“The Cbl interactome and its functions”. Nat. Rev. Mol. Cell Biol.6 (12): 907–18. (2005). doi:10.1038/nrm1762. PMID16227975.
“Regulation of Cbl phosphorylation by the Abl tyrosine kinase and the Nck SH2/SH3 adaptor”. Oncogene20 (30): 4058–69. (July 2001). doi:10.1038/sj.onc.1204528. PMID11494134.
“The Cbl proteins are binding partners for the Cool/Pix family of p21-activated kinase-binding proteins”. FEBS Lett.550 (1–3): 119–23. (August 2003). doi:10.1016/S0014-5793(03)00853-6. PMID12935897.
“The endophilin-CIN85-Cbl complex mediates ligand-dependent downregulation of c-Met”. Nature416 (6877): 187–90. (March 2002). doi:10.1038/416187a. PMID11894096.
“Recruitment of Pyk2 and Cbl to lipid rafts mediates signals important for actin reorganization in growing neurites”. J. Cell Sci.117 (Pt 12): 2557–68. (May 2004). doi:10.1242/jcs.01148. PMID15128873.
“The adapter type protein CMS/CD2AP binds to the proto-oncogenic protein c-Cbl through a tyrosine phosphorylation-regulated Src homology 3 domain interaction”. J. Biol. Chem.276 (7): 4957–63. (February 2001). doi:10.1074/jbc.M005784200. PMID11067845.
“CD2AP/CMS regulates endosome morphology and traffic to the degradative pathway through its interaction with Rab4 and c-Cbl”. Traffic4 (2): 97–112. (February 2003). doi:10.1034/j.1600-0854.2003.40205.x. PMID12559036.
“c-Cbl associates directly with the C-terminal tail of the receptor for the macrophage colony-stimulating factor, c-Fms, and down-modulates this receptor but not the viral oncogene v-Fms”. J. Biol. Chem.277 (17): 14635–40. (April 2002). doi:10.1074/jbc.M109214200. PMID11847211.
“Interleukin-2 stimulation induces tyrosine phosphorylation of p120-Cbl and CrkL and formation of multimolecular signaling complexes in T lymphocytes and natural killer cells”. J. Biol. Chem.273 (7): 3986–93. (February 1998). doi:10.1074/jbc.273.7.3986. PMID9461587.
“CSF-1 stimulation induces the formation of a multiprotein complex including CSF-1 receptor, c-Cbl, PI 3-kinase, Crk-II and Grb2”. Oncogene14 (19): 2331–8. (May 1997). doi:10.1038/sj.onc.1201074. PMID9178909.
“Cbl functions downstream of Src kinases in Fc gamma RI signaling in primary human macrophages”. J. Leukoc. Biol.65 (4): 523–34. (April 1999). doi:10.1002/jlb.65.4.523. PMID10204582.
“The involvement of the proto-oncogene p120 c-Cbl and ZAP-70 in CD2-mediated T cell activation”. Int. Immunol.13 (1): 13–22. (January 2001). doi:10.1093/intimm/13.1.13. PMID11133830.
“c-Cbl is involved in Met signaling in B cells and mediates hepatocyte growth factor-induced receptor ubiquitination”. J. Immunol.169 (7): 3793–800. (October 2002). doi:10.4049/jimmunol.169.7.3793. PMID12244174.
“Steel factor induces tyrosine phosphorylation of CRKL and binding of CRKL to a complex containing c-kit, phosphatidylinositol 3-kinase, and p120(CBL)”. J. Biol. Chem.272 (15): 10248–53. (April 1997). doi:10.1074/jbc.272.15.10248. PMID9092574.
“Differential signaling after beta1 integrin ligation is mediated through binding of CRKL to p120(CBL) and p110(HEF1)”. J. Biol. Chem.272 (22): 14320–6. (May 1997). doi:10.1074/jbc.272.22.14320. PMID9162067.
“Erythropoietin and IL-3 induce tyrosine phosphorylation of CrkL and its association with Shc, SHP-2, and Cbl in hematopoietic cells”. Biochem. Biophys. Res. Commun.239 (2): 412–7. (October 1997). doi:10.1006/bbrc.1997.7480. PMID9344843.
“EGF-dependent association of phospholipase C-gamma1 with c-Cbl”. Exp. Cell Res.277 (1): 86–94. (July 2002). doi:10.1006/excr.2002.5545. PMID12061819.
