The DOI matches its Crossref record; 92 of the 92 references it cites were found in a registry or an index.
Systems‐wide analysis of BCR signalosomes and downstream phosphorylation and ubiquitylation
Open accessAbstract
B‐cell receptor (BCR) signaling is essential for the development and function of B cells; however, the spectrum of proteins involved in BCR signaling is not fully known. Here we used quantitative mass spectrometry‐based proteomics to monitor the dynamics of BCR signaling complexes (signalosomes) and to investigate the dynamics of downstream phosphorylation and ubiquitylation signaling. We identify most of the previously known components of BCR signaling, as well as many proteins that have not yet been implicated in this system. BCR activation leads to rapid tyrosine phosphorylation and ubiquitylation of the receptor‐proximal signaling components, many of which are co‐regulated by both the modifications. We illustrate the power of multilayered proteomic analyses for discovering novel BCR signaling components by demonstrating that BCR‐induced phosphorylation of RAB7A at S72 prevents its association with effector proteins and with endo‐lysosomal compartments. In addition, we show that BCL10 is modified by LUBAC‐mediated linear ubiquitylation, and demonstrate an important function of LUBAC in BCR‐induced NF‐κB signaling. Our results offer a global and integrated view of BCR signaling, and the provided datasets can serve as a valuable resource for further understanding BCR signaling networks.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“Anti-IgM antibodies stimulate B cells through the B cell receptor (BCR) thereby activating further downstream signaling cascades like the phosphatidylinositol 3-kinase (PI3K), protein kinase B (AKT) and mitogen-activated protein kinase (MAPK) pathways [51–53].”
From The oncoprotein TBX3 is controlling severity in experimental arthritis (2019) · cites this paper as [53]
Experimental — accuracy not yet measured
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
Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources
Huang, D. W., Sherman, B. T., & Lempicki, R. A. (2009) · Nature Protocols · doi:10.1038/nprot.2008.211 · Cited by 35,890
Cox, J., & Mann, M. (2008) · Nature Biotechnology · doi:10.1038/nbt.1511 · Cited by 14,855
Huang, D. W., Sherman, B. T., & Lempicki, R. A. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkn923 · Cited by 14,108
Universal sample preparation method for proteome analysis
Wiśniewski, J. R., Zougman, A., Nagaraj, N., & Mann, M. (2009) · Nature Methods · doi:10.1038/nmeth.1322 · Cited by 8,352
Ong, S.-E., Blagoev, B., Kratchmarova, I., Kristensen, D. B., Steen, H., Pandey, A., & Mann, M. (2002) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m200025-mcp200 · Cited by 5,574
Andromeda: A Peptide Search Engine Integrated into the MaxQuant Environment
Cox, J., Neuhauser, N., Michalski, A., Scheltema, R. A., Olsen, J. V., & Mann, M. (2011) · Journal of Proteome Research · doi:10.1021/pr101065j · Cited by 5,503
Rappsilber, J., Mann, M., & Ishihama, Y. (2007) · Nature Protocols · doi:10.1038/nprot.2007.261 · Cited by 4,641
Elias, J. E., & Gygi, S. P. (2007) · Nature Methods · doi:10.1038/nmeth1019 · Cited by 3,925
Global, In Vivo, and Site-Specific Phosphorylation Dynamics in Signaling Networks
Olsen, J. V., Blagoev, B., Gnad, F., Maček, B., Kumar, C., Mortensen, P., & Mann, M. (2006) · Cell · doi:10.1016/j.cell.2006.09.026 · Cited by 3,562
ProteomeXchange provides globally coordinated proteomics data submission and dissemination
