The DOI matches its Crossref record; 81 of the 81 references it cites were found in a registry or an index.
A diverse family of proteins containing tumor necrosis factor receptor-associated factor domains.
Open accessAbstract
We have identified three new tumor necrosis factor-receptor associated factor (TRAF) domain-containing proteins in humans using bioinformatics approaches, including: MUL, the product of the causative gene in Mulibrey Nanism syndrome; USP7 (HAUSP), an ubiquitin protease; and SPOP, a POZ domain-containing protein. Unlike classical TRAF family proteins involved in TNF family receptor (TNFR) signaling, the TRAF domains (TDs) of MUL, USP7, and SPOP are located near the NH(2) termini or central region of these proteins, rather than carboxyl end. MUL and USP7 are capable of binding in vitro via their TDs to all of the previously identified TRAF family proteins (TRAF1, TRAF2, TRAF3, TRAF4, TRAF5, and TRAF6), whereas the TD of SPOP interacts weakly with TRAF1 and TRAF6 only. The TD of MUL also interacted with itself, whereas the TDs of USP7 and SPOP did not self-associate. Analysis of various MUL and USP7 mutants by transient transfection assays indicated that the TDs of these proteins are necessary and sufficient for suppressing NF-kappaB induction by TRAF2 and TRAF6 as well as certain TRAF-binding TNF family receptors. In contrast, the TD of SPOP did not inhibit NF-kappaB induction. Immunofluorescence confocal microscopy indicated that MUL localizes to cytosolic bodies, with targeting to these structures mediated by a RBCC tripartite domain within the MUL protein. USP7 localized predominantly to the nucleus, in a TD-dependent manner. Data base searches revealed multiple proteins containing TDs homologous to those found in MUL, USP7, and SPOP throughout eukaryotes, including yeast, protists, plants, invertebrates, and mammals, suggesting that this branch of the TD family arose from an ancient gene. We propose the moniker TEFs (TD-encompassing factors) for this large family of proteins.
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
“Thus, truncation of amino acids 1–207 abolishes its ability to enter the nucleus.”
From USP7 Is a Master Regulator of Genome Stability (2020) · cites this paper as Zapata et al., 2001
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
1 retracted
Ansieau, S., Scheffrahn, I., Mosialos, G., Brand, H. E., Duyster, J., Kaye, K. M., Harada, J. N., Dougall, B., Hübinger, G., Kieff, E. D., et al. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.24.14053 · Cited by 75
RetractedGapped BLAST and PSI-BLAST: a new generation of protein database search programs
Altschul, S. (1997) · Nucleic Acids Research · doi:10.1093/nar/25.17.3389 · Cited by 73,302
Comparative Protein Modelling by Satisfaction of Spatial Restraints
Šali, A., & Blundell, T. L. (1993) · Journal of Molecular Biology · doi:10.1006/jmbi.1993.1626 · Cited by 12,977
Analysis of the genome sequence of the flowering plant Arabidopsis thaliana
Initiative, T. A. G. (2000) · Nature · doi:10.1038/35048692 · Cited by 9,301
Phosphorylation meets ubiquitination: the control of NF-κB activity
Karin, M., & Ben-Neriah, Y. (2000) · Annual Review of Immunology · doi:10.1146/annurev.immunol.18.1.621 · Cited by 4,766
