Cited by 395Protein Kinase Regulation and GTPase SignalingUbiquitin and proteasome pathwaysProtein Tyrosine Phosphatases

The DOI matches its Crossref record; 125 of the 126 references it cites were found in a registry or an index.

The Cbl interactome and its functions

Schmidt, Mirko H.H., Dikic, Ivan·2005·Nature Reviews Molecular Cell Biology

DOI 10.1038/nrm1762

Open this paper in CoChat — free account

Abstract

Cbl proteins are ubiquitin ligases and multifunctional adaptor proteins that are implicated in the regulation of signal transduction in various cell types and in response to different stimuli. Cbl-associated proteins can assemble together at a given time or space inside the cell, and such an interactome can form signal competent networks that control many physiological processes. Dysregulation of spatial or temporal constraints in the Cbl interactome results in the development of human pathologies such as immune diseases, diabetes and cancer.

Integrity signals

Registry

Crossref · 10.1038/nrm1762

Cites

125 of 125 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

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?

Cell Signaling by Receptor Tyrosine Kinases
Lemmon, M. A., & Schlessinger, J. (2010) · Cell · doi:10.1016/j.cell.2010.06.011 · Cited by 7,929
Untangling the ErbB signalling network
Yarden, Y., & Sliwkowski, M. X. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35052073 · Cited by 6,974
Cell Signaling by Receptor Tyrosine Kinases
Schlessinger, J. (2000) · Cell · doi:10.1016/s0092-8674(00)00114-8 · Cited by 3,774
Rab proteins as membrane organizers
Zerial, M., & McBride, H. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35052055 · Cited by 3,381
Mechanisms Underlying Ubiquitination
Pickart, C. M. (2001) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.70.1.503 · Cited by 3,184
Themes and variations on ubiquitylation
Weissman, A. M. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35056563 · Cited by 1,507
Protein regulation by monoubiquitin
Hicke, L. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35056583 · Cited by 1,227
Proteolysis: from the lysosome to ubiquitin and the proteasome
Ciechanover, A. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1552 · Cited by 1,133
The Tyrosine Kinase Negative Regulator c-Cbl as a RING-Type, E2-Dependent Ubiquitin-Protein Ligase
Joazeiro, C. A. P., Wing, S. S., Huang, H.-K., Leverson, J. D., Hunter, T. R., & Liu, Y. (1999) · Science · doi:10.1126/science.286.5438.309 · Cited by 1,036
Ubiquitin Ligase Activity and Tyrosine Phosphorylation Underlie Suppression of Growth Factor Signaling by c-Cbl/Sli-1
Levkowitz, G., Waterman, H., Ettenberg, S. A., Katz, M., Tsygankov, A. Y., Alroy, I., Lavi, S., Iwaï, K., Reiss, Y., Ciechanover, A. J., et al. (1999) · Molecular Cell · doi:10.1016/s1097-2765(00)80231-2 · Cited by 1,003

Flagged first, then by citations

Show all 126 references

1 of the 126 references couldn’t be matched to a known paper.

