterization of the In Vitro HIV-1 Capsid Assembly Pathway
Barklis, E., Alfadhli, A., McQuaw, C. M., Yalamuri, S. M., Still, A., Barklis, R. L., Kukull, B., & López, C. S. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.01.058 · Cited by 53 · see citing works
Self-citation
Membrane-induced alterations in HIV-1 gag and matrix protein-protein interactions
Scarlata, S., Ehrlich, L. S., & Carter, C. A. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1997.1615 · Cited by 48 · see citing works
HIV-1 Gag: Flipped out for PI(4,5)P 2
Freed, E. O. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0604715103 · Cited by 40 · see citing works
Assembly of Retrovirus Capsid-Nucleocapsid Proteins in the Presence of Membranes or RNA
Zuber, G., McDermott, J. E., Karanjia, S., Zhao, W.-Y., Schmid, M., & Barklis, E. (2000) · Journal of Virology · doi:10.1128/jvi.74.16.7431-7441.2000 · Cited by 33 · see citing works
Self-citation
High Affinity Nucleocapsid Protein Binding to the μΨ RNA Packaging Signal of Rous Sarcoma Virus
Zhou, J., McAllen, J. K., Tailor, Y., & Summers, M. F. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.04.046 · Cited by 30 · see citing works
Analysis of human immunodeficiency virus matrix domain replacements.
Scholz, I. G., Still, A., Dhenub, T. C., Coday, K., Webb, M., & Barklis, E. (2008) · Virology · doi:10.1016/j.virol.2007.10.010 · Cited by 29 · see citing works
Self-citation
Characterization of replication defects induced by mutations in the basic domain and C-terminus of HIV-1 matrix
Bhatia, A. K., Campbell, N., Panganiban, A. T., & Ratner, L. (2007) · Virology · doi:10.1016/j.virol.2007.06.046 · Cited by 24 · see citing works

Flagged first, then by citations

1 of the 59 references couldn’t be matched to a known paper.

