The DOI matches its Crossref record; 15 of the 15 references it cites were found in a registry or an index.
An Essential Role for LEDGF/p75 in HIV Integration
Abstract
Chromosomal integration enables human immunodeficiency virus (HIV) to establish a permanent reservoir that can be therapeutically suppressed but not eradicated. Participation of cellular proteins in this obligate replication step is poorly understood. We used intensified RNA interference and dominant-negative protein approaches to show that the cellular transcriptional coactivator lens epithelium–derived growth factor (LEDGF)/p75 (p75) is an essential HIV integration cofactor. The mechanism requires both linkages of a molecular tether that p75 forms between integrase and chromatin. Fractionally minute levels of endogenous p75 are sufficient to enable integration, showing that cellular factors that engage HIV after entry may elude identification in less intensive knockdowns. Perturbing the p75-integrase interaction may have therapeutic potential.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
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?
In the citing paper
“However, while LEDGF/p75 is critical, it is not strictly essential for HIV-1 integration and replication. This assertion is supported by the fact that HIV-1 was able to replicate, albeit at a much-reduced level, in LEDGF knockdown cells, and the replication could be restored upon expression of LEDGF/p75 (Llano et al. 2006, Shun et al. 2007).”
From Beyond reverse transcription: molecular mechanisms and emerging paradigms in retroviral replication (2026) · cites this paper as Llano et al. 2006
Citations
Cites
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
HIV-1 Integrase Forms Stable Tetramers and Associates with LEDGF/p75 Protein in Human Cells
Cherepanov, P., Maertens, G., Proost, P., Devreese, B., Van Beeumen, J., Engelborghs, Y., De Clercq, E., & Debyser, Z. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m209278200 · Cited by 704
A role for LEDGF/p75 in targeting HIV DNA integration
Ciuffi, A., Llano, M., Poeschla, E., Hoffmann, C., Leipzig, J., Shinn, P., Ecker, J. R., & Bushman, F. (2005) · Nature Medicine · doi:10.1038/nm1329 · Cited by 658
Self-citationLEDGF/p75 Is Essential for Nuclear and Chromosomal Targeting of HIV-1 Integrase in Human Cells
Maertens, G., Cherepanov, P., Pluymers, W., Busschots, K., De Clercq, E., Debyser, Z., & Engelborghs, Y. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m303594200 · Cited by 493
Llano, M., Vanegas, M., Fregoso, O., Saenz, D., Chung, S., Peretz, M., & Poeschla, E. M. (2004) · Journal of Virology · doi:10.1128/jvi.78.17.9524-9537.2004 · Cited by 305
Self-citationGe, H., Si, Y., & Roeder, R. G. (1998) · The EMBO Journal · doi:10.1093/emboj/17.22.6723 · Cited by 299
Cherepanov, P., Devroe, E., Silver, P. A., & Engelman, A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m406307200 · Cited by 287
Solution structure of the HIV-1 integrase-binding domain in LEDGF/p75
Cherepanov, P., Sun, Z.-Y. J., Rahman, S., Maertens, G., Wagner, G., & Engelman, A. (2005) · Nature Structural & Molecular Biology · doi:10.1038/nsmb937 · Cited by 235
Vandekerckhove, L., Christ, F., Maele, B. V., Rijck, J. D., Gijsbers, R., den Haute, C. V., Witvrouw, M., & Debyser, Z. (2006) · Journal of Virology · doi:10.1128/jvi.80.4.1886-1896.2006 · Cited by 210
The Interaction of LEDGF/p75 with Integrase Is Lentivirus-specific and Promotes DNA Binding
Busschots, K., Vercammen, J., Emiliani, S., Benarous, R., Engelborghs, Y., Christ, F., & Debyser, Z. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m411681200 · Cited by 208
Cited by
Sorted by citations
Items 301–400 of 544
Blocking Nuclear Import of Pre-Integration Complex: An Emerging Anti-HIV-1 Drug Discovery Paradigm