Tumor suppressor p53 is a direct transcriptional activator of the human bax gene
Toshiyuki, M., & Reed, J. C. (1995) · Cell · doi:10.1016/0092-8674(95)90412-3 · Cited by 4,063
Self-citationBeighton, P., & Beighton, G. (1997) · Springer eBooks · doi:10.1007/978-1-4471-0925-9_118 · Cited by 3,165
Deng, L., Wang, C., Spencer, E., Yang, L., Braun, A., You, J., Slaughter, C., Pickart, C., & Chen, Z. J. (2000) · Cell · doi:10.1016/s0092-8674(00)00126-4 · Cited by 1,872
A novel form of Epstein-Barr virus latency in normal B cells in vivo
Miyashita, E. M., Yang, B., Lam, K. M. C., Crawford, D., & Thorley‐Lawson, D. A. (1995) · Cell · doi:10.1016/0092-8674(95)90513-8 · Cited by 1,591
TRAF6 is a signal transducer for interleukin-1
Cao, Z., Xiong, J., Takeuchi, M., Kurama, T., & Goeddel, D. V. (1996) · Nature · doi:10.1038/383443a0 · Cited by 1,305
Flagged first, then by citations
Research works printed but not linked: 6
- Uren, 1996, Trends Biochem. Sci., 21, 244
- Galang, 1994, Oncogene, 9, 2913
- Krajewska, 1998, Am. J. Pathol., 152, 1549
- Jin, 1997, Cancer Res., 57, 404
- Albagli, 1995, Oncogene, 6, 1193
- Holt, 1999, Curr. Biol., 2000, R5
Cited by
Sorted by citations
Items 101–200 of 227
Vugmeyster, Y., Borodovsky, A., Maurice, M. M., Maehr, R., Furman, M. H., & Ploegh, H. L. (2002) · Molecular Immunology · doi:10.1016/s0161-5890(02)00123-2 · Cited by 36
MacroH2A1.2 binds the nuclear protein Spop
Takahashi, I., Kameoka, Y., & Hashimoto, K. (2002) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/s0167-4889(02)00249-5 · Cited by 36
Impacts of cadmium on male fertility: Lessons learnt so far
Joseph, I. E., Oyagbemi, A. A., & Oyeyemi, M. O. (2022) · Andrologia · doi:10.1111/and.14516 · Cited by 32
Huang, S., Hsu, P., Chen, M., Li, W., More, S. V., Lu, K., & Wang, Y. (2011) · International Journal of Cancer · doi:10.1002/ijc.26401 · Cited by 31
Deubiquitinase USP7 contributes to the pathogenicity of spinal and bulbar muscular atrophy
Pluciennik, A., Liu, Y., Molotsky, E., Marsh, G. B., Ranxhi, B., Arnold, F. J., St.-Cyr, S., Davidson, B. L., Pourshafie, N., Lieberman, A. P., et al. (2020) · Journal of Clinical Investigation · doi:10.1172/jci134565 · Cited by 30
Jian-yin, M., Huang, F., Lin, H., & Wang, X. (2013) · Marine Drugs · doi:10.3390/md11010266 · Cited by 29
Li, H., Zhang, X., Qiu, Q., An, Z., Qi, Y., Huang, D., & Zhang, Y. (2013) · Aquatic Toxicology · doi:10.1016/j.aquatox.2013.05.015 · Cited by 28
Chao, C., Hou, S., Huang, C., Hou, C., Chen, P., & Liu, J. (2017) · Molecular Medicine Reports · doi:10.3892/mmr.2017.7222 · Cited by 28
Critical review of Epstein–Barr virus microRNAs relation with EBV‐associated gastric cancer
Zebardast, A., Tehrani, S. S., Latifi, T., & Sadeghi, F. (2021) · Journal of Cellular Physiology · doi:10.1002/jcp.30297 · Cited by 27
Intersubunit and Domain Interactions of the Meprin B Metalloproteinase
Ishmael, F. T., Shier, V. K., Ishmael, S. S., & Bond, J. S. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m414218200 · Cited by 27
Huang, C.-J., Chen, C.-Y., Chen, H.-H., Tsai, S., & Choo, K. (2003) · Gene · doi:10.1016/j.gene.2003.09.022 · Cited by 27
Structural and evolutionary insights into astacin metallopeptidases