Vizcaíno, J. A., Deutsch, E. W., Wang, R., Csordás, A., Reisinger, F., Ríos, D., Dianes, J. A., Sun, Z., Farrah, T., Bandeira, N., et al. (2014) · Nature Biotechnology · doi:10.1038/nbt.2839 · Cited by 2,735
Integration of biological networks and gene expression data using Cytoscape
Cline, M. S., Smoot, M., Cerami, E., Kuchinsky, A., Landys, N., Workman, C., Christmas, R., Avila-Campilo, I., Creech, M., Gross, B., et al. (2007) · Nature Protocols · doi:10.1038/nprot.2007.324 · Cited by 2,507
Systematic and Quantitative Assessment of the Ubiquitin-Modified Proteome
Kim, W., Bennett, E. J., Huttlin, E. L., Guo, A., Li, J., Possemato, A. P., Sowa, M. E., Rad, R., Rush, A. J., Comb, M. J., et al. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.08.025 · Cited by 1,643
Frequent mutation of histone-modifying genes in non-Hodgkin lymphoma
Morin, R. D., Mendez-Lago, M., Mungall, A. J., Goya, R., Mungall, K. L., Corbett, R. D., Johnson, N. A., Severson, T. M., Chiu, R., Field, M., et al. (2011) · Nature · doi:10.1038/nature10351 · Cited by 1,614
Whole-genome sequencing identifies recurrent mutations in chronic lymphocytic leukaemia
Puente, X. S., Pinyol, M., Quesada, V., Conde, L., Ordóñez, G. R., Villamor, N., Escaramís, G., Jares, P., Beà, S., González, M., et al. (2011) · Nature · doi:10.1038/nature10113 · Cited by 1,529
Rab7: A Key to Lysosome Biogenesis
Bucci, C., Thomsen, P., Nicoziani, P., McCarthy, J., & van Deurs, B. (2000) · Molecular Biology of the Cell · doi:10.1091/mbc.11.2.467 · Cited by 1,108
Higher-energy C-trap dissociation for peptide modification analysis
Olsen, J. V., Maček, B., Lange, O., Makarov, A., Horning, S. R., & Mann, M. (2007) · Nature Methods · doi:10.1038/nmeth1060 · Cited by 1,032
Sharma, K., D’Souza, R. C. J., Tyanova, S., Schaab, C., Wiśniewski, J. R., Cox, J., & Mann, M. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.07.036 · Cited by 985
Nonproteolytic Functions of Ubiquitin in Cell Signaling
Chen, Z. J., & Sun, L. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.01.014 · Cited by 948
Wagner, S., Beli, P., Weinert, B. T., Nielsen, M. L., Cox, J., Mann, M., & Choudhary, C. (2011) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m111.013284 · Cited by 922
Self-citationMichalski, A., Damoc, E., Hauschild, J.-P., Lange, O., Wieghaus, A., Makarov, A., Nagaraj, N., Cox, J., Mann, M., & Horning, S. (2011) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m111.011015 · Cited by 832
Weinert, B. T., Scholz, C. W., Wagner, S., Iešmantavičius, V., Su, D., Daniel, J. A., & Choudhary, C. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.07.024 · Cited by 774
Self-citationSpecific Recognition of Linear Ubiquitin Chains by NEMO Is Important for NF-κB Activation
Rahighi, S., Ikeda, F., Kawasaki, M., Akutsu, M., Suzuki, N., Kato, R., Kensche, T., Uejima, T., Bloor, S., Komander, D., et al. (2009) · Cell · doi:10.1016/j.cell.2009.03.007 · Cited by 761
The pCL vector system: rapid production of helper-free, high-titer, recombinant retroviruses
Naviaux, R. K., Costanzi, E., Haas, M., & Verma, I. M. (1996) · Journal of Virology · doi:10.1128/jvi.70.8.5701-5705.1996 · Cited by 735
Sun, L., Deng, L., Ea, C.-K., Xia, Z.-P., & Chen, Z. J. (2004) · Molecular Cell · doi:10.1016/s1097-2765(04)00236-9 · Cited by 700
Establishment and Characterization of BALB/c Lymphoma Lines with B Cell Properties
Kim, K. J., Kanellopoulos‐Langevin, C., Merwin, R. M., Sachs, D. H., & Asofsky, R. (1979) · The Journal of Immunology · doi:10.4049/jimmunol.122.2.549 · Cited by 667
