The DOI matches its Crossref record; 61 of the 61 references it cites were found in a registry or an index.
LEDGF/p75 functions downstream from preintegration complex formation to effect gene-specific HIV-1 integration
Open accessAbstract
LEDGF/p75 directly interacts with lentiviral integrase proteins and can modulate their enzymatic activities and chromosomal association. A novel genetic knockout model was established that allowed us for the first time to analyze HIV-1 integration in the absence of LEDGF/p75 protein. Supporting a crucial role for the cofactor in viral replication, HIV-1 vector integration and reporter gene expression were significantly reduced in LEDGF-null cells. Yet, integrase processed the viral cDNA termini normally and maintained its local target DNA sequence preference during integration. Preintegration complexes extracted from knockout cells moreover supported normal levels of DNA strand transfer activity in vitro. In contrast, HIV-1 lost its strong bias toward integrating into transcription units, displaying instead increased affinity for promoter regions and CpG islands. Our results reveal LEDGF/p75 as a critical targeting factor, commandeering lentiviruses from promoter- and/or CpG island-proximal pathways that are favored by other members of Retroviridae . Akin to yeast retrotransposons, disrupting the lentiviral targeting mechanism significantly perturbs overall integration.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
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?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“The genic proviruses that did form under these conditions uncharacteristically congregated around transcription start sites87,99–101.”
From Structure and function of retroviral integrase (2022) · cites this paper as [99]
Experimental — accuracy not yet measuredThe cited source says what the claim attributes to it.
In the citing paper
“Knockout of the PSIP1 gene, which encodes for LEDGF/p75, similarly suppressed levels of vDNA integration in cells several fold98,99.”
From Structure and function of retroviral integrase (2022) · cites this paper as [99]
The cited source says what the claim attributes to it.
In the citing paper
“Alterations that disrupted LEDGF/p75 binding to chromatin or IN ablated its cofactor function during HIV-1 infection99,103,112.”
From Structure and function of retroviral integrase (2022) · cites this paper as [99]
The cited source says what the claim attributes to it.
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 Shun et al. 2007
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
HIV-1 Integration in the Human Genome Favors Active Genes and Local Hotspots
Schröder, A. R. W., Shinn, P., Chen, H., Berry, C., Ecker, J. R., & Bushman, F. (2002) · Cell · doi:10.1016/s0092-8674(02)00864-4 · Cited by 1,832
Transcription Start Regions in the Human Genome Are Favored Targets for MLV Integration
Wu, X., Li, Y., Crise, B., & Burgess, S. M. (2003) · Science · doi:10.1126/science.1083413 · Cited by 1,305
Retroviral DNA Integration: ASLV, HIV, and MLV Show Distinct Target Site Preferences
Mitchell, R., Beitzel, B. F., Schröder, A. R. W., Shinn, P., Chen, H., Berry, C. C., Ecker, J. R., & Bushman, F. D. (2004) · PLoS Biology · doi:10.1371/journal.pbio.0020234 · Cited by 1,002
Deininger, P. L., & Batzer, M. A. (1999) · Molecular Genetics and Metabolism · doi:10.1006/mgme.1999.2864 · Cited by 911
Inducible gene targeting in mice using the Cre/lox system.
