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 · see citing works

<i>Coot</i> : 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 · see citing works

<i>Phaser</i> 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 · see citing works

<i>PHENIX</i> : 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 · see citing works

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 2,330 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

The antiretroviral enzyme APOBEC3G is degraded by the proteasome in response to HIV-1 Vif

Sheehy, A. M., Gaddis, N., & Malim, M. H. (2003) · Nature Medicine · doi:10.1038/nm945 · Cited by 961 · see citing works

Species-Specific Exclusion of APOBEC3G from HIV-1 Virions by Vif

Mariani, R., Chen, D., Schröfelbauer, B., Navarro, F., König, R., Bollman, B., Münk, C., Nymark-McMahon, H., & Landau, N. R. (2003) · Cell · doi:10.1016/s0092-8674(03)00515-4 · Cited by 903 · see citing works

Structure of the VHL-ElonginC-ElonginB Complex: Implications for VHL Tumor Suppressor Function

Stebbins, C. E., Kaelin, W. G., & Pavletich, N. P. (1999) · Science · doi:10.1126/science.284.5413.455 · Cited by 852 · see citing works

HIV-1 Vif protein binds the editing enzyme APOBEC3G and induces its degradation

Marin, M., Rose, K. M., Kozak, S. L., & Kabat, D. (2003) · Nature Medicine · doi:10.1038/nm946 · Cited by 794 · see citing works

Differential Requirements for Runx Proteins in CD4 Repression and Epigenetic Silencing during T Lymphocyte Development

Taniuchi, I., Osato, M., Egawa, T., Sunshine, M. J., Bae, S., Komori, T., Ito, Y., & Littman, D. R. (2002) · Cell · doi:10.1016/s0092-8674(02)01111-x · Cited by 732 · see citing works

HIV-1 Vif Blocks the Antiviral Activity of APOBEC3G by Impairing Both Its Translation and Intracellular Stability

Stopak, K., de Noronha, C. M. C., Yonemoto, W. M., & Greene, W. C. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00353-8 · Cited by 723 · see citing works

Hypermutation of HIV-1 DNA in the Absence of the Vif Protein

Lecossier, D., Bouchonnet, F., Clavel, F., & Hance, A. J. (2003) · Science · doi:10.1126/science.1083338 · Cited by 652 · see citing works

The Vif Protein of HIV Triggers Degradation of the Human Antiretroviral DNA Deaminase APOBEC3G

Conticello, S. G., Harris, R. S., & Neuberger, M. S. (2003) · Current Biology · doi:10.1016/j.cub.2003.10.034 · Cited by 468 · see citing works

Vif hijacks CBF-β to degrade APOBEC3G and promote HIV-1 infection

Jäger, S., Kim, D. Y., Hultquist, J. F., Shindo, K., LaRue, R. S., Kwon, E., Li, M., Anderson, B. D., Yen, L., Stanley, D., et al. (2012) · Nature · doi:10.1038/nature10693 · Cited by 352 · see citing works

T-cell differentiation factor CBF-β regulates HIV-1 Vif-mediated evasion of host restriction

Zhang, W., Du, J., Evans, S. L., Yu, Y., & Yu, X.-F. (2011) · Nature · doi:10.1038/nature10718 · Cited by 265 · see citing works

Structural assembly of cullin-RING ubiquitin ligase complexes

Zimmerman, E. S., Schulman, B. A., & Zheng, N. (2010) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2010.08.010 · Cited by 227 · see citing works

Identification of Two Distinct Human Immunodeficiency Virus Type 1 Vif Determinants Critical for Interactions with Human APOBEC3G and APOBEC3F

Russell, R. A., & Pathak, V. K. (2007) · Journal of Virology · doi:10.1128/jvi.00395-07 · Cited by 216 · see citing works

Primate lentiviral virion infectivity factors are substrate receptors that assemble with cullin 5–E3 ligase through a HCCH motif to suppress APOBEC3G

Luo, K., Xiao, Z., Ehrlich, E. S., Yu, Y., Liu, B., Zheng, S. S., & Yu, X.-F. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0502440102 · Cited by 178 · see citing works

Crystal structure of the SOCS2–elongin C–elongin B complex defines a prototypical SOCS box ubiquitin ligase

Bullock, A. N., Debreczeni, J. E., Edwards, A. M., Sundström, M., & Knapp, S. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0601638103 · Cited by 165 · see citing works

Structural Insight into the Human Immunodeficiency Virus Vif SOCS Box and Its Role in Human E3 Ubiquitin Ligase Assembly

Stanley, B. J., Ehrlich, E. S., Short, L., Yu, Y., Xiao, Z., Yu, X.-F., & Xiong, Y. (2008) · Journal of Virology · doi:10.1128/jvi.00767-08 · Cited by 131 · see citing works

Assembly of HIV-1 Vif-Cul5 E3 ubiquitin ligase through a novel zinc-binding domain-stabilized hydrophobic interface in Vif

Xiao, Z., Ehrlich, E. S., Yu, Y., Luo, K., Wang, T., Tian, C., & Yu, X.-F. (2006) · Virology · doi:10.1016/j.virol.2006.02.002 · Cited by 130 · see citing works

