Cited by 288HIV Research and TreatmentT-cell and Retrovirus StudiesHIV/AIDS drug development and treatment

The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.

Role of the matrix protein in the virion association of the human immunodeficiency virus type 1 envelope glycoprotein

Open access

Dorfman, T, Mammano, F, Haseltine, W A, Göttlinger, H G·1994·Journal of Virology

DOI 10.1128/jvi.68.3.1689-1696.1994PMC PMC236628

Open this paper in CoChat — free account Open PDF

Abstract

The matrix (MA) protein of human immunodeficiency virus type 1 (HIV-1) forms an inner coat directly underneath the lipid envelope of the virion. The outer surface of the lipid envelope surrounding the capsid is coated by the viral Env glycoproteins. We report here that the HIV-1 capsid-Env glycoprotein association is very sensitive to minor alterations in the MA protein. The results indicate that most of the MA domain of the Gag precursor, except for its carboxy terminus, is essential for this association. Viral particles produced by proviruses with small missense or deletion mutations in the region coding for the amino-terminal 100 amino acids of the MA protein lacked both the surface glycoprotein gp120 and the transmembrane glycoprotein gp41, indicating a defect at the level of Env glycoprotein incorporation. Alterations at the carboxy terminus of the MA domain had no significant effect on the levels of particle-associated Env glycoprotein or on virus replication. The presence of HIV-1 MA protein sequences was sufficient for the stable association of HIV-1 Env glycoprotein with hybrid particles that contain the capsid (CA) and nucleocapsid (NC) proteins of visna virus. The association of HIV-1 Env glycoprotein with the hybrid particles was dependent upon the presence of the HIV-1 MA protein domain, as HIV-1 Env glycoprotein was not efficiently recruited into virus particles when coexpressed with authentic visna virus Gag proteins.

Integrity signals

Registry

Crossref · 10.1128/jvi.68.3.1689-1696.1994

Cites

0 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?

Role of capsid precursor processing and myristoylation in morphogenesis and infectivity of human immunodeficiency virus type 1
Göttlinger, H. G., Sodroski, J. G., & Haseltine, W. A. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.15.5781 · Cited by 841
Self-citation
A large deletion in the matrix domain of the human immunodeficiency virus gag gene redirects virus particle assembly from the plasma membrane to the endoplasmic reticulum
Fäcke, M., Janetzko, A., Shoeman, R. L., & Kräusslich, H. G. (1993) · Journal of Virology · doi:10.1128/jvi.67.8.4972-4980.1993 · Cited by 198 · cited 2×
“virus particle release from the cell membrane (7).”
Background
A single amino acid substitution within the matrix protein of a type D retrovirus converts its morphogenesis to that of a type C retrovirus
Rhee, S. S., & Hunter, E. (1990) · Cell · doi:10.1016/0092-8674(90)90289-q · Cited by 160