Mevissen, T. E. T., Hospenthal, M. K., Geurink, P. P., Elliott, P. R., Akutsu, M., Arnaudo, N., Ekkebus, R., Kulathu, Y., Wauer, T., El Oualid, F., et al. (2013) · Cell · doi:10.1016/j.cell.2013.05.046 · Cited by 626
Decoding signalling networks by mass spectrometry-based proteomics
Choudhary, C., & Mann, M. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2900 · Cited by 594
Self-citationGlobal analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling
Xu, G., Paige, J. S., & Jaffrey, S. R. (2010) · Nature Biotechnology · doi:10.1038/nbt.1654 · Cited by 537
Characterization of NEDD8, a Developmentally Down-regulated Ubiquitin-like Protein
Kamitani, T., Kito, K., Nguyen, H. P., & Yeh, E. T. H. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.45.28557 · Cited by 535
NetPath: a public resource of curated signal transduction pathways
Kandasamy, K., Mohan, S. S., Raju, R., Keerthikumar, S., Kumar, G. S. S., Venugopal, A. K., Telikicherla, D., Navarro, J. D., Mathivanan, S., Pecquet, C., et al. (2010) · Genome biology · doi:10.1186/gb-2010-11-1-r3 · Cited by 499
Rab‐interacting lysosomal protein (RILP): the Rab7 effector required for transport to lysosomes
Cantalupo, G., Alifano, P., Roberti, V., Bruni, C. B., & Bucci, C. (2001) · The EMBO Journal · doi:10.1093/emboj/20.4.683 · Cited by 488
Staudt, L. M. (2010) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a000109 · Cited by 485
Efficient protection and isolation of ubiquitylated proteins using tandem ubiquitin‐binding entities
Hjerpe, R., Aillet, F., Lopitz‐Otsoa, F., Lang, V., England, P., & Rodríguez, M. S. (2009) · EMBO Reports · doi:10.1038/embor.2009.192 · Cited by 484
Germline loss-of-function mutations in SPRED1 cause a neurofibromatosis 1–like phenotype
Brems, H., Chmara, M., Sahbatou, M., Denayer, E., Taniguchi, K., Kato, R., Somers, R., Messiaen, L. M., Schepper, S. D., Fryns, J., et al. (2007) · Nature Genetics · doi:10.1038/ng2113 · Cited by 475
Brdička, T., Pavlis̆tová, D., Leo, A., Bruyns, E., Kořínek, V., Angelisová, P., Scherer, J., Shevchenko, A., Shevchenko, A., Hilgert, I., et al. (2000) · The Journal of Experimental Medicine · doi:10.1084/jem.191.9.1591 · Cited by 461
Spred is a Sprouty-related suppressor of Ras signalling
Wakioka, T., Sasaki, A. T., Kato, R., Shouda, T., Matsumoto, A., Miyoshi, K., Tsuneoka, M., Komiya, S., Baron, R., & Yoshimura, A. (2001) · Nature · doi:10.1038/35088082 · Cited by 454
Activation of the canonical IKK complex by K63/M1-linked hybrid ubiquitin chains
Emmerich, C. H., Ordureau, A., Strickson, S., Arthur, J. S. C., Pedrioli, P. G. A., Komander, D., & Cohen, P. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1314715110 · Cited by 442
Targeting pathological B cell receptor signalling in lymphoid malignancies
Young, R. M., & Staudt, L. M. (2013) · Nature Reviews Drug Discovery · doi:10.1038/nrd3937 · Cited by 421
Mass Spectrometry–Based Proteomics and Network Biology
Bensimon, A., Heck, A. J. R., & Aebersold, R. H. (2012) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-072909-100424 · Cited by 421
Mutational and structural analysis of diffuse large B-cell lymphoma using whole-genome sequencing
Morin, R. D., Mungall, K., Pleasance, E., Mungall, A. J. J., Goya, R., Huff, R. D., Scott, D. W., Ding, J., Roth, A. J. L., Chiu, R., et al. (2013) · Blood · doi:10.1182/blood-2013-02-483727 · Cited by 407
Zhou, H., Ye, M., Dong, J., Corradini, E., Cristobal, A., Heck, A. J. R., Zou, H., & Mohammed, S. (2013) · Nature Protocols · doi:10.1038/nprot.2013.010 · Cited by 381
B Cells Use Mechanical Energy to Discriminate Antigen Affinities