Sorted by citations

HIV-1 assembly, release and maturation
Freed, E. O. (2015) · Nature Reviews Microbiology · doi:10.1038/nrmicro3490 · Cited by 654 · see citing works
Structural Determinants and Mechanism of HIV-1 Genome Packaging
Lu, K., Heng, X., & Summers, M. F. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.04.029 · Cited by 260 · see citing works
Global changes in the RNA binding specificity of HIV-1 Gag regulate virion genesis
Kutluay, S. B., Zang, T., Blanco-Melo, D., Powell, C., Jannain, D., Errando, M., & Bieniasz, P. D. (2014) · Cell · doi:10.1016/j.cell.2014.09.057 · Cited by 257 · see citing works
Opposing mechanisms involving RNA and lipids regulate HIV-1 Gag membrane binding through the highly basic region of the matrix domain
Chukkapalli, V., Oh, S. J., & Ono, A. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0908661107 · Cited by 229 · see citing works
HIV Gag polyprotein: processing and early viral particle assembly
Bell, N. M., & Lever, A. M. L. (2013) · Trends in Microbiology · doi:10.1016/j.tim.2012.11.006 · Cited by 222 · see citing works
Host factors involved in retroviral budding and release
Martin‐Serrano, J., & Neil, S. J. D. (2011) · Nature Reviews Microbiology · doi:10.1038/nrmicro2596 · Cited by 196 · see citing works
Molecular determinants that regulate plasma membrane association of HIV-1 Gag
Chukkapalli, V., & Ono, A. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.04.015 · Cited by 129 · see citing works
Relationships between plasma membrane microdomains and HIV‐1 assembly
Ono, A. (2010) · Biology of the Cell · doi:10.1042/bc20090165 · Cited by 115 · see citing works
HIV-1 Gag Extension: Conformational Changes Require Simultaneous Interaction with Membrane and Nucleic Acid
Datta, S. A. K., Heinrich, F., Raghunandan, S., Krueger, S., Curtis, J. E., Rein, A. R., & Nanda, H. (2010) · Journal of Molecular Biology · doi:10.1016/j.jmb.2010.11.051 · Cited by 114 · see citing works
The Life-Cycle of the HIV-1 Gag–RNA Complex
Mailler, É., Bernacchi, S., Marquet, R., Paillart, J., Vivet‐Boudou, V., & Smyth, R. P. (2016) · Viruses · doi:10.3390/v8090248 · Cited by 113 · see citing works
HIV-1 Gag protein can sense the cholesterol and acyl chain environment in model membranes
Dick, R. A., Goh, S. L., Feigenson, G. W., & Vogt, V. M. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1209408109 · Cited by 108 · see citing works
Maturation of the matrix and viral membrane of HIV-1
Qu, K., Ke, Z., Žíla, V., Anders‐Össwein, M., Glass, B., Muecksch, F., Müller, R., Schultz, C., Müller, B., Kräusslich, H., et al. (2021) · Science · doi:10.1126/science.abe6821 · Cited by 103 · see citing works
Diverse interactions of retroviral Gag proteins with RNAs
Rein, A. R., Datta, S. A. K., Jones, C. P., & Musier‐Forsyth, K. (2011) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2011.04.001 · Cited by 97 · see citing works
New Insights into HIV Assembly and Trafficking
Balasubramaniam, M., & Freed, E. O. (2011) · Physiology · doi:10.1152/physiol.00051.2010 · Cited by 96 · see citing works
Infectious RNA: Human Immunodeficiency Virus (HIV) Biology, Therapeutic Intervention, and the Quest for a Vaccine
van Heuvel, Y., Schatz, S., Rosengarten, J. F., & Stitz, J. (2022) · Toxins · doi:10.3390/toxins14020138 · Cited by 96 · see citing works
Distinct binding interactions of HIV-1 Gag to Psi and non-Psi RNAs: Implications for viral genomic RNA packaging
Webb, J. A., Jones, C. P., Parent, L. J., Rouzina, I. F., & Musier‐Forsyth, K. (2013) · RNA · doi:10.1261/rna.038869.113 · Cited by 95 · see citing works
Matrix domain modulates HIV-1 Gag's nucleic acid chaperone activity via inositol phosphate binding
Jones, C. P., Datta, S. A. K., Rein, A., Rouzina, I., & Musier-Forsyth, K. (2011) · Journal of Virology · doi:10.1128/jvi.01809-10 · Cited by 94 · see citing works
HIV Genome-Wide Protein Associations: a Review of 30 Years of Research
Li, G., & Clercq, E. D. (2016) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00065-15 · Cited by 90 · see citing works
Structural and Molecular Determinants of Membrane Binding by the HIV-1 Matrix Protein
Mercredi, P. Y., Bucca, N., Loeliger, B., Gaines, C. R., Mehta, M., Bhargava, P., Tedbury, P. R., Charlier, L., Floquet, N., Muriaux, D. M., et al. (2016) · Journal of Molecular Biology · doi:10.1016/j.jmb.2016.03.005 · Cited by 87 · see citing works
HIV-1 matrix protein binding to RNA
Alfadhli, A., McNett, H., Tsagli, S., Bächinger, H. P., Peyton, D. H., & Barklis, E. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.04.063 · Cited by 87 · see citing works
Self-citation
Nucleocapsid Promotes Localization of HIV-1 Gag to Uropods That Participate in Virological Synapses between T Cells
Llewellyn, G. N., Hogue, I. B., Grover, J. R., & Ono, A. (2010) · PLoS Pathogens · doi:10.1371/journal.ppat.1001167 · Cited by 85 · see citing works
HIV Type 1 Gag as a Target for Antiviral Therapy
Waheed, A. A., & Freed, E. O. (2011) · AIDS Research and Human Retroviruses · doi:10.1089/aid.2011.0230 · Cited by 81 · see citing works