Sauer, B. (1998) · Methods · doi:10.1006/meth.1998.0593 · Cited by 858
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
Self-citationA 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
HIV-1 DNA integration: Mechanism of viral DNA cleavage and DNA strand transfer
Engelman, A., Mizuuchi, K., & Craigie, R. (1991) · Cell · doi:10.1016/0092-8674(91)90297-c · Cited by 655
Self-citationAn essential role for LEDGF/p75 in HIV integration
Llano, M., Saenz, D. T., Meehan, A., Wongthida, P., Peretz, M., Walker, W. H., Teo, W., & Poeschla, E. M. (2006) · Science · doi:10.1126/science.1132319 · Cited by 537
Breaking barriers to transcription elongation
Saunders, A., Core, L. J., & Lis, J. T. (2006) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1981 · Cited by 525
Cited by
Sorted by citations
Items 201–300 of 470
Synthesis and Evaluation of Aryl Quinolines as HIV-1 Integrase Multimerization Inhibitors
Jentsch, N. G., Hart, A. P., Hume, J. D., Sun, J., McNeely, K. A., Lama, C., Pigza, J. A., Donahue, M. G., & Kessl, J. J. (2018) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.8b00269 · Cited by 32
Shkriabai, N., Dharmarajan, V., Slaughter, A., Kessl, J. J., Larue, R. C., Feng, L., Fuchs, J. R., Griffin, P. R., & Kvaratskhelia, M. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.589572 · Cited by 30
Hoyte, A. C., Jamin, A. V., Koneru, P. C., Kobe, M. J., Larue, R. C., Fuchs, J. R., Engelman, A. N., & Kvaratskhelia, M. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.816645 · Cited by 30
Self-citationHIV-1 capsid and viral DNA integration
Dwivedi, R., Prakash, P., Kumbhar, B. V., Balasubramaniam, M., & Dash, C. (2023) · mBio · doi:10.1128/mbio.00212-22 · Cited by 31
Psip1/Ledgf p75 restrainsHoxgene expression by recruiting both trithorax and polycomb group proteins
Pradeepa, M. M., Grimes, G. R., Taylor, G. C. A., Sutherland, H. G. E., & Bickmore, W. A. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku647 · Cited by 34
Novel integrase inhibitors for HIV
Prada, N., & Markowitz, M. H. (2010) · Expert Opinion on Investigational Drugs · doi:10.1517/13543784.2010.501078 · Cited by 30
Winans, S., & Goff, S. P. (2020) · PLOS Pathogens · doi:10.1371/journal.ppat.1009147 · Cited by 29
Mullins, J. I., & Frenkel, L. M. (2017) · The Journal of Infectious Diseases · doi:10.1093/infdis/jiw636 · Cited by 29
Janssens, J., De Wit, F., Parveen, N., & Debyser, Z. (2022) · mBio · doi:10.1128/mbio.00007-22 · Cited by 28
Sowd, G. A., & Aiken, C. (2021) · PLoS Pathogens · doi:10.1371/journal.ppat.1009190 · Cited by 28
Bedwell, G. J., Jang, S., Li, W., Singh, P. K., & Engelman, A. (2021) · Nucleic Acids Research · doi:10.1093/nar/gkab514 · Cited by 28
Self-citationSapp, N., Burge, N. L., Cox, K. L., Thapa, S., Prakash, P., Balasubramaniam, M., Christensen, D. E., Li, M., Linderberger, J., Kvaratskhelia, M., et al. (2022) · Journal of Virology · doi:10.1128/jvi.01011-22 · Cited by 31
Naughtin, M., Haftek-Terreau, Z., Xavier, J., Meyer, S., Silvain, M., Jaszczyszyn, Y., Levy, N., Miele, V., Benleulmi, M. S., Ruff, M., et al. (2015) · PLoS ONE · doi:10.1371/journal.pone.0129427 · Cited by 34
Sites of retroviral DNA integration: From basic research to clinical applications
Serrao, E., & Engelman, A. (2015) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2015.1102859 · Cited by 32
Self-citationBasu, A., Drame, A., Muñoz, R., Gijsbers, R., Debyser, Z., León, M. A. D., & Casiano, C. A. (2011) · The Prostate · doi:10.1002/pros.21463 · Cited by 28
