The DOI matches its Crossref record; 36 of the 36 references it cites were found in a registry or an index.
NF-κB RelA Phosphorylation Regulates RelA Acetylation
Open accessAbstract
The nuclear functions of NF-kappaB p50/RelA heterodimers are regulated in part by posttranslational modifications of its RelA subunit, including phosphorylation and acetylation. Acetylation at lysines 218, 221, and 310 differentially regulates RelA's DNA binding activity, assembly with IkappaBalpha, and transcriptional activity. However, it remains unclear whether the acetylation is regulated or simply due to stimulus-coupled nuclear translocation of NF-kappaB. Using anti-acetylated lysine 310 RelA antibodies, we detected p300-mediated acetylation of RelA in vitro and in vivo after stimulation of cells with tumor necrosis factor alpha (TNF-alpha). Coexpression of catalytically inactive mutants of the catalytic subunit of protein kinase A/mitogen- and stress-activated kinase 1 or IKK1/IKK2, which phosphorylate RelA on serine 276 or serine 536, respectively, sharply inhibited RelA acetylation on lysine 310. Furthermore, phosphorylation of RelA on serine 276 or serine 536 increased assembly of phospho-RelA with p300, which enhanced acetylation on lysine 310. Reconstitution of RelA-deficient murine embryonic fibroblasts with RelA S276A or RelA S536A decreased TNF-alpha-induced acetylation of lysine 310 and expression of the endogenous NF-kappaB-responsive E-selectin gene. These findings indicate that the acetylation of RelA at lysine 310 is importantly regulated by prior phosphorylation of serines 276 and 536. Such phosphorylated and acetylated forms of RelA display enhanced transcriptional activity.
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?
In the citing paper
“Extracellular inflammatory signals including lipopolysaccharide (LPS), pro-inflammatory cytokines, reactive oxygen species, advanced glycation end products, and oxidized low-density lipoprotein trigger the phosphorylation of IKKβ, which in turn phosphorylates IκBα for ubiquitination and degradation by proteasome [13–18].”
From Edible blue-green algae reduce the production of pro-inflammatory cytokines by inhibiting NF-κB pathway in macrophages and splenocytes (2013) · cites this paper as [13]
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
Jenuwein, T., & Allis, C. D. (2001) · Science · doi:10.1126/science.1063127 · Cited by 9,756
The language of covalent histone modifications
Strahl, B. D., & Allis, C. D. (2000) · Nature · doi:10.1038/47412 · Cited by 8,679
THE NF-κB AND IκB PROTEINS: New Discoveries and Insights
Baldwin, A. S. (1996) · Annual Review of Immunology · doi:10.1146/annurev.immunol.14.1.649 · Cited by 5,882
Chen, X., Xiu, M., Xing, J., Yu, S., Min, D., & Guo, F. (2017) · Cellular Physiology and Biochemistry · doi:10.1159/000479439 · Cited by 5,760
Missing Pieces in the NF-κB Puzzle
Ghosh, S., & Karin, M. (2002) · Cell · doi:10.1016/s0092-8674(02)00703-1 · Cited by 3,638 · cited 2×
“The liberated NF-B complex rapidly translocates to the nucleus, ending the first phase ( 13 ).”