“Coordinated regulation of the tyrosine phosphorylation of Cbl by Fyn and Syk tyrosine kinases”. J. Biol. Chem.273 (15): 8867–74. (April 1998). doi:10.1074/jbc.273.15.8867. PMID9535867.
“Tyrosine phosphorylation of p120cbl in BCR/abl transformed hematopoietic cells mediates enhanced association with phosphatidylinositol 3-kinase”. Oncogene14 (18): 2217–28. (May 1997). doi:10.1038/sj.onc.1201049. PMID9174058.
“Gads is a novel SH2 and SH3 domain-containing adaptor protein that binds to tyrosine-phosphorylated Shc”. Oncogene17 (24): 3073–82. (December 1998). doi:10.1038/sj.onc.1202337. PMID9872323.
“The proto-oncogene p120(Cbl) is a downstream substrate of the Hck protein-tyrosine kinase”. Biochem. Biophys. Res. Commun.257 (1): 129–38. (April 1999). doi:10.1006/bbrc.1999.0427. PMID10092522.
“Identification of c-Cbl as a new ligase for insulin-like growth factor-I receptor with distinct roles from Mdm2 in receptor ubiquitination and endocytosis”. Cancer Res.68 (14): 5669–77. (July 2008). doi:10.1158/0008-5472.CAN-07-6364. PMID18632619.
“p85 subunit of PI3 kinase does not bind to human Flt3 receptor, but associates with SHP2, SHIP, and a tyrosine-phosphorylated 100-kDa protein in Flt3 ligand-stimulated hematopoietic cells”. Biochem. Biophys. Res. Commun.254 (2): 440–5. (January 1999). doi:10.1006/bbrc.1998.9959. PMID9918857.
“FGFR2-Cbl interaction in lipid rafts triggers attenuation of PI3K/Akt signaling and osteoblast survival”. Bone42 (6): 1032–9. (June 2008). doi:10.1016/j.bone.2008.02.009. PMID18374639.
“Specific association of the beta isoform of the p85 subunit of phosphatidylinositol-3 kinase with the proto-oncogene c-cbl”. J. Biol. Chem.270 (31): 18260–3. (August 1995). doi:10.1074/jbc.270.31.18260. PMID7629144.
“Sequences surrounding the Src-homology 3 domain of phospholipase Cgamma-1 increase the domain's association with Cbl”. Biochem. Biophys. Res. Commun.249 (2): 537–41. (August 1998). doi:10.1006/bbrc.1998.9177. PMID9712732.
“APS, an adaptor protein containing Pleckstrin homology (PH) and Src homology-2 (SH2) domains inhibits the JAK-STAT pathway in collaboration with c-Cbl”. Leukemia13 (5): 760–7. (May 1999). doi:10.1038/sj/leu/2401397. PMID10374881.
“CIN85 participates in Cbl-b-mediated down-regulation of receptor tyrosine kinases”. J. Biol. Chem.277 (42): 39666–72. (October 2002). doi:10.1074/jbc.M205535200. PMID12177062.
“SETA is a multifunctional adapter protein with three SH3 domains that binds Grb2, Cbl, and the novel SB1 proteins”. Cell. Signal.12 (11–12): 769–79. (December 2000). doi:10.1016/S0898-6568(00)00129-7. PMID11152963.
“A novel Src homology 2 domain-containing molecule, Src-like adapter protein-2 (SLAP-2), which negatively regulates T cell receptor signaling”. J. Biol. Chem.277 (21): 19131–8. (May 2002). doi:10.1074/jbc.M110318200. PMID11891219.
“The c-Cbl-associated protein and c-Cbl are two new partners of the SH2-containing inositol polyphosphate 5-phosphatase SHIP2”. Biochem. Biophys. Res. Commun.300 (2): 494–500. (January 2003). doi:10.1016/S0006-291X(02)02894-2. PMID12504111.
“Evidence for direct interaction between Sprouty and Cbl”. J. Biol. Chem.276 (8): 5866–75. (February 2001). doi:10.1074/jbc.M006945200. PMID11053437.
“Cbl-mediated negative regulation of the Syk tyrosine kinase. A critical role for Cbl phosphotyrosine-binding domain binding to Syk phosphotyrosine 323”. J. Biol. Chem.273 (52): 35273–81. (December 1998). doi:10.1074/jbc.273.52.35273. PMID9857068.