Characterization of Conserved Motifs in HIV-1 Vif Required for APOBEC3G and APOBEC3F Interaction

He, Z., Zhang, W., Chen, G., Xu, R., & Yu, X.-F. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.06.061 · Cited by 129 · see citing works

Human Immunodeficiency Virus Type 1 Vif Protein Is an Integral Component of an mRNP Complex of Viral RNA and Could Be Involved in the Viral RNA Folding and Packaging Process

Zhang, H., Pomerantz, R., Dornadula, G., & Sun, Y. (2000) · Journal of Virology · doi:10.1128/jvi.74.18.8252-8261.2000 · Cited by 127 · see citing works

CBFβ Stabilizes HIV Vif to Counteract APOBEC3 at the Expense of RUNX1 Target Gene Expression

Kim, D. Y., Kwon, E., Hartley, P. D., Crosby, D. C., Mann, S., Krogan, N. J., & Gross, J. D. (2013) · Molecular Cell · doi:10.1016/j.molcel.2012.12.012 · Cited by 116 · see citing works

Structural basis for the heterodimeric interaction between the acute leukaemia‐associated transcription factors AML1 and CBFβ

Warren, A. J., Bravo, J., Williams, R. L., & Rabbitts, T. H. (2000) · The EMBO Journal · doi:10.1093/emboj/19.12.3004 · Cited by 107 · see citing works

A Patch of Positively Charged Amino Acids Surrounding the Human Immunodeficiency Virus Type 1 Vif SLVx4Yx9Y Motif Influences Its Interaction with APOBEC3G

Chen, G., He, Z., Wang, T., Xu, R., & Yu, X.-F. (2009) · Journal of Virology · doi:10.1128/jvi.00653-09 · Cited by 90 · see citing works

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 50 · see citing works

Structural basis of intersubunit recognition in elongin BC–cullin 5–SOCS box ubiquitin–protein ligase complexes

Kim, Y. K., Kwak, M., Ku, B., Suh, H., Joo, K., Lee, J., Jung, J. U., & Oh, B. (2013) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444913011220 · Cited by 41 · see citing works

Molecular Architecture of the Ankyrin SOCS Box Family of Cul5-Dependent E3 Ubiquitin Ligases

Muniz, J. R. C., Guo, K., Kershaw, N. J., Ayinampudi, V., von Delft, F., Babon, J. J., & Bullock, A. N. (2013) · Journal of Molecular Biology · doi:10.1016/j.jmb.2013.06.015 · Cited by 34 · see citing works

HIV Type 1 Viral Infectivity Factor and the RUNX Transcription Factors Interact with Core Binding Factor β on Genetically Distinct Surfaces

Hultquist, J. F., McDougle, R. M., Anderson, B. D., & Harris, R. S. (2012) · AIDS Research and Human Retroviruses · doi:10.1089/aid.2012.0142 · Cited by 29 · see citing works

PROTAC targeted protein degraders: the past is prologue

Békés, M., Langley, D. R., & Crews, C. M. (2022) · Nature Reviews Drug Discovery · doi:10.1038/s41573-021-00371-6 · Cited by 3,395 · see citing works

Ubiquitin ligases: structure, function, and regulation

Zheng, N., & Shabek, N. (2017) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060815-014922 · Cited by 1,499 · see citing works

Catalytic in vivo protein knockdown by small-molecule PROTACs

Bondeson, D. P., Mares, A., Smith, I. E. D., Ko, E., Campos, S., Miah, A. H., Mulholland, K. E., Routly, N., Buckley, D. L., Gustafson, J. L., et al. (2015) · Nature Chemical Biology · doi:10.1038/nchembio.1858 · Cited by 1,356 · see citing works

Targeted protein degradation: expanding the toolbox

Schapira, M., Calabrese, M. F., Bullock, A. N., & Crews, C. M. (2019) · Nature Reviews Drug Discovery · doi:10.1038/s41573-019-0047-y · Cited by 960 · see citing works

APOBECs and virus restriction

Harris, R. S., & Dudley, J. P. (2015) · Virology · doi:10.1016/j.virol.2015.03.012 · Cited by 518 · see citing works

The RUNX family: developmental regulators in cancer

Ito, Y., Bae, S.-C., & Chuang, L. S. H. (2015) · Nature Reviews Cancer · doi:10.1038/nrc3877 · Cited by 399 · see citing works

HIV-1 and interferons: who's interfering with whom?