Show all 0 references

Sorted by citations

Items 201–264 of 264

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 16
“Notably, several site-directed mutagenesis and biochemical studies performed in HIV-1 also favor the concept that an association between the MA and the gp41 CD is necessary for Env incorporation into virions [82–87].”
Background
Envelope glycoproteins are dispensable for insertion of host HLA-DR molecules within nascent human immunodeficiency virus type 1 particles.
Martin, G., Beauséjour, Y., Thibodeau, J., & Tremblay, M. (2005) · Virology · doi:10.1016/j.virol.2005.02.021 · Cited by 14
“During viral assembly, the matrix (MA) domain of Pr55 interacts with Env, a process leading to the packaging of Env glycoproteins into newly formed viral entities (Dorfman et al., 1994; Freed and Martin, 1995; Yu et al., 1992).”
Background
Effect of Extension of the Cytoplasmic Domain of Human Immunodeficiency Type 1 Virus Transmembrane Protein gp41 on Virus Replication
Chan, W.-E., Wang, Y.-L., Lin, H.-H., & Chen, S. S.-L. (2004) · Journal of Virology · doi:10.1128/jvi.78.10.5157-5169.2004 · Cited by 12
“incorporation into nascent virions (10, 11, 48, 49).”
Background
Role of matrix protein in the type D retrovirus replication cycle: importance of the arginine residue at position 55.
Yasuda, J., & Hunter, E. (2000) · Virology · doi:10.1006/viro.1999.0179 · Cited by 13
Comprehensive Insights into the Molecular Basis of HIV Glycoproteins
Elalouf, A., Maoz, H., & Yaniv‐Rosenfeld, A. (2024) · Applied Sciences · doi:10.3390/app14188271 · Cited by 12
Myristoylation of Human Immunodeficiency Virus Type 1 gag Protein Is Required for Efficient env Protein Transportation to the Surface of Cells
Shiraishi, T., Misumi, S., Takama, M., Takahashi, I., & Shoji, S. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.4696 · Cited by 11
trans-Dominant Interference with Human Immunodeficiency Virus Type 1 Replication and Transmission in CD4+ Cells by an Envelope Double Mutant
Chen, S. S., Lee, S.-F., Chuang, C.-K., & Raj, V. (1999) · Journal of Virology · doi:10.1128/jvi.73.10.8290-8302.1999 · Cited by 12
Distinct functions for the membrane-proximal ectodomain region (MPER) of HIV-1 gp41 in cell-free and cell–cell viral transmission and cell–cell fusion
Narasimhulu, V. G. S., Bellamy-McIntyre, A. K., Laumaea, A., Lay, C.-S., Harrison, D. N., King, H. A. D., Drummer, H. E., & Poumbourios, P. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra117.000537 · Cited by 11
“The introduction of L8S/S9R mutations into MA has been shown previously to inhibit Env incorporation into virions (59) and to block cell–cell transmission (60).”
BackgroundMethod
Human Immunodeficiency Virus
Guatelli, J., Siliciano, R. F., Kuritzkes, D. R., & Richman, D. D. (2009) · Wiley eBooks · doi:10.1128/9781555815981.ch33 · Cited by 2
Structural characterization of HIV-1 matrix mutants implicated in envelope incorporationPreprint
Eastep, G. N., Ghanam, R., Green, T., & Saad, J. (2020) · bioRxiv · doi:10.1101/2020.10.14.339457 · Cited by 10
“Genetic and biochemical studies suggested that the MA domain of Gag and the gp41CT play distinct, yet complementary, roles in Env incorporation into budding particles (42,44,45,49,50,54-59).”
Background
REPLICATION OF HIV-1 ENVELOPE PROTEIN CYTOPLASMIC DOMAIN VARIANTS IN PERMISSIVE AND RESTRICTIVE CELLS
Staubus, A., Alfadhli, A., Barklis, R. L., & Barklis, E. (2019) · Virology · doi:10.1016/j.virol.2019.09.008 · Cited by 10
“They are cell typedependent, and are affected by mutations in the HIV-1 Gag protein matrix (MA) and Env cytoplasmic tail (CT) domains (Checkley et al., 2011; Freed and Martin, 1995, 1996; Murakami and Freed, 2000a, 2000b; Tedbury et al., 2013, 2016; Yu et al., 1992; Wang et al., 1993; Dorfman et al., 1994; Reil et al.…”