Sorted by citations

Ubiquitination in disease pathogenesis and treatment
Popovic, D., Vucic, D., & Đikić, I. (2014) · Nature Medicine · doi:10.1038/nm.3739 · Cited by 1,443
Post-translational modifications in signal integration
Deribe, Y. L., Pawson, T., & Dikic, I. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1842 · Cited by 876
Ubiquitin-Binding Proteins: Decoders of Ubiquitin-Mediated Cellular Functions
Husnjak, K., & Đikić, I. (2012) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-051810-094654 · Cited by 794
Protein posttranslational modifications in health and diseases: Functions, regulatory mechanisms, and therapeutic implications
Zhong, Q., Xiao, X., Qiu, Y., Xu, Z., Chen, C., Chong, B., Zhao, X., Hai, S., Li, S., An, Z., et al. (2023) · MedComm · doi:10.1002/mco2.261 · Cited by 442
Noonan syndrome and clinically related disorders
Tartaglia, M., Gelb, B. D., & Zenker, M. (2011) · Best Practice & Research Clinical Endocrinology & Metabolism · doi:10.1016/j.beem.2010.09.002 · Cited by 432
Fibroblast growth factor signaling in skeletal development and diseasePreprint
Ornitz, D. M., & Marie, P. J. (2015) · Genes & Development · doi:10.1101/gad.266551.115 · Cited by 419
RINGs of good and evil: RING finger ubiquitin ligases at the crossroads of tumour suppression and oncogenesis
Lipkowitz, S., & Weissman, A. M. (2011) · Nature reviews. Cancer · doi:10.1038/nrc3120 · Cited by 422
Ubiquitin and ubiquitin-like proteins in cancer pathogenesis
Hoeller, D., Hecker, C.-M., & Đikić, I. (2006) · Nature reviews. Cancer · doi:10.1038/nrc1994 · Cited by 423
Gain-of-function of mutated C-CBL tumour suppressor in myeloid neoplasms
Sanada, M., Suzuki, T., Shih, L., Otsu, M., Kato, M., Yamazaki, S., Tamura, A., Honda, H., Sakata‐Yanagimoto, M., Kumano, K., et al. (2009) · Nature · doi:10.1038/nature08240 · Cited by 401
New mutations and pathogenesis of myeloproliferative neoplasms
Vainchenker, W., Delhommeau, F., Constantinescu, S. N., & Bernard, O. (2011) · Blood · doi:10.1182/blood-2011-02-292102 · Cited by 411
Frequent CBL mutations associated with 11q acquired uniparental disomy in myeloproliferative neoplasms
Grand, F., Hidalgo-Curtis, C., Ernst, T., Zoi, K., Zoi, C., McGuire, C., Kreil, S., Jones, A. V., Score, J., Metzgeroth, G., et al. (2009) · Blood · doi:10.1182/blood-2008-12-194548 · Cited by 379
The switchable integrin adhesome
Zaidel‐Bar, R., & Geiger, B. (2010) · Journal of Cell Science · doi:10.1242/jcs.066183 · Cited by 350
The role of ubiquitylation in receptor endocytosis and endosomal sorting
Haglund, K., & Đikić, I. (2012) · Journal of Cell Science · doi:10.1242/jcs.091280 · Cited by 322
Gastric cancer exosomes promote tumour cell proliferation through PI3K/Akt and MAPK/ERK activation
Qu, J.-L., Qu, X.-J., Zhao, M.-F., Teng, Y.-E., Zhang, Y., Hou, K., Jiang, Y.-H., Yang, X., & Liu, Y.-P. (2009) · Digestive and Liver Disease · doi:10.1016/j.dld.2009.04.006 · Cited by 313
The Cbl family proteins: Ring leaders in regulation of cell signaling
Swaminathan, G., & Tsygankov, A. Y. (2006) · Journal of Cellular Physiology · doi:10.1002/jcp.20694 · Cited by 296
Mutations in CBL occur frequently in juvenile myelomonocytic leukemia
Loh, M. L., Sakai, D. S., Flotho, C., Kang, M. W., Fliegauf, M., Archambeault, S., Mullighan, C. G., Chen, L., Bergsträßer, E., Bueso-Ramos, C., et al. (2009) · Blood · doi:10.1182/blood-2009-01-198416 · Cited by 287
Induction of Siglec-G by RNA Viruses Inhibits the Innate Immune Response by Promoting RIG-I Degradation
Chen, W., Han, C., Xie, B., Hu, X., Yu, Q., Shi, L., Wang, Q., Li, D., Wang, J., Zheng, P., et al. (2013) · Cell · doi:10.1016/j.cell.2013.01.011 · Cited by 276
Heterozygous germline mutations in the CBL tumor-suppressor gene cause a Noonan syndrome-like phenotype
Martinelli, S., De Luca, A., Stellacci, E., Rossi, C., Checquolo, S., Lepri, F., Caputo, V., Silvano, M., Buscherini, F., Consoli, F., et al. (2010) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2010.06.015 · Cited by 259