Natkanski, E., Lee, W.-Y. J., Mistry, B., Casal, A., Molloy, J. E., & Tolar, P. (2013) · Science · doi:10.1126/science.1237572 · Cited by 311
Self-citationNew insights into pre-BCR and BCR signalling with relevance to B cell malignancies
Rickert, R. C. (2013) · Nature reviews. Immunology · doi:10.1038/nri3487 · Cited by 307
Povlsen, L. K., Beli, P., Wagner, S., Poulsen, S. L., Sylvestersen, K. B., Poulsen, J. W., Nielsen, M. L., Bekker‐Jensen, S., Mailand, N., & Choudhary, C. (2012) · Nature Cell Biology · doi:10.1038/ncb2579 · Cited by 288
Self-citationIodoacetamide-induced artifact mimics ubiquitination in mass spectrometry
Nielsen, M. L., Vermeulen, M., Bonaldi, T., Cox, J., Moroder, L., & Mann, M. (2008) · Nature Methods · doi:10.1038/nmeth0608-459 · Cited by 287
Kelstrup, C. D., Young, C., Lavallee, R. J., Nielsen, M. L., & Olsen, J. V. (2012) · Journal of Proteome Research · doi:10.1021/pr3000249 · Cited by 285
Didangelos, A., Yin, X., Mandal, K., Saje, A., Smith, A., Xu, Q., Jahangiri, M., & Mayr, M. (2011) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m111.008128 · Cited by 285
OTULIN Restricts Met1-Linked Ubiquitination to Control Innate Immune Signaling
Fiil, B. K., Damgaard, R. B., Wagner, S., Keusekotten, K., Fritsch, M., Bekker‐Jensen, S., Mailand, N., Choudhary, C., Komander, D., & Gyrd‐Hansen, M. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.06.004 · Cited by 275
Self-citationStructural Basis for Recognition of Diubiquitins by NEMO
Lo, Y.-C., Lin, S., Rospigliosi, C. C., Conze, D. B., Wu, C.-J., Ashwell, J. D., Eliezer, D., & Wu, H. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.01.012 · Cited by 257
Antigen Receptor Signaling to NF- B via CARMA1, BCL10, and MALT1Preprint
Thome, M., Charton, J. E., Pelzer, C., & Hailfinger, S. (2010) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a003004 · Cited by 241
A20 Negatively Regulates T Cell Receptor Signaling to NF-κB by Cleaving Malt1 Ubiquitin Chains
Düwel, M., Welteke, V., Oeckinghaus, A., Baens, M., Kloo, B., Ferch, U., Darnay, B. G., Ruland, J., Marynen, P., & Krappmann, D. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0803313 · Cited by 233
Firefly luciferase mutants as sensors of proteome stress
Gupta, R., Kasturi, P., Bracher, A., Loew, C., Zheng, M., Villella, A., Garza, D., Hartl, F. U., & Raychaudhuri, S. (2011) · Nature Methods · doi:10.1038/nmeth.1697 · Cited by 219
Self-citationDifferential modification of Ras proteins by ubiquitination.
Jura, N., Scotto–Lavino, E., Sobczyk, A., & Bar-Sagi, D. (2006) · Molecules and Cells · doi:10.1016/j.molcel.2006.02.011 · Cited by 219
Linear ubiquitin chains: NF-κB signalling, cell death and beyond
Iwaï, K., Fujita, H., & Sasaki, Y. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3836 · Cited by 215
Burst-enhancing role of the IgG membrane tail as a molecular determinant of memory
Martin, S. W., & Goodnow, C. C. (2002) · Nature Immunology · doi:10.1038/ni752 · Cited by 214
Hayakawa, S., Shiratori, S., Yamato, H., Kameyama, T., Kitatsuji, C., Kashigi, F., Goto, S., Kameoka, S., Fujikura, D., Yamada, T., et al. (2010) · Nature Immunology · doi:10.1038/ni.1963 · Cited by 214
Singh, D. K., Kumar, D., Siddiqui, Z., Basu, S. K., Kumar, V., & Rao, K. V. S. (2005) · Cell · doi:10.1016/j.cell.2005.02.036 · Cited by 206
The ubiquitin ligase Peli1 negatively regulates T cell activation and prevents autoimmunity
Chang, M., Jin, W., Chang, J., Xiao, Y., Brittain, G. C., Yu, J., Zhou, X., Wang, Y.-H., Cheng, X., Li, P., et al. (2011) · Nature Immunology · doi:10.1038/ni.2090 · Cited by 205
