Structural basis for hijacking CBF-β and CUL5 E3 ligase complex by HIV-1 Vif

[20] Processing of X-ray diffraction data collected in oscillation mode

Otwinowski, Z., & Minor, W. (1997) · Methods in Enzymology · doi:10.1016/s0076-6879(97)76066-x · Cited by 33,475

Coot : model-building tools for molecular graphics

Emsley, P., & Cowtan, K. (2004) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444904019158 · Cited by 30,571

Phaser crystallographic software

McCoy, A. J., Grosse-Kunstleve, R. W., Adams, P. D., Winn, M. D., Storoni, L. C., & Read, R. J. (2007) · Journal of Applied Crystallography · doi:10.1107/s0021889807021206 · Cited by 20,612

PHENIX : building new software for automated crystallographic structure determination

Adams, P. D., Grosse-Kunstleve, R. W., Hung, L.-W., Ioerger, T. R., McCoy, A. J., Moriarty, N. W., Read, R. J., Sacchettini, J. C., Sauter, N. K., & Terwilliger, T. C. (2002) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444902016657 · Cited by 4,361

Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein

Sheehy, A. M., Gaddis, N., Choi, J. D., & Malim, M. H. (2002) · Nature · doi:10.1038/nature00939 · Cited by 2,407

Structure of the Cul1–Rbx1–Skp1–F boxSkp2 SCF ubiquitin ligase complex

Zheng, N., Schulman, B. A., Song, L., Miller, J. J., Jeffrey, P. D., Wang, P., Chu, C., Koepp, D. M., Elledge, S. J., Pagano, M., et al. (2002) · Nature · doi:10.1038/416703a · Cited by 1,507

Broad antiretroviral defence by human APOBEC3G through lethal editing of nascent reverse transcripts

Mangeat, B., Turelli, P., Caron, G., Friedli, M., Perrin, L., & Trono, D. (2003) · Nature · doi:10.1038/nature01709 · Cited by 1,486

DNA Deamination Mediates Innate Immunity to Retroviral Infection

Harris, R. S., Bishop, K. N., Sheehy, A. M., Craig, H. M., Petersen‐Mahrt, S. K., Watt, I. N., Neuberger, M. S., & Malim, M. H. (2003) · Cell · doi:10.1016/s0092-8674(03)00423-9 · Cited by 1,267

Induction of APOBEC3G Ubiquitination and Degradation by an HIV-1 Vif-Cul5-SCF Complex

Yu, X., Yu, Y., Liu, B., Luo, K., Kong, W., Mao, P., & Yu, X.-F. (2003) · Science · doi:10.1126/science.1089591 · Cited by 1,194

The cytidine deaminase CEM15 induces hypermutation in newly synthesized HIV-1 DNA

Zhang, H., Yang, B., Pomerantz, R. J., Zhang, C., Arunachalam, S., & Gao, L. (2003) · Nature · doi:10.1038/nature01707 · Cited by 1,061

Viral Manipulations of the Cullin-RING Ubiquitin Ligases

Liu, Y., & Tan, X. (2020) · Advances in experimental medicine and biology · doi:10.1007/978-981-15-1025-0_7 · Cited by 17

Mammalian Genomic Manipulation with Orthogonal Bxb1 DNA Recombinase Sites for the Functional Characterization of Protein Variants

Roelle, S. M., Kamath, N. D., & Matreyek, K. A. (2023) · ACS Synthetic Biology · doi:10.1021/acssynbio.3c00355 · Cited by 16

Vif determines the requirement for CBF-β in APOBEC3 degradation

Yoshikawa, R., Takeuchi, J. S., Yamada, E., Nakano, Y., Ren, F., Tanaka, H., Münk, C., Harris, R. S., Miyazawa, T., Koyanagi, Y., et al. (2014) · Journal of General Virology · doi:10.1099/jgv.0.000027 · Cited by 17

Role of cullin-elonginB-elonginC E3 complex in bovine immunodeficiency virus and maedi-visna virus Vif-mediated degradation of host A3Z2-Z3 proteins

Zhang, J., Wu, J., Wang, W., Wu, H., Yu, B., Wang, J., Lv, M., Wang, X., Zhang, H., Kong, W., et al. (2014) · Retrovirology · doi:10.1186/preaccept-1535827771128175 · Cited by 16