Retroviral Integrase: Then and Now
Andrake, M., & Skalka, A. M. (2015) · Annual Review of Virology · doi:10.1146/annurev-virology-100114-055043 · Cited by 34
The future of integrase inhibitors of HIV-1
Malet, I., Cálvez, V., & Marcelin, A. (2012) · Current Opinion in Virology · doi:10.1016/j.coviro.2012.08.005 · Cited by 27
Kumar, D., Sharma, P., Shabu, Kaur, R., Lobe, M. M. M., Gupta, G. K., & Ntie‐Kang, F. (2021) · RSC Advances · doi:10.1039/d0ra10655k · Cited by 27
Brady, T., Kelly, B. J., Male, F., Roth, S. L., Bailey, A., Malani, N., Gijsbers, R., O’Doherty, U., & Bushman, F. D. (2013) · Journal of Virological Methods · doi:10.1016/j.jviromet.2013.01.004 · Cited by 30
Ciuffi, A. (2016) · Clinical Microbiology and Infection · doi:10.1016/j.cmi.2016.02.013 · Cited by 27
Patel, D., Antwi, J., Koneru, P. C., Serrao, E., Forli, S., Kessl, J. J., Feng, L., Deng, N., Levy, R. M., Fuchs, J. R., et al. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.753384 · Cited by 29
Self-citationThe FACT Complex Promotes Avian Leukosis Virus DNA Integration
Winans, S., Larue, R. C., Abraham, C. M., Shkriabai, N., Skopp, A., Winkler, D., Kvaratskhelia, M., & Beemon, K. L. (2017) · Journal of Virology · doi:10.1128/jvi.00082-17 · Cited by 26
Mouse T-cells restrict replication of human immunodeficiency virus at the level of integration
Tervo, H.-M., Goffinet, C., & Keppler, O. T. (2008) · Retrovirology · doi:10.1186/1742-4690-5-58 · Cited by 26
Serial number tagging reveals a prominent sequence preference of retrotransposon integration
Chatterjee, A. G., Esnault, C., Guo, Y., Hung, S., McQueen, P. G., & Levin, H. L. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku534 · Cited by 27
Human gene therapy vectors derived from feline lentiviruses
Barraza, R., & Poeschla, E. M. (2008) · Veterinary Immunology and Immunopathology · doi:10.1016/j.vetimm.2008.01.009 · Cited by 26
HIV-1 Integrase-DNA Recognition Mechanisms
Kessl, J. J., McKee, C. J., Eidahl, J. O., Shkriabai, N., Katz, A., & Kvaratskhelia, M. (2009) · Viruses · doi:10.3390/v1030713 · Cited by 27
Jang, S., Bedwell, G. J., SINGH, S. P., Yu, H. J., Arnarson, B., Singh, P. K., Radhakrishnan, R., Douglas, A. W., Ingram, Z., Freniere, C., et al. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkae769 · Cited by 28
Self-citationStructural Properties of HIV Integrase·Lens Epithelium-derived Growth Factor Oligomers
Gupta, K., Diamond, T. L., Hwang, Y. S., Bushman, F. D., & Duyne, G. D. V. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.114413 · Cited by 24
Elvitegravir: a once-daily, boosted, HIV-1 integrase inhibitor
Lampiris, H. W. (2011) · Expert Review of Anti-infective Therapy · doi:10.1586/eri.11.157 · Cited by 25
The Chromodomain of Tf1 Integrase Promotes Binding to cDNA and Mediates Target Site Selection
Chatterjee, A. G., Leem, Y. E., Kelly, F. D., & Levin, H. L. (2008) · Journal of Virology · doi:10.1128/jvi.01588-08 · Cited by 24
Vranckx, L. S., Demeulemeester, J., Debyser, Z., & Gijsbers, R. (2016) · PLoS ONE · doi:10.1371/journal.pone.0164167 · Cited by 24
Mechanisms of LTR‐Retroelement Transposition: Lessons from Drosophila melanogaster
Нефедова, Л. Н., & Kim, A. I. (2017) · Viruses · doi:10.3390/v9040081 · Cited by 24
Schaller, T., Bulli, L., Pollpeter, D., Betancor, G., Kutzner, J., Apolonia, L., Herold, N., Burk, R., & Malim, M. H. (2017) · Journal of Virology · doi:10.1128/jvi.00463-17 · Cited by 27