MEF2B mutations lead to deregulated expression of the oncogene BCL6 in diffuse large B cell lymphoma
Ying, C. Y., Dominguez-Sola, D., Fabi, M., Lorenz, I. C., Hussein, S., Bansal, M., Califano, A., Pasqualucci, L., Basso, K., & Dalla‐Favera, R. (2013) · Nature Immunology · doi:10.1038/ni.2688 · Cited by 203
Mahrour, N., Redwine, W. B., Florens, L., Swanson, S. K., Martin-Brown, S., Bradford, W. D., Staehling-Hampton, K., Washburn, M. P., Conaway, R. C., & Conaway, J. W. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m706987200 · Cited by 196
Ubiquitination of K-Ras Enhances Activation and Facilitates Binding to Select Downstream Effectors
Sasaki, A. T., Carracedo, A., Locasale, J. W., Anastasiou, D., Takeuchi, K., Kahoud, E. R., Haviv, S., Asara, J. M., Pandolfi, P. P., & Cantley, L. C. (2011) · Science Signaling · doi:10.1126/scisignal.2001518 · Cited by 182
A Distinct Signaling Pathway Used by the IgG-Containing B Cell Antigen Receptor
Wakabayashi, C., Adachi, T., Wienands, J., & Tsubata, T. (2002) · Science · doi:10.1126/science.1076963 · Cited by 177
Wilker, P. R., Kohyama, M., Sandau, M. M., Albring, J. C., Nakagawa, O., Schwarz, J. J., & MURPHY, K. M. M. (2008) · Nature Immunology · doi:10.1038/ni.1609 · Cited by 176
Structure of the Rab7:REP-1 Complex
Rak, A., Pylypenko, O., Niculae, A., Pyatkov, K. I., Goody, R. S., & Alexandrov, K. A. (2004) · Cell · doi:10.1016/j.cell.2004.05.017 · Cited by 164
Rab7: roles in membrane trafficking and disease
Zhang, M., Chen, L., Wang, S., & Wang, T. (2009) · Bioscience Reports · doi:10.1042/bsr20090032 · Cited by 157
McKEAN, D. J., Infante, A. J., Nilson, A. E., Kimoto, M., Fathman, C. G., Walker, E., & Warner, N. L. (1981) · The Journal of Experimental Medicine · doi:10.1084/jem.154.5.1419 · Cited by 150
Yang, Y., Schmitz, R., Mitala, J., Whiting, A., Xiao, W., Ceribelli, M., Wright, G. W., Zhao, H., Yang, Y., Xu, W., et al. (2014) · Cancer Discovery · doi:10.1158/2159-8290.cd-13-0915 · Cited by 146
Essential Role for IκB Kinase β in Remodeling Carma1-Bcl10-Malt1 Complexes upon T Cell Activation
Wegener, E., Oeckinghaus, A., Papadopoulou, N., Lavitas, L.-M., Schmidt‐Supprian, M., Ferch, U., Mak, T. W., Ruland, J., Heissmeyer, V., & Krappmann, D. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.05.027 · Cited by 141
Rigbolt, K. T. G., Vanselow, J. T., & Blagoev, B. (2011) · Molecular & Cellular Proteomics · doi:10.1074/mcp.o110.007450 · Cited by 138
NEMO recognition of ubiquitinated Bcl10 is required for T cell receptor-mediated NF-κB activation
Wu, C.-J., & Ashwell, J. D. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0712313105 · Cited by 137
Defective immune responses in mice lacking LUBAC‐mediated linear ubiquitination in B cells
Sasaki, Y., Sano, S., Nakahara, M., Murata, S., Kometani, K., Aiba, Y., Sakamoto, S., Watanabe, Y., Tanaka, K., Kurosaki, T., et al. (2013) · The EMBO Journal · doi:10.1038/emboj.2013.184 · Cited by 133
Taniguchi, K., Kohno, R.-I., Ayada, T., Kato, R., Ichiyama, K., Morisada, T., Oike, Y., Yonemitsu, Y., Maehara, Y., & Yoshimura, A. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.01600-06 · Cited by 132
B Cell Developmental Requirement for the G α i2 Gene
Dalwadi, H. N., Wei, B., Schrage, M. I., Su, T. T., Rawlings, D. J., & Braun, J. G. (2003) · The Journal of Immunology · doi:10.4049/jimmunol.170.4.1707 · Cited by 126
Integrating and annotating the interactome using the MiMI plugin for cytoscape
Gao, J., Ade, A. S., Tarcea, V. G., Weymouth, T. E., Mirel, B. R., Jagadish, H. V., & States, D. J. (2008) · Bioinformatics · doi:10.1093/bioinformatics/btn501 · Cited by 125
