A diverse family of proteins containing tumor necrosis factor receptor-associated factor domains.
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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.
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Truncation of amino acids 1-207 of USP7 abolishes its ability to enter the nucleus.
“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
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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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
Self-citationBeighton, P., & Beighton, G. (1997) · Springer eBooks · doi:10.1007/978-1-4471-0925-9_118 · Cited by 3,165 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
TUMOR NECROSIS FACTOR RECEPTOR AND Fas SIGNALING MECHANISMS
Wallach, D., Varfolomeev, E. E., Malinin, N. L., Goltsev, Y. V., Kovalenko, A. V., & Boldin, M. (1999) · Annual Review of Immunology · doi:10.1146/annurev.immunol.17.1.331 · Cited by 1,299 · see citing works
TNF-Dependent Recruitment of the Protein Kinase RIP to the TNF Receptor-1 Signaling Complex
Hsu, H., Huang, J., Shu, H.-B., Baichwal, V., & Goeddel, D. V. (1996) · Immunity · doi:10.1016/s1074-7613(00)80252-6 · Cited by 1,182 · see citing works
Rothe, M., Wong, S. C., Henzel, W. J., & Goeddel, D. V. (1994) · Cell · doi:10.1016/0092-8674(94)90532-0 · Cited by 1,054 · see citing works
TRAF2-Mediated Activation of NF-κB by TNF Receptor 2 and CD40
Rothe, M., Sarma, V. J., Dixit, V. M., & Goeddel, D. V. (1995) · Science · doi:10.1126/science.7544915 · Cited by 1,050 · see citing works
ASK1 Is Essential for JNK/SAPK Activation by TRAF2
Nishitoh, H., Saitoh, M., Mochida, Y., Takeda, K., Nakano, H., Rothe, M., Miyazono, K., & Ichijo, H. (1998) · Molecular Cell · doi:10.1016/s1097-2765(00)80283-x · Cited by 647 · see citing works
Arch, R. H., Gedrich, R. W., & Thompson, C. B. (1998) · Genes & Development · doi:10.1101/gad.12.18.2821 · Cited by 611 · see citing works
Muzio, M., Natoli, G., Saccani, S., Levrero, M., & Mantovani, A. (1998) · The Journal of Experimental Medicine · doi:10.1084/jem.187.12.2097 · Cited by 573 · see citing works
Song, H. Y., Régnier, C. H., Kirschning, C. J., Goeddel, D. V., & Rothe, M. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.18.9792 · Cited by 554 · see citing works
Role of PML in Cell Growth and the Retinoic Acid Pathway
Wang, Z. G., Delva, L., Gaboli, M. P., Rivi, R., Giorgio, M., Cordon‐Cardo, C., Grosveld, F. G., & Pandolfi, P. P. (1998) · Science · doi:10.1126/science.279.5356.1547 · Cited by 516 · see citing works
Everett, R. D., Meredith, M., Orr, A., Cross, A., Kathoria, M., & Parkinson, J. (1997) · The EMBO Journal · doi:10.1093/emboj/16.7.1519 · Cited by 491 · see citing works
Devergne, O., Hatzivassiliou, E., Izumi, K. M., Kaye, K. M., Kleijnen, M. F., Kieff, E. D., & Mosialos, G. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.12.7098 · Cited by 491 · see citing works
Regulation of Translation in Eukaryotic Systems
Kozak, M. (1992) · Annual Review of Cell Biology · doi:10.1146/annurev.cb.08.110192.001213 · Cited by 467 · see citing works
Baud, V., Liu, Z.-G., Bennett, B. L., Suzuki, N., Xia, Y., & Karin, M. (1999) · Genes & Development · doi:10.1101/gad.13.10.1297 · Cited by 464 · see citing works
RIP2 Is a Novel NF-κB-activating and Cell Death-inducing Kinase
McCarthy, J. V., Ni, J., & Dixit, V. M. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.27.16968 · Cited by 438 · see citing works
The astacin family of metalloendopeptidases
Bond, J. S., & Beynon, R. J. (1995) · Protein Science · doi:10.1002/pro.5560040701 · Cited by 410 · see citing works
Everett, R. D., Freemont, P. S., Saitoh, H., Dasso, M., Orr, A., Kathoria, M., & Parkinson, J. (1998) · Journal of Virology · doi:10.1128/jvi.72.8.6581-6591.1998 · Cited by 399 · see citing works
Structural basis for self-association and receptor recognition of human TRAF2
Park, Y. C., Burkitt, V., Villa, A. R., Tong, L., & Wu, H. (1999) · Nature · doi:10.1038/19110 · Cited by 359 · see citing works
Chelbi‐Alix, M. K., & de Thé, H. (1999) · Oncogene · doi:10.1038/sj.onc.1202366 · Cited by 331 · see citing works
Identification of CARDIAK, a RIP-like kinase that associates with caspase-1
Thome, M., Hofmann, K., Burns, K., Martinon, F., Bodmer, J.-L., Mattmann, C., & Tschopp, J. (1998) · Current Biology · doi:10.1016/s0960-9822(07)00352-1 · Cited by 319 · see citing works
The BCL-6 POZ domain and other POZ domains interact with the co-repressors N-CoR and SMRT
Huynh, K. D., & Bardwell, V. J. (1998) · Oncogene · doi:10.1038/sj.onc.1202197 · Cited by 311 · see citing works
The Structural Basis for the Recognition of Diverse Receptor Sequences by TRAF2
Ye, H., Park, Y. C., Kreishman, M., Kieff, E. D., & Wu, H. (1999) · Molecular Cell · doi:10.1016/s1097-2765(00)80334-2 · Cited by 292 · see citing works
TANK, a co-inducer with TRAF2 of TNF- and CD 40L-mediated NF-kappaB activation.Preprint
Cheng, G., & Baltimore, D. (1996) · Genes & Development · doi:10.1101/gad.10.8.963 · Cited by 288 · see citing works
Pullen, S. S., Miller, H. G., Everdeen, D. S., Dang, T. T., Crute, J. J., & Kehry, M. R. (1998) · Biochemistry · doi:10.1021/bi981067q · Cited by 244 · see citing works
Localization of nascent RNA and CREB binding protein with the PML-containing nuclear body
LaMorte, V. J., Dyck, J. A., Ochs, R., & Evans, R. M. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.9.4991 · Cited by 239 · see citing works
Régnier, C. H., Tomasetto, C., Moog‐Lutz, C., Chenard, M., Wendling, C., Basset, P., & Rio, M. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.43.25715 · Cited by 228 · see citing works
RING fingers and B-boxes: zinc-binding protein-protein interaction domains
Borden, K. L. B. (1998) · Biochemistry and Cell Biology · doi:10.1139/bcb-76-2-3-351 · Cited by 228 · see citing works
RING fingers and B-boxes: zinc-binding protein-protein interaction domains
Borden, K. L. B. (1998) · Biochemistry and Cell Biology · doi:10.1139/o98-021 · Cited by 214 · see citing works
I-TRAF is a novel TRAF-interacting protein that regulates TRAF-mediated signal transduction.