Evidence in support of RNA-mediated inhibition of phosphatidylserine-dependent HIV-1 Gag membrane binding in cells
Chukkapalli, V., Inlora, J., Todd, G. C., & Ono, A. (2013) · Journal of Virology · doi:10.1128/jvi.00075-13 · Cited by 76 · see citing works
Trio engagement via plasma membrane phospholipids and the myristoyl moiety governs HIV-1 matrix binding to bilayers
Vlach, J., & Saad, J. S. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1216655110 · Cited by 75 · see citing works
Gag Localization and Virus-Like Particle Release Mediated by the Matrix Domain of Human T-Lymphotropic Virus Type 1 Gag Are Less Dependent on Phosphatidylinositol-(4,5)-Bisphosphate than Those Mediated by the Matrix Domain of HIV-1 Gag
Inlora, J., Chukkapalli, V., Derse, D., & Ono, A. (2011) · Journal of Virology · doi:10.1128/jvi.02383-10 · Cited by 73 · see citing works
Definition of a high-affinity Gag recognition structure mediating packaging of a retroviral RNA genome
Gherghe, C., Lombo, T., Leonard, C. W., Datta, S. A. K., Bess, J. W., Gorelick, R. J., Rein, A., & Weeks, K. M. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1006897107 · Cited by 69 · see citing works
Role of host tRNAs and aminoacyl-tRNA synthetases in retroviral replication
Jin, D., & Musier-Forsyth, K. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.rev118.002957 · Cited by 67 · see citing works
“Using in vitro liposome-binding assays, it was initially reported that RNA binding to MA prevents Gag binding to non-PI(4,5)P2 membrane lipids (78, 79) and that PI(4,5)P2 outcompetes RNA for MA interaction (80).”
Background
Virus assembly and plasma membrane domains: Which came first?
Kerviel, A., Thomas, A., Chaloin, L., Favard, C., & Muriaux, D. M. (2012) · Virus Research · doi:10.1016/j.virusres.2012.08.014 · Cited by 64 · see citing works
Membrane Binding of HIV-1 Matrix Protein: Dependence on Bilayer Composition and Protein Lipidation
Barros, M., Heinrich, F., Datta, S. A. K., Rein, A. R., Karageorgos, I. L., Nanda, H., & Lösche, M. (2016) · Journal of Virology · doi:10.1128/jvi.02820-15 · Cited by 63 · see citing works
Nucleic acid chaperone activity of retroviral Gag proteins
Rein, A. R. (2010) · RNA Biology · doi:10.4161/rna.7.6.13685 · Cited by 62 · see citing works
Multiple, Switchable Protein:RNA Interactions Regulate Human Immunodeficiency Virus Type 1 Assembly
Bieniasz, P. D., & Telesnitsky, A. (2018) · Annual Review of Virology · doi:10.1146/annurev-virology-092917-043448 · Cited by 62 · see citing works
Highly Sensitive Analysis of the Interaction between HIV-1 Gag and Phosphoinositide Derivatives Based on Surface Plasmon Resonance
Anraku, K., Fukuda, R., Takamune, N., Misumi, S., Okamoto, Y., Otsuka, M., & Fujita, M. (2010) · Biochemistry · doi:10.1021/bi9019274 · Cited by 59 · see citing works
HIV-1 Gag Associates with Specific Uropod-Directed Microdomains in a Manner Dependent on Its MA Highly Basic Region
Llewellyn, G. N., Grover, J. R., Olety, B., & Ono, A. (2013) · Journal of Virology · doi:10.1128/jvi.00040-13 · Cited by 56 · see citing works
Retroviral matrix and lipids, the intimate interaction
Hamard-Péron, É., & Muriaux, D. M. (2011) · Retrovirology · doi:10.1186/1742-4690-8-15 · Cited by 56 · see citing works
Role of the HIV-1 Matrix Protein in Gag Intracellular Trafficking and Targeting to the Plasma Membrane for Virus Assembly
Ghanam, R. H., Samal, A. B., Fernandez, T. F., & Saad, J. S. (2012) · Frontiers in Microbiology · doi:10.3389/fmicb.2012.00055 · Cited by 55 · see citing works
Membrane Binding and Subcellular Localization of Retroviral Gag Proteins Are Differentially Regulated by MA Interactions with Phosphatidylinositol-(4,5)-Bisphosphate and RNA
Inlora, J., Collins, D. R., Trubin, M. E., Chung, J. Y. J., & Ono, A. (2014) · mBio · doi:10.1128/mbio.02202-14 · Cited by 55 · see citing works
Analysis of HIV-1 Gag Protein Interactions via Biotin Ligase Tagging
Ritchie, C., Cylinder, I., Platt, E. J., & Barklis, E. (2015) · Journal of Virology · doi:10.1128/jvi.03584-14 · Cited by 54 · see citing works
Self-citation
Membrane interaction of retroviral Gag proteins
Dick, R. A., & Vogt, V. M. (2014) · Frontiers in Microbiology · doi:10.3389/fmicb.2014.00187 · Cited by 54 · see citing works
A Conformational Transition Observed in Single HIV-1 Gag Molecules during In Vitro Assembly of Virus-Like Particles
Munro, J. B., Nath, A., Farber, M. B., Datta, S. A. K., Rein, A. R., Rhoades, E. R., & Mothes, W. (2014) · Journal of Virology · doi:10.1128/jvi.03353-13 · Cited by 50 · see citing works
Retroviral Gag protein–RNA interactions: Implications for specific genomic RNA packaging and virion assembly
Olson, E. D., & Musier‐Forsyth, K. (2018) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2018.03.015 · Cited by 49 · see citing works
Reconstitution of selective HIV-1 RNA packaging in vitro by membrane-bound Gag assemblies
Carlson, L.-A., Bai, Y., Keane, S. C., Doudna, J. A., & Hurley, J. H. (2016) · eLife · doi:10.7554/elife.14663 · Cited by 48 · see citing works
Roles played by acidic lipids in HIV-1 Gag membrane binding