Moloney leukemia virus 10 (MOV10) inhibits the degradation of APOBEC3G through interference with the Vif-mediated ubiquitin–proteasome pathway

Chen, C., Ma, X., Hu, Q., Li, X., Huang, F., Zhang, J., Pan, T. S., Xia, J., Liu, C., & Zhang, H. (2017) · Retrovirology · doi:10.1186/s12977-017-0382-1 · Cited by 16

Vif-CBFβ interaction is essential for Vif-induced cell cycle arrest

Du, J., Rui, Y., Zheng, W., Li, P., Kang, J., Zhao, K., Sun, T., & Yu, X. (2019) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2019.02.136 · Cited by 15

Discovery of L15 as a novel Vif PROTAC degrader with antiviral activity against HIV-1

Luo, D., Luo, R., Wang, W., Deng, R., Wang, S., Ma, X., Pu, C., Liu, Y., Zhang, H., Yu, S., et al. (2024) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2024.129880 · Cited by 15

Design, synthesis and biological evaluation of indole derivatives as Vif inhibitors

Pu, C., Luo, R., Zhang, M., Hou, X., Yan, G., Jiang, L., Zheng, Y., & Li, R. (2017) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2017.07.026 · Cited by 16

Simian Immunodeficiency Virus Vif and Human APOBEC3B Interactions Resemble Those between HIV-1 Vif and Human APOBEC3G

Wang, J., Shaban, N. M., Land, A. M., Brown, W. L., & Harris, R. S. (2018) · Journal of Virology · doi:10.1128/jvi.00447-18 · Cited by 15

Targeting Cullin-RING Ubiquitin Ligases and the Applications in PROTACs

Gong, L., Cui, D., Xiong, X., & Zhao, Y. (2020) · Advances in experimental medicine and biology · doi:10.1007/978-981-15-1025-0_19 · Cited by 13

Requirement of HIV-1 Vif C-terminus for Vif-CBF-β interaction and assembly of CUL5-containing E3 ligase

Wang, H., Lv, G., Zhou, X., Li, Z., Liu, X., Yu, X.-F., & Zhang, W. (2014) · BMC Microbiology · doi:10.1186/s12866-014-0290-7 · Cited by 15

APOBEC3F Determinants of HIV-1 Vif Sensitivity

Land, A. M., Shaban, N. M., Evans, L., Hultquist, J. F., Albin, J. S., & Harris, R. S. (2014) · Journal of Virology · doi:10.1128/jvi.02362-14 · Cited by 13

Structure of CRL2Lrr1, the E3 ubiquitin ligase that promotes DNA replication termination in vertebrates

Zhou, H., Zaher, M. S., Walter, J. C., & Brown, A. (2021) · Nucleic Acids Research · doi:10.1093/nar/gkab1174 · Cited by 13

Polymorphisms of the cytidine deaminase APOBEC3F have different HIV-1 restriction efficiencies

Mohammadzadeh, N., Follack, T. B., Love, R. P., Stewart, K., Sanche, S. E., & Chelico, L. (2018) · Virology · doi:10.1016/j.virol.2018.11.004 · Cited by 14

The von Hippel–Lindau Cullin-RING E3 ubiquitin ligase regulates APOBEC3 cytidine deaminases

Scholtés, G. K., Sawyer, A. M., Vaca, C. C., Clerc, I., Roh, M., Song, C., & D’Aquila, R. T. (2021) · Translational research · doi:10.1016/j.trsl.2021.05.002 · Cited by 14

Characterization of an A3G-VifHIV-1-CRL5-CBFβ Structure Using a Cross-linking Mass Spectrometry Pipeline for Integrative Modeling of Host–Pathogen Complexes

Kaake, R. M., Echeverria, I., Kim, S. J., Dollen, J. V., Chesarino, N. M., Feng, Y., Yu, C., Ta, H. M., Chelico, L., Huang, L., et al. (2021) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2021.100132 · Cited by 13

Inhibition of ATM-directed antiviral responses by HIV-1 Vif

Wong, H. T., Luperchio, A. M., Riley, S., & Salamango, D. J. (2023) · PLoS Pathogens · doi:10.1371/journal.ppat.1011634 · Cited by 12