Zhan, P., Liu, X., & Clercq, E. D. (2010) · Current Medicinal Chemistry · doi:10.2174/092986710790416335 · Cited by 16
Guatelli, J., Siliciano, R. F., Kuritzkes, D. R., & Richman, D. D. (2016) · ASM Press eBooks · doi:10.1128/9781555819439.ch34 · Cited by 16
De novo design of small molecule inhibitors targeting the LEDGF/p75-HIVintegrase interaction
Cavalluzzo, C., Voet, A. R. D., Christ, F., Singh, B. K., Sharma, A. K., Debyser, Z., Maeyer, M. D., & der Eycken, E. V. V. (2011) · RSC Advances · doi:10.1039/c1ra00582k · Cited by 15
Recent 5-Year Findings and Technological Advances in the Proteomic Study of HIV-Associated Disorders
Zhang, L., Jia, X., Jin, J., Lu, H., & Tan, Z. (2017) · Genomics Proteomics & Bioinformatics · doi:10.1016/j.gpb.2016.11.002 · Cited by 14
Mass spectrometry-based footprinting of protein–protein interactions
McKee, C. J., Kessl, J. J., Norris, J. O., Shkriabai, N., & Kvaratskhelia, M. (2008) · Methods · doi:10.1016/j.ymeth.2008.10.023 · Cited by 15
Nucleocytoplasmic shuttling of HIV-1 integrase is controlled by the viral Rev protein
Levin, A., Hayouka, Z., Friedler, A., & Loyter, A. (2010) · Nucleus · doi:10.4161/nucl.1.2.11300 · Cited by 15
The Feline Immunodeficiency Virus Envelope Signal Peptide Is a Tetherin Antagonizing Protein
Morrison, J. H., & Poeschla, E. M. (2023) · mBio · doi:10.1128/mbio.00161-23 · Cited by 13
Self-citationProteomics in the investigation of HIV‐1 interactions with host proteins
Li, M. (2014) · PROTEOMICS - CLINICAL APPLICATIONS · doi:10.1002/prca.201400101 · Cited by 16
Burlein, C., Wang, C., Xu, M., Bhatt, T., Stahlhut, M. W., Ou, Y., Adam, G. C., Heath, J., Klein, D. J., Sanders, J. M., et al. (2017) · ACS Chemical Biology · doi:10.1021/acschembio.7b00550 · Cited by 14
Optimized binding of substituted quinoline ALLINIs within the HIV-1 integrase oligomer
Sun, J., Patel, K., Hume, J. D., Pigza, J. A., Donahue, M. G., & Kessl, J. J. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.100363 · Cited by 14
LEDGF/p75 TATA-Less Promoter Is Driven by the Transcription Factor Sp1
Desfarges, S., Abderrahmani, A., Hernández‐Novoa, B., Muñoz, M., & Ciuffi, A. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.10.010 · Cited by 14
Involvement of human topoisomerase II isoforms in HIV-1 reverse transcription
Sunnam, L. B., Satyanarayana, N., & Kondapi, A. K. (2013) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2013.01.010 · Cited by 14
Fragment hopping approach directed at design of HIV IN-LEDGF/p75 interaction inhibitors
Luca, L. D., Ferro, S., Morreale, F. E., Christ, F., Debyser, Z., Chimirri, A., & Gitto, R. (2012) · Journal of Enzyme Inhibition and Medicinal Chemistry · doi:10.3109/14756366.2012.703184 · Cited by 14
Lessons Learned: HIV Points the Way Towards Precision Treatment of Mixed-Lineage Leukemia
Čermáková, K., Weydert, C., Christ, F., Rijck, J. D., & Debyser, Z. (2016) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2016.05.005 · Cited by 14
Woodward, C. L., & Chow, S. A. (2010) · Nucleus · doi:10.4161/nucl.1.1.10571 · Cited by 14
Evidence for Tethering of Human Cytomegalovirus Genomes to Host Chromosomes
Mauch-Mücke, K., Schön, K., Paulus, C., & Nevels, M. M. (2020) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2020.577428 · Cited by 14
Hendrix, J., van Heertum, B., Vanstreels, E., Daelemans, D., & Rijck, J. D. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.525964 · Cited by 14
Host Cell Factors and HIV-1 Integration
Engelman, A. (2007) · Future HIV Therapy · doi:10.2217/17469600.1.4.415 · Cited by 13
Interactions of Host Proteins with the Murine Leukemia Virus Integrase
Studamire, B., & Goff, S. P. (2010) · Viruses · doi:10.3390/v2051110 · Cited by 14
Bennett, G. R., Peters, R., Wang, X., Hanne, J., Sobol, R. W., Bundschuh, R. A., Fishel, R. A., & Yoder, K. E. (2014) · PLoS ONE · doi:10.1371/journal.pone.0103164 · Cited by 12