Unconventional post-translational modifications in immunological signaling
Mowen, K. A., & David, M. (2014) · Nature Immunology · doi:10.1038/ni.2873 · Cited by 124
Disease mutations in Rab7 result in unregulated nucleotide exchange and inappropriate activation
McCray, B. A., Skordalakes, E., & Taylor, J. P. (2009) · Human Molecular Genetics · doi:10.1093/hmg/ddp567 · Cited by 119
Groß, O., Grupp, C., Steinberg, C., Zimmermann, S., Strasser, D., Hannesschläger, N., Reindl, W., Jonsson, A. H., Huo, H., Littman, D. R., et al. (2008) · Blood · doi:10.1182/blood-2007-11-123513 · Cited by 117
Marion, S., Mazzolini, J., Herit, F., Bourdoncle, P., Kambou-Pene, N., Hailfinger, S., Sachse, M., Ruland, J., Benmerah, A., Échard, A., et al. (2012) · Developmental Cell · doi:10.1016/j.devcel.2012.09.021 · Cited by 97
Kensche, T., Tokunaga, F., Ikeda, F., Gotō, E., Iwaï, K., & Đikić, I. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.347195 · Cited by 97
B cell receptor signaling and autoimmunity
Hasler, P., & Zouali, M. (2001) · The FASEB Journal · doi:10.1096/fj.00-0860rev · Cited by 86
Murine Models of B-Cell Lymphomas: Promising Tools for Designing Cancer Therapies
Donnou, S., Galand, C., Touitou, V., Sautès‐Fridman, C., Fábry, Z., & Fisson, S. (2012) · Advances in Hematology · doi:10.1155/2012/701704 · Cited by 73
Krøll, J., Shi, X., Caprioli, A., Liu, H.-H., Waskow, C., Lin, K.-M., Miyazaki, T., Rodewald, H.-R., & Sato, T. N. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.19.8531-8540.2005 · Cited by 73
A Novel Mechanism for TNFR-Associated Factor 6-Dependent CD40 Signaling
Rowland, S. L., Tremblay, M. M., Ellison, J. M., Stunz, L. L., Bishop, G. A., & Hostager, B. S. (2007) · The Journal of Immunology · doi:10.4049/jimmunol.179.7.4645 · Cited by 67
Self-citationConvergence of Ubiquitylation and Phosphorylation Signaling in Rapamycin-treated Yeast Cells
Iešmantavičius, V., Weinert, B. T., & Choudhary, C. (2014) · Molecular & Cellular Proteomics · doi:10.1074/mcp.o113.035683 · Cited by 61
Self-citationEngagement of the B-cell antigen receptor activates STAT through Lyn in a Jak-independent pathway
Wang, L., Kurosaki, T., & Corey, S. J. (2006) · Oncogene · doi:10.1038/sj.onc.1210092 · Cited by 57
DUB-Resistant Ubiquitin to Survey Ubiquitination Switches in Mammalian Cells
Békés, M., Okamoto, K., Crist, S. B., Jones, M. V., Chapman, J. R., Brasher, B. B., Melandri, F. D., Ueberheide, B. M., Denchi, E. L., & Huang, T. T. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.10.008 · Cited by 51
Tanno, H., Yamaguchi, T., Goto, E., Ishido, S., & Komada, M. (2012) · Molecular Biology of the Cell · doi:10.1091/mbc.e11-09-0817 · Cited by 44
Impaired B Cell Development and Function in the Absence of IκBNS
Touma, M., Keskin, D. B., 白木, 文., Saito, I., Koyasu, S., Reinherz, E. L., & Clayton, L. K. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1002109 · Cited by 43
Targeting the B-cell receptor signaling pathway in B lymphoid malignancies
Buchner, M., & Müschen, M. (2014) · Current Opinion in Hematology · doi:10.1097/moh.0000000000000048 · Cited by 42
Phosphorylation of Bcl10 Negatively Regulates T-Cell Receptor-Mediated NF-κB Activation
Zeng, H., Di, L., Fu, G., Chen, Y., Gao, X., Xu, L., Lin, X., & Wen, R. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.01645-06 · Cited by 39
Signaling-mediated control of ubiquitin ligases in endocytosis
Polo, S. (2012) · BMC Biology · doi:10.1186/1741-7007-10-25 · Cited by 38
HOIL-1L Interacting Protein (HOIP) Is Essential for CD40 Signaling