A naturally occurring bovine APOBEC3 confers resistance to bovine lentiviruses: implication for the co-evolution of bovids and their lentiviruses

Yamada, E., Yoshikawa, R., Nakano, Y., Misawa, N., Kobayashi, T., Ren, F., Izumi, T., Miyazawa, T., Koyanagi, Y., & Sato, K. (2016) · Scientific Reports · doi:10.1038/srep33988 · Cited by 13

Inhibition of APOBEC 3G activity impedes double‐stranded DNA repair

Prabhu, P., Shandilya, S. M. D., Britan‐Rosich, E., Nagler, A., Schiffer, C. A., & Kotler, M. (2015) · FEBS Journal · doi:10.1111/febs.13556 · Cited by 12

Computed insight into a peptide inhibitor preventing the induced fit mechanism of MurA enzyme from Pseudomonas aeruginosa

Lima, A. H., dos Santos, A. M., Alves, C. N., & Lameira, J. (2016) · Chemical Biology & Drug Design · doi:10.1111/cbdd.12882 · Cited by 12

The assembly of Vif ubiquitin E3 ligase for APOBEC3 degradation

Kim, D. Y. (2014) · Archives of Pharmacal Research · doi:10.1007/s12272-014-0519-x · Cited by 13

Core Binding Factor β Protects HIV, Type 1 Accessory Protein Viral Infectivity Factor from MDM2-mediated Degradation

Matsui, Y., Shindo, K., Nagata, K., Yoshinaga, N., Shirakawa, K., Kobayashi, M., & Takaori‐Kondo, A. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.734673 · Cited by 12

Demystifying Cell Cycle Arrest by HIV-1 Vif

Salamango, D. J., & Harris, R. S. (2021) · Trends in Microbiology · doi:10.1016/j.tim.2021.01.001 · Cited by 11

Regulation of Antiviral Innate Immunity Through APOBEC Ribonucleoprotein Complexes

Salter, J. D., Polevoda, B. V., Bennett, R. P., & Smith, H. C. (2019) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-3-030-28151-9_6 · Cited by 11

Interactions between HIV proteins and host restriction factors: implications for potential therapeutic intervention in HIV infection

Rashid, F., Zaongo, S. D., Iqbal, H., Harypursat, V., Song, F., & Chen, Y. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1390650 · Cited by 13

A Conserved uORF Regulates APOBEC3G Translation and Is Targeted by HIV-1 Vif Protein to Repress the Antiviral Factor

Libre, C., Seissler, T., Guerrero, S. X., Batisse, J., Verriez, C., Stupfler, B., Gilmer, O., Cabrera-Rodríguez, R., Weber, M. M., Valenzuela-Fernández, A., et al. (2021) · Biomedicines · doi:10.3390/biomedicines10010013 · Cited by 12

The Road Less Traveled: HIV's Use of Alternative Routes through Cellular Pathways

Marx, A., & Alian, A. (2015) · Journal of Virology · doi:10.1128/jvi.03684-14 · Cited by 11

Identification of a tripartite interaction between the N-terminus of HIV-1 Vif and CBFβ that is critical for Vif function

Desimmie, B. A., Smith, J. L., Matsuo, H., Hu, W.-S., & Pathak, V. K. (2017) · Retrovirology · doi:10.1186/s12977-017-0346-5 · Cited by 12

CAEV Vif Hijacks ElonginB/C, CYPA and Cullin5 to Assemble the E3 Ubiquitin Ligase Complex Stepwise to Degrade oaA3Z2-Z3

Zhao, Z., Li, Z., Huan, C., Wang, H., Su, X., & Zhang, W. (2019) · Frontiers in Microbiology · doi:10.3389/fmicb.2019.00565 · Cited by 11

Interruption of Vif/Elongin C interaction: In silico and experimental elucidation of the underlying molecular mechanism of benzimidazole-based APOBEC3G stabilizers

Radwan, M. O., Takaya, D., Koga, R., Iwamaru, K., Tateishi, H., Ali, T. F. S., Takaori‐Kondo, A., Otsuka, M., Honma, T., & Fujita, M. (2020) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2020.115409 · Cited by 10

Exploiting Ubiquitin Ligases for Induced Target Degradation as an Antiviral Strategy