Quantitative analysis of HIV-1 preintegration complexes
Engelman, A., Öztop, I., Vandegraaff, N., & Raghavendra, N. K. (2009) · Methods · doi:10.1016/j.ymeth.2009.02.005 · Cited by 24
Self-citationDNA minicircles clarify the specific role of DNA structure on retroviral integration
Pasi, M., Mornico, D., Volant, S., Juchet, A., Batisse, J., Bouchier, C., Parissi, V., Ruff, M., Lavery, R., & Lavigne, M. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw651 · Cited by 26
Xue, W., Liu, H., & Yao, X. (2014) · PLoS ONE · doi:10.1371/journal.pone.0090799 · Cited by 23
TOX4 and NOVA1 Proteins Are Partners of the LEDGF PWWP Domain and Affect HIV-1 Replication
Morchikh, M., Naughtin, M., Nunzio, F. D., Xavier, J., Charneau, P., Jacob, Y., & Lavigne, M. (2013) · PLoS ONE · doi:10.1371/journal.pone.0081217 · Cited by 27
The Interaction Between Lentiviral Integrase and LEDGF: Structural and Functional Insights
Hare, S., & Cherepanov, P. (2009) · Viruses · doi:10.3390/v1030780 · Cited by 26
Self-citationChromatin tethering and retroviral integration: Recent discoveries and parallels with DNA viruses
Meehan, A. M., & Poeschla, E. M. (2009) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2009.10.001 · Cited by 24
Impact of Chromatin on HIV Replication
Agosto, L. M., Gagné, M., & Henderson, A. J. (2015) · Genes · doi:10.3390/genes6040957 · Cited by 23
Wang, W., Zhou, J., Halambage, U. D., Jurado, K. A., Jamin, A. V., Wang, Y., Engelman, A., & Aiken, C. (2017) · Journal of Virology · doi:10.1128/jvi.02155-16 · Cited by 22
Self-citationAn overview of intracellular interactions between immunodeficiency viruses and their hosts
Bieniasz, P. D. (2012) · AIDS · doi:10.1097/qad.0b013e328353bd04 · Cited by 22
Xu, X., Powell, D. W., Lambring, C. J., Puckett, A. H., Deschenes, L., Prough, R. A., Poeschla, E. M., & Samuelson, D. J. (2012) · Molecular Carcinogenesis · doi:10.1002/mc.21977 · Cited by 22
Garcia-Rivera, J. A., Bueno, M. T. D., Morales, E., Kugelman, J. R., Rodríguez, D. F., & Llano, M. (2009) · Journal of Virology · doi:10.1128/jvi.01043-09 · Cited by 23
Capsid-CPSF6 interaction: Master regulator of nuclear HIV-1 positioning and integration
Achuthan, V., Perreira, J. M., Ahn, J. J., Brass, A. L., & Engelman, A. (2019) · JoLS Journal of Life Sciences · doi:10.36069/jols/20190604 · Cited by 25
Self-citationMultivalent interactions essential for lentiviral integrase function
Ballandras-Colas, A., Chivukula, V., Gruszka, D. T., Shan, Z., Singh, P. K., Pye, V. E., McLean, R. K., Bedwell, G. J., Li, W., Nans, A., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-29928-8 · Cited by 23
Self-citationEbina, H., Kanemura, Y., Suzuki, Y., Urata, K., Misawa, N., & Koyanagi, Y. (2012) · Virology · doi:10.1016/j.virol.2012.02.004 · Cited by 21
Retrotransposon Target Site Selection by Imitation of a Cellular Protein
Brady, T., Fuerst, P. G., Dick, R. A., Schmidt, C. L., & Voytas, D. F. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.01502-07 · Cited by 21
Šenigl, F., Auxt, M., & Hejnar, J. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks197 · Cited by 21
Hickey, A., Esnault, C., Majumdar, A., Chatterjee, A. G., Iben, J., McQueen, P. G., Yang, A. X., Mizuguchi, T., Grewal, S. I. S., & Levin, H. L. (2015) · Genetics · doi:10.1534/genetics.115.181602 · Cited by 21
The Multifaceted Contributions of Chromatin to HIV-1 Integration, Transcription, and Latency
Crignis, E. D., & Mahmoudi, T. (2016) · International review of cytology · doi:10.1016/bs.ircmb.2016.08.006 · Cited by 23