Protein interaction screening by quantitative immunoprecipitation combined with knockdown (QUICK)
Selbach, M., & Mann, M. (2006) · Nature Methods · doi:10.1038/nmeth972 · Cited by 244
Mutations of E3 Ubiquitin Ligase Cbl Family Members Constitute a Novel Common Pathogenic Lesion in Myeloid Malignancies
Makishima, H., Cazzolli, H., Szpurka, H., Dunbar, A. J., Tiu, R. V., Huh, J., Muramatsu, H., O’Keefe, C. L., Hsi, E. D., PAQUETTE, R. L., et al. (2009) · Journal of Clinical Oncology · doi:10.1200/jco.2009.23.7503 · Cited by 223
14-3-3 proteins as potential oncogenes
Tzivion, G., Gupta, V. S., Kaplun, L., & Balan, V. (2006) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2006.03.004 · Cited by 222
Flt3-dependent transformation by inactivating c-Cbl mutations in AML
Sargin, B., Choudhary, C., Crosetto, N., Schmidt, M. H. H., Grundler, R., Rensinghoff, M., Thiessen, C., Tickenbrock, L., Schwäble, J., Brandts, C., et al. (2007) · Blood · doi:10.1182/blood-2007-01-066076 · Cited by 220
Self-citation
Integrative Survival-Based Molecular Profiling of Human Pancreatic Cancer
Donahue, T. R., Tran, L. M., Hill, R., Li, Y., Kovochich, A., Calvopina, J. H., Patel, S. G., Wu, N., Hindoyan, A. A., Farrell, J. J., et al. (2012) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-11-1539 · Cited by 212
Structural basis for autoinhibition and phosphorylation-dependent activation of c-Cbl
Dou, H., Buetow, L., Hock, A., Sibbet, G. J., Vousden, K. H., & Huang, D. T. C. (2012) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2231 · Cited by 216
H19non coding RNA-derived miR-675 enhances tumorigenesis and metastasis of breast cancer cells by downregulating c-Cbl and Cbl-b
Vennin, C., Spruyt, N., Dahmani, F. Z., Julien, S., Bertucci, F., Finetti, P., Chassat, T., Bourette, R. P., Bourhis, X. L., & Adriaenssens, É. (2015) · Oncotarget · doi:10.18632/oncotarget.4976 · Cited by 202
Intra-endosomal membrane traffic
van der Goot, F. G., & Grüenberg, J. (2006) · Trends in Cell Biology · doi:10.1016/j.tcb.2006.08.003 · Cited by 200
When ubiquitination meets phosphorylation: a systems biology perspective of EGFR/MAPK signalling
Nguyen, L. K., Kölch, W., & Kholodenko, B. Ν. (2013) · Cell Communication and Signaling · doi:10.1186/1478-811x-11-52 · Cited by 198
Threshold‐controlled ubiquitination of the EGFR directs receptor fate
Sigismund, S., Algisi, V., Nappo, G., Conte, A., Pascolutti, R., Cuomo, A., Bonaldi, T., Argenzio, E., Verhoef, L. G. G. C., Maspero, E., et al. (2013) · The EMBO Journal · doi:10.1038/emboj.2013.149 · Cited by 172
Recent advances in the pathogenesis and treatment of juvenile myelomonocytic leukaemia
Loh, M. L. (2011) · British Journal of Haematology · doi:10.1111/j.1365-2141.2010.08525.x · Cited by 159
c-Cbl-Mediated Neddylation Antagonizes Ubiquitination and Degradation of the TGF-β Type II Receptor
Zuo, W., Huang, F., Chiang, Y. J., Li, M., Du, J. C., Ding, Y., Zhang, T., Lee, H. W., Jeong, L. S., Chen, Y., et al. (2013) · Molecular Cell · doi:10.1016/j.molcel.2012.12.002 · Cited by 161
Molecular Mechanisms of SH2- and PTB-Domain-Containing Proteins in Receptor Tyrosine Kinase SignalingPreprint
Wagner, M. J., Stacey, M. M., Liu, B. A., & Pawson, T. J. (2013) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a008987 · Cited by 162
Molecular Basis of Signaling Specificity of Insulin and IGF Receptors: Neglected Corners and Recent Advances
Siddle, K. (2012) · Frontiers in Endocrinology · doi:10.3389/fendo.2012.00034 · Cited by 160
Germline mutations of the CBL gene define a new genetic syndrome with predisposition to juvenile myelomonocytic leukaemia
Perez, B., Mechinaud, F. M., Galambrun, C., Romdhane, N. B., Isidor, B., Philip, N., Derain-Court, J., Cassinat, B., Lachenaud, J., Kaltenbach, S., et al. (2010) · Journal of Medical Genetics · doi:10.1136/jmg.2010.076836 · Cited by 149