Rothe, M., Xiong, J., Shu, H., Williamson, K., Goddard, A. D., & Goeddel, D. V. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.16.8241 · Cited by 212 · see citing works
Crystallographic analysis of CD40 recognition and signaling by human TRAF2
McWhirter, S. M., Pullen, S. S., Holton, J. M., Crute, J. J., Kehry, M. R., & Alber, T. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.15.8408 · Cited by 195 · see citing works
TRAF Family Proteins Interact with the Common Neurotrophin Receptor and Modulate Apoptosis Induction
Ye, X., Mehlen, P., Rabizadeh, S., VanArsdale, T. L., Zhang, H., Shin, H., Wang, J. J. ‐., Leo, E., Zapata, J. M., Hauser, C. A., et al. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.42.30202 · Cited by 190 · see citing works
Self-citationGene encoding a new RING-B-box-Coiled-coil protein is mutated in mulibrey nanism
Avela, K., Lipsanen‐Nyman, M., Idänheimo, N., Seemanová, E., Rosengren, S. S., Mäkelä, T. P., Perheentupa, J., de la Chapelle, A., & Lehesjoki, A. (2000) · Nature Genetics · doi:10.1038/77053 · Cited by 189 · see citing works
Park, Y. C., Ye, H., Hsia, C. Y., Segal, D., Rich, R. L., Liou, H.-C., Myszka, D. G., & Wu, H. (2000) · Cell · doi:10.1016/s0092-8674(00)80889-2 · Cited by 188 · see citing works
CD40 Signaling through Tumor Necrosis Factor Receptor-associated Factors (TRAFs)
Pullen, S. S., Dang, T. T., Crute, J. J., & Kehry, M. R. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.20.14246 · Cited by 186 · see citing works
Gedrich, R. W., Gilfillan, M. C., Duckett, C. S., Dongen, J. L. V., & Thompson, C. B. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.22.12852 · Cited by 172 · see citing works
The Promyelocytic Leukemia Gene Product (PML) Forms Stable Complexes with the Retinoblastoma Protein
Alcalay, M., Tomassoni, L., Colombo, E., Stoldt, S., Grignani, F., Fagioli, M., Székely, L., Helin, K., & Pelicci, P. G. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.2.1084 · Cited by 160 · see citing works
Liu, H., Su, Y.-C., Becker, E., Treisman, J. E., & Skolnik, E. Y. (1999) · Current Biology · doi:10.1016/s0960-9822(99)80023-2 · Cited by 158 · see citing works
Wong, C. W., & Privalsky, M. L. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.42.27695 · Cited by 156 · see citing works
Webster, M.-T., Rozycka, M., Sara, E., Davis, E., Smalley, M. J., Young, N., Dale, T. C., & Wooster, R. F. (2000) · Genes Chromosomes and Cancer · doi:10.1002/1098-2264(200008)28:4 · Cited by 154 · see citing works
Pullen, S. S., Labadia, M. E., Ingraham, R. H., McWhirter, S. M., Everdeen, D. S., Alber, T., Crute, J. J., & Kehry, M. R. (1999) · Biochemistry · doi:10.1021/bi9909905 · Cited by 150 · see citing works
Molecular basis for CD40 signaling mediated by TRAF3
Ni, C., Welsh, K., Leo, E., Chiou, C.-K., Wu, H., Reed, J. C., & Ely, K. R. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.19.10395 · Cited by 143 · see citing works
Self-citationIdentification of a novel nuclear speckle‐type protein, SPOP
Nagai, Y., Kojima, T., Muro, Y., Hachiya, T., Nishizawa, Y., Wakabayashi, T., & Hagiwara, M. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)01340-9 · Cited by 124 · see citing works
Everett, R. D., Meredith, M., & Orr, A. (1999) · Journal of Virology · doi:10.1128/jvi.73.1.417-426.1999 · Cited by 122 · see citing works
Galang, C. K., Der, C. J., & Hauser, C. A. (1994) · PubMed · Cited by 120 · see citing works
Hoeflich, K. P., Yeh, W., Yao, Z., Mak, T. W., & Woodgett, J. R. (1999) · Oncogene · doi:10.1038/sj.onc.1202975 · Cited by 114 · see citing works
Everett, R. D., Meredith, M., Orr, A., Cross, A., Kathoria, M., & Parkinson, J. (1997) · The EMBO Journal · doi:10.1093/emboj/16.3.566 · Cited by 111 · see citing works
Involvement of the rfp tripartite motif in protein-protein interactions and subcellular distribution
Cao, T., Borden, K. L. B., Freemont, P. S., & Etkin, L. D. (1997) · Journal of Cell Science · doi:10.1242/jcs.110.14.1563 · Cited by 107 · see citing works
Boucher, L.-M., Marengère, L. E. M., Lu, Y., Thukral, S. K., & Mak, T. W. (1997) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1997.6509 · Cited by 100 · see citing works
Leo, E., Welsh, K., Matsuzawa, S., Zapata, J. M., Kitada, S., Mitchell, R. S., Ely, K. R., & Reed, J. C. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.32.22414 · Cited by 96 · see citing works
Self-citationHarris, P. C., Ward, C. J., Peral, B., & Hughes, J. R. (1995) · Journal of the American Society of Nephrology · doi:10.1681/asn.v641125 · Cited by 90 · see citing works