Retroviral DNA Transposition: Themes and Variations
Skala, A. M. (2014) · Microbiology Spectrum · doi:10.1128/microbiolspec.mdna3-0005-2014 · Cited by 22
Intensive RNAi with lentiviral vectors in mammalian cells
Miest, T. S., Saenz, D. T., Meehan, A. M., Llano, M., & Poeschla, E. M. (2008) · Methods · doi:10.1016/j.ymeth.2008.11.001 · Cited by 21
Mulky, A., Cohen, T. V., Козлов, С. В., Korbei, B., Foisner, R., Stewart, C. L., & KewalRamani, V. N. (2008) · Journal of Virology · doi:10.1128/jvi.00076-08 · Cited by 21
Moalic, Y., Félix, H., Takeuchi, Y., Jestin, A., & Blanchard, Y. (2008) · Journal of Virology · doi:10.1128/jvi.00856-08 · Cited by 21
HIV-1 IN/Pol recruits LEDGF/p75 into viral particles
Desimmie, B. A., Weydert, C., Schrijvers, R., Vets, S., Demeulemeester, J., Proost, P., Paron, I., Rijck, J. D., Mast, J., Bannert, N., et al. (2015) · Retrovirology · doi:10.1186/s12977-014-0134-4 · Cited by 20
Bina, M., Wyss, P. J., Novorolsky, E., Zulkelfi, N., Xue, J., Price, R. A., Fay, M., Gutmann, Z., Fogler, B. D., & Wang, D. (2013) · BMC Genomics · doi:10.1186/1471-2164-14-927 · Cited by 22
Role of host-encoded proteins in restriction of retroviral integration
Suzuki, Y., Chew, M. L., & Suzuki, Y. (2012) · Frontiers in Microbiology · doi:10.3389/fmicb.2012.00227 · Cited by 25
Zheng, Y., Ao, Z., Jayappa, K. D., & Yao, X. (2010) · Virology Journal · doi:10.1186/1743-422x-7-68 · Cited by 20
Lo, Y.-T., Tian, T., Nadeau, P. E., Park, J., & Mergia, A. (2009) · Journal of Virology · doi:10.1128/jvi.02435-09 · Cited by 23
Pleiotropic Nature of HIV‐1 Integrase Mutations
Engelman, A. (2011) · Wiley eBooks · doi:10.1002/9781118015377.ch6 · Cited by 24
Self-citationGupta, K., Allen, A., Giraldo, C., Eilers, G., Sharp, R., Hwang, Y., Murali, H., Cruz, K., Janmey, P., Bushman, F., et al. (2021) · Structure · doi:10.1016/j.str.2020.12.001 · Cited by 19
“The IN-binding domain of LEDGF/p75 (IBD) binds tightly to the dimer interface of the CCD, facilitating HIV integration at active transcription units within the host genome (Ciuffi et al., 2005; Schroder et al., 2002; Shun et al., 2007).”
BackgroundDual role of host cell factors in HIV-1 replication: restriction and enhancement of the viral cycle.
Coiras, M., López‐Huertas, M. R., del Cojo, M. S., Mateos, E., & Alcamı́, J. (2010) · PubMed · Cited by 19
Ubiquitination and SUMOylation in HIV Infection: Friends and Foes
Colomer-Lluch, M., Castro‐Gonzalez, S., & Serra-Moreno, R. (2019) · Current Issues in Molecular Biology · doi:10.21775/cimb.035.159 · Cited by 21
A point mutation in HIV-1 integrase redirects proviral integration into centromeric repeats
Winans, S., Yu, H. J., Santos, K. D. L., Wang, G. Z., KewalRamani, V. N., & Goff, S. P. (2022) · Nature Communications · doi:10.1038/s41467-022-29097-8 · Cited by 20
Majumdar, A., Chatterjee, A. G., Ripmaster, T. L., & Levin, H. L. (2010) · Journal of Virology · doi:10.1128/jvi.01719-10 · Cited by 19
Alpha-enolase in viral target cells suppresses the human immunodeficiency virus type 1 integration
Kishimoto, N., Yamamoto, K., Iga, N., Kirihara, C., Abe, T., Takamune, N., & Misumi, S. (2020) · Retrovirology · doi:10.1186/s12977-020-00539-9 · Cited by 19
Knockdown of the Cellular Protein LRPPRC Attenuates HIV-1 Infection
Schweitzer, C. J., Matthews, J. M., Madson, C. J., Donnellan, M. R., Cerny, R. L., & Belshan, M. (2012) · PLoS ONE · doi:10.1371/journal.pone.0040537 · Cited by 19