BackgroundModulation of NF‐κB‐dependent transcription and cell survival by the SIRT1 deacetylase
Yeung, F., Hoberg, J. E., Ramsey, C. S., Keller, M. D., Jones, D. R., Frye, R. A., & Mayo, M. W. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600244 · Cited by 2,750
Phosphorylated CREB binds specifically to the nuclear protein CBP
Chrivia, J. C., Kwok, R. P. S., Lamb, N., Hagiwara, M., Montminy, M. R., & Goodman, R. H. (1993) · Nature · doi:10.1038/365855a0 · Cited by 2,052
CBP/p300 in cell growth, transformation, and development
Goodman, R. H., & Smolik, S. (2000) · Genes & Development · doi:10.1101/gad.14.13.1553 · Cited by 1,778
Shaping the nuclear action of NF-κB
Chen, L., & Greene, W. C. (2004) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1368 · Cited by 1,248
Self-citationDuration of Nuclear NF-κB Action Regulated by Reversible Acetylation
Chen, L., Fischle, W., Verdin, E. M., & Greene, W. C. (2001) · Science · doi:10.1126/science.1062374 · Cited by 1,231
Self-citation
Cited by
Sorted by citations
Items 201–300 of 438
Kaffe, E., Fiorotto, R., Pellegrino, F., Mariotti, V., Amenduni, M., Cadamuro, M., Fabris, L., Strazzabosco, M., & Spirlı̀, C. (2017) · Hepatology · doi:10.1002/hep.29652 · Cited by 45
Hou, Y., Chiu, W., Yeh, C., & Yeh, S. (2011) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00066.2011 · Cited by 45
Low-level arsenic causes chronic inflammation and suppresses expression of phagocytic receptors
Prasad, P., & Sinha, D. (2017) · Environmental Science and Pollution Research · doi:10.1007/s11356-017-8744-8 · Cited by 43
LncRNA HOXA-AS2 represses endothelium inflammation by regulating the activity of NF-κB signaling
Zhu, X., Liu, Y., Yu, J., Du, J., Guo, R., Feng, Y., Zhong, G., Jiang, Y., & Lin, J. (2018) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2018.12.012 · Cited by 43
Wu, X., Qi, J., Bradner, J. E., Xiao, G., & Chen, L. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.485029 · Cited by 45
Self-citationMir, S. U. R., Jin, L., & Craven, R. J. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.324921 · Cited by 42
Schiaffino, L., Bonafede, R., Scambi, I., Parrella, E., Pizzi, M., & Mariotti, R. (2018) · Scientific Reports · doi:10.1038/s41598-018-30659-4 · Cited by 42
Dai, Y., Chen, S., Wang, L., Pei, X., Funk, V. L., Kramer, L. B., Dent, P., & Grant, S. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.284216 · Cited by 42
Wu, L., Xu, B., Fan, W., Zhu, X., Wang, G., & Zhang, A. (2013) · FEBS Journal · doi:10.1111/febs.12391 · Cited by 42
Tsuchiya, Y., Osaki, K., Kanamoto, M., Nakao, Y., Takahashi, E., Higuchi, T., & Kamata, H. (2017) · FEBS Letters · doi:10.1002/1873-3468.12912 · Cited by 40
Transcription Factors in Cartilage Homeostasis and Osteoarthritis
Neefjes, M., van Caam, A., & van der Kraan, P. M. (2020) · Biology · doi:10.3390/biology9090290 · Cited by 44
Lin, C., Lee, C., Chu, T., Cheng, C., Luo, S., Hsiao, L., & Yang, C. (2007) · Journal of Cellular Physiology · doi:10.1002/jcp.20987 · Cited by 41
Dong, X., & Feng, P. (2011) · PLoS Pathogens · doi:10.1371/journal.ppat.1002336 · Cited by 39
Castellucci, M., Rossato, M., Calzetti, F., Tamassia, N., Zeminian, S., Cassatella, M. A., & Bazzoni, F. (2015) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2015.04.023 · Cited by 40
Targeting Chromatin Remodeling in Inflammation and Fibrosis
Yang, J., Tian, B., & Brasier, A. R. (2016) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2016.11.001 · Cited by 40