Verma, R. (2021) · Advances in experimental medicine and biology · doi:10.1007/978-981-16-0267-2_13 · Cited by 10

Specific Deubiquitinating Enzymes Promote Host Restriction Factors Against HIV/SIV Viruses

Gao, W., Rui, Y., Li, G., Zhai, C., Su, J., Liu, H., Zheng, W., Zheng, B., Zhang, W., Yang, Y., et al. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.740713 · Cited by 11

Comparative Thermodynamic Analysis of Zinc Binding to the His/Cys Motif in Virion Infectivity Factor

Ghimire-Rijal, S., & Maynard, E. L. (2014) · Inorganic Chemistry · doi:10.1021/ic402907g · Cited by 10

Identification of a Conserved Interface of Human Immunodeficiency Virus Type 1 and Feline Immunodeficiency Virus Vifs with Cullin 5

Gu, Q., Zhang, Z., Gertzen, C. G. W., Häussinger, D., Gohlke, H., & Münk, C. (2017) · Journal of Virology · doi:10.1128/jvi.01697-17 · Cited by 9

High-speed atomic force microscopy directly visualizes conformational dynamics of the HIV Vif protein in complex with three host proteins

Pan, Y., Shlyakhtenko, L. S., & Lyubchenko, Y. L. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.014442 · Cited by 9

Feline Immunodeficiency Virus Vif N-Terminal Residues Selectively Counteract Feline APOBEC3s

Gu, Q., Zhang, Z., Ortiz, L. C., Franco, A. C., Häussinger, D., & Münk, C. (2016) · Journal of Virology · doi:10.1128/jvi.01593-16 · Cited by 9

Host AKT-mediated phosphorylation of HIV-1 accessory protein Vif potentiates infectivity via enhanced degradation of the restriction factor APOBEC3G

Raja, R., Wang, C., Mishra, R., Das, A., Ali, A., & Banerjea, A. C. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.101805 · Cited by 10

Reassessing APOBEC3G Inhibition by HIV-1 Vif-Derived Peptides

Richards, C. M., Li, M., Perkins, A. L., Rathore, A. S., Harki, D. A., & Harris, R. S. (2016) · Journal of Molecular Biology · doi:10.1016/j.jmb.2016.11.012 · Cited by 8

Inhibition of Vif-Mediated Degradation of APOBEC3G through Competitive Binding of Core-Binding Factor Beta

Miyagi, E., Welbourn, S., Sukegawa, S., Fábryová, H., Kao, S., & Strebel, K. (2020) · Journal of Virology · doi:10.1128/jvi.01708-19 · Cited by 9

Conformational Dynamics of the HIV-Vif Protein Complex

Ball, K. A., Chan, L. M., Stanley, D. J., Tierney, E., Thapa, S., Ta, H. M., Burton, L. A., Binning, J. M., Jacobson, M. P., & Gross, J. D. (2019) · Biophysical Journal · doi:10.1016/j.bpj.2019.03.014 · Cited by 7

Distinct MCM10 Proteasomal Degradation Profiles by Primate Lentiviruses Vpr Proteins

Chang, H., Siarot, L., Matsuura, R., Lo, C., Sato, H., Otsuki, H., & Aida, Y. (2020) · Viruses · doi:10.3390/v12010098 · Cited by 7

Structural insights into PPP2R5A degradation by HIV-1 Vif

Hu, Y., Delviks‐Frankenberry, K. A., Wu, C., Arizaga, F., Pathak, V. K., & Xiong, Y. (2024) · Nature Structural & Molecular Biology · doi:10.1038/s41594-024-01314-6 · Cited by 6

APOBEC3G Antagonism by Vif, or When Structure Meets Biological and Evolutionary Studies

Li, Y.-L., Langley, C. A., Emerman, M., & Gross, J. D. (2025) · Annual Review of Virology · doi:10.1146/annurev-virology-092623-091351 · Cited by 6

HIV-1 Vif Gained Breadth in APOBEC3G Specificity after Cross-Species Transmission of Its Precursors

Chesarino, N. M., & Emerman, M. (2021) · Journal of Virology · doi:10.1128/jvi.02071-21 · Cited by 6

Ringside views

Malim, M. H. (2014) · Nature · doi:10.1038/505167a · Cited by 6

Identification and characterization of loop7 motif and its role in regulating biological function of human APOBEC3G through molecular modeling and biological assay