Doyle, T., Goujon, C., & Malim, M. H. (2015) · Nature Reviews Microbiology · doi:10.1038/nrmicro3449 · Cited by 280 · see citing works

Intrinsic host restrictions to HIV-1 and mechanisms of viral escape

Simon, V. R., Bloch, N., & Landau, N. R. (2015) · Nature Immunology · doi:10.1038/ni.3156 · Cited by 260 · see citing works

Targeting Cullin–RING E3 ubiquitin ligases for drug discovery: structure, assembly and small-molecule modulation

Bulatov, E., & Ciulli, A. (2015) · Biochemical Journal · doi:10.1042/bj20141450 · Cited by 237 · see citing works

Chasing molecular glue degraders: screening approaches

Domostegui, A., Nieto-Barrado, L., Perez-Lopez, C., & Mayor-Ruiz, C. (2022) · Chemical Society Reviews · doi:10.1039/d2cs00197g · Cited by 200 · see citing works

APOBEC Enzymes as Targets for Virus and Cancer Therapy

Olson, M. E., Harris, R. S., & Harki, D. A. (2017) · Cell chemical biology · doi:10.1016/j.chembiol.2017.10.007 · Cited by 159 · see citing works

An E3 ligase guide to the galaxy of small-molecule-induced protein degradation

Jevtić, P., Haakonsen, D. L., & Rapé, M. (2021) · Cell chemical biology · doi:10.1016/j.chembiol.2021.04.002 · Cited by 144 · see citing works

Suppression of APOBEC3-mediated restriction of HIV-1 by Vif

Feng, Y., Baig, T. T., Love, R. P., & Chelico, L. (2014) · Frontiers in Microbiology · doi:10.3389/fmicb.2014.00450 · Cited by 113 · see citing works

Development of benzimidazole derivatives to inhibit HIV-1 replication through protecting APOBEC3G protein

Pan, T. S., He, X., Chen, B., Chen, H., Geng, G., Luo, H., Zhang, H., & Bai, C. (2015) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2015.03.050 · Cited by 114 · see citing works

Natural Polymorphisms in Human APOBEC3H and HIV-1 Vif Combine in Primary T Lymphocytes to Affect Viral G-to-A Mutation Levels and Infectivity

Refsland, E. W., Hultquist, J. F., Luengas, E. M., Ikeda, T., Shaban, N. M., Law, E. K., Brown, W. L., Reilly, C., Emerman, M., & Harris, R. S. (2014) · PLoS Genetics · doi:10.1371/journal.pgen.1004761 · Cited by 103 · see citing works

Potential APOBEC-mediated RNA editing of the genomes of SARS-CoV-2 and other coronaviruses and its impact on their longer term evolution

Ratcliff, J., & Peter Simmonds, K. (2021) · Virology · doi:10.1016/j.virol.2020.12.018 · Cited by 98 · see citing works

Cullin E3 Ligases and Their Rewiring by Viral Factors

Mahon, C., Krogan, N., Craik, C., & Pick, E. (2014) · Biomolecules · doi:10.3390/biom4040897 · Cited by 101 · see citing works

The role of cullin 5-containing ubiquitin ligases

Okumura, F., Akiko, J.-O., Nakatsukasa, K., & Kamura, T. (2016) · Cell Division · doi:10.1186/s13008-016-0016-3 · Cited by 96 · see citing works

Cullin-RING E3 Ubiquitin Ligases: Bridges to Destruction

Nguyen, H. C., Wang, W., & Xiong, Y. (2017) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-3-319-46503-6_12 · Cited by 92 · see citing works

The Ubiquitin-Conjugating System: Multiple Roles in Viral Replication and Infection

Calistri, A., Munegato, D., Carli, I., Parolin, C., & Palù, G. (2014) · Cells · doi:10.3390/cells3020386 · Cited by 91 · see citing works

APOBEC3D and APOBEC3F Potently Promote HIV-1 Diversification and Evolution in Humanized Mouse Model

Sato, K., Takeuchi, J. S., Misawa, N., Izumi, T., Kobayashi, T., Kimura, Y., Iwami, S., Takaori‐Kondo, A., Hu, W.-S., Aihara, K., et al. (2014) · PLoS Pathogens · doi:10.1371/journal.ppat.1004453 · Cited by 87 · see citing works

Insights into Cullin-RING E3 Ubiquitin Ligase Recruitment: Structure of the VHL-EloBC-Cul2 Complex

Nguyen, H. C., Yang, H., Fribourgh, J. L., Wolfe, L. S., & Xiong, Y. (2015) · Structure · doi:10.1016/j.str.2014.12.014 · Cited by 84 · see citing works

Promiscuous RNA Binding Ensures Effective Encapsidation of APOBEC3 Proteins by HIV-1

Apolonia, L., Schulz, R., Curk, T., Rocha, P., Swanson, C. M., Schaller, T., Ule, J., & Malim, M. H. (2015) · PLoS Pathogens · doi:10.1371/journal.ppat.1004609 · Cited by 87 · see citing works

Broad-spectrum antiviral agents

Zhu, J., Meng, W., Wang, X.-J., & Wang, H. R. (2015) · Frontiers in Microbiology · doi:10.3389/fmicb.2015.00517 · Cited by 86 · see citing works

Structure of the Vif-binding domain of the antiviral enzyme APOBEC3G

Kouno, T., Luengas, E. M., Shigematsu, M., Shandilya, S. M. D., Zhang, J., Chen, L., Hara, M., Schiffer, C. A., Harris, R. S., & Matsuo, H. (2015) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3033 · Cited by 79 · see citing works

Mechanistic Insight into Antiretroviral Potency of 2′-Deoxy-2′-β-fluoro-4′-azidocytidine (FNC) with a Long-Lasting Effect on HIV‑1 Prevention