Jhou, J., Chen, S.-J., Huang, H., Lin, W., Huang, D.-Y., & Tzeng, S. (2017) · Experimental & Molecular Medicine · doi:10.1038/emm.2017.144 · Cited by 40
Paul, A., Danley, M., Saha, B., Tawfik, O. W., & Paul, S. (2015) · Scientific Reports · doi:10.1038/srep12520 · Cited by 45
Novotny, G. W., Lundh, M., Backe, M. B., Christensen, D. P., Hansen, J. B., Dahllöf, M. S., Pallesen, E. M. H., & Mandrup-Poulsen, T. R. (2012) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2012.09.014 · Cited by 37
Chrysostomou, S., Roy, R., Prischi, F., Thamlikitkul, L., Chapman, K. L., Mufti, U., Peach, R. L., Ding, L., Hancock, D. C., Moore, C., et al. (2021) · Science Translational Medicine · doi:10.1126/scitranslmed.aba4627 · Cited by 39
NF-κB Inducing Kinase Regulates Intestinal Immunity and Homeostasis
Wang, B., & Shen, J. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.895636 · Cited by 42
Pejanovic, N., Hochrainer, K., Liu, T., Aerne, B. L., Soares, M. P., & Anrather, J. (2012) · PLoS ONE · doi:10.1371/journal.pone.0042020 · Cited by 39
Pathak, S. K., Sköld, A. E., Mohanram, V., Persson, C. M., Johansson, U., & Spetz, A. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.336545 · Cited by 39
EVI1 Acts as an Inducible Negative-Feedback Regulator of NF-κB by Inhibiting p65 Acetylation
Xu, X., Woo, C.-H., Steere, R. R., Lee, B. C., Huang, Y., Wu, J. T., Pang, J., Lim, J. H., Xu, H., Zhang, W., et al. (2012) · The Journal of Immunology · doi:10.4049/jimmunol.1103527 · Cited by 38
Clavijo, P. E., & Frauwirth, K. A. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1100793 · Cited by 40
Layman, W. S., Williams, D. M., Dearman, J., Sauceda, M. A., & Zuo, J. (2015) · Cell Death Discovery · doi:10.1038/cddiscovery.2015.12 · Cited by 37
Sun, Y., Xie, Y., Du, L., Sun, J., & Liu, Z. (2018) · Cardiovascular Therapeutics · doi:10.1111/1755-5922.12320 · Cited by 38
Zhu, L., Ni, H., Chen, R., Chang, L., Shi, H., Qiu, D., Zhang, Z., Wu, D., Jiang, Z., Xin, H., et al. (2018) · Journal of Neurochemistry · doi:10.1111/jnc.14478 · Cited by 37
Mu, H. H., Calderone, T. L., Davies, M. A., Prieto, V. G., Wang, H., Mills, G. B., Bar‐Eli, M., & Gershenwald, J. E. (2012) · American Journal Of Pathology · doi:10.1016/j.ajpath.2012.03.003 · Cited by 37
Álvarez, Y., Rodríguez, M. R., Municio, C., Hugo, E., Alonso, S., Ibarrola, N., Fernández, N., & Crespo, M. S. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.391839 · Cited by 37
Li, Q., Liu, F., Dang, R., Feng, C., Xiao, R., Hua, Y., Wang, W., Jia, Z., & Liu, D. (2020) · Journal of Cellular Physiology · doi:10.1002/jcp.29780 · Cited by 36
Wang, P., Yang, C., Lü, J., Ren, Y., Goltzman, D., & Miao, D. (2023) · Journal of Orthopaedic Translation · doi:10.1016/j.jot.2023.04.003 · Cited by 35
Gu, Q., Kong, Y., Yu, Z., Li, B., & Xiao, Y. (2011) · Biochimie · doi:10.1016/j.biochi.2011.02.009 · Cited by 36
Romero, N., Waesberghe, C. V., & Favoreel, H. W. (2020) · Journal of Virology · doi:10.1128/jvi.00196-20 · Cited by 34
Tsuchiya, R., Tanaka, T., Hozumi, Y., Nakano, T., Okada, M., Topham, M. K., Iino, M., & Goto, K. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2014.11.011 · Cited by 33
Shi, H., & Berger, E. A. (2018) · Mediators of Inflammation · doi:10.1155/2018/3020675 · Cited by 33
Actin cytoskeleton differentially modulates NF-κB-mediated IL-8 expression in myelomonocytic cells
Kustermans, G., Mjiyad, N. E., Horion, J., Jacobs, N., Piette, J. G., & Legrand-Poels, S. (2008) · Biochemical Pharmacology · doi:10.1016/j.bcp.2008.08.017 · Cited by 36