Zhai, C., Ma, L., Zhang, Z., Ding, J., Wang, J., Zhang, Y., Li, X., Guo, F., Yu, L., Zhou, J., et al. (2017) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2017.05.002 · Cited by 6

Crystal structure of the yeast Rad7-Elc1 complex and assembly of the Rad7-Rad16-Elc1-Cul3 complex

Liu, L., Huo, Y., Li, J., & Jiang, T. (2019) · DNA repair · doi:10.1016/j.dnarep.2019.02.012 · Cited by 7

Elongin B promotes breast cancer progression by ubiquitinating tumor suppressor p14/ARF

Sui, X.-Y., Ma, X.-Y., Hou, Y., Cao, S.-W., Wang, Z.-Q., Jia, L., Fan, L., Shao, Z.-M., & Zhang, W. (2024) · Cell Biology and Toxicology · doi:10.1007/s10565-024-09864-7 · Cited by 7

Unique nonstructural proteins of Pneumonia Virus of Mice (PVM) promote degradation of interferon (IFN) pathway components and IFN-stimulated gene proteins

Dhar, J., & Barik, S. (2016) · Scientific Reports · doi:10.1038/srep38139 · Cited by 5

Defining Pharmacological Targets by Analysis of Virus–Host Protein Interactions

Llano, M., & Peña-Hernández, M. A. (2017) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2017.11.001 · Cited by 6

Jembrana disease virus Vif antagonizes the inhibition of bovine APOBEC3 proteins through ubiquitin-mediate protein degradation

Su, X., Wang, H., Zhou, X., Li, Z., Zheng, B., & Zhang, W. (2018) · Virology · doi:10.1016/j.virol.2018.03.028 · Cited by 8

HIV-1 vif mediates ubiquitination of the proximal protomer in the APOBEC3H dimer to induce degradation

Skorupka, K. A., Matsuoka, K., Hassan, B. A., Ghirlando, R., Balachandran, V., Chen, T.-H., Walters, K. J., Schiffer, C. A., Wolf, M., Iwatani, Y., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-60984-y · Cited by 5

Multiple lysines combined in HIV-1 Vif determines the responsiveness to CBF-β

Ai, Y., & Ma, J. (2015) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2015.01.001 · Cited by 4

Conserved Interaction of Lentiviral Vif Molecules with HIV-1 Gag and Differential Effects of Species-Specific Vif on Virus Production

Zheng, W., Ling, L., Li, Z., Wang, H., Rui, Y., Gao, W., Wang, S., Su, X., Wei, W., & Yu, X.-F. (2017) · Journal of Virology · doi:10.1128/jvi.00064-17 · Cited by 4

Dominant Negative Mutants of Human Immunodeficiency Virus Type 1 Viral Infectivity Factor (Vif) Disrupt Core-Binding Factor Beta-Vif Interaction

Duan, S., Yu, X., Wang, C., Meng, L., Gai, Y., Zhou, Y. M., Gu, T., Yu, B., Wu, J., & Yu, X. (2022) · Journal of Virology · doi:10.1128/jvi.00555-22 · Cited by 4

Suppression of HIV-1 Integration by Targeting HIV-1 Integrase for Degradation with A Chimeric Ubiquitin Ligase

Zhang, Z., Yuan, S., Xu, S., Guo, D., Chen, L., Hou, W., & Wang, M. (2020) · Virologica Sinica · doi:10.1007/s12250-020-00311-5 · Cited by 4

Investigation of Potent Lead for Acquired Immunodeficiency Syndrome from Traditional Chinese Medicine

Hung, T.-C., Lee, W., Chen, K., Chan, Y.-C., & Chen, C. Y. (2014) · BioMed Research International · doi:10.1155/2014/205890 · Cited by 4

Virome-wide ubiquitin ligase discovery reveals diverse mechanisms of immune evasion.