miR-216a rescues dexamethasone suppression of osteogenesis, promotes osteoblast differentiation and enhances bone formation, by regulating c-Cbl-mediated PI3K/AKT pathway
Li, H., Li, T., Fan, J., Li, T., Fan, L., Wang, S., Weng, X., Han, Q., & Zhao, R. C. (2015) · Cell Death and Differentiation · doi:10.1038/cdd.2015.99 · Cited by 140
Sprouty proteins: modified modulators, matchmakers or missing links?
Guy, G. R., Jackson, R. A., Yusoff, P., & Chow, S. Y. (2009) · Journal of Endocrinology · doi:10.1677/joe-09-0110 · Cited by 130
The Roles of the Ubiquitin–Proteasome System in the Endoplasmic Reticulum Stress Pathway
Qu, J., Zou, T., & Lin, Z. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22041526 · Cited by 133
Proteostatic and Metabolic Control of Stemness
García‐Prat, L., Sousa‐Victor, P., & Muñoz‐Cánoves, P. (2017) · Cell stem cell · doi:10.1016/j.stem.2017.04.011 · Cited by 125
Mutations of an E3 ubiquitin ligase c-Cbl but not TET2 mutations are pathogenic in juvenile myelomonocytic leukemia
Muramatsu, H., Makishima, H., Jankowska, A. M., Cazzolli, H., O’Keefe, C. L., Yoshida, N., Xu, Y., Nishio, N., Hama, A., Yagasaki, H., et al. (2009) · Blood · doi:10.1182/blood-2009-06-226340 · Cited by 115
The E3 ubiquitin ligase c-Cbl restricts development and functions of hematopoietic stem cellsPreprint
Rathinam, C., Thien, C. B. F., Langdon, W. Y., Gu, H., & Flavell, R. A. (2008) · Genes & Development · doi:10.1101/gad.1651408 · Cited by 114
Bedside to bench in juvenile myelomonocytic leukemia: insights into leukemogenesis from a rare pediatric leukemia
Chang, T. Y., Dvorak, C. C., & Loh, M. L. (2014) · Blood · doi:10.1182/blood-2014-03-300319 · Cited by 109
Ubc4/5 and c-Cbl Continue to Ubiquitinate EGF Receptor after Internalization to Facilitate Polyubiquitination and Degradation
Umebayashi, K., Stenmark, H., & Yoshimori, T. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-10-0988 · Cited by 113
Kaposi’s sarcoma-associated herpesvirus interacts with EphrinA2 receptor to amplify signaling essential for productive infection
Chakraborty, S., Veettil, M. V., Bottero, V., & Chandran, B. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1119592109 · Cited by 105
A Restricted Spectrum of Mutations in the SMAD4 Tumor-Suppressor Gene Underlies Myhre Syndrome
Caputo, V., Cianetti, L., Niceta, M., Carta, C., Ciolfi, A., Bocchinfuso, G., Carrani, E., Dentici, M. L., Biamino, E., Belligni, E. F., et al. (2012) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2011.12.011 · Cited by 106
Neutrophil activation via β2 integrins (CD11/CD18): Molecular mechanisms and clinical implications
Schymeinsky, J., Mócsai, A., & Walzog, B. (2007) · Thrombosis and Haemostasis · doi:10.1160/th07-02-0156 · Cited by 105
Abl Tyrosine Kinase Regulates Endocytosis of the Epidermal Growth Factor Receptor
Tanos, B. E., & Pendergast, A. M. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m603126200 · Cited by 103
Molecular Pathways: Cbl Proteins in Tumorigenesis and Antitumor Immunity—Opportunities for Cancer Treatment
Liyasova, M., Ma, K., & Lipkowitz, S. (2014) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-13-2490 · Cited by 102
miR-124-3p functions as a tumor suppressor in breast cancer by targeting CBL
Wang, Y., Chen, L., Wu, Z., Wang, M., Jin, F., Wang, N., Hu, X., Liu, Z., Zhang, C., Zen, K., et al. (2016) · BMC Cancer · doi:10.1186/s12885-016-2862-4 · Cited by 102
Genetic predispositions to childhood leukemia
Stieglitz, E., & Loh, M. L. (2013) · Therapeutic Advances in Hematology · doi:10.1177/2040620713498161 · Cited by 111
Myeloid Leukemia Development in c-Cbl RING Finger Mutant Mice Is Dependent on FLT3 Signaling
Rathinam, C., Thien, C. B. F., Flavell, R. A., & Langdon, W. Y. (2010) · Cancer Cell · doi:10.1016/j.ccr.2010.09.008 · Cited by 104
Essential Role of E3 Ubiquitin Ligase Activity in Cbl-b–Regulated T Cell Functions