Antiretroviral APOBEC3 cytidine deaminases alter HIV-1 provirus integration site profiles
Ajoge, H. O., Renner, T. M., Bélanger, K., Greig, M., Dankar, S. K., Kohio, H. P., Coleman, M. D., Ndashimye, E., Arts, E. J., Langlois, M., et al. (2023) · Nature Communications · doi:10.1038/s41467-022-35379-y · Cited by 20
The Drug-Induced Interface That Drives HIV-1 Integrase Hypermultimerization and Loss of Function
Singer, M. R., Dinh, T., Levintov, L., Annamalai, A. S., Rey, J. S., Briganti, L., Cook, N., Pye, V. E., Taylor, I. A., Kim, K., et al. (2023) · mBio · doi:10.1128/mbio.03560-22 · Cited by 19
Self-citationComparative Analysis of HIV-1 and Murine Leukemia Virus Three-Dimensional Nuclear Distributions
Quercioli, V., Primio, C. D., Casini, A., Mulder, L. C. F., Vranckx, L. S., Borrenberghs, D., Gijsbers, R., Debyser, Z., & Cereseto, A. (2016) · Journal of Virology · doi:10.1128/jvi.03188-15 · Cited by 19
Zinc Finger Endonuclease Targeting PSIP1 Inhibits HIV-1 Integration
Badía, R., Pauls, E., Riveira‐Muñoz, E., Clotet, B., Esté, J. A., & Ballana, E. (2014) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.02690-14 · Cited by 17
Debyser, Z., Bruggemans, A., Belle, S. V., Janssens, J., & Christ, F. (2021) · Advances in experimental medicine and biology · doi:10.1007/978-981-16-0267-2_4 · Cited by 18
Su, K., Wang, D., Ye, J., Kim, Y., & Chow, S. A. (2009) · Methods · doi:10.1016/j.ymeth.2009.01.001 · Cited by 19
Labrador, M., Sha, K., Li, A., & Corces, V. G. (2008) · Genetics · doi:10.1534/genetics.108.094318 · Cited by 17
Targeting Virus-host Interactions of HIV Replication
Weydert, C., Rijck, J. D., Christ, F., & Debyser, Z. (2015) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026615666150901115106 · Cited by 16
Centrophilic Retrotransposons of Plant Genomes
Bousios, A., Kakutani, T., & Henderson, I. R. (2025) · Annual Review of Plant Biology · doi:10.1146/annurev-arplant-083123-082220 · Cited by 16
Retroviral integration profiles: their determinants and implications for gene therapy
Lim, K. (2012) · BMB Reports · doi:10.5483/bmbrep.2012.45.4.207 · Cited by 16
Zheng, Y., Jayappa, K. D., Ao, Z., Qiu, X., Su, R., & Yao, X. (2019) · Virology Journal · doi:10.1186/s12985-019-1134-8 · Cited by 16
Mugisha, C. S., Dinh, T., Kumar, A., Tenneti, K., Eschbach, J. E., Davis, K., Gifford, R. J., Kvaratskhelia, M., & Kutluay, S. B. (2022) · mBio · doi:10.1128/mbio.00431-22 · Cited by 17
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
BRD4 modulator ZL0580 and LEDGINs additively block and lock HIV-1 transcription
Pellaers, E., Janssens, J., Wils, L., Denis, A., Bhat, A., Belle, S. V., Feng, D., Christ, F., Zhan, P., & Debyser, Z. (2025) · Nature Communications · doi:10.1038/s41467-025-59398-7 · Cited by 16
Non-Enzymatic Functions of Retroviral Integrase: The Next Target for Novel Anti-HIV Drug Development
Masuda, T. (2011) · Frontiers in Microbiology · doi:10.3389/fmicb.2011.00210 · Cited by 17
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
Wellensiek, B. P., Ramakrishnan, R., Sundaravaradan, V., Mehta, R., Harris, D. T., & Ahmad, N. (2008) · Virology · doi:10.1016/j.virol.2008.10.052 · Cited by 15
Goffinet, C., Allespach, I., Oberbremer, L., Golden, P. L., Foster, S. A., Johns, B. A., Weatherhead, J. G., Novick, S. J., Chiswell, K., Garvey, E. P., et al. (2009) · Journal of Virology · doi:10.1128/jvi.00683-09 · Cited by 15
Isolation of a Human Betaretrovirus from Patients with Primary Biliary Cholangitis