Glassman, C., Baek, K., Hou, G.-P., Zeng, Q.-R., Nardone, C., Juergens, K. B., Fujimura, E., O’Leary, C. N., Li, M. Z., Paulo, J. A., et al. (2026) · Science · doi:10.1126/science.aec6299 · Cited by 3

New Insights Into the Lineage-Specific Expansion and Functional Diversification of Lamprey AID/APOBEC Family

Chen, Y., Luo, L., Deng, L., Tian, X., Chen, S., Xu, A., & Yuan, S. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.822616 · Cited by 3

HIV-1 VIF and human APOBEC3G interaction directly observed through molecular specific labeling using a new dual promotor vector

Myint, W., Schiffer, C. A., & Matsuo, H. (2022) · Journal of Magnetic Resonance · doi:10.1016/j.jmr.2022.107230 · Cited by 3

Aromatic disulfides as potential inhibitors against interaction between deaminase APOBEC3G and HIV infectivity factor

Yan, X., Chen, C., Wang, C., Lan, W., Wang, J., & Cao, C. (2022) · Acta Biochimica et Biophysica Sinica · doi:10.3724/abbs.2022049 · Cited by 3

Evolutionary Conservation of PP2A Antagonism and G2/M Cell Cycle Arrest in Maedi-Visna Virus Vif

Luperchio, A. M., Jönsson, S., & Salamango, D. J. (2022) · Viruses · doi:10.3390/v14081701 · Cited by 3

Efficient production of protein complexes in mammalian cells using a poxvirus vector

Drillien, R., Pradeau‐Aubreton, K., Batisse, J., Mezher, J., Schenckbecher, E., Marguin, J., Ennifar, E., & Ruff, M. (2022) · PLoS ONE · doi:10.1371/journal.pone.0279038 · Cited by 3

Clues for two-step virion infectivity factor regulation by core binding factor beta

Ai, Y., Ma, J., & Wang, X. (2017) · Journal of General Virology · doi:10.1099/jgv.0.000749 · Cited by 3

Post-entry Restriction Factors of SIVcpz

Twizerimana, A. P., Scheck, R., Häussinger, D., & Münk, C. (2018) · Future Virology · doi:10.2217/fvl-2018-0093 · Cited by 3

Maedi–visna virus Vif protein uses motifs distinct from HIV-1 Vif to bind zinc and the cofactor required for A3 degradation

Knecht, K. M., Hu, Y., Rubene, D., Cook, M., Ziegler, S. J., Jönsson, S., & Xiong, Y. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.015828 · Cited by 3

APOBEC3F/G and Vif: Action and Counteractions

Libre, C., Batisse, J., Guerrero, S. X., Marquet, R., & Paillart, J. (2015) · Springer eBooks · doi:10.1007/978-1-4614-9610-6_376-1 · Cited by 3

Structural basis for recruitment of host CypA and E3 ubiquitin ligase by maedi-visna virus Vif

Hu, Y., Gudnadóttir, R. B., Knecht, K. M., Arizaga, F., Jönsson, S., & Xiong, Y. (2023) · Science Advances · doi:10.1126/sciadv.add3422 · Cited by 2

Direct inhibition of human APOBEC3 deaminases by HIV-1 Vif independent of the proteolysis pathway

Kamba, K., Wan, L., Unzai, S., Morishita, R., Takaori‐Kondo, A., Nagata, T., & Katahira, M. (2023) · Biophysical Journal · doi:10.1016/j.bpj.2023.12.015 · Cited by 2

Design of Vif-Derived Peptide Inhibitors with Anti-HIV-1 Activity by Interrupting Vif-CBFβ Interaction

Gai, Y., Duan, S., Wang, S., Liu, K., Yu, X., Yang, C., Li, G., Zhou, Y., Yu, B., Wu, J., et al. (2024) · Viruses · doi:10.3390/v16040490 · Cited by 2

Integrated protein-protein interaction and RNA interference screens reveal novel restriction and dependency factors for a tick-borne flavivirus in its human hostPreprint

Sourisseau, M., Unterfinger, Y., Lemasson, M., Chazal, M., Gracias, S., Caignard, G., Piumi, F., Grot, A., Moutailler, S., Vitour, D., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.11.03.514869 · Cited by 3

Variability in HIV-1 transmitted/founder virus susceptibility to combined APOBEC3F and APOBEC3G host restriction

Gaba, A., Yousefi, M., Bhattacharjee, S., & Chelico, L. (2024) · Journal of Virology · doi:10.1128/jvi.01606-24 · Cited by 2