“Ligand-induced ubiquitination of the epidermal growth factor receptor involves the interaction of the c-Cbl RING finger and UbcH7”. J. Biol. Chem.274 (44): 31707–12. (October 1999). doi:10.1074/jbc.274.44.31707. PMID10531381.
“Regulation of Cbl molecular interactions by the co-receptor molecule CD43 in human T cells”. J. Biol. Chem.276 (1): 729–37. (January 2001). doi:10.1074/jbc.M008494200. PMID11024037.
“Activation-modulated association of 14-3-3 proteins with Cbl in T cells”. J. Biol. Chem.271 (24): 14591–5. (June 1996). doi:10.1074/jbc.271.24.14591. PMID8663231.
“A novel phosphotyrosine-binding domain in the N-terminal transforming region of Cbl interacts directly and selectively with ZAP-70 in T cells”. J. Biol. Chem.271 (39): 24063–8. (September 1996). doi:10.1074/jbc.271.39.24063. PMID8798643.
“Structure of the amino-terminal domain of Cbl complexed to its binding site on ZAP-70 kinase”. Nature398 (6722): 84–90. (March 1999). doi:10.1038/18050. PMID10078535.
“The Cbl interactome and its functions”. Nat. Rev. Mol. Cell Biol.6 (12): 907–18. (2005). doi:10.1038/nrm1762. PMID16227975.
“Regulation of Cbl phosphorylation by the Abl tyrosine kinase and the Nck SH2/SH3 adaptor”. Oncogene20 (30): 4058–69. (July 2001). doi:10.1038/sj.onc.1204528. PMID11494134.
“The Cbl proteins are binding partners for the Cool/Pix family of p21-activated kinase-binding proteins”. FEBS Lett.550 (1–3): 119–23. (August 2003). doi:10.1016/S0014-5793(03)00853-6. PMID12935897.
“The endophilin-CIN85-Cbl complex mediates ligand-dependent downregulation of c-Met”. Nature416 (6877): 187–90. (March 2002). doi:10.1038/416187a. PMID11894096.
“Recruitment of Pyk2 and Cbl to lipid rafts mediates signals important for actin reorganization in growing neurites”. J. Cell Sci.117 (Pt 12): 2557–68. (May 2004). doi:10.1242/jcs.01148. PMID15128873.
“The adapter type protein CMS/CD2AP binds to the proto-oncogenic protein c-Cbl through a tyrosine phosphorylation-regulated Src homology 3 domain interaction”. J. Biol. Chem.276 (7): 4957–63. (February 2001). doi:10.1074/jbc.M005784200. PMID11067845.
“CD2AP/CMS regulates endosome morphology and traffic to the degradative pathway through its interaction with Rab4 and c-Cbl”. Traffic4 (2): 97–112. (February 2003). doi:10.1034/j.1600-0854.2003.40205.x. PMID12559036.
“c-Cbl associates directly with the C-terminal tail of the receptor for the macrophage colony-stimulating factor, c-Fms, and down-modulates this receptor but not the viral oncogene v-Fms”. J. Biol. Chem.277 (17): 14635–40. (April 2002). doi:10.1074/jbc.M109214200. PMID11847211.
“Interleukin-2 stimulation induces tyrosine phosphorylation of p120-Cbl and CrkL and formation of multimolecular signaling complexes in T lymphocytes and natural killer cells”. J. Biol. Chem.273 (7): 3986–93. (February 1998). doi:10.1074/jbc.273.7.3986. PMID9461587.
“CSF-1 stimulation induces the formation of a multiprotein complex including CSF-1 receptor, c-Cbl, PI 3-kinase, Crk-II and Grb2”. Oncogene14 (19): 2331–8. (May 1997). doi:10.1038/sj.onc.1201074. PMID9178909.
“Cbl functions downstream of Src kinases in Fc gamma RI signaling in primary human macrophages”. J. Leukoc. Biol.65 (4): 523–34. (April 1999). doi:10.1002/jlb.65.4.523. PMID10204582.
“The involvement of the proto-oncogene p120 c-Cbl and ZAP-70 in CD2-mediated T cell activation”. Int. Immunol.13 (1): 13–22. (January 2001). doi:10.1093/intimm/13.1.13. PMID11133830.
“Differential interaction of Crkl with Cbl or C3G, Hef-1, and gamma subunit immunoreceptor tyrosine-based activation motif in signaling of myeloid high affinity Fc receptor for IgG (Fc gamma RI)”. J. Immunol.161 (10): 5555–63. (November 1998). PMID9820532.