Strassheim, D., Riddle, S. R., Burke, D. L., Geraci, M. W., & Stenmark, K. R. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0901045 · Cited by 32
Ampofo, E., Rudzitis‐Auth, J., Dahmke, I. N., Rößler, O. G., Thiel, G., Montenarh, M., Menger, M. D., & Laschke, M. W. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2015.07.013 · Cited by 32
Activation of NF-κB Is a Novel Target of KRAS-Induced Endometrial Carcinogenesis
Mizumoto, Y., Kyo, S., Kiyono, T., Takakura, M., Nakamura, M., Maida, Y., Mori, N., Bono, Y., Sakurai, H., & Inoue, M. (2011) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-10-2291 · Cited by 32
Computational Reconstruction of NFκB Pathway Interaction Mechanisms during Prostate Cancer
Börnigen, D., Tyekucheva, S., Wang, X., Rider, J. R., Lee, G. M., Mucci, L. A., Sweeney, C. J., & Huttenhower, C. (2016) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1004820 · Cited by 30
Bandyopadhaya, A., Tsurumi, A., & Rahme, L. G. (2017) · Frontiers in Microbiology · doi:10.3389/fmicb.2017.01211 · Cited by 29
NF-κB activation by Helicobacter pylorirequires Akt-mediated phosphorylation of p65
Takeshima, E., Tomimori, K., Kawakami, H., Ishikawa, C., Sawada, S., Tomita, M., Senba, M., Kinjo, F., Mimuro, H., Sasakawa, C., et al. (2009) · BMC Microbiology · doi:10.1186/1471-2180-9-36 · Cited by 32
RetractedZhao, Y., Tian, B., Sadygov, R. G., Zhang, Y., & Brasier, A. R. (2016) · Journal of Proteomics · doi:10.1016/j.jprot.2016.07.014 · Cited by 31
The histone deacetylase Hdac1 regulates inflammatory signalling in intestinal epithelial cells
Gonneaud, A., Gagné, J. M., Turgeon, N., & Asselin, C. (2014) · Journal of Inflammation · doi:10.1186/s12950-014-0043-2 · Cited by 32
Herpes Simplex Virus 1 UL2 Inhibits the TNF-α–Mediated NF-κB Activity by Interacting With p65/p50
Cai, M., Liao, Z., Zou, X., Xu, Z., Wang, Y., Li, T., Li, Y., Ou, X., Deng, Y., Guo, Y., et al. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.00549 · Cited by 30
The NF-κB signalling pathway regulates GLUT6 expression in endometrial cancer
Caruana, B. T., & Byrne, F. L. (2020) · Cellular Signalling · doi:10.1016/j.cellsig.2020.109688 · Cited by 31
Li, K., Zhang, Z., Mei, Y., Yang, Q., Qiao, S., Ni, C., Yao, Y., Li, X., Li, M., Wei, D., et al. (2021) · Theranostics · doi:10.7150/thno.51976 · Cited by 30
Field, J. T., Martens, M. D., Mughal, W., Hai, Y., Chapman, D. C., Hatch, G. M., Ivanco, T. L., Diehl‐Jones, W. L., & Gordon, J. W. (2018) · Cell Death Discovery · doi:10.1038/s41420-018-0104-z · Cited by 30
Ishinaga, H., Jono, H., Lim, J. H., Komatsu, K., Xu, X., Lee, J., Woo, C.-H., Xu, H., Feng, X., Chen, L., et al. (2008) · Biochemical Journal · doi:10.1042/bj20080781 · Cited by 29
Self-citationYang, Y., Song, S., Li, S., Kang, J., Li, Y., Zhao, N., Ye, D., Qin, F., Du, Y., Sun, J., et al. (2024) · Cell Death and Disease · doi:10.1038/s41419-024-06656-z · Cited by 29
NFκB function and regulation in cutaneous T-cell lymphoma.
Chang, T., & Vancurova, I. (2013) · Europe PMC (PubMed Central) · Cited by 28
HDAC6-Selective Inhibitor Overcomes Bortezomib Resistance in Multiple Myeloma
Lee, S. W., Yeon, S.-K., Kim, G. W., Lee, D. H., Jeon, Y. H., Yoo, J. H., Kim, S. Y., & Kwon, S. H. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22031341 · Cited by 28
Kim, Y.-M., Cao, D., REED, W. A., Wu, W., Jaspers, I., Tal, T. L., Bromberg, P. A., & Samet, J. M. (2006) · Cellular Signalling · doi:10.1016/j.cellsig.2006.08.003 · Cited by 28