Paolino, M., Thien, C. B. F., Gruber, T., Hinterleitner, R., Baier, G., Langdon, W. Y., & Penninger, J. M. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1003390 · Cited by 98
Kaposi’s Sarcoma Associated Herpesvirus Entry into Target Cells
Chakraborty, S., Veettil, M. V., & Chandran, B. (2012) · Frontiers in Microbiology · doi:10.3389/fmicb.2012.00006 · Cited by 94
Quiescence Entry, Maintenance, and Exit in Adult Stem Cells
Mohammad, K., Dakik, P., Medkour, Y., Mitrofanova, D., & Titorenko, V. I. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20092158 · Cited by 94
Modulation of Immune Cell Functions by the E3 Ligase Cbl-b
Lutz‐Nicoladoni, C., Wolf, D. G. F., & Sopper, S. (2015) · Frontiers in Oncology · doi:10.3389/fonc.2015.00058 · Cited by 93
Chemically Diverse Toxicants Converge on Fyn and c-Cbl to Disrupt Precursor Cell Function
Li, Z., Dong, T., Pröschel, C., & Noble, M. (2007) · PLoS Biology · doi:10.1371/journal.pbio.0050035 · Cited by 92
The Multiple Layers of Ubiquitin-Dependent Cell Cycle Control
Wickliffe, K. E., Williamson, A. P., Jin, L., & Rapé, M. (2009) · Chemical Reviews · doi:10.1021/cr800414e · Cited by 91
Interaction of KSHV with Host Cell Surface Receptors and Cell Entry
Veettil, M. V., Bandyopadhyay, C., Dutta, D., & Chandran, B. (2014) · Viruses · doi:10.3390/v6104024 · Cited by 83
c-Cbl-Dependent Monoubiquitination and Lysosomal Degradation of gp130
Tanaka, Y., Tanaka, N., Saeki, Y., Tanaka, K., Murakami, M., Hirano, T., Ishii, N., & Sugamura, K. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.01784-07 · Cited by 82
EGFR Trafficking in Physiology and Cancer
Caldieri, G., Malabarba, M. G., Fiore, P. P. D., & Sigismund, S. (2018) · Progress in molecular and subcellular biology · doi:10.1007/978-3-319-96704-2_9 · Cited by 85
Quantitative analysis reveals how EGFR activation and downregulation are coupled in normal but not in cancer cells
Capuani, F., Conte, A., Argenzio, E., Marchetti, L., Priami, C., Polo, S., Fiore, P. P. D., Sigismund, S., & Ciliberto, A. (2015) · Nature Communications · doi:10.1038/ncomms8999 · Cited by 79
Association with HSP90 Inhibits Cbl-Mediated Down-regulation of Mutant Epidermal Growth Factor Receptors
Yang, S., Qu, S., Perez-Tores, M., Sawai, A., Rosen, N. X., Solit, D. B., & Arteaga, C. L. (2006) · Cancer Research · doi:10.1158/0008-5472.can-06-1042 · Cited by 81
E3 ubiquitin ligase-mediated regulation of bone formation and tumorigenesis
Sévère, N., Dieudonné, F., & Pj, M. (2013) · Cell Death and Disease · doi:10.1038/cddis.2012.217 · Cited by 80
Ubiquitin-dependent regulation of G protein-coupled receptor trafficking and signaling
Marchese, A., & Trejo, J. (2012) · Cellular Signalling · doi:10.1016/j.cellsig.2012.11.024 · Cited by 83
Cytoplasmic Relaxation of Active Eph Controls Ephrin Shedding by ADAM10
Janes, P. W., Wimmer-Kleikamp, S. H., Frangakis, A. S., Treble, K., Griesshaber, B., Sabet, O., Grabenbauer, M., Ting, A. Y., Säftig, P., Bastiaens, P. I. H., et al. (2009) · PLoS Biology · doi:10.1371/journal.pbio.1000215 · Cited by 78
Epigenome-wide association study of rheumatoid arthritis identifies differentially methylated loci in B cells
Julià, A., Absher, D., Lasanta, M. L., Palau, N., Pluma, A., Jones, L. W., Glossop, J. R., Farrell, W. E., Myers, R., & Marsal, S. (2017) · Human Molecular Genetics · doi:10.1093/hmg/ddx177 · Cited by 79
Genetic and epigenetic alterations of myeloproliferative disorders
Feenstra, J. D. M., & Královics, R. (2012) · International Journal of Hematology · doi:10.1007/s12185-012-1235-2 · Cited by 81
A TNF- and c-Cbl-dependent FLIPS-degradation pathway and its function in Mycobacterium tuberculosis–induced macrophage apoptosis
Kundu, M., Pathak, S. K., Kumawat, K., Basu, S., Chatterjee, G., Pathak, S., Noguchi, T., Takeda, K., Ichijo, H., Thien, C. B. F., et al. (2009) · Nature Immunology · doi:10.1038/ni.1754 · Cited by 74
Bag1 directly routes immature BCR-ABL for proteasomal degradation