Background
Chimeric HIV-1 containing SIV matrix exhibit enhanced assembly in murine cells and replicate in a cell-type-dependent manner in human T cells
Chen, P., Hübner, W., Riviere, K., Liu, Y., & Chen, B. K. (2006) · Virology · doi:10.1016/j.virol.2006.02.022 · Cited by 6
“The MA domain of Gag is responsible for targeting HIV-1 assembly to specific membrane compartments in the cell (Facke et al., 1993; Freed et al., 1994).”
Background
The HIV-1 Matrix Domain of Gag Is Required for Vpu Responsiveness during Particle Release
Lee, Y.-H., Schwartz, M. D., & Panganiban, A. T. (1997) · Virology · doi:10.1006/viro.1997.8711 · Cited by 9
Advances in HIV-1 Assembly and Release
Freed, E. (2013) · Springer: New York · doi:10.1007/978-1-4614-7729-7 · Cited by 9
In Vivo Analysis of Infectivity, Fusogenicity, and Incorporation of a Mutagenic Viral Glycoprotein Library Reveals Determinants for Virus Incorporation
Salamango, D., Alam, K. K., Burke, D. H., & Johnson, M. C. (2016) · Journal of Virology · doi:10.1128/jvi.00804-16 · Cited by 8
Deletions in the fifth alpha helix of HIV-1 matrix block virus release
Sanford, B. L., Li, Y., Maly, C. J., Madson, C. J., Chen, H., Zhou, Y., & Belshan, M. (2014) · Virology · doi:10.1016/j.virol.2014.08.017 · Cited by 8
“Deletion of amino acids 98–100 abolished ENV incorporation (Dorfman et al., 1994).”
Construction of infectious SIV/HIV-2 chimeras
Ranjbar, S., Bhattacharya, U., Oram, J., Stott, E., & Almond, N. (2000) · AIDS (London) · doi:10.1097/00002030-200011100-00009 · Cited by 8
“Others have observed important biophysical and biochemical interactions between the long intracytoplasmic tail of the viral transmembrane and matrix proteins that are critical in determining whether virus particles are infectious [21,22].”
Background
HIV-1 Matrix Protein p17 Modulates in Vivo Preactivated Murine T-Cell Response and Enhances the Induction of Systemic and Mucosal Immunity Against Intranasally Co-administered Antigens
Fiorentini, S., Becker, P., Marini, E., Marconi, P., Avolio, M., Tosti, G., Link, C., Manservigi, R., Guzmán, C., & Caruso, A. (2006) · Viral immunology · doi:10.1089/vim.2006.19.177 · Cited by 7
Mechanism and Kinetics of HIV-1 Protease Activation
Tabler, C. O., & Tilton, J. C. (2024) · Viruses · doi:10.3390/v16121826 · Cited by 8
Probing Gag-Env dynamics at HIV-1 assembly sites using live-cell microscopy
Muecksch, F., Klaus, S., Laketa, V., Müller, B., & Kräusslich, H. (2024) · Journal of Virology · doi:10.1128/jvi.00649-24 · Cited by 7
“We have previously shown that Gag PM localization and late stages of HIV-1 assembly are not PI(4,5)P 2 -dependent in the absence of the MA domain (24), and it is known that mutations in MA affect Env incorporation into nascent virions (7, 9, 10).”
Background
Rab11-FIP1C Is Dispensable for HIV-1 Replication in Primary CD4+ T Cells, but Its Role Is Cell Type Dependent in Immortalized Human T-Cell Lines
Céspedes, M. V. F.-D., Hoffman, H. K., Carter, H., Simons, L. M., Naing, L., Ablan, S. D., Scheiblin, D., Hultquist, J., van Engelenburg, S. V., & Freed, E. (2022) · Journal of Virology · doi:10.1128/jvi.00876-22 · Cited by 6
Emergence of a Three Codon Deletion in gag p17 in HIV Type 1 Subtype C Long-Term Survivors, and General Population Spread
McCormack, G. P., Glynn, J., Clewley, J., Crampin, A., Travers, S. A. A., Redmond, N., Keane, T., Sibande, F., Mulawa, D., & Fine, P. (2006) · AIDS Research and Human Retroviruses · doi:10.1089/aid.2006.22.195 · Cited by 6
Cross-Reactivity of Anti-HIV-1-p17-Derivative Peptide (P30–52) Antibody to Env V3 Peptide
Ota, A., Tanaka-Taya, K., & Ueda, S. (1999) · Hybridoma · doi:10.1089/hyb.1999.18.149 · Cited by 6
HIV-1 Budding
Göttlinger, H. G. (2013) · Springer eBooks · doi:10.1007/978-1-4614-7729-7_5 · Cited by 1