Domain swapping and SMYD1 interactions with the PWWP domain of human hepatoma-derived growth factor
Chen, L., Huang, Y., Huang, S., Hsieh, Y., Guan, H., Chen, N.-C., Chuankhayan, P., Yoshimura, M., Tai, M., & Chen, C. (2018) · Scientific Reports · doi:10.1038/s41598-017-18510-8 · Cited by 13
Rapid, Controlled and Intensive Lentiviral Vector-Based RNAi
Llano, M., Gaznick, N., & Poeschla, E. M. (2009) · Methods in molecular biology · doi:10.1007/978-1-59745-170-3_18 · Cited by 13
Self-citationLevin, A., Hayouka, Z., Friedler, A., Brack‐Werner, R., Volsky, D. J., & Loyter, A. (2010) · Journal of General Virology · doi:10.1099/vir.0.019760-0 · Cited by 13
Virus–Host Interactions in Retrovirus Integration
Engelman, A. N., & Maertens, G. N. (2018) · Retrovirus-Cell Interactions · doi:10.1016/b978-0-12-811185-7.00004-2 · Cited by 12
Schlafen14 Impairs HIV-1 Expression in a Codon Usage-Dependent Manner
Valenzuela, C. A., Saucedo, S., & Llano, M. (2024) · Viruses · doi:10.3390/v16040502 · Cited by 14
Self-citationHIV-1 integrase binding to genomic RNA 5′-UTR induces local structural changes in vitro and in virio
Liu, S., Koneru, P. C., Li, W., Pathirage, C., Engelman, A., Kvaratskhelia, M., & Musier‐Forsyth, K. (2021) · Retrovirology · doi:10.1186/s12977-021-00582-0 · Cited by 16
Montoya, V. R., Ready, T. M., Felton, A., Fine, S. R., OhAinle, M., & Emerman, M. (2023) · mBio · doi:10.1128/mbio.00009-23 · Cited by 13
Eilers, G., Gupta, K., Allen, A., Montermoso, S., Murali, H., Sharp, R. B., Hwang, Y., Bushman, F. D., & Duyne, G. D. V. (2023) · PLoS Pathogens · doi:10.1371/journal.ppat.1011097 · Cited by 11
Desimmie, B. A., Demeulemeester, J., Christ, F., & Debyser, Z. (2012) · Drug Discovery Today Technologies · doi:10.1016/j.ddtec.2012.10.002 · Cited by 12
Lopez, A. P., Kugelman, J. R., Garcia-Rivera, J. A., Urias, E., Salinas, S. A., Fernández-Zapico, M. E., & Llano, M. (2016) · Journal of Molecular Biology · doi:10.1016/j.jmb.2016.05.013 · Cited by 13
Self-citationStructural Insights to Human Immunodeficiency Virus (HIV-1) Targets and Their Inhibition
Vanangamudi, M., Nair, P. C., Maida Engels, S. E., Senthilkumar, P., & Namasivayam, V. (2021) · Advances in experimental medicine and biology · doi:10.1007/978-981-16-0267-2_3 · Cited by 12
Borrenberghs, D., Zurnic, I., Wit, F. D., Acke, A., Dirix, L., Cereseto, A., Debyser, Z., & Hendrix, J. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky1157 · Cited by 11
Targeting Cellular Cofactors in HIV Therapy
Dürr, R., Keppler, O. T., Christ, F., Crespan, E., Garbelli, A., Maga, G., & Dietrich, U. (2014) · Topics in medicinal chemistry · doi:10.1007/7355_2014_45 · Cited by 12
Cavalluzzo, C., Christ, F., Voet, A. R. D., Sharma, A. K., Singh, B. K., Zhang, K. Y. J., Lescrinier, E., Maeyer, M. D., Debyser, Z., & der Eycken, E. V. V. (2013) · Journal of Peptide Science · doi:10.1002/psc.2543 · Cited by 11
Mackler, R. M., Jones, N. D., Gardner, A. M., Lopez, M. A., Howard, C. J., Fishel, R. A., & Yoder, K. E. (2019) · PLoS ONE · doi:10.1371/journal.pone.0212764 · Cited by 10
Belle, S. V., Ashkar, S. E., Čermáková, K., Matthijssens, F., Goossens, S., Canella, A., Hodges, H. C., Christ, F., Rijck, J. D., Vlierberghe, P. V., et al. (2021) · Cells · doi:10.3390/cells10010192 · Cited by 12
Voet, A. R. D., Maeyer, M. D., Debyser, Z., & Christ, F. (2009) · Future Medicinal Chemistry · doi:10.4155/fmc.09.86 · Cited by 11
Wang, H., Shun, M.-C., Li, X., Nunzio, F. D., Hare, S., Cherepanov, P., & Engelman, A. (2014) · Molecular Therapy — Methods & Clinical Development · doi:10.1038/mtm.2013.2 · Cited by 11
Development of an RNAi-Based Gene Therapy against HIV-1
ter Brake, O., & Berkhout, B. (2008) · Royal Society of Chemistry eBooks · doi:10.1039/9781847558275-00296 · Cited by 11
An intrinsic host defense against HIV-1 integration?