Sun, L. J., Peng, Y., Yu, W., Zhang, Y., Liang, L., Song, C., Hou, J., Qiao, Y., Wang, Q., Chen, J., et al. (2020) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.0c00940 · Cited by 74 · see citing works

The structural basis for HIV-1 Vif antagonism of human APOBEC3G

Li, Y.-L., Langley, C. A., Azumaya, C. M., Echeverria, I., Chesarino, N. M., Emerman, M., Cheng, Y., & Gross, J. D. (2023) · Nature · doi:10.1038/s41586-023-05779-1 · Cited by 74 · see citing works

RNA-directed remodeling of the HIV-1 protein Rev orchestrates assembly of the Rev–Rev response element complex

Jayaraman, B., Crosby, D. C., Homer, C. M., Ribeiro, I., Mavor, D., & Frankel, A. D. (2014) · eLife · doi:10.7554/elife.04120 · Cited by 69 · see citing works

HIV-1 Vif suppresses antiviral immunity by targeting STING

Wang, Y., Gui, Q., Zhu, L., Zhao, Z., Liu, Y., Han, W., Zhang, X., Zhang, Y., Xiong, T., Zeng, H., et al. (2021) · Cellular and Molecular Immunology · doi:10.1038/s41423-021-00802-9 · Cited by 69 · see citing works

CUL5-ARIH2 E3-E3 ubiquitin ligase structure reveals cullin-specific NEDD8 activation

Kostrhon, S., Prabu, J. R., Baek, K., Horn‐Ghetko, D., von Gronau, S., Klügel, M., Basquin, J., Alpi, A. F., & Schulman, B. A. (2021) · Nature Chemical Biology · doi:10.1038/s41589-021-00858-8 · Cited by 62 · see citing works

HIV-1 viral infectivity factor interacts with microtubule-associated protein light chain 3 and inhibits autophagy

Borel, S., Robert-Hebmann, V., Alfaisal, J., Jain, A., Faure, M., Espert, L., Chaloin, L., Paillart, J., Johansen, T., & Biard‐Piechaczyk, M. (2014) · AIDS · doi:10.1097/qad.0000000000000554 · Cited by 65 · see citing works

3D molecular models of whole HIV-1 virions generated with cellPACK

Johnson, G. T., Goodsell, D. S., Autin, L., Forli, S., Sanner, M. F., & Olson, A. J. (2014) · Faraday Discussions · doi:10.1039/c4fd00017j · Cited by 62 · see citing works

Identification of the HIV-1 Vif and Human APOBEC3G Protein Interface

Letko, M. C., Booiman, T., Kootstra, N. A., Simon, V. R., & Ooms, M. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.10.068 · Cited by 60 · see citing works

BTB domains: A structural view of evolution, multimerization, and protein–protein interactions

Bonchuk, A. N., Balagurov, K., & Georgiev, P. G. (2022) · BioEssays · doi:10.1002/bies.202200179 · Cited by 64 · see citing works

Structure-Guided Analysis of the Human APOBEC3-HIV Restrictome

Aydin, H., Taylor, M. W., & Lee, J. E. (2014) · Structure · doi:10.1016/j.str.2014.02.011 · Cited by 60 · see citing works

Structural Insights into HIV-1 Vif-APOBEC3F Interaction

Nakashima, M., Ode, H., Kawamura, T., Kitamura, S., Naganawa, Y., Awazu, H., Tsuzuki, S., Matsuoka, K., Nemoto, M., Hachiya, A., et al. (2015) · Journal of Virology · doi:10.1128/jvi.02369-15 · Cited by 59 · see citing works

APOBEC3G-Mediated G-to-A Hypermutation of the HIV-1 Genome: The Missing Link in Antiviral Molecular Mechanisms

Okada, A., & Iwatani, Y. (2016) · Frontiers in Microbiology · doi:10.3389/fmicb.2016.02027 · Cited by 59 · see citing works

Structural Biology of CRL Ubiquitin Ligases

Rusnac, D.-V., & Zheng, N. (2020) · Advances in experimental medicine and biology · doi:10.1007/978-981-15-1025-0_2 · Cited by 52 · see citing works

The HDAC6/APOBEC3G complex regulates HIV-1 infectiveness by inducing Vif autophagic degradation

Valera, M.-S., de Armas‐Rillo, L., González, J. B., Ziglio, S., Batisse, J., Dubois, N., Marrero‐Hernández, S., Borel, S., García-Expósito, L., Biard‐Piechaczyk, M., et al. (2015) · Retrovirology · doi:10.1186/s12977-015-0181-5 · Cited by 57 · see citing works

Making Sense of Multifunctional Proteins: Human Immunodeficiency Virus Type 1 Accessory and Regulatory Proteins and Connections to Transcription

Faust, T. B., Binning, J. M., Gross, J. D., & Frankel, A. D. (2017) · Annual Review of Virology · doi:10.1146/annurev-virology-101416-041654 · Cited by 58 · see citing works

HIV suppression by host restriction factors and viral immune evasion

Jia, X., Zhao, Q., & Xiong, Y. (2015) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2015.04.004 · Cited by 58 · see citing works

The RNA Binding Specificity of Human APOBEC3 Proteins Resembles That of HIV-1 Nucleocapsid