Self-citation
Structural maturation of the matrix lattice is not required for HIV-1 particle infectivity
Chen, L., Hikichi, Y., Rey, J. S., Akıl, C., Zhu, Y., Veler, H., Shen, Y., Perilla, J. R., Freed, E. O., & Zhang, P. (2025) · Science Advances · doi:10.1126/sciadv.adv4356 · Cited by 6
Second site reversion of HIV-1 envelope protein baseplate mutations maps to the matrix protein
Alfadhli, A., Romanaggi, C., Barklis, R. L., & Barklis, E. (2024) · Journal of Virology · doi:10.1128/jvi.01742-23 · Cited by 5
“Multiple investigations have characterized MA mutations that either impair Env incorporation into virus particles or facilitate the assembly of otherwise incorporation-deficient Env mutants into virions (1, 2, 25, 26, 32, 36–38, 40, 42–45, 48).”
Background
Differences and commonalities in plasma membrane recruitment of the two morphogenetically distinct retroviruses HIV-1 and MMTV
Junková, P., Pleskot, R., Prchal, J., Sýs, J., & Ruml, T. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.011991 · Cited by 5
Cellular Trafficking Mechanisms in the Assembly and Release of HIV
Giese, S., & Marsh, M. (2013) · Springer eBooks · doi:10.1007/978-1-4614-7729-7_2 · Cited by 6
The gag proteins of human immunodeficiency virus type 1: mechanisms of virus assembly and possibilities for interference
Modrow, S., Kattenbeck, B., von Poblotzki, A., Niedrig, M., Wagner, R., & Wolf, H. J. (1994) · Medical Microbiology and Immunology · doi:10.1007/bf00194171 · Cited by 8
“The fact that both synthetic peptides derived from Pr55gag-protein sequences influence virus morphogenesis and the identical original amino acid regions are important for particle formation led us to the conclusion that intrinsic and defined functions of the gag protein are affected [24, 25, 54].”
Influential
Perspectives for a Protective HIV‐1 Vaccine
Schiavone, M., Quinto, I., & Scala, G. (2008) · Advances in pharmacology · doi:10.1016/s1054-3589(07)56014-x · Cited by 4
Humoral Immunity to HIV-1:
Nara, P. L. (1996) · doi:10.1007/978-1-4899-0191-0_12 · Cited by 5
Beyond reverse transcription: molecular mechanisms and emerging paradigms in retroviral replication
Jehad, M. A., Ali, L. M., Pillai, V. N., Prabhu, S. G., Mustafa, F., & Rizvi, T. A. (2026) · FEMS Microbiology Reviews · doi:10.1093/femsre/fuaf066 · Cited by 5
“…of HIV-1 MA, and especially its trimeriza-tion, has also been shown to be crucial for the incorporation of envelope glycoprotein into the nascently forming virus particles (Dorfman et al. 1994 , Freed and Martin 1995 , Cosson 1996 , Cannon et al. 1997 , Tedbury et al. 2016 , Eastep et al. 2021 ).”
The central domain of the matrix protein of HIV-1: influence on protein structure and virus infectivity
Ellenrieder, A.-D., Kremer, W., Kattenbeck, B., Hantschel, O. D., Horn, G., Kalbitzer, H. R., & Modrow, S. (2004) · Biological Chemistry · doi:10.1515/bc.2004.026 · Cited by 4
“The processed matrix protein contributes to virus maturation by its specific assembly to the characteristic morphology of infectious virus particles and by interactions with the viral envelope glycoproteins (Yu et al., 1992; Dorfman et al., 1994b; Nermut et al., 1994; Fuller et al., 1997), to the nuclear localization…”
BackgroundResult
The HIV gp41 Fusion Protein Inhibits T-Cell Activation through the Lentiviral Lytic Peptide 2 Motif.
Klug, Y. A., Schwarzer, R., Rotem, E., Charni, M., Nudelman, A., Gramatica, A., Zarmi, B., Rotter, V., & Shai, Y. (2019) · Biochemistry · doi:10.1021/acs.biochem.8b01175 · Cited by 3
Analysis of the functional compatibility of SIV capsid sequences in the context of the FIV gag precursor
Ovejero, C. A., Affranchino, J. L., & González, S. A. (2017) · PLoS ONE · doi:10.1371/journal.pone.0177297 · Cited by 3