Bieniasz, P. D. (2007) · Journal of Clinical Investigation · doi:10.1172/jci31290 · Cited by 11
Biochemical and biophysical analyses of concerted (U5/U3) integration
Grandgenett, D. P., Bera, S., Pandey, K. K., Vora, A. C., Zahm, J. A., & Sinha, S. (2008) · Methods · doi:10.1016/j.ymeth.2008.11.002 · Cited by 11
Development of an RNAi based gene therapy against HIV-1
ter Brake, O. (2007) · UvA-DARE (University of Amsterdam) · Cited by 11
Optimizing the Multimerization Properties of Quinoline-Based Allosteric HIV-1 Integrase Inhibitors
Sun, J., & Kessl, J. J. (2024) · Viruses · doi:10.3390/v16020200 · Cited by 10
Rathore, U., Haas, P., Kumar, V. E., Hiatt, J. B., Haas, K. M., Bouhaddou, M., Swaney, D. L., Stevenson, E. J., Zuliani‐Alvarez, L., McGregor, M., et al. (2024) · mBio · doi:10.1128/mbio.02222-23 · Cited by 10
Rational fragment-based design of compounds targeting the PWWP domain of the HRP family
Vantieghem, T., Aslam, N. A., Osipov, E. M., Akele, M. Z., Belle, S. V., Beelen, S., Drexler, M., Paulovcakova, T., Lux, V., Fearon, D., et al. (2024) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2024.116960 · Cited by 10
HIV-1 Integrase Inhibition: Looking at Cofactor Interactions
Christ, F., & Debyser, Z. (2015) · Future Medicinal Chemistry · doi:10.4155/fmc.15.162 · Cited by 10
Characterization of the Role of Host Cellular Factor Histone Deacetylase 10 during HIV-1 Replication
Ran, X., Ao, Z., Olukitibi, T. A., & Yao, X. (2019) · Viruses · doi:10.3390/v12010028 · Cited by 10
Interaction of HRP‐2 isoforms with HDGF. Chromatin binding of a specific heteromer
Thakar, K., Votteler, I., Kelkar, D., Shidore, T., Gupta, S., Kelm, S., & Dietz, F. (2011) · FEBS Journal · doi:10.1111/j.1742-4658.2011.08464.x · Cited by 10
Targeting Protein–Protein Interactions for HIV Therapeutics
Rice, A. P., & Sutton, R. E. (2007) · Future HIV Therapy · doi:10.2217/17469600.1.4.369 · Cited by 10
Productive Replication and Evolution of HIV-1 in Ferret Cells
Fadel, H. J., Saenz, D. T., Guevara, R. B., von Messling, V., Peretz, M., & Poeschla, E. M. (2011) · Journal of Virology · doi:10.1128/jvi.06035-11 · Cited by 10
Self-citationGérard, A., Soler, N., Ségéral, E., Belshan, M., & Emiliani, S. (2013) · Retrovirology · doi:10.1186/1742-4690-10-13 · Cited by 12
Agharbaoui, F. E., Hoyte, A. C., Ferro, S., Gitto, R., Buemi, M. R., Fuchs, J. R., Kvaratskhelia, M., & Luca, L. D. (2016) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2016.07.077 · Cited by 11
An Unusual Helix Turn Helix Motif in the Catalytic Core of HIV-1 Integrase Binds Viral DNA and LEDGF
Merad, H., Porumb, H., Zargarian, L., René, B., Hobaika, Z., Maroun, R. G., Mauffret, O., & Fermandjian, S. (2008) · PLoS ONE · doi:10.1371/journal.pone.0004081 · Cited by 10
Multi-Substituted Quinolines as HIV-1 Integrase Allosteric Inhibitors
Dinh, L. P., Sun, J., Glenn, C. D., Patel, K., Pigza, J. A., Donahue, M. G., Yet, L., & Kessl, J. J. (2022) · Viruses · doi:10.3390/v14071466 · Cited by 9
Role of LEDGF/p75 (PSIP1) in oncogenesis. Insights in molecular mechanism and therapeutic potential
Akele, M. Z., Iervolino, M., Belle, S. V., Christ, F., & Debyser, Z. (2024) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2024.189248 · Cited by 9