Gomis‐Rüth, F. X., & Stöcker, W. (2023) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.1080836 · Cited by 26
Wilms’ tumor and novel TRIM37 mutations in an Australian patient with mulibrey nanism
Hämäläinen, R. H., Mowat, D. R., Gabbett, M. T., O’Brien, T., Kallijärvi, J., & Lehesjoki, A. (2006) · Clinical Genetics · doi:10.1111/j.1399-0004.2006.00700.x · Cited by 26
Daxx-mediated transcriptional repression of MMP1 gene is reversed by SPOP
La, M., Kim, K., Park, J., Won, J., Lee, J., Fu, Y., Meadows, G. G., & Joe, C. O. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.06.022 · Cited by 26
Jagiello, P., Hammans, C., Wieczorek, S., Arning, L., Stefanski, A., Strehl, H., Epplen, J. T., & Genčík, M. (2003) · Human Mutation · doi:10.1002/humu.10220 · Cited by 25
Wang, M., Ma, H., Cheng, T., Liu, S., Ye, X., Zhou, D., Li, Y., Hui, N., & Li, X. (2017) · Journal of Functional Foods · doi:10.1016/j.jff.2017.05.049 · Cited by 24
Yoon, J. H., Cho, Y., & Park, H. H. (2013) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s139900471302333x · Cited by 24
Analogies Between Drosophila and Mammalian TRAF Pathways
Wajant, H., & Scheurich, P. (2003) · Progress in molecular and subcellular biology · doi:10.1007/978-3-642-18670-7_3 · Cited by 24
Li, Z., Yu, Y., Wang, M., Xu, H., Han, B., Jiang, P., Ma, H., Li, Y., Cheng, T., Zhou, D., et al. (2019) · Scientific Reports · doi:10.1038/s41598-018-29099-x · Cited by 23
Kallijärvi, J., Hämäläinen, R. H., Karlberg, N., Sainio, K., & Lehesjoki, A. (2006) · Histochemistry and Cell Biology · doi:10.1007/s00418-006-0162-9 · Cited by 23
De Novo Variants in SPOP Cause Two Clinically Distinct Neurodevelopmental Disorders
Sá, M. J. N., Tekle, G. E., de Brouwer, A. P. M., Sawyer, S. L., del Gaudio, D., Parker, M. J., Kanani, F., van den Boogaard, M. H., van Gassen, K. L. I., Allen, M. I. V., et al. (2020) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2020.02.001 · Cited by 23
Identification of candidate lung cancer susceptibility genes in mouse using oligonucleotide arrays
Lemon, W. J., Bernert, H., Sun, H., Wang, Y., & You, M. (2002) · Journal of Medical Genetics · doi:10.1136/jmg.39.9.644 · Cited by 22
Kaewkod, T., Sangboonruang, S., Khacha-ananda, S., Charoenrak, S., Bovonsombut, S., & Tragoolpua, Y. (2022) · Food Science and Technology · doi:10.1590/fst.107521 · Cited by 21
Luo, Y., Li, X., Huang, X., Wong, Y., Chen, T., Zhang, Y., & Zheng, W. (2011) · Chemical and Pharmaceutical Bulletin · doi:10.1248/cpb.59.1227 · Cited by 21
Structural Revelations of TRAF2 Function in TNF Receptor Signaling Pathway
Chung, J. Y., Lu, M., Yin, Q., & Wu, H. (2007) · Springer eBooks · doi:10.1007/978-0-387-70630-6_8 · Cited by 21
Bellows, M. L., & Floudas, C. A. (2010) · Current Drug Targets · doi:10.2174/138945010790711914 · Cited by 20
Anti-HIV-1 activity of Trim 37
Tabah, A. A., Tardif, K. D., & Mansky, L. M. (2013) · Journal of General Virology · doi:10.1099/vir.0.057653-0 · Cited by 19
TRAF4, at the Crossroad between Morphogenesis and Cancer
Rousseau, A., Rio, M., & Alpy, F. (2011) · Cancers · doi:10.3390/cancers3022734 · Cited by 19
Recognition of TRAIP with TRAFs: Current understanding and associated diseases
Sajjad, N., Mir, R., Khan, J., Rather, I. A., & Bhat, E. A. (2019) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2019.105589 · Cited by 18
Xiang, Q., Ju, H., & Nicholas, J. (2019) · Journal of Virology · doi:10.1128/jvi.01553-19 · Cited by 18
Peluffo, M. C., Young, K. A., Hennebold, J. D., & Stouffer, R. L. (2008) · Molecular Reproduction and Development · doi:10.1002/mrd.20970 · Cited by 18
BTB/POZ domain of speckle‐type POZ protein (SPOP) confers proapoptotic function in HeLa cells
Byun, B., Tak, H., & Joe, C. O. (2007) · BioFactors · doi:10.1002/biof.5520310303 · Cited by 18
Gao, J., Chen, S., Zhang, L., Cheng, B., Xu, A., Wu, L., & Zhang, X. (2014) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf505079v · Cited by 18
Apoptosis and Male Infertility
Latchoumycandane, C., Vaithinathan, S., D’Cruz, S. C., & Mathur, P. P. (2020) · Springer eBooks · doi:10.1007/978-3-030-32300-4_37 · Cited by 18
Induction of cell apoptosis in non‐small cell lung cancer cells by cyclin A1 small interfering RNA
Cho, N. H., Choi, Y. P., Moon, D. S., Kim, H., Kang, S., Ding, O., Rha, S. Y., Yang, Y. J., & Cho, S.-H. (2006) · Cancer Science · doi:10.1111/j.1349-7006.2006.00292.x · Cited by 17
Lee, Y., Cui, J., Lee, J. H., Han, A., Lee, E. Y., Jang, H. H., & Seo, E. K. (2016) · Molecules · doi:10.3390/molecules21010120 · Cited by 16
Gao, X., Yu, B., Yu, J., Mao, X., Huang, Z., Luo, Y., Luo, J., Zheng, P., He, J., & Chen, D. (2020) · Food & Function · doi:10.1039/c9fo02652e · Cited by 15
Regulators of apoptosis as anticancer targets
Tolcher, A. W. (2002) · Hematology/Oncology Clinics of North America · doi:10.1016/s0889-8588(02)00046-1 · Cited by 16
Friend or foe? Reciprocal regulation between E3 ubiquitin ligases and deubiquitinases
Bolhuis, D. L., Emanuele, M. J., & Brown, N. G. (2024) · Biochemical Society Transactions · doi:10.1042/bst20230454 · Cited by 15
QNZ alleviated hepatocellular carcinoma by targeting inflammatory pathways in a rat model
Al-Gayyar, M. M. H., Alattar, A., Alshaman, R., & Hamdan, A. M. (2021) · Cytokine · doi:10.1016/j.cyto.2021.155710 · Cited by 15
Albarbar, B., Dunnill, C., & Georgopoulos, N. T. (2015) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2015.05.001 · Cited by 15
Phylogenetic Analysis of Brassica rapa MATH-Domain Proteins
Zhao, L., Huang, Y., Hu, Y., He, X., Shen, W., Liu, C., & Ruan, Y. (2013) · Current Genomics · doi:10.2174/1389202911314030007 · Cited by 15
Nowar, R., Osman, E. E. A., Abou‐Seri, S. M., Moghazy, S. M. E., & Ella, D. A. A. E. (2018) · Future Medicinal Chemistry · doi:10.4155/fmc-2017-0284 · Cited by 15
Taherzadeh-Soureshjani, P., & Chehelgerdi, M. (2020) · Cancer Nanotechnology · doi:10.1186/s12645-020-00066-4 · Cited by 14
Ubiquitin Ligases in Malignant Lymphoma
Lim, M. S., & Elenitoba‐Johnson, K. S. J. (2004) · Leukemia & lymphoma/Leukemia and lymphoma · doi:10.1080/10428190410001663635 · Cited by 14
Lee, G., Lim, H., Seo, J., Kang, K., Kim, D. K., You, J., Oh, J.-S., Seo, Y.-S., & Kim, J. (2022) · Translational Cancer Research · doi:10.21037/tcr-21-2410 · Cited by 11
Novel insights into the impact of the SUMOylation pathway in hematological malignancies (Review)
Wang, L., Qian, J., Yang, Y., & Gu, C. (2021) · International Journal of Oncology · doi:10.3892/ijo.2021.5253 · Cited by 11
Barbeito, P., Martin-Morales, R., Palencia‐Campos, A., Cerrolaza, J., Rivas-Santos, C., Gallego-Colastra, L., Caparros-Martin, J. A., Martin-Bravo, C., Martín-Hurtado, A., Sánchez-Bellver, L., et al. (2023) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2023.1190258 · Cited by 10
Zheng, X., Xu, Y., Liu, B., Yan, Q., Zhang, Y., Li, X., Zhang, X., Pu, X.-J., Li, S., Chen, Z., et al. (2019) · Evidence-based Complementary and Alternative Medicine · doi:10.1155/2019/9076269 · Cited by 10
Thi, T., Yeh, C., Wu, G., Hsu, C., Chang, H., & Chen, H. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23031176 · Cited by 9
Boddin, J., Ip, W.-H., Wilkens, B., von Stromberg, K., Ching, W., Koyuncu, E., Bertzbach, L. D., & Dobner, T. (2022) · mBio · doi:10.1128/mbio.00144-22 · Cited by 10
Guan, F., Wang, Q., Wang, M., Yu, S., Chen, Y., Yin, M., Zhao, Y., Xu, F., Liu, F., & Zhang, J. (2015) · Molecules · doi:10.3390/molecules20046419 · Cited by 10
Apoptosis and Male Infertility
Vaithinathan, S., D’Cruz, S. C., & Mathur, P. P. (2012) · Springer eBooks · doi:10.1007/978-1-4614-3335-4_31 · Cited by 9
Integrative “Omic” Analysis for Tamoxifen Sensitivity through Cell Based Models
Weng, L., Ziliak, D. M., LaCroix, B. L., Geeleher, P., & Huang, R. S. (2014) · PLoS ONE · doi:10.1371/journal.pone.0093420 · Cited by 9
Astacins: Proteases in Development and Tissue Differentiation
Stöcker, W., & Gomis‐Rüth, F. X. (2013) · Springer eBooks · doi:10.1007/978-3-7091-0885-7_7 · Cited by 8
Joseph, T. P., Chanda, W., Mohammad, A., Kanwal, S., Batool, S., Zhang, M., Zhong, M., & Huang, M. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18112407 · Cited by 8
Abd‐Allah, W. H., Salman, A., & Saad, S. S. (2019) · Drug Development Research · doi:10.1002/ddr.21573 · Cited by 8
Comparison of Target Recognition by TRAF1 and TRAF2
Kim, C. M., & Park, H. H. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21082895 · Cited by 8
TRAF-like Proteins Regulate Cellular Survival in the Planarian Schmidtea mediterranea
Ziman, B., Barghouth, P. G., Maciel, E. I., & Oviedo, N. J. (2020) · iScience · doi:10.1016/j.isci.2020.101665 · Cited by 9
(2006) · The Internet Journal of Pharmacology · doi:10.5580/16c · Cited by 8
Role of PrPc Related to Apoptosis
Fan, D., Ge, F. L., Guo, X., Ji, Q., Liang, J., Li, T. T., Liu, Z., Lu, Y., Wang, J. Z. Y., Yao, L., et al. (2006) · Technische Universität Dortmund Eldorado (Technische Universität Dortmund) · doi:10.17877/de290r-8288 · Cited by 8
Masperone, L., Codrich, M., Persichetti, F., Gustincich, S., Zucchelli, S., & Legname, G. (2022) · Molecular Neurobiology · doi:10.1007/s12035-021-02666-6 · Cited by 7
Curcumin induce apoptosis of CNE-2z cells via caspase-dependent mitochondrial intrinsic pathway
Wu, Q. (2011) · African Journal of Pharmacy and Pharmacology · doi:10.5897/ajpp10.221 · Cited by 7
The Vital Phenomena of Apoptosis: A Review
Agrawal, S. N. (2019) · South Asian Research Journal of Medical Sciences · doi:10.36346/sarjms.2019.v01i01.004 · Cited by 7
Mulibrey Nanism - a Novel Peroxisomal Disorder
Kallijärvi, J., Lehesjoki, A., & Lipsanen‐Nyman, M. (2003) · Advances in experimental medicine and biology · doi:10.1007/978-1-4419-9072-3_3 · Cited by 7
Dubble or Nothing? Is HAUSP Deubiquitylating Enzyme the Final Arbiter of p53 Levels?
Wood, S. A. (2002) · Science s STKE · doi:10.1126/stke.2002.143.pe34 · Cited by 7
USP7 at the Crossroads of Ubiquitin Signaling, Cell Cycle, and Tumorigenesis
Lusardi, M., Rapetti, F., Spallarossa, A., Massone, M., Cichero, E., & Brullo, C. (2025) · Molecules · doi:10.3390/molecules30204038 · Cited by 6
Song, X., Hu, R., Chen, Y., Xiao, M., Zhang, H., Wu, S., & Lü, Q. (2024) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjad083 · Cited by 6
Wang, M., Zhang, Z., Zhang, Z., Vikis, H. G., Yan, Y., Wang, Y., & You, M. (2007) · Cancer Research · doi:10.1158/0008-5472.can-06-3157 · Cited by 6
Cartilage polysaccharide induces apoptotic cell death of L1210 cells
Liu, A., Yang, N., Song, W., Cao, D., & Wang, W. (2009) · Leukemia & lymphoma/Leukemia and lymphoma · doi:10.1080/10428190902893827 · Cited by 5
Bertenshaw, G. P., & Bond, J. S. (2004) · Handbook of Proteolytic Enzymes · doi:10.1016/b978-0-12-079611-3.50167-1 · Cited by 5
Meng, Z., Wang, Y., Kong, X., Cen, M., & Duan, Z. (2024) · Poultry Science · doi:10.1016/j.psj.2024.103461 · Cited by 4
Zhu, W., Li, G., Shi, H., Ruan, Y., & Liu, C. (2024) · Plants · doi:10.3390/plants13233402 · Cited by 4
Mulibrey nanism and immunological complications: a comprehensive case report and literature review
Gazzin, A., Pala, F., Bosticardo, M., Niemela, J. E., Stoddard, J. L., Biasin, E., Quarello, P., Carli, D., Ferroni, F., Delmonte, O. M., et al. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1303251 · Cited by 4
TRAF1 from a Structural Perspective
Jang, H., Kim, S., Kim, D. Y., Han, J. H., & Park, H. H. (2024) · Biomolecules · doi:10.3390/biom14050510 · Cited by 4
Choo, K., Hsu, M., Chong, K., & Huang, C.-J. (2006) · Gene · doi:10.1016/j.gene.2006.08.031 · Cited by 4
Mita, A. C., Mita, M. M., & Rowinsky, E. K. (2004) · Clinical Colorectal Cancer · doi:10.3816/ccc.2004.n.014 · Cited by 4
Prasad, S. B. (2022) · Elsevier eBooks · doi:10.1016/b978-0-323-99883-3.00015-9 · Cited by 3
Tharanga, E. M. T., Nadarajapillai, K., Warnakula, W. A. D. L. R., Kim, G., Lim, C., Yang, H., Jayasinghe, J. D. H. E., Jeyakanesh, J. T., Sirisena, D. M. K. P., Arachchi, U. P. E., et al. (2024) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2024.110089 · Cited by 3
Anand, H., Misro, M. M., Sharma, S. B., & Prakash, S. (2012) · APOPTOSIS · doi:10.1007/s10495-012-0749-7 · Cited by 3
Fraser, B., Maranchuk, R. A., & Foley, E. (2014) · Frontiers in Immunology · doi:10.3389/fimmu.2014.00322 · Cited by 3
Dubble or Nothing? Is HAUSP Deubiquitylating Enzyme the Final Arbiter of p53 Levels?
Wood, S. A. (2002) · Science Signaling · doi:10.1126/scisignal.1432002pe34 · Cited by 3
Apoptosis and Male Infertility
Vaithinathan, S., D’Cruz, S. C., & Mathur, P. P. (2013) · Springer eBooks · doi:10.1007/978-1-4614-9158-3_12 · Cited by 3
RING Fingers and Relatives: Determinators of Protein Fate
Lorick, K. L., Tsai, Y. C., Yang, Y., & Weissman, A. M. (2007) · Wiley eBooks · doi:10.1002/9783527619320.ch4 · Cited by 3
Recent Progress of Ubiquitin-Specific-Processing Protease 7 Inhibitors
Chi, L., Wang, H., Yu, F., Gao, C., Dai, H., Si, X., Liu, L., Wang, Z., Zheng, J.-H., Ke, Y., et al. (2023) · Russian Journal of Bioorganic Chemistry · doi:10.1134/s1068162023020073 · Cited by 2
Ubiquitin-Specific Protease USP7
Faesen, A. C., Sixma, T. K., & Everett, R. D. (2012) · Elsevier eBooks · doi:10.1016/b978-0-12-382219-2.00463-4 · Cited by 2