Olety, B., & Ono, A. (2014) · Virus Research · doi:10.1016/j.virusres.2014.06.015 · Cited by 47 · see citing works
Myristate Exposure in the Human Immunodeficiency Virus Type 1 Matrix Protein Is Modulated by pH
Fledderman, E. L., Fujii, K., Ghanam, R. H., Waki, K., Prevelige, P. E., Freed, E. O., & Saad, J. S. (2010) · Biochemistry · doi:10.1021/bi101245j · Cited by 45 · see citing works
Interrelationship between Cytoplasmic Retroviral Gag Concentration and Gag–Membrane Association
Fogarty, K., Berk, S., Grigsby, I. F., Chen, Y., Mansky, L. M., & Mueller, J. D. (2013) · Journal of Molecular Biology · doi:10.1016/j.jmb.2013.11.025 · Cited by 45 · see citing works
Molecular Mechanism of Arenavirus Assembly and Budding
Urata, S., & Yasuda, J. (2012) · Viruses · doi:10.3390/v4102049 · Cited by 45 · see citing works
Rous Sarcoma Virus Gag Has No Specific Requirement for Phosphatidylinositol-(4,5)-Bisphosphate for Plasma Membrane Association In Vivo or for Liposome Interaction In Vitro
Chan, J., Dick, R. A., & Vogt, V. M. (2011) · Journal of Virology · doi:10.1128/jvi.00760-11 · Cited by 43 · see citing works
Assembly and Replication of HIV-1 in T Cells with Low Levels of Phosphatidylinositol-(4,5)-Bisphosphate
Monde, K., Chukkapalli, V., & Ono, A. (2011) · Journal of Virology · doi:10.1128/jvi.02266-10 · Cited by 43 · see citing works
HIV-1 matrix protein p17 misfolding forms toxic amyloidogenic assemblies that induce neurocognitive disorders
Zeinolabediny, Y., Caccuri, F., Colombo, L., Morelli, F., Romeo, M., Rossi, A., Schiarea, S., Ciaramelli, C., Airoldi, C., Weston, R., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-10875-0 · Cited by 40 · see citing works
HIV-1 Matrix Protein Interactions with tRNA: Implications for Membrane Targeting
Gaines, C. R., Tkacik, E., Rivera-Oven, A., Somani, P., Achimovich, A. M., Alabi, T., Zhu, A. G., Getachew, N., Yang, A. L., McDonough, M., et al. (2018) · Journal of Molecular Biology · doi:10.1016/j.jmb.2018.04.042 · Cited by 40 · see citing works
Inhibition of HIV-1 Gag–membrane interactions by specific RNAs
Todd, G. C., Duchon, A., Inlora, J., Olson, E. D., Musier-Forsyth, K., & Ono, A. (2017) · RNA · doi:10.1261/rna.058453.116 · Cited by 39 · see citing works
Effect of Multimerization on Membrane Association of Rous Sarcoma Virus and HIV-1 Matrix Domain Proteins
Dick, R. A., Kamynina, E., & Vogt, V. M. (2013) · Journal of Virology · doi:10.1128/jvi.01659-13 · Cited by 38 · see citing works
Analysis of HIV-1 Matrix-Envelope Cytoplasmic Tail Interactions
Alfadhli, A., Staubus, A. O., Tedbury, P. R., Novikova, M., Freed, E. O., & Barklis, E. (2019) · Journal of Virology · doi:10.1128/jvi.01079-19 · Cited by 36 · see citing works
Self-citation
The roles of lipids and nucleic acids in HIV-1 assembly
Alfadhli, A., & Barklis, E. (2014) · Frontiers in Microbiology · doi:10.3389/fmicb.2014.00253 · Cited by 34 · see citing works
Self-citation
Biochemical Reconstitution of HIV-1 Assembly and Maturation
Kucharska, I., Ding, P., Zadrozny, K. K., Dick, R. A., Summers, M. F., Ganser‐Pornillos, B. K., & Pornillos, O. (2019) · Journal of Virology · doi:10.1128/jvi.01844-19 · Cited by 34 · see citing works
How HIV-1 Gag Manipulates Its Host Cell Proteins: A Focus on Interactors of the Nucleocapsid Domain
Klingler, J., Anton, H., Réal, É., Zeiger, M., Moog, C., Mély, Y., & Boutant, E. (2020) · Viruses · doi:10.3390/v12080888 · Cited by 34 · see citing works
Phosphatidylinositol-(4,5)-Bisphosphate Acyl Chains Differentiate Membrane Binding of HIV-1 Gag from That of the Phospholipase Cδ1 Pleckstrin Homology Domain
Olety, B., Veatch, S. L., & Ono, A. (2015) · Journal of Virology · doi:10.1128/jvi.00794-15 · Cited by 32 · see citing works
Basic Motifs Target PSGL-1, CD43, and CD44 to Plasma Membrane Sites Where HIV-1 Assembles
Grover, J. R., Veatch, S. L., & Ono, A. (2014) · Journal of Virology · doi:10.1128/jvi.02178-14 · Cited by 31 · see citing works
The HIV-1 Nucleocapsid Protein Recruits Negatively Charged Lipids To Ensure Its Optimal Binding to Lipid Membranes
Kempf, N., Postupalenko, V. Y., Bora, S., Didier, P., Arntz, Y., de ROCQUIGNY, H., & Mély, Y. (2014) · Journal of Virology · doi:10.1128/jvi.02931-14 · Cited by 30 · see citing works
A Highly Conserved Residue in the C-Terminal Helix of HIV-1 Matrix Is Required for Envelope Incorporation into Virus Particles
Brandano, L. A., & Stevenson, M. (2011) · Journal of Virology · doi:10.1128/jvi.06047-11 · Cited by 30 · see citing works
Solution Properties of Murine Leukemia Virus Gag Protein: Differences from HIV-1 Gag
Datta, S. A. K., Zuo, X., Clark, P. K., Campbell, S. J., Wang, Y., & Rein, A. R. (2011) · Journal of Virology · doi:10.1128/jvi.05889-11 · Cited by 30 · see citing works
The Interplay between HIV-1 Gag Binding to the Plasma Membrane and Env Incorporation
Murphy, R. E., & Saad, J. S. (2020) · Viruses · doi:10.3390/v12050548 · Cited by 30 · see citing works
Structural and molecular determinants of HIV-1 Gag binding to the plasma membrane
Vlach, J., & Saad, J. S. (2015) · Frontiers in Microbiology · doi:10.3389/fmicb.2015.00232 · Cited by 29 · see citing works