York, A., Kutluay, S. B., Errando, M., & Bieniasz, P. D. (2016) · PLoS Pathogens · doi:10.1371/journal.ppat.1005833 · Cited by 58 · see citing works

Molecular Determinants for Recognition of Divergent SAMHD1 Proteins by the Lentiviral Accessory Protein Vpx

Schwefel, D., Boucherit, V., Christodoulou, E., Walker, P. A., Stoye, J. P., Bishop, K. N., & Taylor, I. A. (2015) · Cell Host & Microbe · doi:10.1016/j.chom.2015.03.004 · Cited by 53 · see citing works

HIV–host interactome revealed directly from infected cells

Luo, Y., Jacobs, E. Y., Greco, T. M., Mohammed, K., Tong, T., Keegan, S., Binley, J. Μ., Cristea, I. M., Fenyö, D., Rout, M. P., et al. (2016) · Nature Microbiology · doi:10.1038/nmicrobiol.2016.68 · Cited by 53 · see citing works

The Role of APOBECs in Viral Replication

Xu, W. K., Byun, H., & Dudley, J. P. (2020) · Microorganisms · doi:10.3390/microorganisms8121899 · Cited by 50 · see citing works

Transcriptional regulation of APOBEC3 antiviral immunity through the CBF-β/RUNX axis

Anderson, B. D., & Harris, R. S. (2015) · Science Advances · doi:10.1126/sciadv.1500296 · Cited by 51 · see citing works

HIV-1 Vif Triggers Cell Cycle Arrest by Degrading Cellular PPP2R5 Phospho-regulators

Salamango, D. J., Ikeda, T., Moghadasi, S. A., Wang, J., McCann, J. L., Serebrenik, A. A., Ebrahimi, D., Jarvis, M. C., Brown, W. L., & Harris, R. S. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.09.057 · Cited by 51 · see citing works

Crystal Structure of DNA Cytidine Deaminase ABOBEC3G Catalytic Deamination Domain Suggests a Binding Mode of Full-length Enzyme to Single-stranded DNA

Lu, X., Zhang, T., Xu, Z., Liu, S., Zhao, B., Lan, W., Wang, C., Ding, J., & Cao, C. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.624262 · Cited by 49 · see citing works

Lineage-Specific Viral Hijacking of Non-canonical E3 Ubiquitin Ligase Cofactors in the Evolution of Vif Anti-APOBEC3 Activity

Kane, J. R., Stanley, D. J., Hultquist, J. F., Johnson, J. R., Mietrach, N., Binning, J. M., Jönsson, S., Barelier, S., Newton, B. W., Johnson, T. L., et al. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.04.038 · Cited by 48 · see citing works

Hepatitis B Virus X Protein Function Requires Zinc Binding

Ramakrishnan, D., Xing, W., Beran, R. K., Chemuru, S., Rohrs, H. W., Niedziela‐Majka, A., Marchand, B., Mehra, U., Zábranský, A., Doležal, M., et al. (2019) · Journal of Virology · doi:10.1128/jvi.00250-19 · Cited by 45 · see citing works

Structural insights for HIV-1 therapeutic strategies targeting Vif

Salter, J. D., Morales, G. A., & Smith, H. C. (2014) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2014.07.001 · Cited by 44 · see citing works

A functional variant that affects exon-skipping and protein expression ofSP140as genetic mechanism predisposing to multiple sclerosis

Matesanz, F., Potenciano, V., Fedetz, M., Ramos‐Mozo, P., Abad‐Grau, M. M., Karaky, M., Barrionuevo, C., Izquierdo, G., Ruíz-Peña, J. L., García-Sanchéz, M.-I., et al. (2015) · Human Molecular Genetics · doi:10.1093/hmg/ddv256 · Cited by 44 · see citing works

Herb-target interaction network analysis helps to disclose molecular mechanism of traditional Chinese medicine

Liang, H., Ruan, H., Ouyang, Q., & Lai, L. (2016) · Scientific Reports · doi:10.1038/srep36767 · Cited by 41 · see citing works

The Binding Interface between Human APOBEC3F and HIV-1 Vif Elucidated by Genetic and Computational Approaches

Richards, C. M., Albin, J. S., Demir, Ö., Shaban, N. M., Luengas, E. M., Land, A. M., Anderson, B. D., Holten, J. R., Anderson, J. S., Harki, D. A., et al. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.10.067 · Cited by 37 · see citing works

Structural basis for HIV-1 antagonism of host APOBEC3G via Cullin E3 ligase

Ito, F., Alvarez-Cabrera, A. L., Liu, S., Yang, H., Shiriaeva, A., Zhou, Z. H., & Chen, X. S. (2023) · Science Advances · doi:10.1126/sciadv.ade3168 · Cited by 37 · see citing works

An analog of camptothecin inactive against Topoisomerase I is broadly neutralizing of HIV-1 through inhibition of Vif-dependent APOBEC3G degradation

Bennett, R. P., Stewart, R. A., Hogan, P. A., Ptak, R. G., Mankowski, M. K., Hartman, T. L., Buckheit, R. W., Snyder, B. A., Salter, J. D., Morales, G. A., et al. (2016) · Antiviral Research · doi:10.1016/j.antiviral.2016.11.001 · Cited by 35 · see citing works