Tsukahara, F., & Maru, Y. (2010) · Blood · doi:10.1182/blood-2009-10-249623 · Cited by 75
Interaction of c-Cbl with Myosin IIA Regulates Bleb Associated Macropinocytosis of Kaposi's Sarcoma-Associated Herpesvirus
Veettil, M. V., Sadagopan, S., Kerur, N., Chakraborty, S., & Chandran, B. (2010) · PLoS Pathogens · doi:10.1371/journal.ppat.1001238 · Cited by 71
From T‐cell activation signals to signaling control of anti‐cancer immunity
Cronin, S. J. F., & Penninger, J. M. (2007) · Immunological Reviews · doi:10.1111/j.1600-065x.2007.00570.x · Cited by 73
c-Cbl targets PD-1 in immune cells for proteasomal degradation and modulates colorectal tumor growth
Lyle, C., Richards, S., Yasuda, K., Napoleon, M. A., Walker, J., Arinze, N. V., Belghasem, M., Vellard, I., Yin, W., Ravid, J. D., et al. (2019) · Scientific Reports · doi:10.1038/s41598-019-56208-1 · Cited by 72
Roles of E3 ubiquitin ligases in cell adhesion and migration
Huang, C. (2010) · Cell Adhesion & Migration · doi:10.4161/cam.4.1.9834 · Cited by 72
c-Cbl, a Ubiquitin E3 Ligase That Targets Active β-Catenin
Chitalia, V. C., Shivanna, S., Martorell, J., Meyer, R., Edelman, E. R., & Rahimi, N. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.473801 · Cited by 69
KSHV Entry and Trafficking in Target Cells—Hijacking of Cell Signal Pathways, Actin and Membrane Dynamics
Kumar, B., & Chandran, B. (2016) · Viruses · doi:10.3390/v8110305 · Cited by 69
Non-proteolytic ubiquitylation in cellular signaling and human disease
Liao, Y., Sumara, I., & Pangou, E. (2022) · Communications Biology · doi:10.1038/s42003-022-03060-1 · Cited by 68
Whole-exome analysis reveals novel somatic genomic alterations associated with outcome in immunochemotherapy-treated diffuse large B-cell lymphoma
Novak, A. J., Asmann, Y. W., Maurer, M. J., Wang, C., Slager, S. L., Hodge, L. S., Manske, M. K., Price-Troska, T. L., Yang, Z.-Z., Zimmermann, M. T., et al. (2015) · Blood Cancer Journal · doi:10.1038/bcj.2015.69 · Cited by 68
Structural basis for a novel intrapeptidyl H‐bond and reverse binding of c‐Cbl‐TKB domain substrates
Ng, C., Jackson, R. A., Buschdorf, J. P., Sun, Q., Guy, G. R., & Sivaraman, J. (2008) · The EMBO Journal · doi:10.1038/emboj.2008.18 · Cited by 66
Intersectin Regulates Epidermal Growth Factor Receptor Endocytosis, Ubiquitylation, and Signaling
Martin, N. P., Mohney, R. P., Dunn, S., Das, M., Scappini, E., & O’Bryan, J. P. (2006) · Molecular Pharmacology · doi:10.1124/mol.106.028274 · Cited by 66
Fbxw7 Controls Angiogenesis by Regulating Endothelial Notch Activity
Izumi, N., Helker, C. S., Ehling, M., Behrens, A., Herzog, W., & Adams, R. H. (2012) · PLoS ONE · doi:10.1371/journal.pone.0041116 · Cited by 65
JAK2V617F and beyond: role of genetics and aberrant signaling in the pathogenesis of myeloproliferative neoplasms
Oh, S. T., & Gotlib, J. R. (2010) · Expert Review of Hematology · doi:10.1586/ehm.10.28 · Cited by 67
Ligand-induced EpoR internalization is mediated by JAK2 and p85 and is impaired by mutations responsible for primary familial and congenital polycythemia
Sulahian, R., Cleaver, O. B., & Huang, L. J.-S. (2009) · Blood · doi:10.1182/blood-2008-09-179572 · Cited by 64
CIN85, a Cbl‐interacting protein, is a component of AMAP1‐mediated breast cancer invasion machinery
Nam, J., Onodera, Y., Mazaki, Y., Miyoshi, H., Hashimoto, S., & Sabe, H. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601534 · Cited by 64
UBASH3B/Sts-1-CBL axis regulates myeloid proliferation in human preleukemia induced by AML1-ETO
Goyama, S., Schibler, J., Gasilina, A., Shrestha, M., Lin, S., Link, K. A., Chen, J., Whitman, S. P., Bloomfield, C. D., Nicolet, D., et al. (2015) · Leukemia · doi:10.1038/leu.2015.275 · Cited by 64
Characterization of Multiple Multivesicular Body Sorting Determinants within Sna3: A Role for the Ubiquitin Ligase Rsp5