HIV-1 Gag as an Antiviral Target: Development of Assembly and Maturation Inhibitors
Spearman, P. W. (2015) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026615666150902102143 · Cited by 29 · see citing works
Beyond Plasma Membrane Targeting: Role of the MA domain of Gag in Retroviral Genome Encapsidation
Parent, L. J., & Gudleski-O'Regan, N. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.04.072 · Cited by 28 · see citing works
Retrovirus-Specific Differences in Matrix and Nucleocapsid Protein-Nucleic Acid Interactions: Implications for Genomic RNA Packaging
Sun, M., Grigsby, I. F., Gorelick, R. J., Mansky, L. M., & Musier‐Forsyth, K. (2013) · Journal of Virology · doi:10.1128/jvi.02151-13 · Cited by 28 · see citing works
Trimer Enhancement Mutation Effects on HIV-1 Matrix Protein Binding Activities
Alfadhli, A., Mack, A. R., Ritchie, C., Cylinder, I., Harper, L., Tedbury, P. R., Freed, E. O., & Barklis, E. (2016) · Journal of Virology · doi:10.1128/jvi.00509-16 · Cited by 27 · see citing works
Self-citation
Determinants of the HIV-1 core assembly pathway
López, C. S., Eccles, J. D., Still, A., Sloan, R., Barklis, R. L., Tsagli, S. M., & Barklis, E. (2011) · Virology · doi:10.1016/j.virol.2011.05.011 · Cited by 26 · see citing works
Self-citation
Relationships between MA-RNA Binding in Cells and Suppression of HIV-1 Gag Mislocalization to Intracellular Membranes
Thornhill, D., Olety, B., & Ono, A. (2019) · Journal of Virology · doi:10.1128/jvi.00756-19 · Cited by 26 · see citing works
Relationship between HIV-1 Gag Multimerization and Membrane Binding
Sumner, C. A., & Ono, A. (2022) · Viruses · doi:10.3390/v14030622 · Cited by 25 · see citing works
Analysis of Small Molecule Ligands Targeting the HIV-1 Matrix Protein-RNA Binding Site
Alfadhli, A., McNett, H., Eccles, J. D., Tsagli, S. M., Noviello, C., Sloan, R., López, C. S., Peyton, D. H., & Barklis, E. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.399865 · Cited by 25 · see citing works
Self-citation
Dynamic Association between HIV-1 Gag and Membrane Domains
Hogue, I. B., Llewellyn, G. N., & Ono, A. (2012) · Molecular Biology International · doi:10.1155/2012/979765 · Cited by 24 · see citing works
Cellular aspartyl proteases promote the unconventional secretion of biologically active HIV-1 matrix protein p17
Caccuri, F., Iaria, M. L., Campilongo, F., Varney, K. M., Rossi, A., Mitola, S. M. F., Schiarea, S., Bugatti, A., Mazzuca, P., Giagulli, C., et al. (2016) · Scientific Reports · doi:10.1038/srep38027 · Cited by 24 · see citing works
Overview of the Nucleic-Acid Binding Properties of the HIV-1 Nucleocapsid Protein in Its Different Maturation States
Mouhand, A., Pasi, M., Catala, M., Zargarian, L., Belfetmi, A., Barraud, P., Mauffret, O., & Tisné, C. (2020) · Viruses · doi:10.3390/v12101109 · Cited by 24 · see citing works
Structural and biophysical characterizations of HIV-1 matrix trimer binding to lipid nanodiscs shed light on virus assembly
Murphy, R. E., Samal, A. B., Vlach, J., Más, V., Prevelige, P. E., & Saad, J. S. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.010997 · Cited by 23 · see citing works
Nucleic acid–induced dimerization of HIV-1 Gag protein
Zhao, H., Datta, S. A. K., Kim, S. H., To, S. C., Chaturvedi, S. K., Rein, A. R., & Schuck, P. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.010580 · Cited by 21 · see citing works
Analysis of quinolinequinone reactivity, cytotoxicity, and anti-HIV-1 properties
Alfadhli, A., Mack, A. R., Harper, L., Berk, S., Ritchie, C., & Barklis, E. (2016) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2016.09.028 · Cited by 21 · see citing works
Self-citation
Functional Equivalence of Retroviral MA Domains in Facilitating Psi RNA Binding Specificity by Gag
Rye-McCurdy, T., Olson, E. D., Liu, S., Binkley, C., Reyes, J. C., Thompson, B., Flanagan, J. M., Parent, L. J., & Musier‐Forsyth, K. (2016) · Viruses · doi:10.3390/v8090256 · Cited by 21 · see citing works
Heparin and heparan sulfate proteoglycans promote HIV-1 p17 matrix protein oligomerization: computational, biochemical and biological implications
Bugatti, A., Paiardi, G., Urbinati, C., Chiodelli, P., Orro, A., Uggeri, M., Milanesi, L., Caruso, A., Caccuri, F., D’Ursi, P., et al. (2019) · Scientific Reports · doi:10.1038/s41598-019-52201-w · Cited by 21 · see citing works
Glutamic Acid Residues in HIV-1 p6 Regulate Virus Budding and Membrane Association of Gag
Friedrich, M., Setz, C., Hahn, F., Matthaei, A., Fraedrich, K., Rauch, P., Henklein, P., Traxdorf, M., Fossen, T., & Schubert, U. (2016) · Viruses · doi:10.3390/v8040117 · Cited by 20 · see citing works
The matrix domain contributes to the nucleic acid chaperone activity of HIV-2 Gag
Pachulska‐Wieczorek, K., Błaszczyk, L., Biesiada, M., Adamiak, R. W., & Purzycka, K. J. (2016) · Retrovirology · doi:10.1186/s12977-016-0245-1 · Cited by 20 · see citing works
Phosphoinositides as Regulators of Protein-Chromatin Interactions
Viiri, K. M., Mäki, M., & Lohi, O. (2012) · Science Signaling · doi:10.1126/scisignal.2002917 · Cited by 19 · see citing works