NAP1L1 regulates NF-κB signaling pathway acting on anti-apoptotic Mcl-1 gene expression
Tanaka, T., Hozumi, Y., Iino, M., & Goto, K. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2017.06.021 · Cited by 24
Spinal NF-kB upregulation contributes to hyperalgesia in a rat model of advanced osteoarthritis
Li, Y., Yang, Y., Guo, J., Guo, X., Feng, Z., & Zhao, X. (2020) · Molecular Pain · doi:10.1177/1744806920905691 · Cited by 27
Zhao, J., Jia, Y., Shen, S., Kim, J., Wang, X., Lee, E., Brownell, I., Cho‐Vega, J. H., Lewis, C. M., Homsi, J., et al. (2020) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-20-0587 · Cited by 30
IKKε modulates RSV-induced NF-κB-dependent gene transcription
Bao, X., Indukuri, H., Liu, T., Liao, S., Tian, B., Brasier, A. R., Garofalo, R. P., & Casola, A. (2010) · Virology · doi:10.1016/j.virol.2010.09.016 · Cited by 26
Park, B., Sung, B., Yadav, V. R., Chaturvedi, M. M., & Aggarwal, B. B. (2011) · Biochemical Pharmacology · doi:10.1016/j.bcp.2011.07.062 · Cited by 26
RetractedRole of dietary antioxidants in human metapneumovirus infection
Komaravelli, N., Kelley, J. P., Garofalo, M. P., Wu, H., Casola, A., & Kolli, D. (2015) · Virus Research · doi:10.1016/j.virusres.2015.01.018 · Cited by 26
Lee, I., Lee, S.-J., Kang, T. M., Kang, W. K., & Park, C. (2012) · Cancer Research · doi:10.1158/0008-5472.can-12-2498 · Cited by 26
Luo, X. M., He, Z., Sun, X., Gu, X., Zhang, W., Gao, J., Li, X., Jia, R., Wei, J., Yu, Y., et al. (2020) · Diabetes Metabolic Syndrome and Obesity · doi:10.2147/dmso.s232279 · Cited by 25
RAB7A Regulates Vimentin Phosphorylation through AKT and PAK
Romanò, R., Calcagnile, M., Margiotta, A., Franci, L., Chiariello, M., Alifano, P., & Bucci, C. (2021) · Cancers · doi:10.3390/cancers13092220 · Cited by 25
Aman, S., Li, Y., Cheng, Y., Yang, Y., Lv, L., Li, B., Xia, K., Li, S., & Wu, H. (2021) · Cell Death Discovery · doi:10.1038/s41420-021-00733-4 · Cited by 25
Basu, S., Pathak, S., Pathak, S. K., Bhattacharyya, A., Banerjee, A., Kundu, M., & Basu, J. (2007) · Cellular Microbiology · doi:10.1111/j.1462-5822.2007.00997.x · Cited by 25
Yang, W. S., Lee, J. M., Han, N. J., Kim, Y. J., Chang, J. W., & Park, S.-K. (2010) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2010.01.018 · Cited by 25
Effect of Iron Deficiency on a Murine Model of Smoke-induced Emphysema
Sato, K., Inoue, S., Igarashi, A., Tokairin, Y., Yamauchi, K., Kimura, T., Nishiwaki, M., Nemoto, T., Nakano, H., Sato, M., et al. (2019) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2018-0239oc · Cited by 25
Self-citationHe, T., Hong, S. Y., Huang, L., Xue, W., Yu, Z., Kwon, H., Kirk, M., Ding, S., Su, K., & Zhang, Z. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.176289 · Cited by 24
Anaphylatoxin C5a-induced toll-like receptor 4 signaling in bovine neutrophils
Stevens, M. G. H., Poucke, M. V., Peelman, L. J., Rainard, P., Spiegeleer, B. M. J. D., Rogiers, C., de Walle, G. R. V., Duchateau, L., & Burvenich, C. (2010) · Journal of Dairy Science · doi:10.3168/jds.2010-3358 · Cited by 24
Tuzcu, H., Ünal, B., Kıraç, E., Konuk, E., Özcan, F., Elpek, G. Ö., Demır, N., & Aslan, M. (2017) · Free Radical Research · doi:10.1080/10715762.2017.1298103 · Cited by 24
RelA is required for IL-1β stimulation of Matrix Metalloproteinase-1 expression in chondrocytes
Raymond, L., Eck, S., Hays, E., Tomek, I. M., Kantor, S., & Vincenti, M. (2006) · Osteoarthritis and Cartilage · doi:10.1016/j.joca.2006.09.011 · Cited by 24
Comprehensive lung injury pathology induced by mTOR inhibitors