Fold prediction by a hierarchy of sequence, threading, and modeling methods
Jaroszwski, Ł., Rychlewski, L., Zhang, B.-H., & Godzik, A. (1998) · Protein Science · doi:10.1002/pro.5560070620 · Cited by 88 · see citing works
Self-citationHolinski‐Feder, E., Reyniers, E., Uhrig, S., Golla, A., Wauters, J., Kroisel, P. M., Bossuyt, P., Rost, I., Jedele, K. B., Zierler, H., et al. (2000) · The American Journal of Human Genetics · doi:10.1086/302703 · Cited by 86 · see citing works
Cloning and Characterization of a Novel RING Finger Protein That Interacts with Class V Myosins
El-Husseini, A., & Vincent, S. R. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.28.19771 · Cited by 83 · see citing works
Eussen, B. H. J., Bartalini, G., Bakker, L., Balestri, P., Lucca, C. D., Hemel, J. O. V., Dauwerse, H., van den Ouweland, A. M. W., Ris‐Stalpers, C., Verhoef, S., et al. (2000) · Journal of Medical Genetics · doi:10.1136/jmg.37.4.287 · Cited by 81 · see citing works
Wallerstein, R. J., Anderson, C. E., Hay, B. N., Gupta, P., Gibas, L. M., Ansari, K., Cowchock, F. S., Weinblatt, V. J., Reid, C., Levitas, A., et al. (1997) · Journal of Medical Genetics · doi:10.1136/jmg.34.3.203 · Cited by 79 · see citing works
Yamamoto, H., Kishimoto, T., & Minamoto, S. (1998) · PubMed · Cited by 71 · see citing works
Yamamoto, H., Kishimoto, T., & Minamoto, S. (1998) · The Journal of Immunology · doi:10.4049/jimmunol.161.9.4753 · Cited by 70 · see citing works
Krajewska, M., Krajewski, S., Zapata, J. M., Arsdale, T. V., Gascoyne, R. D., Berern, K., McFadden, G., Shabaik, A. S., Hugh, J. C., Reynolds, A. B., et al. (1998) · Europe PMC (PubMed Central) · Cited by 68 · see citing works
Self-citationStructural and Functional Heterogeneity of Nuclear Bodies
Bloch, D. B., Chiche, J., Orth, D., de la Monte, S. M., Rosenzweig, A., & Bloch, K. D. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.6.4423 · Cited by 62 · see citing works
Zapata, J., Matsuzawa, S., Godzik, A., Leo, E., Wasserman, S., & Reed, J. C. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.16.12102 · Cited by 61 · see citing works
Self-citationTRAF protiens and meprins share a conserved domain
Uren, A. G., & Vaux, D. L. (1996) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(96)30022-4 · Cited by 60 · see citing works
Zheng, P., Pang, J. C., Hui, A. B., & Ng, H. (2000) · Cancer Genetics and Cytogenetics · doi:10.1016/s0165-4608(00)00265-x · Cited by 58 · see citing works
Shi, C.-S., Leonardi, A., Kyriakis, J. M., Siebenlist, U. K., & Kehrl, J. H. (1999) · The Journal of Immunology · doi:10.4049/jimmunol.163.6.3279 · Cited by 48 · see citing works
BERP, a Novel Ring Finger Protein, Binds to α-Actinin-4
El-Husseini, A., Kwasnicka, D. A., Yamada, T., Hirohashi, S., & Vincent, S. R. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1999.2045 · Cited by 42 · see citing works
The α-Thalassemia/Mental Retardation Syndromes
Gibbons, R. J., & Higgs, D. R. (1996) · Medicine · doi:10.1097/00005792-199603000-00001 · Cited by 30 · see citing works
A surprising role for the proteasome in the regulation of herpesvirus infection
Everett, R. D. (1999) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(99)01433-4 · Cited by 26 · see citing works
Ming, J. E., Blagowidow, N., Knoll, J. H. M., Rollings, L., Fortina, P. M., McDonald‐McGinn, D. M., Spinner, N. B., & Zackai, E. H. (2000) · American Journal of Medical Genetics · doi:10.1002/(sici)1096-8628(20000501)92:1 · Cited by 24 · see citing works
Jin, Y., Merterns, F., Persson, B., Gullestad, H. P., Jin, C., Warloe, T., Salemark, L., Jonsson, N., Risberg, B. Å., Mandahl, N., et al. (1997) · PubMed · Cited by 23 · see citing works
El‐Hodiri, H. M., Che, S., Nelman-Gonzalez, M. A., Kuang, J., & Etkin, L. D. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.33.20463 · Cited by 18 · see citing works
Robinson, P. A., Lomonte, P., Leek, J. P., Markham, A. F., & Everett, R. D. (1998) · Cytogenetic and Genome Research · doi:10.1159/000015142 · Cited by 7 · see citing works
A random walk from the cello to the lab
Bonhoeffer, S. (1999) · Current Biology · doi:10.1016/s0960-9822(99)80030-x · Cited by 1 · see citing works
Rodriguez-Palmero, M. (1999) · doi:10.1002/(sici)1521-4141(199912)29:12
Self-citation
Flagged first, then by citations
Research works printed but not linked: 6