Hostager, B. S., Kashiwada, M., Colgan, J. D., & Rothman, P. B. (2011) · PLoS ONE · doi:10.1371/journal.pone.0023061 · Cited by 35
Self-citation
Flagged first, then by citations
Cited by
Sorted by citations
Phosphoproteomics reveals that Parkinson's disease kinase LRRK2 regulates a subset of Rab GTPases
Steger, M., Tonelli, F., Ito, G., Davies, P., Trost, M., Vetter, M., Wachter, S., Lorentzen, E., Duddy, G., Wilson, S., et al. (2016) · eLife · doi:10.7554/elife.12813 · Cited by 1,042
Steger, M., Diez, F., Dhekne, H. S., Lis, P., Nirujogi, R. S., Karayel, O., Tonelli, F., Martinez, T. N., Lorentzen, E., Pfeffer, S. R., et al. (2017) · eLife · doi:10.7554/elife.31012 · Cited by 482
The deubiquitinase OTULIN is an essential negative regulator of inflammation and autoimmunity
Damgaard, R. B., Walker, J. A., Marco-Casanova, P., Morgan, N. V., Titheradge, H. L., Elliott, P. R., McHale, D., Maher, E. R., McKenzie, A. N. J., & Komander, D. (2016) · Cell · doi:10.1016/j.cell.2016.07.019 · Cited by 348
The Other Function: Class II-Restricted Antigen Presentation by B Cells
Adler, L. N., Jiang, W., Bhamidipati, K., Millican, M., Macaubas, C., Hung, S.-C., & Mellins, E. (2017) · Frontiers in Immunology · doi:10.3389/fimmu.2017.00319 · Cited by 159
Cytoskeletal control of B cell responses to antigens
Tolar, P. (2017) · Nature reviews. Immunology · doi:10.1038/nri.2017.67 · Cited by 153
Self-citation
Metadata
- Authors
- Satpathy, S., Wagner, S. A., Beli, P., Gupta, R., Kristiansen, T. A., Malinova, D., Francavilla, C., Tolar, P., Bishop, G. A., Hostager, B. S., & Choudhary, C.
- Affiliations
- University of Copenhagen (DK)
- National Institute for Medical Research (GB)
- University of Iowa (US)
- Corresponding author
- Choudhary, Chunaram
- ORCID
- Venue
- Molecular Systems Biology
- Published
- 2015-06-01
- Volume
- 11
- Issue
- 6
- Pages
- 810-810
- ISSN
- 1744-4292 (ISSN-L)
- PMC
- PMC4501846
- OpenAlex
- W1894912312
- Cited by
- 124
- References
- 92
- Citations by year
- 2026: 3 · 2025: 3 · 2024: 9 · 2023: 10 · 2022: 9 · 2021: 17 · 2020: 19 · 2019: 7 · 2018: 14 · 2017: 15 · 2016: 16 · 2015: 2
- FWCI
- 5.18
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Molecular Systems Biology (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Research at the University of Copenhagen (University of Copenhagen) (publishedVersion, other-oa)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
- Figshare (submittedVersion, cc-by)
- Research Explorer (The University of Manchester) (submittedVersion)
- Funders
- EMBO long‐term Fellowship
- Novo Nordisk Foundation (NNF14CC0001)
- EMBO Young Investigator Program
- Sapere Aude Program
- Danish Council for Independent Research
- Biological Sciences Funding Program
- Medical Research Council UK (U117597138)
- LOEWE Program Ubiquitin Networks (Ub‐Net) of the State of Hesse
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › NF-κB Signaling Pathways
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Life Sciences › Immunology and Microbiology › Immunology › T-cell and B-cell Immunology
- Keywords
- B cell receptor signaling, signalosome, tyrosine phosphorylation, ubiquitination, LUBAC, Rab7, BCL10, NF-κB signaling, B cell development
- MeSH terms
- B-Cell CLL-Lymphoma 10 Protein, B-Lymphocytes, HeLa Cells, Humans, Membrane Proteins, Phosphorylation, Receptors, Antigen, B-Cell, Signal Transduction, NF-kappa B, Proteomics, Ubiquitin-Protein Ligases, Adaptor Proteins, Signal Transducing, Ubiquitination, HEK293 Cells
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