Li, P., Tan, J., Liu, M., Zhang, X. Y., Chen, W. Z., & Wang, C. X. (2011) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2011.10507387 · Cited by 9
Zhang, Y., Guo, W., Feng, Y., Yang, L., Lin, H., Zhou, P., Zhao, K., Jiang, L., Yao, B., & Feng, N. (2023) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2023.08.023 · Cited by 9
Bao, L., Hannon, C., Cruz-Migoni, A., Ptchelkine, D., Sun, M., Miller, A., Bunjobpol, W., Quevedo, C. E., Derveni, M., Chambers, J. S., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-16742-2 · Cited by 9
HIV integrase inhibitors that inhibit strand transfer interact with RAG1 and hamper its activities
Nilavar, N. M., & Raghavan, S. C. (2021) · International Immunopharmacology · doi:10.1016/j.intimp.2021.107515 · Cited by 9
Host Factors in Retroviral Integration and the Selection of Integration Target Sites
Craigie, R., & Bushman, F. D. (2015) · ASM Press eBooks · doi:10.1128/9781555819217.ch45 · Cited by 10
Gallay, K., Blot, G., Chahpazoff, M., Yajjou, H., Confort, M.-P., de Boisséson, C., Roux, A. L., Luengo, C., Fiorini, F., Lavigne, M., et al. (2019) · Virology · doi:10.1016/j.virol.2019.04.002 · Cited by 10
Green, V., Arbuthnot, P., & Weinberg, M. S. (2012) · Virology Journal · doi:10.1186/1743-422x-9-272 · Cited by 8
Hernanz, M. P. G., Diaz, J. M. T., Sorel, N., Bobin, A., Dindinaud, E., Bouyer, S., Desmier, D., Brizard, F., Leleu, X. P., Maillard, N., et al. (2019) · Cancer Medicine · doi:10.1002/cam4.2051 · Cited by 8
Therapeutic Genes for Anti-HIV/AIDS Gene Therapy
Bovolenta, C., Porcellini, S., & Alberici, L. (2013) · Current Pharmaceutical Biotechnology · doi:10.2174/138920101405131111104009 · Cited by 8
HIV-1 Integrase Drug Discovery Comes of Age
Demeulemeester, J., Maeyer, M. D., & Debyser, Z. (2013) · Topics in medicinal chemistry · doi:10.1007/7355_2013_33 · Cited by 8
Gabizon, R., Faust, O., Benyamini, H., Nir, S., Loyter, A., & Friedler, A. (2012) · MedChemComm · doi:10.1039/c2md20225e · Cited by 8
Methods for the Analyses of Inhibitor-Induced Aberrant Multimerization of HIV-1 Integrase
Kessl, J. J., Sharma, A., & Kvaratskhelia, M. (2015) · Methods in molecular biology · doi:10.1007/978-1-4939-3046-3_10 · Cited by 8
Prospective Strategies for Targeting HIV-1 Integrase Function
Luo, Y., & Muesing, M. A. (2010) · Future Medicinal Chemistry · doi:10.4155/fmc.10.205 · Cited by 8
Levin, A., Hayouka, Z., Helfer, M., Brack‐Werner, R., Friedler, A., & Loyter, A. (2010) · Biopolymers · doi:10.1002/bip.21469 · Cited by 8
Kohio, H. P., Ajoge, H. O., Coleman, M. D., Ndashimye, E., Gibson, R. M., Arts, E. J., & Barr, S. D. (2023) · Viruses · doi:10.3390/v15020465 · Cited by 7
Identification and Optimization of a Novel HIV-1 Integrase Inhibitor
Adu‐Ampratwum, D., Pan, Y., Koneru, P. C., Antwi, J., Hoyte, A. C., Kessl, J. J., Griffin, P. R., Kvaratskhelia, M., Fuchs, J. R., & Larue, R. C. (2022) · ACS Omega · doi:10.1021/acsomega.1c06378 · Cited by 8
Nombela, I., Michiels, M., Looveren, D. V., Marcelis, L., Ashkar, S. E., Belle, S. V., Bruggemans, A., Tousseyn, T., Schwaller, J., Christ, F., et al. (2022) · Microbiology Spectrum · doi:10.1128/spectrum.01478-22 · Cited by 7
Nondividing Cells: A Safer Bet for Integrating Vectors?