Interactions of HIV-1 Proteins as Targets for Developing Anti-HIV-1 Peptides
Chandra, K., Maes, M., & Friedler, A. (2015) · Future Medicinal Chemistry · doi:10.4155/fmc.15.46 · Cited by 3
Evidence that Vpu Modulates HIV-1 Gag-Envelope Interaction towards Envelope Incorporation and Infectivity in a Cell Type Dependent Manner
Gautam, A., & Bhattacharya, J. (2013) · PLoS ONE · doi:10.1371/journal.pone.0061388 · Cited by 3
GPG-NH2 acts via the metabolite αHGA to target HIV-1 Env to the ER-associated protein degradation pathway
Jejcic, A., Höglund, S., & Vahlne, A. (2010) · Retrovirology · doi:10.1186/1742-4690-7-20 · Cited by 3
“The exceptionally long cytosolic tail of gp41, which stretches 150 aa into the particles, interacts with p55Gag and cellular proteins and may therefore play a role in the formation of proper internal viral structures [13-16].”
Effects of mutations in an HIV‐1 gag gene containing a 107‐codon tandem repeat in the matrix region on assembly and processing of the protein product
Liao, W., Chiu, H.-C., & Wang, C.-T. (2004) · Journal of Medical Virology · doi:10.1002/jmv.20209 · Cited by 2
“porated into virions via putative interactions with the MA [Dorfman et al., 1994; Lodge et al., 1994; Freed and Martin, 1995; Cosson, 1996].”
Background
Comparative Analysis of the Roles of Simian Immunodeficiency and Bovine Leukemia Virus Matrix Proteins in Gag Assembly in Insect Cells
KAKKER, N. K., Mikhailov, M. V., Jones, I. M., & Roy, P. (2002) · Virology · doi:10.1006/viro.2002.1441 · Cited by 3
Genomic and antigenic variation among rotavirus strains circulating in a large city of Argentina
Espul, C., Cuello, H., Martínez, N. E., de Centorbi, O. N. P., O’Ryan, M., Jackson, L., Campos, F., & Matson, D. O. (2000) · Journal of Medical Virology · doi:10.1002/1096-9071(200008)61:4 · Cited by 10
Introduction to Retroviruses
Goff, S. P. (2004) · Elsevier eBooks · doi:10.1016/b978-012764051-8/50006-8 · Cited by 4
Human Immunodeficiency Virus From Virus Structure to Pathogenesis
Gelderblom, H. R., & Böller, K. (2005) · Kluwer Academic Publishers eBooks · doi:10.1007/0-306-47650-9_11 · Cited by 2
Seroprevalence of antibodies to hepatitis E virus in the normal blood donor population and two aboriginal communities in Malaysia
Seow, H. F., Mahomed, N. M. B., Mak, J.-W., Riddell, M. A., Li, F., & Anderson, D. A. (1999) · Journal of Medical Virology · doi:10.1002/(sici)1096-9071(199910)59:2 · Cited by 37
Interaction of TSG101 with the PTAP Motif in Distinct Locations of Gag Determines the Incorporation of HTLV-1 Env into the Retroviral Virion
Maeda, Y., Monde, K., Terasawa, H., Tanaka, Y., & Sawa, T. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms242216520 · Cited by 1
Single-molecule 3D imaging of HIV cellular entry by liquid-phase electron tomographyPreprint
Kong, L., Liu, J., Zhang, M., Lu, Z., Ren, A., Liu, J., Li, J., & Ren, G. (2022) · Research Square · doi:10.21203/rs.3.rs-1298112/v1 · Cited by 2
Identifying possible sites for antibody neutralization escape: Implications for unique functional properties of the C-terminal tail of Human Immunodeficiency Virus Type 1 gp41.
Lu, Z., Huang, Y.-S., Tan, Y., Yu, Y., Wang, J., & Chen, Y.-H. (2016) · Immunology Letters · doi:10.1016/j.imlet.2016.04.005 · Cited by 1
The dominant-negative action of a fusion protein containing the cytoplasmic domain of human immunodeficiency virus type 1 transmembrane protein gp41 in virus replication
Chan, W.-E., & Chen, S. S.-L. (2007) · Journal of Biomedical Science · doi:10.1007/s11373-007-9186-y · Cited by 2
Anti-P30-52 Monoclonal Antibody Cross-Reacted to Env V3 and Inhibited the Viral Multiplication of HIV-1-Infected MT-4 Cells
Ota, A., BAUTISTA, A. N., YADAV, M. L., & Ueda, S. (1999) · Hybridoma · doi:10.1089/hyb.1999.18.139 · Cited by 1