Aparicio, G., Blanco, M., Médina, V., Fernández, O., Jiménez, P., Lema, M., Figueroa, A., & Aparicio, L. M. A. (2009) · Clinical & Translational Oncology · doi:10.1007/s12094-009-0394-y · Cited by 25
Zhang, J., Zhang, Y., Wang, J., Zhang, S.-S., Zhao, Y., Ren, H., Chu, Y., Feng, L., & Wang, C. (2019) · Experimental Cell Research · doi:10.1016/j.yexcr.2019.04.022 · Cited by 23
Choudhary, S., Rosenblatt, K. P., Fang, L., Tian, B., Wu, Z.-H., & Brasier, A. R. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.224923 · Cited by 23
Thr435 phosphorylation regulates RelA (p65) NF-κB subunit transactivation
O'Shea, J. M., & Perkins, N. D. (2009) · Biochemical Journal · doi:10.1042/bj20091630 · Cited by 24
Diamant, G., Bahat, A., & Dikstein, R. (2016) · Nature Communications · doi:10.1038/ncomms11547 · Cited by 23
O'Gorman, A., Colleran, A., Ryan, A. E., Mann, J., & Egan, L. J. (2010) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00460.2009 · Cited by 23
The NF-κB Nucleolar Stress Response Pathway
Thoms, H. C., & Stark, L. A. (2021) · Biomedicines · doi:10.3390/biomedicines9091082 · Cited by 24
Jeong, H., Shin, J. Y., Kim, M., Na, J., & Ju, B. (2018) · Journal of Investigative Dermatology · doi:10.1016/j.jid.2018.11.012 · Cited by 22
Martin, R., Sun, Y., MacKinnon, S., Cuccia, L., Pagé, V., Hébert, T. E., & Tanny, J. C. (2020) · Molecular and Cellular Biology · doi:10.1128/mcb.00048-20 · Cited by 22
Kim, J. K., Han, N. R., Park, S. M., Jegal, K. H., Jung, J. Y., Jung, E. H., Kim, E. O., Kim, D., Jung, D. H., Lee, J. R., et al. (2019) · Food and Chemical Toxicology · doi:10.1016/j.fct.2019.111044 · Cited by 22
Human Bocavirus NS1 and NS1-70 Proteins Inhibit TNF-α-Mediated Activation of NF-κB by targeting p65
Liu, Q., Zhang, Z., Zheng, Z., Zheng, C., Liu, Y., Hu, Q., Ke, X., & Wang, H. (2016) · Scientific Reports · doi:10.1038/srep28481 · Cited by 21
Han, X., Tang, J., Chen, T., & Ren, G. (2018) · Journal of Cellular Biochemistry · doi:10.1002/jcb.27455 · Cited by 21
Kim, Y., Kim, H., Ko, H., Amor, E. C., Lee, J. W., & Yang, H. O. (2011) · Food and Chemical Toxicology · doi:10.1016/j.fct.2011.11.050 · Cited by 21
Chang, P.-Y., & Miyamoto, S. (2006) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-05-0259 · Cited by 21
Metge, B. J., Liu, S., Riker, A. I., Fodstad, Ø., Samant, R. S., & Shevde, L. A. (2010) · Oncology · doi:10.1159/000292363 · Cited by 20
Agnati, L. F., Guidolin, D., Leo, G., Guescini, M., Pizzi, M., Stocchi, V., Spano, P., Ghidoni, R., Ciruela, F., Genedani, S., et al. (2011) · Journal of Receptors and Signal Transduction · doi:10.3109/10799893.2011.599393 · Cited by 20
Chuang, T., Rehan, A., & Khorram, O. (2020) · Fertility and Sterility · doi:10.1016/j.fertnstert.2019.12.002 · Cited by 20
Gupta, A., Brooks, C., & Storey, K. B. (2020) · Cryobiology · doi:10.1016/j.cryobiol.2020.10.012 · Cited by 19
Hypo‐phosphorylation leads to nuclear retention of NF‐κB p65 due to impaired IκBα gene synthesis
Hochrainer, K., Racchumi, G., & Anrather, J. (2007) · FEBS Letters · doi:10.1016/j.febslet.2007.10.056 · Cited by 20
Horion, J., Gloire, G., Mjiyad, N. E., Quivy, V., Vermeulen, L., Berghe, W. V., Haegeman, G., Lint, C. M. V., Piette, J. G., & Habraken, Y. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m609166200 · Cited by 20
Hermida‐Prado, F., Xie, Y., Sherman, S., Nagy, Z., Russo, D., Akhshi, T. K., Chu, Z., Feit, A. S., Campisi, M., Chen, M., et al. (2023) · Cancer Research · doi:10.1158/0008-5472.can-23-1711 · Cited by 19