Properties and Functions of Feline Immunodeficiency Virus Gag Domains in Virion Assembly and Budding
González, S. A., & Affranchino, J. L. (2018) · Viruses · doi:10.3390/v10050261 · Cited by 18 · see citing works
Comparative Structural Effects of HIV-1 Gag and Nucleocapsid Proteins in Binding to and Unwinding of the Viral RNA Packaging Signal
Bell, N. M., Kenyon, J. C., Balasubramanian, S., & Lever, A. M. L. (2012) · Biochemistry · doi:10.1021/bi2017969 · Cited by 18 · see citing works
Molecular Determinants Directing HIV-1 Gag Assembly to Virus-Containing Compartments in Primary Macrophages
Inlora, J., Chukkapalli, V., Bedi, S., & Ono, A. (2016) · Journal of Virology · doi:10.1128/jvi.01004-16 · Cited by 17 · see citing works
Structural basis for targeting avian sarcoma virus Gag polyprotein to the plasma membrane for virus assembly
Vlach, J., Eastep, G. N., Ghanam, R. H., Watanabe, S. M., Carter, C. A., & Saad, J. S. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.003944 · Cited by 17 · see citing works
Rendezvous at Plasma Membrane: Cellular Lipids and tRNA Set up Sites of HIV-1 Particle Assembly and Incorporation of Host Transmembrane Proteins
Thornhill, D., Murakami, T., & Ono, A. (2020) · Viruses · doi:10.3390/v12080842 · Cited by 16 · see citing works
CLIP-related methodologies and their application to retrovirology
Bieniasz, P. D., & Kutluay, S. B. (2018) · Retrovirology · doi:10.1186/s12977-018-0417-2 · Cited by 14 · see citing works
Structural elements in the Gag polyprotein of feline immunodeficiency virus involved in Gag self-association and assembly
Cerfoglio, J. C. A., González, S. A., & Affranchino, J. L. (2014) · Journal of General Virology · doi:10.1099/vir.0.065151-0 · Cited by 14 · see citing works
Molecular Determinants in tRNA D-arm Required for Inhibition of HIV-1 Gag Membrane Binding
Sumner, C. A., Kotani, O., Liu, S., Musier‐Forsyth, K., Sato, H., & Ono, A. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.167390 · Cited by 13 · see citing works
Influence of HIV-1 Genomic RNA on the Formation of Gag Biomolecular Condensates
Monette, A., Niu, M., Maldonado, R. J. K., Chang, J. T., Lambert, G. S., Flanagan, J. M., Cochrane, A., Parent, L. J., & Mouland, A. J. (2023) · Journal of Molecular Biology · doi:10.1016/j.jmb.2023.168190 · Cited by 13 · see citing works
Mapping of the Self-Interaction Domains in the Simian Immunodeficiency Virus Gag Polyprotein
Rauddi, M. L., Donald, C. L. M., Affranchino, J. L., & González, S. A. (2010) · AIDS Research and Human Retroviruses · doi:10.1089/aid.2010.0137 · Cited by 13 · see citing works
Nucleic Acid Binding by Mason-Pfizer Monkey Virus CA Promotes Virus Assembly and Genome Packaging
Füzik, T., Píchalová, R., Schur, F. K. M., Strohalmová, K., Křížová, I., Hadravová, R., Rumlová, M., Briggs, J. A. G., Ulbrich, P., & Ruml, T. (2016) · Journal of Virology · doi:10.1128/jvi.03197-15 · Cited by 13 · see citing works
Lipid biosensor interactions with wild type and matrix deletion HIV-1 Gag proteins
Barklis, E., Staubus, A. O., Mack, A. R., Harper, L., Barklis, R. L., & Alfadhli, A. (2018) · Virology · doi:10.1016/j.virol.2018.03.004 · Cited by 13 · see citing works
Self-citation
Modulation of the HIV nucleocapsid dynamics finely tunes its RNA-binding properties during virion genesis
Mouhand, A., Belfetmi, A., Catala, M., Larue, V., Zargarian, L., Brachet, F., Gorelick, R. J., van Heijenoort, C., Mirambeau, G., Barraud, P., et al. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky612 · Cited by 13 · see citing works
Mechanistic Differences between Nucleic Acid Chaperone Activities of the Gag Proteins of Rous Sarcoma Virus and Human Immunodeficiency Virus Type 1 Are Attributed to the MA Domain
Rye-McCurdy, T., Nadaraia-Hoke, S., Gudleski-O'Regan, N., Flanagan, J. M., Parent, L. J., & Musier‐Forsyth, K. (2014) · Journal of Virology · doi:10.1128/jvi.00736-14 · Cited by 12 · see citing works
The influence of myristoylation, liposome surface charge and nucleic acid interaction in the partition properties of HIV-1 Gag-N-terminal peptides to membranes
Socas, L. B. P., & Ambroggio, E. E. (2020) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2020.183421 · Cited by 12 · see citing works
Understanding the Process of Envelope Glycoprotein Incorporation into Virions in Simian and Feline Immunodeficiency Viruses
Affranchino, J. L., & González, S. A. (2014) · Viruses · doi:10.3390/v6010264 · Cited by 12 · see citing works
Roles of Virion-Incorporated CD162 (PSGL-1), CD43, and CD44 in HIV-1 Infection of T Cells
Murakami, T., & Ono, A. (2021) · Viruses · doi:10.3390/v13101935 · Cited by 11 · see citing works
Coordination of Genomic RNA Packaging with Viral Assembly in HIV-1
Hellmund, C., & Lever, A. M. L. (2016) · Viruses · doi:10.3390/v8070192 · Cited by 10 · see citing works
Membrane Binding of the Rous Sarcoma Virus Gag Protein Is Cooperative and Dependent on the Spacer Peptide Assembly Domain
Dick, R. A., Barros, M., Jin, D., Lösche, M., & Vogt, V. M. (2015) · Journal of Virology · doi:10.1128/jvi.02733-15 · Cited by 10 · see citing works