Goubran, M., Wang, W., Indik, S., Faschinger, A., Wasilenko, S. T., Bintner, J., Carpenter, E. J., Zhang, G., Nuin, P. A. S., MacIntyre, G., et al. (2022) · Viruses · doi:10.3390/v14050886 · 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
Saeed, M. Q., Dufour, N., Bartholmae, C., Sieranska, U., Knopf, M., Thierry, E., Thierry, S., Delelis, O., Grandchamp, N., Pilet, H., et al. (2014) · Molecular Therapy — Nucleic Acids · doi:10.1038/mtna.2014.65 · Cited by 14
Woodward, C. L., & Chow, S. A. (2010) · Nucleus · doi:10.4161/nucl.1.1.10571 · Cited by 14
Singh, P., Li, W., Bedwell, G., Fadel, H., Poeschla, E., & Engelman, A. (2022) · Viruses · doi:10.3390/v14091883 · Cited by 13
Self-citationHendrix, 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
Self-citationInteractions of Host Proteins with the Murine Leukemia Virus Integrase
Studamire, B., & Goff, S. P. (2010) · Viruses · doi:10.3390/v2051110 · Cited by 14
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
1,2,3,4‐Tetrahydroisoquinolines as inhibitors of HIV ‐1 integrase and human LEDGF /p75 interaction
George, A., Reddy, A. G. K., Satyanarayana, G., & Raghavendra, N. K. (2018) · Chemical Biology & Drug Design · doi:10.1111/cbdd.13175 · Cited by 13
Self-citationOptimized 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
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
Self-citationBelle, 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
Jayakumar, S., Taylor, G. C. A., von Kriegsheim, A., & Pradeepa, M. M. (2021) · Wellcome Open Research · doi:10.12688/wellcomeopenres.11589.4 · Cited by 12
Metadata
- Authors
- Shun, M.-C., Raghavendra, N. K., Vandegraaff, N., Daigle, J. E., Hughes, S., Kellam, P., Cherepanov, P., & Engelman, A.
- Affiliations
- Harvard University (US)
- Imperial College London (GB)
- University College London (GB)
- Venue
- Genes & Development
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2007-07-15
- Volume
- 21
- Issue
- 14
- Pages
- 1767-1778
- ISSN
- 0890-9369 (ISSN-L)
- 1549-5477
- PMC
- PMC1920171
- OpenAlex
- W2106494657
- Cited by
- 467
- References
- 61
- Citations by year
- 2026: 13 · 2025: 11 · 2024: 11 · 2023: 13 · 2022: 26 · 2021: 24 · 2020: 13 · 2019: 17 · 2018: 18 · 2017: 24 · 2016: 26 · 2015: 32 · 2014: 37 · 2013: 26 · 2012: 32
- Type
- posted content
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Genes & Development (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- UCL Discovery (University College London) (submittedVersion)
- Funders
- National Institutes of Health
- Medical Research Council
- National Institute of Allergy and Infectious Diseases (AI39394, R01AI039394, R37AI039394)
- Topics
- Life Sciences › Immunology and Microbiology › Virology › HIV Research and Treatment
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Virus-based gene therapy research
- Health Sciences › Medicine › Infectious Diseases › HIV/AIDS drug development and treatment
- Keywords
- LEDGF/p75, HIV-1 integration, preintegration complex, CpG islands, DNA strand transfer, retroviral replication
- MeSH terms
- Animals, Base Sequence, Binding Sites, Cell Line, DNA, Humans, Leukemia Virus, Murine, Promoter Regions, Genetic, Transcription Factors, HIV-1, Consensus Sequence, Virus Integration, Gene Deletion, CpG Islands, Integrases, Intercellular Signaling Peptides and Proteins, Adaptor Proteins, Signal Transducing, Mice, In Vitro Techniques
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