The use of genetic sequencing technologies to determine HIV-1 viral tropism and to evaluate the effects of maraviroc on patient viral populations
McGovern, R. A. (2015) · cIRcle (University of British Columbia) · doi:10.14288/1.0166738
Synthesis of Functional and Variable HIV-1 Envelope Glycoproteins
Clapham, P. R. (2013) · Springer eBooks · doi:10.1007/978-1-4614-7729-7_4
The Entire SU Subunit is Required for the Incorporation of the HIV-1 Envelope Glycoprotein Complex into Virions
Li, Y.-Y., & Perez, L. G. (2004) · Virus genes · doi:10.1023/a:1007935927150 · Cited by 1
Gene Therapy and Research Applications of Intrabodies for Human Infectious Diseases
Marasco, W. A. (1997) · Springer eBooks · doi:10.1007/978-3-662-07992-8_8
Rab11-FIP1C is dispensable for HIV-1 replication in primary CD4+ T cells but its role is cell-type-dependent in immortalized human T-cell lines
de Céspedes, M. V., Hoffman, H. K., Carter, H., Simons, L. M., Naing, L., Ablan, S. D., Hultquist, J., van Engelenburg, S. V., & Freed, E. (2022) · bioRxiv · doi:10.1101/2022.06.03.494784
“The MA domain of Gag plays a central role in HIV-1 Env incorporation [(36, 37, 41-44); 121 for reviews, see (1, 3, 45)] and is thought to organize into hexamers of trimers on the inner 122 leaflet of the viral envelope (46-48).”
Background
Caractérisation de l'interaction entre Gag(NCp7) et la protéine cellulaire RPL7 : aspects moléculaire et fonctionnel
Mekdad, H. E. (2014) · theses.fr (ABES) · doi:10.70675/2880b607z8df6z44baz8659z6e3a5058715e
Virus Assembly as a Target for Antiretroviral Therapy
Barklis, E. (2013) · Springer eBooks · doi:10.1007/978-1-4614-7729-7_8 · Cited by 1
Structural Disorder in Matrix Proteins of HIV‐Related Viruses
Goh, G. K., Xue, B., Dunker, A. K., & Uversky, V. N. (2011) · Wiley eBooks · doi:10.1002/9781118135570.ch6
Antikörperreifung in der frühen HIV-Infektion und ihre Anwendung in Inzidenztesten
Loschen, S. (2010) · doi:10.18452/16164
P09-09. Impact of immune-driven sequence variation in HIV-1 subtype C Gag-Protease on viral fitness and disease progression
Wright, J., Brockman, M. A., Brumme, Z. L., Walker, B. D., Goulder, P., & Ndung’u, T. (2009) · Retrovirology · doi:10.1186/1742-4690-6-s3-p122
“The N-terminal 100 amino acids of the matrix protein are required for the incorporation of envelope glycoproteins into virion particles [46], including specific interacting residues at Gag codons 8, 9, 13, 16, 17, 18, 31, 35, and 63 [4750].”
Background
Investigation of the sequences and structural elements required for HIV-2 infectivity and genome dimerisation
L’hernault, A. (2009) · doi:10.21954/ou.ro.00010062
Tissue Compartmentalization and Tropism of HIV-1: A Dissertation
Brese, R. L. (2016) · doi:10.13028/m23k5t
“Capsid (CA) CA proteins surround the viral core in the virion, protecting the nucleocapsid, and are involved with assembly during the replication cycle (Dorfman et al, 1994b; Franke et al, 1994; Thali et al, 1994; Ganser-Pornillos et al, 2007).”
Background
Investigation of the C-Terminal Helix of HIV-1 Matrix: A Region Essential for Multiple Functions in the Viral Life Cycle: A Dissertation
Brandano, L. A. (2011) · The Journal of the American Medical Association (JAMA) Network (American Medical Association) · doi:10.13028/5zmj-9x81
Structure-function relationship of the baculovirus envelope fusion protein F
Long, G. (2007) · doi:10.18174/17088
In depth analysis of the HIV-specific CD8 T cell response in seropositives exposed to a mixed subtype epidemic
Geldmacher, C. (2006) · doi:10.22028/d291-20792
“Furthermore, because of its affinity for the cytoplasmic domain of gp41, p17 also plays an important role in positioning viral cores at the budding sites inside the infected cell (Dorfman et al., 1994; Yu et al., 1992).”
Background