The structural mechanism of HIV-2 Vif antagonism of human APOBEC3H

Niu, Y., Lilly, M., Ronayne, E. K., Emerman, M., Chesarino, N. M., & Gross, J. D. (2026) · Nature Communications · doi:10.1038/s41467-026-75045-1 · Cited by 1

Strain-specific epistasis shapes fitness landscapes of APOBEC3G antagonism by HIV-1 Vif proteins

Langley, C. A., Lilly, M., Malik, H. S., & Emerman, M. (2026) · Science Advances · doi:10.1126/sciadv.aed4872 · Cited by 1

An improved method for purification and refolding of recombinant HIV Vif expressed inEscherichia coli

Duarte, C. A., & Palomino, M. (2017) · Biotechnology and Applied Biochemistry · doi:10.1002/bab.1557 · Cited by 1

Same same but different - Antiviral factors interfering with the infectivity of HIV particles

Kriesel, F., Schelle, L., & Baldauf, H. (2020) · Microbes and Infection · doi:10.1016/j.micinf.2020.05.009 · Cited by 1

The unique structure of the highly conserved PPLP region in HIV-1 Vif is critical for the formation of APOBEC3 recognition interfaces

Iwatani, Y., Matsuoka, K., Ode, H., Kubota, M., Nakata, Y., Setoyama, Y., Kojima, K., Imahashi, M., & Yokomaku, Y. (2025) · mBio · doi:10.1128/mbio.03332-24 · Cited by 1

Contribution of APOBEC3-Driven Mutagenesis to HIV Evolution and HIV Drug Resistance

Dillon-White, M., & Simon, V. R. (2014) · Springer eBooks · doi:10.1007/978-1-4939-0667-3_8-1 · Cited by 1

Application of fluorescent-based technology detecting protein-protein interactions to monitor the binding of hepatitis B virus X protein to DNA-damage-binding protein 1

Omagari, K., Asamitsu, K., & Tanaka, Y. (2021) · Biophysics and Physicobiology · doi:10.2142/biophysico.bppb-v18.008 · Cited by 1

Contribution of APOBEC3-Driven Mutagenesis to HIV Evolution and HIV Drug Resistance

Dillon-White, M., & Simon, V. R. (2017) · Springer eBooks · doi:10.1007/978-1-4939-0694-9_8 · Cited by 1

Characterization of Vif domains that mediate Feline Immunodeficiency Virus antagonism of APOBEC3-H and APOBEC3-CH restrictionPreprint

Sims, O. L., Maynard, E. L., & Poeschla, E. M. (2017) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/144113 · Cited by 1

A conserved uORF impacts APOBEC3G translation and is essential for translational inhibition by the HIV-1 Vif proteinPreprint

Libre, C., Seissler, T., Guerrero, S. X., Batisse, J., Verriez, C., Stupfler, B., Gilmer, O., Weber, M. M., Cimarelli, A., Etienne, L., et al. (2021) · HAL · doi:10.1101/2021.01.13.426487 · Cited by 1

Hijacking through mimicry

Larochelle, S. (2014) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2774

Structural biology: Deadly deception

Cheung, F. (2014) · Nature China · doi:10.1038/nchina.2014.4

CBFß and HIV Infection

Kim, D. Y., & Gross, J. D. (2017) · Advances in experimental medicine and biology · doi:10.1007/978-981-10-3233-2_25 · Cited by 1

HIV-1 Viral Infectivity Factor Recruitment of Cellular Protein Complexes to Counter Host Antiviral Response

Evans, S. L. (2014)

The Vif protein of maedi-visna virus. Protein interaction and new roles

Aðalbjörnsdóttir, A. (2016)

ROLE OF APOBEC3 ENZYMES IN HIV-1 EVOLUTION

Mohammadzadeh, N. (2018) · HARVEST (University of Saskatchewan)

CHARACTERIZATION OF APOBEC3 REPERTOIRES AND EFFECTS ON RETROVIRAL REPLICATION

Follack, T. B. (2018) · HARVEST (University of Saskatchewan)

HIV-1 Vif protein is stabilized by AKT-mediated phosphorylation to enhance APOBEC3G degradationPreprint

Raja, R., Wang, C., & Banerjea, A. C. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.09.28.462184