ASK1 restores the antiviral activity of APOBEC3G by disrupting HIV-1 Vif-mediated counteraction

Miyakawa, K., Matsunaga, S., Kanou, K., Matsuzawa, A., Morishita, R., Kudoh, A., Shindo, K., Yokoyama, M., Sato, H., Kimura, H., et al. (2015) · Nature Communications · doi:10.1038/ncomms7945 · Cited by 33 · see citing works

Structural basis of antagonism of human APOBEC3F by HIV-1 Vif

Hu, Y., Desimmie, B. A., Nguyen, H. C., Ziegler, S. J., Cheng, T. C., Chen, J. L., Wang, J., Wang, H., Zhang, K., Pathak, V. K., et al. (2019) · Nature Structural & Molecular Biology · doi:10.1038/s41594-019-0343-6 · Cited by 33 · see citing works

Identification of small molecule compounds targeting the interaction of HIV-1 Vif and human APOBEC3G by virtual screening and biological evaluation

Ma, L., Zhang, Z., Liu, Z., Pan, Q., Wang, J., Li, X., Guo, F., Liang, C., Hu, L., Zhou, J., et al. (2018) · Scientific Reports · doi:10.1038/s41598-018-26318-3 · Cited by 32 · see citing works

Structural basis of chimpanzee APOBEC3H dimerization stabilized by double-stranded RNA

Matsuoka, T., Nagae, T., Ode, H., Awazu, H., Kurosawa, T., Hamano, A., Matsuoka, K., Hachiya, A., Imahashi, M., Yokomaku, Y., et al. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky676 · Cited by 31 · see citing works

Cellular Requirements for Bovine Immunodeficiency Virus Vif-Mediated Inactivation of Bovine APOBEC3 Proteins

Zhang, W., Wang, H., Li, Z., Liu, X., Liu, G., Harris, R. S., & Yu, X.-F. (2014) · Journal of Virology · doi:10.1128/jvi.02072-14 · Cited by 32 · see citing works

The Structural Interface between HIV-1 Vif and Human APOBEC3H

Ooms, M., Letko, M. C., & Simon, V. R. (2016) · Journal of Virology · doi:10.1128/jvi.02289-16 · Cited by 31 · see citing works

Stably expressed APOBEC3H forms a barrier for cross-species transmission of simian immunodeficiency virus of chimpanzee to humans

Zhang, Z., Gu, Q., de Manuel, M., Bravo, I. G., Marquès‐Bonet, T., Häussinger, D., & Münk, C. (2017) · PLoS Pathogens · doi:10.1371/journal.ppat.1006746 · Cited by 31 · see citing works

Molecular Biology and Diversification of Human Retroviruses

Meissner, M. E., Talledge, N., & Mansky, L. M. (2022) · Frontiers in Virology · doi:10.3389/fviro.2022.872599 · Cited by 31 · see citing works

Are Evolution and the Intracellular Innate Immune System Key Determinants in HIV Transmission?

Sumner, R. P., Thorne, L., Fink, D., Khan, H., Milne, R. S. B., & Towers, G. J. (2017) · Frontiers in Immunology · doi:10.3389/fimmu.2017.01246 · Cited by 28 · see citing works

Antagonism of PP2A is an independent and conserved function of HIV-1 Vif and causes cell cycle arrest

Marelli, S., Williamson, J. C., Protasio, A. V., Naamati, A., Greenwood, E. J. D., Deane, J. E., Lehner, P. J., & Matheson, N. J. (2020) · eLife · doi:10.7554/elife.53036 · Cited by 30 · see citing works

Structural perspectives on HIV‐1 Vif and APOBEC3 restriction factor interactions

Azimi, F. C., & Lee, J. E. (2019) · Protein Science · doi:10.1002/pro.3729 · Cited by 28 · see citing works

Synthesis, biological evaluation and molecular docking study of N-(2-methoxyphenyl)-6-((4-nitrophenyl)sulfonyl)benzamide derivatives as potent HIV-1 Vif antagonists

Zhou, M., Luo, R., Hou, X., Wang, R., Yan, G., Chen, H., Zhang, R., Shi, J., Zheng, Y., Li, R., et al. (2017) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2017.01.010 · Cited by 29 · see citing works

Structural Insights into APOBEC3-Mediated Lentiviral Restriction

Delviks‐Frankenberry, K. A., Desimmie, B. A., & Pathak, V. K. (2020) · Viruses · doi:10.3390/v12060587 · Cited by 30 · see citing works

Examination of the APOBEC3 Barrier to Cross Species Transmission of Primate Lentiviruses

Gaba, A., Flath, B., & Chelico, L. (2021) · Viruses · doi:10.3390/v13061084 · Cited by 27 · see citing works

Identification of an HIV-1 replication inhibitor which rescues host restriction factor APOBEC3G in Vif–APOBEC3G complex

Zhang, S., Zhong, L., Chen, B., Pan, T. S., Zhang, X., Liang, L., Li, Q., Zhang, Z., Chen, H., Zhou, J., et al. (2015) · Antiviral Research · doi:10.1016/j.antiviral.2015.07.009 · Cited by 28 · see citing works