Authors: Dorfman, T., Mammano, F., Haseltine, W. A., & Göttlinger, H. G.
Affiliations: Dana-Farber Cancer Institute (US)
ORCID: Mammano, F
Haseltine, W A
Göttlinger, H G
Venue: Journal of Virology
Publisher: American Society for Microbiology
Published: 1994-03
Volume: 68
Issue: 3
Pages: 1689-1696
ISSN: 0022-538X (ISSN-L)
1098-5514
DOI: 10.1128/jvi.68.3.1689-1696.1994
PMC: PMC236628
OpenAlex: W1557860493
Cited by: 288
References: 0
Citations by year: 2025: 2 · 2024: 4 · 2023: 1 · 2022: 7 · 2021: 1 · 2020: 4 · 2019: 5 · 2018: 3 · 2017: 3 · 2016: 4 · 2015: 4 · 2014: 8 · 2013: 13 · 2012: 9
FWCI: 8.13
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: journals.asm.org/non-commercial-tdm-license (tdm)
Locations: Journal of Virology (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: National Cancer Institute (CA06516, P30CA006516)
National Institute of Allergy and Infectious Diseases (AI29873, AI28691, P30AI028691)
Topics: Life Sciences › Immunology and Microbiology › Virology › HIV Research and Treatment
Life Sciences › Immunology and Microbiology › Immunology › T-cell and Retrovirus Studies
Health Sciences › Medicine › Infectious Diseases › HIV/AIDS drug development and treatment
Keywords: HIV-1 matrix protein, HIV-1 envelope glycoprotein, Gag precursor, gp120, gp41, visna virus, viral assembly, C-terminal domain, missense mutations, deletion mutations
MeSH terms: Cells, Cultured, DNA Mutational Analysis, Humans, Morphogenesis, Protein Binding, RNA, Viral, Structure-Activity Relationship, Viral Matrix Proteins, Virion, HIV-1, Gene Products, env

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

Role of the matrix protein in the virion association of the human immunodeficiency virus type 1 envelope glycoprotein

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Metadata

Record

About these checks