APOBEC3F/G and Vif: Action and Counteractions

Libre, C., Batisse, J., Guerrero, S. X., Marquet, R., & Paillart, J. (2018) · Springer eBooks · doi:10.1007/978-1-4939-7101-5_376

HIV Restriction Factor APOBEC3G and Prospects for Its Use in Gene Therapy for HIV

Tikhonov, A., Mintaev, R. R., Glazkova, D. V., Bogoslovskaya, E. V., & Shipulin, G. A. (2022) · Molecular Biology · doi:10.1134/s0026893322040112

Selection and characterization of aptamers targeting the Vif-CBFβ-ELOB-ELOC-CUL5 complex

Kumagai, K., Kamba, K., Suzuki, T., Sekikawa, Y., Yuki, C., Hamada, M., Nagata, K., Takaori‐Kondo, A., Wan, L., Katahira, M., et al. (2024) · The Journal of Biochemistry · doi:10.1093/jb/mvae040

Coevolution of Lentiviral Vif with Host A3F and A3G: Insights from Computational Modelling and Ancestral Sequence Reconstruction

Huebert, D. N. G., Ghorbani, A., Lam, S. Y. B., & Larijani, M. (2025) · Viruses · doi:10.3390/v17030393

A testis-specific E3 ubiquitin ligase complex governs spermiogenesis and male fertility

Wu, T., Tu, C., Feng, Y., Qu, W., Chen, J., Wu, H., Gao, W., Xu, B., Yu, X., Bao, M., et al. (2026) · Nature Communications · doi:10.1038/s41467-026-70025-x

Autophagy inhibition in HIV-1-infected CD4 T lymphocytes : the role of Vif and Vpr accessory proteins

Alfaisal, J. (2016) · theses.fr (ABES) · doi:10.70675/912b4531z9f61z4aacz89bez526a9131ecb9

Contrôle traductionnel des facteurs de restriction APOBEC3G/F par la protéine Vif du VIH-1

Libre, C. (2016) · theses.fr (ABES) · doi:10.70675/1d41e245z435ez4f3cz912fzcf0856f0867e

Translational inhibition of the restriction factor APOBEC3G (A3G) by the HIV-1 Vif protein : role of a uORF in the 5'-UTR of A3G mRNA and identification of cellular factors

Seissler, T. (2019) · theses.fr (ABES) · doi:10.70675/c99208dbz03c5z4123za5fdz2c67e0e36e9d

Disrupting E3 ubiquitin ligase protein–protein interactions in cancer: chemical modalities, mechanisms, and therapeutic opportunities

Kamel, E. M., Khadrawy, S. M., Ali, M. A. M., Ahmed, N. A., Yassin, N. Y. S., Alkhedhairi, S., Alkhayl, F. F. A., & Lamsabhi, A. M. (2026) · Biochemical Pharmacology · doi:10.1016/j.bcp.2026.117951

Structural Basis of Intermolecular Interactions Between APOBEC3 and HIV-1 Vif

Ode, H., & Iwatani, Y. (2026) · Viruses · doi:10.3390/v18070787

Characterization of the Interaction of Full-Length HIV-1 Vif Protein with its Key Regulator CBFβ and CRL5 E3 Ubiquitin Ligase Components

Zhou, X., Evans, S. L., Han, X., Liu, Y., & Yu, X.-F. (2012) · PLoS ONE · doi:10.1371/journal.pone.0033495 · Cited by 55

Hijacking through mimicry

Larochelle, S. (2014) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2774

Characterization of the Interaction of Full-Length HIV-1 Vif Protein with its Key Regulator CBFb and CRL5 E3 Ubiquitin Ligase

Zhou, X., Evans, S. L., Han, X., Liu, Y., & Yu, X.-F. (2012)

Ringside views

Malim, M. H. (2014) · Nature · doi:10.1038/505167a · Cited by 6

Evolutionarily Conserved Requirement for Core Binding Factor Beta in the Assembly of the Human Immunodeficiency Virus/Simian Immunodeficiency Virus Vif-Cullin 5-RING E3 Ubiquitin Ligase

Han, X., Liang, W., Hua, D., Zhou, X., Du, J., Evans, S. L., Gao, Q., Wang, H., Viqueira, R., Wei, W., et al. (2014) · Journal of Virology · doi:10.1128/jvi.03833-13 · Cited by 27