Transitional B Cells Exhibit a B Cell Receptor-Specific Nuclear Defect in Gene Transcription
Andrews, S. F., & Rawlings, D. J. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0802368 · Cited by 19
Furrer, A., Hottiger, M. O., & Valaperti, A. (2016) · Molecular Immunology · doi:10.1016/j.molimm.2016.04.009 · Cited by 19
Effects of diesel exhaust particles on the condition of mouse ocular surface
Yang, Q., Tang, L., Shen, M., Wang, Y., Wei, Y. L., Jeyalatha, M. V., Chen, P., Dong, F., Wang, G., Wu, S.-P., et al. (2018) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2018.07.101 · Cited by 19
Nuclear Translocation of p65 is Controlled by Sec6 via the Degradation of IκBα
Tanaka, T., & Iino, M. (2015) · Journal of Cellular Physiology · doi:10.1002/jcp.25122 · Cited by 20
He, Z., Zhao, J., Zhang, J., Jung, J. U., & Feng, P. (2013) · Journal of Virology · doi:10.1128/jvi.01716-13 · Cited by 19
Buensuceso, A. V., Fritz, J. L., Collins, O. M., Valdés, Y. R., Borrelli, M. J., DiMattia, G. E., & Shepherd, T. G. (2022) · Scientific Reports · doi:10.1038/s41598-022-06796-2 · Cited by 18
Caveolin-1 suppresses Human Immunodeficiency virus-1 replication by inhibiting acetylation of NF-κB
Simmons, G. E., Jr., Taylor, H. E., & Hildreth, J. E. K. (2012) · Virology · doi:10.1016/j.virol.2012.05.016 · Cited by 18
Chakraborty, S., Islam, S., Saha, S., & Ain, R. (2018) · Scientific Reports · doi:10.1038/s41598-018-26590-3 · Cited by 18
The development of immune-modulating compounds to disrupt HIV latency
Remoli, A. L., Marsili, G., Battistini, A., & Sgarbanti, M. (2012) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2012.05.003 · Cited by 18
Metadata
- Authors
- Chen, L.-F., Williams, S. A., Mu, Y., Nakano, H., Duerr, J. M., Buckbinder, L., & Greene, W. C.
- Affiliations
- Gladstone Institutes (US)
- Juntendo University (JP)
- Pfizer (United States) (US)
- Corresponding author
- Chen, Lin-Feng
- Greene, Warner C.
- Venue
- Molecular and Cellular Biology
- Publisher
- Informa UK Limited
- Published
- 2005-09-01
- Volume
- 25
- Issue
- 18
- Pages
- 7966-7975
- ISSN
- 0270-7306 (ISSN-L)
- 1098-5549
- PMC
- PMC1234328
- OpenAlex
- W2117817795
- Cited by
- 438
- References
- 36
- Citations by year
- 2026: 10 · 2025: 8 · 2024: 13 · 2023: 12 · 2022: 11 · 2021: 24 · 2020: 25 · 2019: 14 · 2018: 24 · 2017: 22 · 2016: 19 · 2015: 15 · 2014: 25 · 2013: 29 · 2012: 34
- FWCI
- 7.32
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Molecular and Cellular Biology (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Foundation for the National Institutes of Health
- Arthritis Foundation
- Pfizer
- Gladstone Institutes
- Center for AIDS Research, University of Washington
- University of California, San Francisco
- National Institute of Mental Health (P30MH059037, P30-MH 59037)
- National Cancer Institute (R01CA089001, R01 CA89001-02)
- National Institute of Allergy and Infectious Diseases (AI07305)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › NF-κB Signaling Pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Signaling Pathways in Disease
- Keywords
- p65 phosphorylation, P300, protein kinase A, TNF-α, E-selectin, transcriptional activity, post-translational modification, embryonic fibroblasts
- MeSH terms
- Acetylation, Animals, Cells, Cultured, Humans, Lysine, Mutation, Nuclear Proteins, Phosphorylation, Serine, Transcription, Genetic, Trans-Activators, NF-kappa B, E1A-Associated p300 Protein, Mice, Transcription Factor RelA
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