- McWhirter, S., Pullen, S., Holton, J., Crute, J., Kehry, M., and Alber, T. (1999) Proc. Natl. Acad. Sci. U. S. A. 96, 8408 -8413
- Ni, C.-Z., Welsh, K., Leo, E., Chiou, C.-K., Wu, H., Reed, J. C., and Ely, K. R. (2000) Proc. Natl. Acad. Sci. U. S. A. 97, 10395-10399
- Song, H. Y., Re ´gnier, C. H., Kirschning, C. J., Goeddel, D. V., and Rothe, M. (1997) Proc. Natl. Acad. Sci. U. S. A. 94, 9792-9796
- Rothe, M., Xiong, J., Shu, H.-B., Williamson, K., Goddard, A., and Goeddel, D. V. (1996) Proc. Natl. Acad. Sci. U. S. A. 93, 8241-8246
- Ansieau, S., Scheffrahn, I., Mosialos, G., Brand, H., Duyster, J., Kaye, K., Harada, J., Dougall, B., Hubinger, G., Kieff, E., Herrmann, F., Leutz, A., and Gruss, H.-J. (1996) Proc. Natl. Acad. Sci. U. S. A. 93, 14053-14058
- LaMorte, V. J., Dyck, J. A., Ochs, R. L., and Evans, R. M. (1998) Proc. Natl. Acad. Sci. U. S. A. 95, 4991-4996
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Ghobrial, I. M., Witzig, T. E., & Adjei, A. A. (2005) · CA A Cancer Journal for Clinicians · doi:10.3322/canjclin.55.3.178 · Cited by 1,353 · see citing works
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Bradley, J. R., & Pober, J. S. (2001) · Oncogene · doi:10.1038/sj.onc.1204788 · Cited by 652 · see citing works
Hu, M., Li, P., Li, M., Li, W., Yao, T., Wu, J.-W., Gu, W. J., Cohen, R. E., & Shi, Y. (2002) · Cell · doi:10.1016/s0092-8674(02)01199-6 · Cited by 648 · see citing works
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Borodovsky, A., Ovaa, H., Kolli, N., Gan-Erdene, T., Wilkinson, K. D., Ploegh, H. L., & Kessler, B. M. (2002) · Chemistry & Biology · doi:10.1016/s1074-5521(02)00248-x · Cited by 588 · see citing works
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Ware, C. F. (2004) · Annual Review of Immunology · doi:10.1146/annurev.immunol.23.021704.115719 · Cited by 441 · see citing works
Self-citationBoutell, C., Sadis, S., & Everett, R. D. (2002) · Journal of Virology · doi:10.1128/jvi.76.2.841-850.2002 · Cited by 386 · see citing works
Structure of the p53 Binding Domain of HAUSP/USP7 Bound to Epstein-Barr Nuclear Antigen 1
Saridakis, V., Sheng, Y., Sarkari, F., Holowaty, M. N., Shire, K., Nguyen, T., Zhang, R. G., Liao, J. C. C., Lee, W., Edwards, A. M., et al. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.02.029 · Cited by 362 · see citing works
Short, K. M., & Cox, T. C. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m512755200 · Cited by 323 · see citing works
Eißner, G., Kölch, W., & Scheurich, P. (2004) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2004.03.011 · Cited by 298 · see citing works
Targeting Apoptosis Pathways in Cancer Therapy
Fulda, S., & Debatin, K. (2004) · Current Cancer Drug Targets · doi:10.2174/1568009043332763 · Cited by 295 · see citing works
Discovery of specific inhibitors of human USP7/HAUSP deubiquitinating enzyme.
Reverdy, C., Conrath, S., Lopez, R., Planquette, C., Atmanene, C., Collura, V., Harpon, J., Battaglia, V., Vivat, V., Sippl, W., et al. (2012) · Chemistry & Biology · doi:10.1016/j.chembiol.2012.02.007 · Cited by 270 · see citing works
Hu, M., Gu, L., Li, M., Jeffrey, P. D., Gu, W., & Shi, Y. (2006) · PLoS Biology · doi:10.1371/journal.pbio.0040027 · Cited by 251 · see citing works
Chen, T., & Wong, Y. (2008) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2008.07.014 · Cited by 231 · see citing works
Ubiquitination and translocation of TRAF2 is required for activation of JNK but not of p38 or NF‐κB
Habelhah, H., Takahashi, S., Cho, S., Kadoya, T., Watanabe, T., & Ronai, Z. A. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600044 · Cited by 207 · see citing works
Meprins, membrane-bound and secreted astacin metalloproteinases
Sterchi, E. E., Stöcker, W., & BOND, J. (2008) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2008.08.002 · Cited by 199 · see citing works
Protein Interaction Domains of the Ubiquitin-specific Protease, USP7/HAUSP
Holowaty, M. N., Sheng, Y., Nguyen, T., Arrowsmith, C. H., & Frappier, L. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m307200200 · Cited by 182 · see citing works
Targeting apoptotic and autophagic pathways for cancer therapeutics
Liu, J., Mou, L., Yu, J., Liu, B., & Bao, J. (2010) · Cancer Letters · doi:10.1016/j.canlet.2010.10.001 · Cited by 171 · see citing works
Chen, T., & Wong, Y. S. (2008) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-008-8329-2 · Cited by 169 · see citing works
Emerging insights into HAUSP (USP7) in physiology, cancer and other diseases.