“CBL-GRB2 interaction in myeloid immunoreceptor tyrosine activation motif signaling”. J. Immunol.160 (10): 5018–27. (May 1998). PMID9590251.
“c-Cbl is involved in Met signaling in B cells and mediates hepatocyte growth factor-induced receptor ubiquitination”. J. Immunol.169 (7): 3793–800. (October 2002). doi:10.4049/jimmunol.169.7.3793. PMID12244174.
“Steel factor induces tyrosine phosphorylation of CRKL and binding of CRKL to a complex containing c-kit, phosphatidylinositol 3-kinase, and p120(CBL)”. J. Biol. Chem.272 (15): 10248–53. (April 1997). doi:10.1074/jbc.272.15.10248. PMID9092574.
“Differential signaling after beta1 integrin ligation is mediated through binding of CRKL to p120(CBL) and p110(HEF1)”. J. Biol. Chem.272 (22): 14320–6. (May 1997). doi:10.1074/jbc.272.22.14320. PMID9162067.
“Erythropoietin and IL-3 induce tyrosine phosphorylation of CrkL and its association with Shc, SHP-2, and Cbl in hematopoietic cells”. Biochem. Biophys. Res. Commun.239 (2): 412–7. (October 1997). doi:10.1006/bbrc.1997.7480. PMID9344843.
“EGF-dependent association of phospholipase C-gamma1 with c-Cbl”. Exp. Cell Res.277 (1): 86–94. (July 2002). doi:10.1006/excr.2002.5545. PMID12061819.
“Coordinated regulation of the tyrosine phosphorylation of Cbl by Fyn and Syk tyrosine kinases”. J. Biol. Chem.273 (15): 8867–74. (April 1998). doi:10.1074/jbc.273.15.8867. PMID9535867.
“High affinity IgG receptor activation of Src family kinases is required for modulation of the Shc-Grb2-Sos complex and the downstream activation of the nicotinamide adenine dinucleotide phosphate (reduced) oxidase”. J. Immunol.163 (11): 6023–34. (December 1999). PMID10570290.
“Tyrosine phosphorylation of p120cbl in BCR/abl transformed hematopoietic cells mediates enhanced association with phosphatidylinositol 3-kinase”. Oncogene14 (18): 2217–28. (May 1997). doi:10.1038/sj.onc.1201049. PMID9174058.
“Gads is a novel SH2 and SH3 domain-containing adaptor protein that binds to tyrosine-phosphorylated Shc”. Oncogene17 (24): 3073–82. (December 1998). doi:10.1038/sj.onc.1202337. PMID9872323.
“A c-Cbl yeast two hybrid screen reveals interactions with 14-3-3 isoforms and cytoskeletal components”. Biochem. Biophys. Res. Commun.240 (1): 46–50. (November 1997). doi:10.1006/bbrc.1997.7608. PMID9367879.
“The protein product of the c-cbl protooncogene is the 120-kDa tyrosine-phosphorylated protein in Jurkat cells activated via the T cell antigen receptor”. J. Biol. Chem.269 (37): 22921–4. (September 1994). PMID8083187.
“Purification and molecular cloning of SH2- and SH3-containing inositol polyphosphate-5-phosphatase, which is involved in the signaling pathway of granulocyte-macrophage colony-stimulating factor, erythropoietin, and Bcr-Abl”. Blood89 (8): 2745–56. (April 1997). PMID9108392.
“The proto-oncogene p120(Cbl) is a downstream substrate of the Hck protein-tyrosine kinase”. Biochem. Biophys. Res. Commun.257 (1): 129–38. (April 1999). doi:10.1006/bbrc.1999.0427. PMID10092522.
“Identification of c-Cbl as a new ligase for insulin-like growth factor-I receptor with distinct roles from Mdm2 in receptor ubiquitination and endocytosis”. Cancer Res.68 (14): 5669–77. (July 2008). doi:10.1158/0008-5472.CAN-07-6364. PMID18632619.
“Role of Src in the modulation of multiple adaptor proteins in FcalphaRI oxidant signaling”. Blood94 (6): 2112–20. (September 1999). PMID10477741.
“p85 subunit of PI3 kinase does not bind to human Flt3 receptor, but associates with SHP2, SHIP, and a tyrosine-phosphorylated 100-kDa protein in Flt3 ligand-stimulated hematopoietic cells”. Biochem. Biophys. Res. Commun.254 (2): 440–5. (January 1999). doi:10.1006/bbrc.1998.9959. PMID9918857.