Brady, T., & Bushman, F. D. (2011) · Molecular Therapy · doi:10.1038/mt.2011.40 · Cited by 7
Primate and feline lentiviruses in current intrinsic immunity research: The cat is back
Poeschla, E. M. (2011) · Veterinary Immunology and Immunopathology · doi:10.1016/j.vetimm.2011.06.014 · Cited by 7
Self-citationHIV-1 integrase modulates the interaction of the HIV-1 cellular cofactor LEDGF/p75 with chromatin
Astiazaran, P., Bueno, M. T. D., Morales, E., Kugelman, J. R., Garcia-Rivera, J. A., & Llano, M. (2011) · Retrovirology · doi:10.1186/1742-4690-8-27 · Cited by 7
Self-citationXu, Z., Zheng, Y., Ao, Z., Clément, M., Mouland, A. J., Kalpana, G. V., Belhumeur, P., Cohen, É. A., & Yao, X. (2008) · Retrovirology · doi:10.1186/1742-4690-5-102 · Cited by 7
Roberts, R. A., Campbell, R. A., Sikakana, P., Sadler, C., Osier, M. R., Xu, Y., Feng, J. Y., Mitchell, M. L., Sakowicz, R., Chester, A. E., et al. (2021) · Toxicological Sciences · doi:10.1093/toxsci/kfab073 · Cited by 6
Schrijvers, R., Demeulemeester, J., Rijck, J. D., Christ, F., Gérard, M., Debyser, Z., & Gijsbers, R. (2012) · AIDS · doi:10.1097/qad.0b013e32835d0d86 · Cited by 6
Stem-loop binding protein is a multifaceted cellular regulator of HIV-1 replication
Li, M., Tucker, L. D., Asara, J. M., Cheruiyot, C. K., Lü, H., Wu, Z. J., Newstein, M., Dooner, M. S., Friedman, J. F., Lally, M., et al. (2016) · Journal of Clinical Investigation · doi:10.1172/jci82360 · Cited by 6
The Impact of Lens Epithelium-Derived Growth Factor p75 Dimerization on Its Tethering Function
Brouns, T., Lux, V., Belle, S. V., Christ, F., Veverka, V., & Debyser, Z. (2024) · Cells · doi:10.3390/cells13030227 · Cited by 5
Help or Hinder: Protein Host Factors That Impact HIV-1 Replication
Moezpoor, M. R., & Stevenson, M. (2024) · Viruses · doi:10.3390/v16081281 · Cited by 7
Levin, A., Benyamini, H., Hayouka, Z., Friedler, A., & Loyter, A. (2010) · FEBS Journal · doi:10.1111/j.1742-4658.2010.07952.x · Cited by 6
Luttge, B. G., Panchal, P., Puri, V., Checkley, M. A., & Freed, E. O. (2013) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2013.08.020 · Cited by 7
Hu, G., Li, X., Li, Y., Sun, X., Liu, G., Li, W., Huang, J. Y., Shen, X., & Tang, Y. (2012) · Chinese Journal of Chemistry · doi:10.1002/cjoc.201200897 · Cited by 6
Thys, W., Busschots, K., McNeely, M., Voet, A. R. D., Christ, F., & Debyser, Z. (2009) · HIV Therapy · doi:10.2217/17584310.3.2.171 · Cited by 6
Spearman, P. W. (2024) · Elsevier eBooks · doi:10.1016/b978-0-12-818619-0.00047-2 · Cited by 10
Adachi, K., Manabe, T., Yamasaki, T., Suma, A., Orita, T., Furuzono, T., Adachi, T., Ohata, Y., Akiyama, Y., & Miyazaki, S. (2024) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2024.129864 · Cited by 5
Viral Protein Dimerization Quality Control: A Design Strategy for a Potential Viral Inhibitor
Du, S., Liu, X., Hu, X., & Zhan, P. (2024) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.4c01540 · Cited by 5
Cornering HIV: Taking advantage of interactions between selective pressures
Ávila-Ríos, S., Reyes‐Terán, G., & Espinosa, E. (2007) · Medical Hypotheses · doi:10.1016/j.mehy.2006.12.012 · Cited by 5
Construction and Testing of orfA +/- FIV Reporter Viruses
Fadel, H. J., Saenz, D. T., & Poeschla, E. M. (2012) · Viruses · doi:10.3390/v4010184 · Cited by 5