HIV-1 Vif's Capacity To Manipulate the Cell Cycle Is Species Specific

Evans, E. L., Becker, J. T., Fricke, S. L., Patel, K., & Sherer, N. M. (2018) · Journal of Virology · doi:10.1128/jvi.02102-17 · Cited by 28 · see citing works

Anti-HIV Activities and Mechanism of 12-O-Tricosanoylphorbol-20-acetate, a Novel Phorbol Ester from Ostodes katharinae

Chen, H., Zhang, R., Luo, R., Yang, L., Wang, R., Hao, X., & Zheng, Y. (2017) · Molecules · doi:10.3390/molecules22091498 · Cited by 26 · see citing works

Core-Binding Factor Subunit Beta Is Not Required for Non-Primate Lentiviral Vif-Mediated APOBEC3 Degradation

Ai, Y., Zhu, D., Wang, C., Su, C., Ma, J., Ma, J., & Wang, X. (2014) · Journal of Virology · doi:10.1128/jvi.01924-14 · Cited by 25 · see citing works

Evolutionary Paradigms from Ancient and Ongoing Conflicts between the Lentiviral Vif Protein and Mammalian APOBEC3 Enzymes

Harris, R. S., & Anderson, B. D. (2016) · PLoS Pathogens · doi:10.1371/journal.ppat.1005958 · Cited by 25 · see citing works

Translational regulation of APOBEC3G mRNA by Vif requires its 5′UTR and contributes to restoring HIV-1 infectivity

Guerrero, S. X., Libre, C., Batisse, J., Mercenne, G., Richer, D., Laumond, G., Decoville, T., Moog, C., Marquet, R., & Paillart, J. (2016) · Scientific Reports · doi:10.1038/srep39507 · Cited by 24 · see citing works

Dual Functionality of HIV-1 Vif in APOBEC3 Counteraction and Cell Cycle Arrest

Salamango, D. J., & Harris, R. S. (2021) · Frontiers in Microbiology · doi:10.3389/fmicb.2020.622012 · Cited by 24 · see citing works

Degradation-Independent Inhibition of APOBEC3G by the HIV-1 Vif Protein

Stupfler, B., Verriez, C., Gallois‐Montbrun, S., Marquet, R., & Paillart, J. (2021) · Viruses · doi:10.3390/v13040617 · Cited by 24 · see citing works

Evolutionarily conserved pressure for the existence of distinct G2/M cell cycle arrest and A3H inactivation functions in HIV-1 Vif

Zhao, K., Du, J., Rui, Y., Zheng, W., Kang, J., Hou, J., Wang, K., Zhang, W., Simon, V. A., & Yu, X.-F. (2015) · Cell Cycle · doi:10.1080/15384101.2014.1000212 · Cited by 25 · see citing works

Structure of the transcribing RNA polymerase II–Elongin complex

Chen, Y., Kokić, G., Dienemann, C., Dybkov, O., Urlaub, H., & Cramer, P. (2023) · Nature Structural & Molecular Biology · doi:10.1038/s41594-023-01138-w · Cited by 24 · see citing works

Cullin 5-RING E3 ubiquitin ligases, new therapeutic targets?

Lamsoul, I., Uttenweiler‐Joseph, S., Moog‐Lutz, C., & Lutz, P. G. (2015) · Biochimie · doi:10.1016/j.biochi.2015.08.003 · Cited by 24 · see citing works

Mapping Region of Human Restriction Factor APOBEC3H Critical for Interaction with HIV-1 Vif

Nakashima, M., Tsuzuki, S., Awazu, H., Hamano, A., Okada, A., Ode, H., Maejima, M., Hachiya, A., Yokomaku, Y., Watanabe, N., et al. (2017) · Journal of Molecular Biology · doi:10.1016/j.jmb.2017.03.019 · Cited by 23 · see citing works

CRL4AMBRA1 targets Elongin C for ubiquitination and degradation to modulate CRL5 signaling

Chen, S., Jang, G. Μ., Hüttenhain, R., Gordon, D. E., Du, D., Newton, B. W., Johnson, J. R., Hiatt, J. B., Hultquist, J. F., Johnson, T. L., et al. (2018) · The EMBO Journal · doi:10.15252/embj.201797508 · Cited by 23 · see citing works

A novel HIV-1 inhibitor that blocks viral replication and rescues APOBEC3s by interrupting vif/CBFβ interaction

Duan, S., Wang, S., Song, Y., Gao, N., Meng, L., Gai, Y., Zhang, Y., Wang, S., Wang, C., Yu, B., et al. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.013404 · Cited by 22 · see citing works

Fab-based inhibitors reveal ubiquitin independent functions for HIV Vif neutralization of APOBEC3 restriction factors

Binning, J. M., Smith, A. M., Hultquist, J. F., Craik, C. S., Cartozo, N. C., Campbell, M. G., Burton, L. A., Greca, F. L., McGregor, M., Ta, H. M., et al. (2018) · PLoS Pathogens · doi:10.1371/journal.ppat.1006830 · Cited by 22 · see citing works