“FGFR2-Cbl interaction in lipid rafts triggers attenuation of PI3K/Akt signaling and osteoblast survival”. Bone42 (6): 1032–9. (June 2008). doi:10.1016/j.bone.2008.02.009. PMID18374639.
“Specific association of the beta isoform of the p85 subunit of phosphatidylinositol-3 kinase with the proto-oncogene c-cbl”. J. Biol. Chem.270 (31): 18260–3. (August 1995). doi:10.1074/jbc.270.31.18260. PMID7629144.
“Sequences surrounding the Src-homology 3 domain of phospholipase Cgamma-1 increase the domain's association with Cbl”. Biochem. Biophys. Res. Commun.249 (2): 537–41. (August 1998). doi:10.1006/bbrc.1998.9177. PMID9712732.
“APS, an adaptor protein containing Pleckstrin homology (PH) and Src homology-2 (SH2) domains inhibits the JAK-STAT pathway in collaboration with c-Cbl”. Leukemia13 (5): 760–7. (May 1999). doi:10.1038/sj/leu/2401397. PMID10374881.
“CIN85 participates in Cbl-b-mediated down-regulation of receptor tyrosine kinases”. J. Biol. Chem.277 (42): 39666–72. (October 2002). doi:10.1074/jbc.M205535200. PMID12177062.
“SETA is a multifunctional adapter protein with three SH3 domains that binds Grb2, Cbl, and the novel SB1 proteins”. Cell. Signal.12 (11–12): 769–79. (December 2000). doi:10.1016/S0898-6568(00)00129-7. PMID11152963.
“A novel Src homology 2 domain-containing molecule, Src-like adapter protein-2 (SLAP-2), which negatively regulates T cell receptor signaling”. J. Biol. Chem.277 (21): 19131–8. (May 2002). doi:10.1074/jbc.M110318200. PMID11891219.
“The c-Cbl-associated protein and c-Cbl are two new partners of the SH2-containing inositol polyphosphate 5-phosphatase SHIP2”. Biochem. Biophys. Res. Commun.300 (2): 494–500. (January 2003). doi:10.1016/S0006-291X(02)02894-2. PMID12504111.
“Evidence for direct interaction between Sprouty and Cbl”. J. Biol. Chem.276 (8): 5866–75. (February 2001). doi:10.1074/jbc.M006945200. PMID11053437.
“Cbl-mediated negative regulation of the Syk tyrosine kinase. A critical role for Cbl phosphotyrosine-binding domain binding to Syk phosphotyrosine 323”. J. Biol. Chem.273 (52): 35273–81. (December 1998). doi:10.1074/jbc.273.52.35273. PMID9857068.
“Requirement of tyrosine-phosphorylated Vav for morphological differentiation of all-trans-retinoic acid-treated HL-60 cells”. Cell Growth Differ.12 (4): 193–200. (April 2001). PMID11331248.
“Ligand-induced ubiquitination of the epidermal growth factor receptor involves the interaction of the c-Cbl RING finger and UbcH7”. J. Biol. Chem.274 (44): 31707–12. (October 1999). doi:10.1074/jbc.274.44.31707. PMID10531381.
“Proto-oncoprotein Vav interacts with c-Cbl in activated thymocytes and peripheral T cells”. J. Immunol.159 (1): 70–6. (July 1997). PMID9200440.
“Regulation of Cbl molecular interactions by the co-receptor molecule CD43 in human T cells”. J. Biol. Chem.276 (1): 729–37. (January 2001). doi:10.1074/jbc.M008494200. PMID11024037.
“Activation-modulated association of 14-3-3 proteins with Cbl in T cells”. J. Biol. Chem.271 (24): 14591–5. (June 1996). doi:10.1074/jbc.271.24.14591. PMID8663231.
“A novel phosphotyrosine-binding domain in the N-terminal transforming region of Cbl interacts directly and selectively with ZAP-70 in T cells”. J. Biol. Chem.271 (39): 24063–8. (September 1996). doi:10.1074/jbc.271.39.24063. PMID8798643.
“Structure of the amino-terminal domain of Cbl complexed to its binding site on ZAP-70 kinase”. Nature398 (6722): 84–90. (March 1999). doi:10.1038/18050. PMID10078535.