HIV-1 matrix protein binding to RNA
Alfadhli, A., McNett, H., Tsagli, S., Bächinger, H. P., Peyton, D. H., & Barklis, E. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.04.063 · Cited by 87 · see citing works
Self-citation
Structural and Molecular Determinants of Membrane Binding by the HIV-1 Matrix Protein
Mercredi, P. Y., Bucca, N., Loeliger, B., Gaines, C. R., Mehta, M., Bhargava, P., Tedbury, P. R., Charlier, L., Floquet, N., Muriaux, D. M., et al. (2016) · Journal of Molecular Biology · doi:10.1016/j.jmb.2016.03.005 · Cited by 87 · see citing works
The roles of lipids and nucleic acids in HIV-1 assembly
Alfadhli, A., & Barklis, E. (2014) · Frontiers in Microbiology · doi:10.3389/fmicb.2014.00253 · Cited by 34 · see citing works
Self-citation
Membrane Binding of HIV-1 Matrix Protein: Dependence on Bilayer Composition and Protein Lipidation
Barros, M., Heinrich, F., Datta, S. A. K., Rein, A. R., & Lösche, M. (2016) · Biophysical Journal · doi:10.1016/j.bpj.2015.11.3084 · Cited by 2 · see citing works
HIV-1 matrix organizes as a hexamer of trimers on membranes containing phosphatidylinositol-(4,5)-bisphosphate
Alfadhli, A., Barklis, R. L., & Barklis, E. (2009) · Virology · doi:10.1016/j.virol.2009.02.048 · Cited by 125 · see citing works
Self-citation