Oestreich, A. J., Aboian, M., Lee, J. R. E., Azmi, I. F., Payne, J. A., Issaka, R. B., Davies, B. A., & Katzmann, D. J. (2006) · Molecular Biology of the Cell · doi:10.1091/mbc.e06-08-0680 · Cited by 64
Clonal Hematopoiesis: Somatic Mutations in Blood Cells and Atherosclerosis
Natarajan, P., Jaiswal, S., & Kathiresan, S. (2018) · Circulation Genomic and Precision Medicine · doi:10.1161/circgen.118.001926 · Cited by 63
Upregulation of E3 Ubiquitin Ligase CBLC Enhances EGFR Dysregulation and Signaling in Lung Adenocarcinoma
Hong, S., Kao, Y.-R., Lee, T., & Wu, C. (2018) · Cancer Research · doi:10.1158/0008-5472.can-17-3858 · Cited by 63
RIN1 orchestrates the activation of RAB5 GTPases and ABL tyrosine kinases to determine the fate of EGFR
Balaji, K., Mooser, C. K., Janson, C., Bliss, J. M., Hojjat, H., & Colicelli, J. (2012) · Journal of Cell Science · doi:10.1242/jcs.113688 · Cited by 64
Cbl-b in T-cell activation
Paolino, M., & Penninger, J. M. (2010) · Seminars in Immunopathology · doi:10.1007/s00281-010-0197-9 · Cited by 61
Molecular basis of juvenile myelomonocytic leukemia
de Vries, A. C. H., Zwaan, C. M., & van den Heuvel‐Eibrink, M. M. (2010) · Haematologica · doi:10.3324/haematol.2009.016865 · Cited by 60
Proteomic snapshot of the EGF‐induced ubiquitin network
Argenzio, E., Bange, T., Oldrini, B., Bianchi, F., Peesari, R., Mari, S., Fiore, P. P. D., Mann, M., & Polo, S. (2011) · Molecular Systems Biology · doi:10.1038/msb.2010.118 · Cited by 59
Advances in the Genetics of High-Risk Childhood B-Progenitor Acute Lymphoblastic Leukemia and Juvenile Myelomonocytic Leukemia: Implications for Therapy
Loh, M. L., & Mullighan, C. G. (2012) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-11-1936 · Cited by 59
INTERSECTINg Pathways in Cell Biology
O’Bryan, J. P. (2010) · Science Signaling · doi:10.1126/scisignal.3152re10 · Cited by 65
Macromolecular juggling by ubiquitylation enzymes
Lorenz, S., Cantor, A. J., Rapé, M., & Kuriyan, J. (2013) · BMC Biology · doi:10.1186/1741-7007-11-65 · Cited by 57
c-Cbl Inhibition Improves Cardiac Function and Survival in Response to Myocardial Ischemia
Rafiq, K., Kolpakov, M. A., Seqqat, R., Guo, J., Guo, X., Zhao, Q., Yu, D., Mohapatra, B. C., Zutshi, N., An, W., et al. (2014) · Circulation · doi:10.1161/circulationaha.113.007004 · Cited by 57
FGFR2-Cbl interaction in lipid rafts triggers attenuation of PI3K/Akt signaling and osteoblast survival
Dufour, C., Guénou, H., Kaabeche, K., Bouvard, D., Sanjay, A., & Marie, P. J. (2008) · Bone · doi:10.1016/j.bone.2008.02.009 · Cited by 56
ANXA1 Binds and Stabilizes EphA2 to Promote Nasopharyngeal Carcinoma Growth and Metastasis
Feng, J., Lu, S., Xiao, T., Huang, W. C., Yi, H. L., Zhu, W., Fan, S., Feng, X., Li, J.-Y., Yu, Z.-Z., et al. (2020) · Cancer Research · doi:10.1158/0008-5472.can-20-0560 · Cited by 56
K63-linked ubiquitin chains are a global signal for endocytosis and contribute to selective autophagy in plants
Saeed, B., Deligne, F., Brillada, C., Dünser, K., Ditengou, F. A., Turek, I., Allahham, A., Grujic, N., Dagdas, Y., Ott, T., et al. (2023) · Current Biology · doi:10.1016/j.cub.2023.02.024 · Cited by 56
Rapidly fatal myeloproliferative disorders in mice with deletion of Casitas B-cell lymphoma (Cbl) and Cbl-b in hematopoietic stem cells
Naramura, M., Nandwani, N., Gu, H., Band, V., & Band, H. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1007575107 · Cited by 55
ESCRT and Membrane Protein Ubiquitination
Migliano, S. M., & Teis, D. (2018) · Progress in molecular and subcellular biology · doi:10.1007/978-3-319-96704-2_4 · Cited by 58
CTEN Prolongs Signaling by EGFR through Reducing Its Ligand-Induced Degradation
Hong, S., Shih, Y.-P., Li, T., Carraway, K. L., & Lo, S. H. (2013) · Cancer Research · doi:10.1158/0008-5472.can-12-4441 · Cited by 54
Ubiquitylation in immune disorders and cancer: from molecular mechanisms to therapeutic implications
Fulda, S., Rajalingam, K., & Đikić, I. (2012) · EMBO Molecular Medicine · doi:10.1002/emmm.201100707 · Cited by 57