A New Class of Antiretroviral Enabling Innate Immunity by Protecting APOBEC3 from HIV Vif-Dependent Degradation

Bennett, R. P., Salter, J. D., & Smith, H. C. (2018) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2018.03.004 · Cited by 22 · see citing works

Structural Basis for a Species-Specific Determinant of an SIV Vif Protein toward Hominid APOBEC3G Antagonism

Binning, J. M., Chesarino, N. M., Emerman, M., & Gross, J. D. (2019) · Cell Host & Microbe · doi:10.1016/j.chom.2019.10.014 · Cited by 21 · see citing works

A role for gorilla APOBEC3G in shaping lentivirus evolution including transmission to humans

Nakano, Y., Yamamoto, K., Ueda, M. T., Soper, A., Konno, Y., Kimura, I., Uriu, K., Kumata, R., Aso, H., Misawa, N., et al. (2020) · PLoS Pathogens · doi:10.1371/journal.ppat.1008812 · Cited by 21 · see citing works

Structural insights into RNA bridging between HIV-1 Vif and antiviral factor APOBEC3G

Kouno, T., Shibata, S., Shigematsu, M., Hyun, J., Kim, T. G., Matsuo, H., & Wolf, M. (2023) · Nature Communications · doi:10.1038/s41467-023-39796-5 · Cited by 21 · see citing works

Characterization of RNA binding and chaperoning activities of HIV-1 Vif protein

Sleiman, D., Bernacchi, S., Guerrero, S. X., Brachet, F., Larue, V., Paillart, J., & Tisné, C. (2014) · RNA Biology · doi:10.4161/rna.29546 · Cited by 20 · see citing works

Functional and Structural Insights into a Vif/PPP2R5 Complex Elucidated Using Patient HIV-1 Isolates and Computational Modeling

Salamango, D. J., McCann, J. L., Demir, Ö., Becker, J. T., Wang, J., Lingappa, J. R., Temiz, N. A., Brown, W. L., Amaro, R. E., & Harris, R. S. (2020) · Journal of Virology · doi:10.1128/jvi.00631-20 · Cited by 20 · see citing works

Possible Footprints of APOBEC3F and/or Other APOBEC3 Deaminases, but Not APOBEC3G, on HIV-1 from Patients with Acute/Early and Chronic Infections

Armitage, A. E., Deforche, K., Welch, J. J., Laethem, K. V., Camacho, R. J., Rambaut, A., & Iversen, A. K. N. (2014) · Journal of Virology · doi:10.1128/jvi.01460-14 · Cited by 20 · see citing works

Coevolutionary analyses require phylogenetically deep alignments and better null models to accurately detect inter-protein contacts within and between species

Avila-Herrera, A., & Pollard, K. S. (2015) · BMC Bioinformatics · doi:10.1186/s12859-015-0677-y · Cited by 20 · see citing works

Role of co-expressed APOBEC3F and APOBEC3G in inducing HIV-1 drug resistance

Mohammadzadeh, N., Love, R. P., Gibson, R. M., Arts, E. J., Poon, A. F. Y., & Chelico, L. (2019) · Heliyon · doi:10.1016/j.heliyon.2019.e01498 · Cited by 18 · see citing works

Redoxal, an inhibitor of de novo pyrimidine biosynthesis, augments APOBEC3G antiviral activity against human immunodeficiency virus type 1

Pery, E., Sheehy, A. M., Nebane, N. M., Misra, V., Mankowski, M. K., Rasmussen, L. A., White, E. L., Ptak, R. G., & Gabuzda, D. H. (2015) · Virology · doi:10.1016/j.virol.2015.06.014 · Cited by 19 · see citing works

Inhibition of base editors with anti-deaminases derived from viruses

Liu, Z., Chen, S., Lai, L., & Li, Z. (2022) · Nature Communications · doi:10.1038/s41467-022-28300-0 · Cited by 18 · see citing works

Identification of HIV-1 Vif Regions Required for CBF-β Interaction and APOBEC3 Suppression

Wang, H., Liu, B., Liu, X., Li, Z., Yu, X.-F., & Zhang, W. (2014) · PLoS ONE · doi:10.1371/journal.pone.0095738 · Cited by 18 · see citing works

Structural basis of HIV-1 Vif-mediated E3 ligase targeting of host APOBEC3H

Ito, F., Alvarez-Cabrera, A. L., Kim, K., Zhou, Z. H., & Chen, X. S. (2023) · Nature Communications · doi:10.1038/s41467-023-40955-x · Cited by 17 · see citing works

Multifaceted HIV‐1 Vif interactions with human E3 ubiquitin ligase and APOBEC3s

Hu, Y., Knecht, K. M., Shen, Q., & Xiong, Y. (2020) · FEBS Journal · doi:10.1111/febs.15550 · Cited by 17 · see citing works

HIV-1 Escape from Small-Molecule Antagonism of Vif

Sharkey, M. E., Sharova, N. P., Mohammed, I., Huff, S. E., Kummetha, I. R., Singh, G., Rana, T. M., & Stevenson, M. (2019) · mBio · doi:10.1128/mbio.00144-19 · Cited by 17 · see citing works

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 50 · see citing works

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 · see citing works

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 · see citing works