Self-citationHIV-1 Integration into Chromatin: New Insights and Future Perspectives
Lesbats, P., Lavigne, M., & Parissi, V. (2011) · Future Virology · doi:10.2217/fvl.11.84 · Cited by 7
Santos, S., Obukhov, Y., Nekhai, S. A., Pushkarsky, T., Břicháček, B., Bukrinsky, M., & Iordanskiy, S. (2016) · Virology · doi:10.1016/j.virol.2016.06.023 · 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
Self-citationCTNNBL1 restricts HIV-1 replication by suppressing viral DNA integration into the cell genome
Liang, G., He, Y., Zhao, L., Ouyang, J., Geng, W., Zhang, X., Han, X., Jiang, Y., Ding, H., Xiong, Y., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.110533 · Cited by 5
LEDGF: a leukemia-specific target
Milne, T. A. (2018) · Blood · doi:10.1182/blood-2017-11-815449 · Cited by 5
Changes in the accessibility of the HIV-1 Integrase C-terminus in the presence of cellular proteins
Benkhelifa‐Ziyyat, S., Bucher, S., Zanta, M.-A., Pasquet, J., & Danos, O. (2010) · Retrovirology · doi:10.1186/1742-4690-7-27 · Cited by 5
Role of Host Proteins in HIV-1 Early Replication
Sunnam, L. B., & Kondapi, A. K. (2016) · InTech eBooks · doi:10.5772/62108 · 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
“Several plausible working models for the function of LEDGF/p75 during HIV-1 integration have been put forward: It (i) protects IN from proteasomal degradation, (ii) functions as a molecular adaptor for tethering the intasome to the target DNA, and (iii) augments strand transfer during integration (Emiliani et al. 2005…”
InfluentialZhang, Y., Zhou, Y., Zhang, Y., Lv, J., Shen, Y., Zhang, D., Liu, B., Zhao, W., Ju, J., Zhu, Q., et al. (2025) · Advanced Science · doi:10.1002/advs.202416809 · Cited by 4
Ishigami, J., Hu, X. F., Schlosser, P., Austin, T. R., Chen, J., Psaty, B. M., Dowdy, D. W., Ballantyne, C. M., Grams, M. E., Coresh, J., et al. (2025) · The Journal of Applied Laboratory Medicine · doi:10.1093/jalm/jfaf179 · Cited by 4
Metadata
- Authors
- Llano, M., Saenz, D. T., Meehan, A., Wongthida, P., Peretz, M., Walker, W. H., Teo, W., & Poeschla, E. M.
- Affiliations
- Mayo Clinic (US)
- Corresponding author
- Poeschla, Eric M.
- Venue
- Science
- Published
- 2006-10-20
- Volume
- 314
- Issue
- 5798
- Pages
- 461-464
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2085489729
- Cited by
- 537
- References
- 15
- Citations by year
- 2026: 8 · 2025: 11 · 2024: 15 · 2023: 10 · 2022: 22 · 2021: 21 · 2020: 16 · 2019: 22 · 2018: 18 · 2017: 22 · 2016: 27 · 2015: 28 · 2014: 43 · 2013: 30 · 2012: 45
- FWCI
- 13.66
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Immunology and Microbiology › Virology › HIV Research and Treatment
- Health Sciences › Medicine › Infectious Diseases › HIV/AIDS drug development and treatment
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Virus-based gene therapy research
- Keywords
- LEDGF/p75, HIV integration, HIV integrase, chromosomal integration, transcriptional coactivator, HIV reservoir, RNAi knockdown, dominant negative protein
- MeSH terms
- Cell Line, Chromatin, Humans, Recombinant Fusion Proteins, Transcription Factors, Virus Replication, CD4-Positive T-Lymphocytes, HIV-1, Virus Integration, HIV Integrase, RNA Interference, Intercellular Signaling Peptides and Proteins, Adaptor Proteins, Signal Transducing
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