Bhattacharya, S., Chakraborty, D., Basu, M., & Ghosh, M. K. (2018) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-018-0012-y · Cited by 162 · see citing works
Zhang, Y., Li, X., Huang, Z., Zheng, W., Fan, C., & Chen, T. (2012) · Nanomedicine Nanotechnology Biology and Medicine · doi:10.1016/j.nano.2012.04.002 · Cited by 160 · see citing works
Structure of TRAF Family: Current Understanding of Receptor Recognition
Park, H. H. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.01999 · Cited by 160 · see citing works
The p75 neurotrophin receptor: multiple interactors and numerous functions
Gentry, J. J., Barker, P. A., & Carter, B. D. (2004) · Progress in brain research · doi:10.1016/s0079-6123(03)46002-0 · Cited by 158 · see citing works
HSV ICP0 recruits USP7 to modulate TLR-mediated innate response
Daubeuf, S., Singh, D., Tan, Y., Liu, H., Federoff, H. J., Bowers, W. J., & Tolba, K. A. (2008) · Blood · doi:10.1182/blood-2008-07-168203 · Cited by 146 · see citing works
Arabidopsis AtCUL3a and AtCUL3b Form Complexes with Members of the BTB/POZ-MATH Protein Family
Weber, H., Bernhardt, A., Dieterle, M., Hano, P., Mutlu, A., Estelle, M. A., Genschik, P., & Hellmann, H. A. (2004) · PLANT PHYSIOLOGY · doi:10.1104/pp.104.052654 · Cited by 145 · see citing works
Canning, M., Boutell, C., Parkinson, J., & Everett, R. D. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m402885200 · Cited by 142 · see citing works
Cell Survival and Apoptosis Signaling as Therapeutic Target for Cancer: Marine Bioactive Compounds
Kalimuthu, S., & Kim, S. (2013) · International Journal of Molecular Sciences · doi:10.3390/ijms14022334 · Cited by 141 · see citing works
Hedgehog Signal and Genetic Disorders
Sasai, N., Toriyama, M., & Kondo, T. (2019) · Frontiers in Genetics · doi:10.3389/fgene.2019.01103 · Cited by 141 · see citing works
Male subfertility and oxidative stress
Evans, E. P. P., Scholten, J. T. M., Mzyk, A., Reyes-San-Martin, C., Elías-Llumbet, A., Hamoh, T., Arts, E. G. J. M., Schirhagl, R., & Cantineau, A. E. (2021) · Redox Biology · doi:10.1016/j.redox.2021.102071 · Cited by 141 · see citing works
Targeting ubiquitin specific proteases for drug discovery
Daviet, L., & Colland, F. (2007) · Biochimie · doi:10.1016/j.biochi.2007.09.013 · Cited by 139 · see citing works
Siah ubiquitin ligase is structurally related to TRAF and modulates TNF-α signaling
Polekhina, G., House, C. M., Traficante, N., Mackay, J. P., Relaix, F., Sassoon, D. A., Parker, M. W., & Bowtell, D. D. L. (2001) · Nature Structural Biology · doi:10.1038/nsb743 · Cited by 137 · see citing works
Ben‐Shlomo, I., Hsu, S. Y., Rauch, R., Kowalski, H. W., & Hsueh, A. J. W. (2003) · Science s STKE · doi:10.1126/stke.2003.187.re9 · Cited by 135 · see citing works
Boutell, C., Canning, M., Orr, A., & Everett, R. D. (2005) · Journal of Virology · doi:10.1128/jvi.79.19.12342-12354.2005 · Cited by 134 · see citing works
Comparative Analysis of Apoptosis and Inflammation Genes of Mice and HumansPreprint
Reed, J. C., Doctor, K. S., Rojas, A. M., Zapata, J. M., Stehlik, C., Fiorentino, L., Damiano, J. S., Roth, W., Matsuzawa, S.-I., Newman, R. M., et al. (2003) · Genome Research · doi:10.1101/gr.1053803 · Cited by 128 · see citing works
Self-citationCD137 (4-1BB) Signalosome: Complexity Is a Matter of TRAFs
Zapata, J. M., Pérez-Chacón, G., Carr-Baena, P., Martínez‐Forero, I., Azpilikueta, A., Otano, I., & Melero, I. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.02618 · Cited by 125 · see citing works
Self-citationZaman, M. M.-U., Nomura, T., Takagi, T., Okamura, T., Jin, W., Shinagawa, T., Tanaka, Y., & Ishii, S. (2013) · Molecular and Cellular Biology · doi:10.1128/mcb.00465-13 · Cited by 125 · see citing works
Zhou, Q., Wang, S., Zhang, H., Lu, Y.-Y., Wang, X., Motoo, Y., & Su, S.-B. (2009) · Acta Pharmacologica Sinica · doi:10.1038/aps.2009.166 · Cited by 121 · see citing works
USP7 Is a Master Regulator of Genome Stability
Valles, G. J., Bezsonova, I., Woodgate, R., & Ashton, N. W. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00717 · Cited by 114 · see citing works
“As this region of the protein does not contain a nuclear localization signal, it has been speculated that binding to USP7 substrates – which are primarily nuclear – may mediate translocation of USP7 into the nucleus (Zapata et al., 2001; Fernandez-Montalvan et al., 2007).”
BackgroundStructure of Homo- and Hetero-oligomeric Meprin Metalloproteases
Bertenshaw, G. P., Norcum, M. T., & Bond, J. S. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m208808200 · Cited by 113 · see citing works
Pozhidaeva, A., Valles, G., Wang, F., Wu, J., Sterner, D. E., Nguyen, P., Weinstock, J., Kumar, K. G. S., Kanyo, J., Wright, D., et al. (2017) · Cell Chemical Biology · doi:10.1016/j.chembiol.2017.09.004 · Cited by 107 · see citing works
Modulation of the p53/MDM2 interplay by HAUSP inhibitors
Tavana, O., & Gu, W. J. (2016) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjw049 · Cited by 108 · see citing works
The Ubiquitination of NF-κB Subunits in the Control of Transcription
Collins, P. E., Mitxitorena, I., & Carmody, R. J. (2016) · Cells · doi:10.3390/cells5020023 · Cited by 103 · see citing works
γ‐Synuclein and the progression of cancer
Ahmad, M., Attoub, S., Singh, M. N., Martin, F. L., & El‐Agnaf, O. M. A. (2007) · The FASEB Journal · doi:10.1096/fj.07-8379rev · Cited by 102 · see citing works
BTBD1 and BTBD2 colocalize to cytoplasmic bodies with the RBCC/tripartite motif protein, TRIM5δ
Xu, L. (2003) · Experimental Cell Research · doi:10.1016/s0014-4827(03)00187-3 · Cited by 102 · see citing works
Berberine: A novel therapeutic strategy for cancer
Samadi, P., Sarvarian, P., Gholipour, E., Asenjan, K. S., Maleki, L. A., Motavalli, R., Hojjat‐Farsangi, M., & Yousefi, M. (2020) · IUBMB Life · doi:10.1002/iub.2350 · Cited by 101 · see citing works
Regulation of USP7: A High Incidence of E3 Complexes
Kim, R. Q., & Sixma, T. K. (2017) · Journal of Molecular Biology · doi:10.1016/j.jmb.2017.05.028 · Cited by 96 · see citing works
Functional and structural insights into astacin metallopeptidases
Gomis‐Rüth, F. X., Trillo‐Muyo, S., & Stöcker, W. (2012) · Biological Chemistry · doi:10.1515/hsz-2012-0149 · Cited by 97 · see citing works
Fernández‐Montalván, A., Bouwmeester, T., Joberty, G., Mader, R., Mahnke, M., Pierrat, B., Schlaeppi, J., Worpenberg, S., & Gerhartz, B. (2007) · The FEBS Journal · doi:10.1111/j.1742-4658.2007.05952.x · Cited by 96 · see citing works
Genetic Alterations of TRAF Proteins in Human Cancers
Zhu, S., Jin, J., Gokhale, S., Lu, A. M., Shan, H., Feng, J., & Xie, P. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.02111 · Cited by 94 · see citing works
The emerging role of speckle-type POZ protein (SPOP) in cancer development
Mani, R. S. (2014) · Drug Discovery Today · doi:10.1016/j.drudis.2014.07.009 · Cited by 93 · see citing works
Arolas, J. L., Broder, C., Jefferson, T., Guevara, T., Sterchi, E. E., Bode, W., Stöcker, W., Becker‐Pauly, C., & Gomis‐Rüth, F. X. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1211076109 · Cited by 92 · see citing works
Phylogeny of the TRAF/MATH Domain
Zapata, J. M., Martínez-García, V., & Lefebvre, S. (2007) · Springer eBooks · doi:10.1007/978-0-387-70630-6_1 · Cited by 88 · see citing works
Self-citationTRIM37 defective in mulibrey nanism is a novel RING finger ubiquitin E3 ligase.
Kallijärvi, J., Lahtinen, U., Hämäläinen, R., Lipsanen-Nyman, M., Palvimo, J., & Lehesjoki, A. (2005) · Experimental Cell Research · doi:10.1016/j.yexcr.2005.04.001 · Cited by 103 · see citing works
Lau, S. T., Lin, Z., Liao, Y., Zhao, M., Cheng, C. H. K., & Leung, P. S. (2009) · Cancer Letters · doi:10.1016/j.canlet.2009.02.017 · Cited by 86 · see citing works
Deubiquitylating enzymes and disease
Singhal, S., Taylor, M. C., & Baker, R. T. (2008) · BMC Biochemistry · doi:10.1186/1471-2091-9-s1-s3 · Cited by 85 · see citing works
Huang, F., Yang, Z., Yu, D., Wang, J., Li, R., & Ding, G. (2012) · Marine Drugs · doi:10.3390/md10102153 · Cited by 84 · see citing works
Chen, T., Zheng, W., Wong, Y., & Yang, F. (2008) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2007.12.002 · Cited by 83 · see citing works
Hu, Y., Yang, Y., You, Q., Liu, W., Gu, H.-Y., Zhao, L., Zhang, K., Wang, W., Wang, X., & Guo, Q. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.10.064 · Cited by 82 · see citing works
TNF Receptor Associated Factor 2 (TRAF2) Signaling in Cancer
Siegmund, D., Wagner, J., & Wajant, H. (2022) · Cancers · doi:10.3390/cancers14164055 · Cited by 81 · see citing works
Wang, J., Zhao, X., Qi, Q., Tao, L., Zhao, Q., Mu, R., Gu, H.-Y., Wang, M., Xu, F., & Guo, Q. (2009) · Food and Chemical Toxicology · doi:10.1016/j.fct.2009.04.034 · Cited by 80 · see citing works
Kim, M. S., Je, E. M., Oh, J. E., Yoo, N. J., & Lee, S. H. (2012) · Apmis · doi:10.1111/apm.12030 · Cited by 80 · see citing works
Qiu, L., Song, L., Yu, Y., Zhao, J., Wang, L., & Zhang, Q. (2009) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2008.10.010 · Cited by 80 · see citing works
Wan, J., Zhang, J., Chen, D., Yu, B., Mao, X., Zheng, P., Yu, J., Luo, J., & He, J. (2018) · Journal of Animal Science and Biotechnology/Journal of animal science and biotechnology · doi:10.1186/s40104-018-0273-x · Cited by 79 · see citing works
Kallijärvi, J., Avela, K., Lipsanen‐Nyman, M., Ulmanen, I., & Lehesjoki, A. (2002) · The American Journal of Human Genetics · doi:10.1086/340256 · Cited by 78 · see citing works
TRAF6-p38/JNK-ATF2 axis promotes microglial inflammatory activation
Li, M., Zhang, D., Ge, X., Zhu, X., Zhou, Y., Zhang, Y., Peng, X., & Shen, A. (2019) · Experimental Cell Research · doi:10.1016/j.yexcr.2019.02.005 · Cited by 75 · see citing works
SPOP and cancer: a systematic review.
Clark, A. D., & Burleson, M. O. (2020) · PubMed Central · Cited by 71 · see citing works
The Anticancer Activities of Wogonin in Murine Sarcoma S180 both in Vitro and in Vivo
Wang, W., Guo, Q., You, Q., Zhang, K., Yang, Y., Yu, J., Liu, W., Zhao, L., Gu, H.-Y., Hu, Y., et al. (2006) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.29.1132 · Cited by 71 · see citing works
TRAF4, the Unique Family Member
Kedinger, V., & Rio, M. (2007) · Advances in experimental medicine and biology · doi:10.1007/978-0-387-70630-6_5 · Cited by 68 · see citing works
Human α-defensin-1 inhibits growth of human lung adenocarcinoma xenograft in nude mice
Xu, N., Wang, Y., Pan, W., Xiao, B., Wen, Y., Chen, X., Chen, L., Deng, H., You, J., Kan, B., et al. (2008) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-08-0010 · Cited by 68 · see citing works
Zhao, Q., Xue, Y., Wang, J., Li, H., Long, T., Li, Z., Wang, Y., Dong, P., & Xue, C. (2011) · Journal of the Science of Food and Agriculture · doi:10.1002/jsfa.4678 · Cited by 66 · see citing works
Identification of PCIF1, a POZ Domain Protein That Inhibits PDX-1 (MODY4) Transcriptional Activity
Liu, A., Desai, B. M., & Stoffers, D. A. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.10.4372-4383.2004 · Cited by 65 · see citing works
Norman, L. P., Jiang, W., Han, X., Saunders, T. L., & Bond, J. S. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.4.1221-1230.2003 · Cited by 63 · see citing works
Expression of HAUSP in gliomas correlates with disease progression and survival of patients
Cheng, C., Niu, C., Yang, Y., Wang, Y., & Lu, M. (2013) · Oncology Reports · doi:10.3892/or.2013.2342 · Cited by 61 · see citing works
USP7 Cooperates with SCML2 To Regulate the Activity of PRC1
Lecona, E., Narendra, V. K., & Reinberg, D. (2015) · Molecular and Cellular Biology · doi:10.1128/mcb.01197-14 · Cited by 59 · see citing works
Involvement of bax/bcl-2 in wogonin-induced apoptosis of human hepatoma cell line SMMC-7721
Wang, W., Guo, Q., You, Q., Zhang, K., Yang, Y., Yu, J., Liu, W., Zhao, L., Gu, H.-Y., Hu, Y., et al. (2006) · Anti-Cancer Drugs · doi:10.1097/01.cad.0000217431.64118.3f · Cited by 58 · see citing works
Gene expression control by protein deubiquitinases
Frappier, L., & Verrijzer, C. P. (2011) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2011.02.005 · Cited by 58 · see citing works
Liu, L., Channavajhala, P. L., Rao, V. R., Moutsatsos, I. K., Wu, L., Zhang, Y., Lin, L.-L., & Qiu, Y. (2009) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2009.06.016 · Cited by 57 · see citing works
Zapata, J. M., & Reed, J. C. (2002) · Science s STKE · doi:10.1126/stke.2002.133.pe27 · Cited by 56 · see citing works
Self-citationBalachandran, C., Sangeetha, B., Duraipandiyan, V., Raj, M. K., Savarimuthu Ignacimuthu, S. J., Al-Dhabi, N. A., Balakrishna, K., Parthasarathy, K., Arulmozhi, N. M., & Arasu, M. V. (2014) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2014.09.019 · Cited by 52 · see citing works
Sun, X. L., Zhong, Y., Luo, H., & Yang, Y. (2017) · Marine Drugs · doi:10.3390/md15070215 · Cited by 50 · see citing works
Wu, G., Song, L., Zhu, J., Hu, Y., Cao, L., Tan, Z., Zhang, S., Li, Z., & Li, J. (2018) · Cancer Research · doi:10.1158/0008-5472.can-18-2063 · Cited by 49 · see citing works
Wang, K. Z. Q., Wara-aswapati, N., Boch, J. A., Yoshida, Y., Hu, C., Galson, D. L., & Auron, P. E. (2006) · Journal of Cell Science · doi:10.1242/jcs.02889 · Cited by 48 · see citing works
Huang, C.-C. F., Weng, J., Wei, T. W., Wu, P., Hsu, P., Chen, Y., Wang, S., Qin, D., Hung, C.-C., Chen, S., et al. (2012) · Molecular and Cellular Biology · doi:10.1128/mcb.00438-12 · Cited by 48 · see citing works
HAUSP/USP7 as an Epstein–Barr virus target
Holowaty, M. N., & Frappier, L. (2004) · Biochemical Society Transactions · doi:10.1042/bst0320731 · Cited by 48 · see citing works
Yi, P., Xia, W., Wu, R., Lonard, D. M., Hung, M., & O’Malley, B. W. (2013) · Genes & Development · doi:10.1101/gad.203760.112 · Cited by 46 · see citing works
The new MATH: homology suggests shared binding surfaces in meprin tetramers and TRAF trimers
Sunnerhagen, M., Pursglove, S. E., & Fladvad, M. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)03330-6 · Cited by 45 · see citing works
Du, L., Li, Z., Xu, J., Wang, J., Xue, Y., Xue, C., Takahashi, K., & Wang, Y. (2012) · Journal of Oleo Science · doi:10.5650/jos.61.321 · Cited by 43 · see citing works
Novel mutations in theTRIM37gene in Mulibrey Nanism
Hämäläinen, R. H., Avela, K., Lambert, J. A., Kallijärvi, J., Eyaid, W., Gronau, J., Ignaszewski, A. P., McFadden, D. E., Sorge, G., Lipsanen‐Nyman, M., et al. (2004) · Human Mutation · doi:10.1002/humu.9233 · Cited by 42 · see citing works
Rong, J., Chen, L., Toth, J. I., Tcherpakov, M., Petroski, M. D., & Reed, J. C. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.175232 · Cited by 41 · see citing works
Self-citationMeprin β metalloprotease gene polymorphisms associated with diabetic nephropathy in the Pima Indians
Eagle, A. R., Hanson, R. L., Jiang, W., Han, X., Matters, G. L., Imperatore, G., Knowler, W. C., & Bond, J. S. (2005) · Human Genetics · doi:10.1007/s00439-005-0019-7 · Cited by 41 · see citing works
ING1 induces apoptosis through direct effects at the mitochondria
Bose, P., Thakur, S. S., Thalappilly, S., Ahn, B. Y., Satpathy, S., Feng, X., Suzuki, K., Kim, S. W., & Riabowol, K. T. (2013) · Cell Death and Disease · doi:10.1038/cddis.2013.321 · Cited by 40 · see citing works
Pozhidaeva, A., Mohni, K. N., Dhe‐Paganon, S., Arrowsmith, C. H., Weller, S. K., Korzhnev, D. M., & Bezsonova, I. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.664805 · Cited by 40 · see citing works
Kim, C. M., Choi, J. Y., Bhat, E. A., Jeong, J., Son, Y., Kim, S., & Park, H. H. (2016) · Scientific Reports · doi:10.1038/srep25526 · Cited by 40 · see citing works
The Evolution and Functional Diversification of the Deubiquitinating Enzyme Superfamily
Vlasschaert, C., Cook, D. P., Xia, X., & Gray, D. A. (2017) · Genome Biology and Evolution · doi:10.1093/gbe/evx020 · Cited by 40 · see citing works
Koyuncu, İ., Gönel, A., Koçyiğit, A., Temiz, E., Durgun, M., & Supuran, C. T. (2018) · Journal of Enzyme Inhibition and Medicinal Chemistry · doi:10.1080/14756366.2018.1481403 · Cited by 39 · see citing works
Lu, H.-F., Wang, H.-L., Chuang, Y.-Y., Tang, Y.-J., Yang, J., Ma, Y., Chiang, J., Lu, C., Yang, J.-L., Lai, T.-Y., et al. (2009) · Neurochemical Research · doi:10.1007/s11064-009-0067-9 · Cited by 39 · see citing works
Tan, T.-T., & White, E. (2007) · Advances in experimental medicine and biology · doi:10.1007/978-1-4020-6554-5_5 · Cited by 39 · see citing works
Assembly of Post-Receptor Signaling Complexes for the Tumor Necrosis Factor Receptor Superfamily
Wu, H. (2004) · Advances in protein chemistry · doi:10.1016/s0065-3233(04)68007-7 · Cited by 39 · see citing works
Antiangiogenic therapy using nanotechnological-based delivery system
Kanwar, J. R., Mahidhara, G., & Kanwar, R. K. (2011) · Drug Discovery Today · doi:10.1016/j.drudis.2011.01.007 · Cited by 37 · see citing works
Gadhave, K., Kumar, P., Kapuganti, S. K., Uversky, V. N., & Giri, R. (2020) · Biomolecules · doi:10.3390/biom10050796 · Cited by 36 · see citing works
TNF-receptor-associated factors as targets for drug development
Zapata, J. M. (2003) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.7.3.411 · Cited by 37 · see citing works
Self-citation
- 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
- Health Sciences › Medicine › Oncology › 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
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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 ›
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