Authors: Alfadhli, A., Still, A., & Barklis, E.
Affiliations: Oregon Health & Science University (US)
Corresponding author: Barklis, Eric
ORCID: Barklis, Eric
Venue: Journal of Virology
Publisher: American Society for Microbiology
Published: 2009-12
Volume: 83
Issue: 23
Pages: 12196-12203
ISSN: 0022-538X (ISSN-L)
1098-5514
DOI: 10.1128/jvi.01197-09
PMC: PMC2786731
OpenAlex: W2122077692
Cited by: 145
References: 59
Citations by year: 2026: 3 · 2025: 2 · 2024: 8 · 2023: 2 · 2022: 4 · 2021: 5 · 2020: 8 · 2019: 10 · 2018: 11 · 2017: 3 · 2016: 17 · 2015: 9 · 2014: 14 · 2013: 10 · 2012: 11
FWCI: 4.66
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: journals.asm.org/non-commercial-tdm-license (tdm)
Locations: Journal of Virology (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: National Institute of General Medical Sciences (GM060170, R01GM060170)
National Institute of Allergy and Infectious Diseases (AI071798, R01AI071798)
Topics: Life Sciences › Immunology and Microbiology › Virology › HIV Research and Treatment
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
Keywords: HIV-1 matrix protein, membrane binding, phosphatidylinositol 4,5-bisphosphate, cholesterol, myristoylation, nucleic acid binding, RNA binding, viral assembly, Gag protein, liposomes
MeSH terms: Cell Membrane, Cholesterol, Humans, Liposomes, Nucleic Acids, Protein Binding, HIV Antigens, HIV-1, Virus Assembly, Phosphatidylinositol 4,5-Diphosphate, gag Gene Products, Human Immunodeficiency Virus

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Analysis of human immunodeficiency virus type 1 matrix binding to membranes and nucleic acids

Abstract

Integrity signals

Claims the paper makes

Claims other papers make about this one

Cites

Cited by

Related

Record

About these checks