Ardecky, R., Madiraj, C., Matsuzawa, S., Zou, J., Ganji, S., Pass, I., Ngo, T. A., Pinkerton, A. B., Sergienko, E. A., Su, Y., et al. (2014) · Cited by 2
Self-citationBajak, E. (2005) · Figshare · Cited by 2
Zapata, J. M., & Reed, J. C. (2002) · Science Signaling · doi:10.1126/scisignal.1332002pe27 · Cited by 2
Self-citationCritical review and future perspectives on the anticancer effects of Stephania tetrandra S. Moore
He, J., Liu, Y., Jiang, Y., & Hou, X. (2025) · Phytochemistry Reviews · doi:10.1007/s11101-025-10095-9 · Cited by 1
Not only as a Cullin3 ligase adaptor, SPOP may also act as a molecular bridge
Ge, Y., Kong, L., Li, Y., & Jin, X. (2026) · Genes & Diseases · doi:10.1016/j.gendis.2026.102189 · Cited by 1
Over-expressed Fas improves the apoptosis of malignant T-cells in vitro and vivo
Li, L., Zhang, R., Chen, Z., Xue, S., Wang, X., & Ruan, C. (2011) · Molecular Biology Reports · doi:10.1007/s11033-011-0689-2 · Cited by 1
Karlberg, N. (2009) · Cited by 1
Marine Compounds and Cancer 2017
Honecker, F. U., & Dyshlovoy, S. A. (2018) · MDPI eBooks · doi:10.3390/books978-3-03842-766-7 · Cited by 1
Al-Eidan, A. A., Draper, B., Wang, S., Coke, B., Skipp, P. J. S., Wang, Y., & Ewing, R. M. (2024) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2024.100878 · Cited by 1
Rowinsky, E. K. (2007) · Springer eBooks · doi:10.1007/978-3-540-28266-2_35 · Cited by 1
Régnier, C. H. (2007) · AfCS-Nature Molecule Pages · doi:10.1038/mp.a002310.01 · Cited by 1
Biochemical and Cell Biological Studies of TRIM37 Defective in Mulibrey Nanism
Kallijärvi, J. (2006) · Työväentutkimus Vuosikirja
Mulibrey nanism: Characterization of hypogonadism, infertility and tumors
Karlberg, S. (2012) · Työväentutkimus Vuosikirja
Metadata
- Authors
- Zapata, J. M., Pawlowski, K., Haas, E., Ware, C. F., Godzik, A., & Reed, J. C.
- Affiliations
- Sanford Burnham Prebys Medical Discovery Institute (US)
- La Jolla Institute for Immunology (US)
- Corresponding author
- Reed, John C.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2001-06
- Volume
- 276
- Issue
- 26
- Pages
- 24242-24252
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1967642652
- Cited by
- 228
- References
- 80
- Citations by year
- 2026: 2 · 2025: 5 · 2024: 7 · 2023: 4 · 2022: 8 · 2021: 4 · 2020: 11 · 2019: 8 · 2018: 9 · 2017: 7 · 2016: 6 · 2015: 5 · 2014: 6 · 2013: 16 · 2012: 13
- FWCI
- 5.29
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- AstraZeneca
- Deutsche Forschungsgemeinschaft
- National Institutes of Health (CA-69381)
- National Cancer Institute (CA 69381, P01CA069381)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › NF-κB Signaling Pathways
- Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
- Life Sciences › Immunology and Microbiology › Immunology › Cytokine Signaling Pathways and Interactions
- Keywords
- TRAF domain, TRAF, USP7, SPOP, POZ domain, TRAF2, TRAF6, TRAF1, TRAF4, TRAF5, NF-κB signaling, protein-protein interaction, protein localization
- MeSH terms
- Tripartite Motif Proteins, Ubiquitin-Specific Peptidase 7, Amino Acid Sequence, Animals, Cytosol, Humans, Molecular Sequence Data, Nuclear Proteins, Endopeptidases, Phylogeny, Proteins, Repressor Proteins, NF-kappa B, Sequence Homology, Amino Acid, Protein Structure, Tertiary, Receptors, Tumor Necrosis Factor, Evolution, Molecular, Jurkat Cells, Computational Biology, Ubiquitin Thiolesterase, Ubiquitin-Protein Ligases, TNF Receptor-Associated Factor 1
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