Authors: Schmidt, M. H. H., & Dikic, I.
Affiliations: Goethe University Frankfurt (DE)
ORCID: Schmidt, Mirko H.H.
Venue: Nature Reviews Molecular Cell Biology
Publisher: Springer Science and Business Media LLC
Published: 2005-10-14
Volume: 6
Issue: 12
Pages: 907-919
ISSN: 1471-0072 (ISSN-L)
1471-0080
DOI: 10.1038/nrm1762
OpenAlex: W2059037016
Cited by: 395
References: 126
Citations by year: 2026: 6 · 2025: 8 · 2024: 8 · 2023: 15 · 2022: 15 · 2021: 9 · 2020: 11 · 2019: 10 · 2018: 12 · 2017: 13 · 2016: 21 · 2015: 23 · 2014: 24 · 2013: 34 · 2012: 38
FWCI: 1.54
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
Locations: Nature Reviews Molecular Cell Biology (publishedVersion)
PubMed (publishedVersion)
Funders: European Molecular Biology Organization
Deutsche Forschungsgemeinschaft
Boehringer Ingelheim Stiftung
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
Keywords: ubiquitin ligase, protein-protein interaction network, adaptor proteins, signal transduction regulation, protein complex formation, immune disorders, diabetes mellitus, cancer
MeSH terms: Actins, Animals, Endocytosis, Humans, Lymphocytes, Signal Transduction, Receptor Protein-Tyrosine Kinases, Multiprotein Complexes, Proto-Oncogene Proteins c-cbl

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

The Cbl interactome and its functions

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks