| CBLC inhibits the proliferation and metastasis of breast cancer cells via ubiquitination and degradation of CTTN. | CBLC inhibits the proliferation and metastasis of breast cancer cells via ubiquitination and degradation of CTTN.
Li W, Lei T, Song X, Deng C, Lu J, Zhang W, Kuang Z, He Y, Zhou Q, Luo Z, Mo F, Yang H, Hang J, Xiao B, Li L. | 12/24/2022 |
| Stabilization of AURKA by the E3 ubiquitin ligase CBLC in lung adenocarcinoma. | Stabilization of AURKA by the E3 ubiquitin ligase CBLC in lung adenocarcinoma.
Hong SY, Lu YC, Hsiao SH, Kao YR, Lee MH, Lin YP, Wang CY, Wu CW. | 05/14/2022 |
| Cbl-c is the most recently identified Cbl protein and is expressed exclusively in epithelial cells. Data mining reveals Cbl-c mutations associated with solid tumors. Subsequent cell-based analysis demonstrates a loss of E3 function and dominant negative effects for one of these mutations. | Loss of function Cbl-c mutations in solid tumors.
Daniels SR, Liyasova M, Kales SC, Nau MM, Ryan PE, Green JE, Lipkowitz S., Free PMC Article | 03/7/2020 |
| ectopic expression of CBLC enhanced the activation of EGFR and downstream ERK1/2 signaling after ligand stimulation by competing with CBL for EGFR binding.. | Upregulation of E3 Ubiquitin Ligase CBLC Enhances EGFR Dysregulation and Signaling in Lung Adenocarcinoma.
Hong SY, Kao YR, Lee TC, Wu CW. | 09/21/2019 |
| Methylmalonic aciduria with homocystinuria cblC is a multisystemic metabolic disease affecting cobalamin metabolism. The presence of retinal alterations in cblC is a common feature and it is reported to develop more frequently and into a more severe form in the early-onset phenotype, suggesting to some extent a correlation with the biochemical phenotype | Optical coherence tomography morphology and evolution in cblC disease-related maculopathy in a case series of very young patients.
Bacci GM, Donati MA, Pasquini E, Munier F, Cavicchi C, Morrone A, Sodi A, Murro V, Garcia Segarra N, Defilippi C, Bussolin L, Caputo R. | 01/6/2018 |
| Data suggest that ubiquitin ligase CBLC controls mostly network organization of the Golgi Apparatus. | The Ubiquitin Ligase CBLC Maintains the Network Organization of the Golgi Apparatus.
Lee WY, Goh G, Chia J, Boey A, Gunko NV, Bard F., Free PMC Article | 06/28/2016 |
| Silencing of CBLC causes increased sensitivity to PARP1 inhibitor olaparib in breast cancer cell line models and that defective homologous recombination (HR) DNA repair is the likely cause. | Complementary genetic screens identify the E3 ubiquitin ligase CBLC, as a modifier of PARP inhibitor sensitivity.
Frankum J, Moudry P, Brough R, Hodny Z, Ashworth A, Bartek J, Lord CJ., Free PMC Article | 03/5/2016 |
| the effects of two pathogenic missense mutations on the the catalytic activities of the human B12-processing chaperone CblC | Pathogenic mutations differentially affect the catalytic activities of the human B12-processing chaperone CblC and increase futile redox cycling.
Gherasim C, Ruetz M, Li Z, Hudolin S, Banerjee R., Free PMC Article | 07/25/2015 |
| This retrospective multicentre study evaluates clinical, biochemical and genetic findings in 88 cblC patients | Clinical presentation and outcome in a series of 88 patients with the cblC defect.
Fischer S, Huemer M, Baumgartner M, Deodato F, Ballhausen D, Boneh A, Burlina AB, Cerone R, Garcia P, Gökçay G, Grünewald S, Häberle J, Jaeken J, Ketteridge D, Lindner M, Mandel H, Martinelli D, Martins EG, Schwab KO, Gruenert SC, Schwahn BC, Sztriha L, Tomaske M, Trefz F, Vilarinho L, Rosenblatt DS, Fowler B, Dionisi-Vici C. | 05/16/2015 |
| The ubiquitin ligase activity of Cbl-c by the direct interaction of the LIM zinc coordinating domain of Hic5 is demonstrated. | Cbl-c ubiquitin ligase activity is increased via the interaction of its RING finger domain with a LIM domain of the paxillin homolog, Hic 5.
Ryan PE, Kales SC, Yadavalli R, Nau MM, Zhang H, Lipkowitz S., Free PMC Article | 06/29/2013 |
| the N terminus of Cbl-c contributes to the binding to the E2 and phosphorylation of Tyr-341 leads to a decrease in affinity and an increase in the E3 activity of Cbl-c | The N terminus of Cbl-c regulates ubiquitin ligase activity by modulating affinity for the ubiquitin-conjugating enzyme.
Ryan PE, Sivadasan-Nair N, Nau MM, Nicholas S, Lipkowitz S., Free PMC Article | 09/20/2010 |
| Data demonstrate that two E3 ligases of different classes, CBLC and AIP4, can interact and cooperate to down-regulate EGFR signaling. | Interaction between two ubiquitin-protein isopeptide ligases of different classes, CBLC and AIP4/ITCH.
Courbard JR, Fiore F, Adélaïde J, Borg JP, Birnbaum D, Ollendorff V. | 01/21/2010 |
| Src is a preferential target of Cbl-c for degradation | Cbl-c suppresses v-Src-induced transformation through ubiquitin-dependent protein degradation.
Kim M, Tezuka T, Tanaka K, Yamamoto T. | 01/21/2010 |
| ubiquitin protein ligase activity is regulated in c-Cbl by phosphorylation-induced conformational change and constitutive activation by tyrosine to glutamate point mutations | Regulation of ubiquitin protein ligase activity in c-Cbl by phosphorylation-induced conformational change and constitutive activation by tyrosine to glutamate point mutations.
Kassenbrock CK, Anderson SM. | 01/21/2010 |
| c-Cbl is a negative regulator of hepatocyte growth factor/receptor tyrosine kinase Met signaling in B cells, mediating ubiquitination and, consequently, proteosomal degradation of Met, with a role in Met-mediated tumorigenesis. | c-Cbl is involved in Met signaling in B cells and mediates hepatocyte growth factor-induced receptor ubiquitination.
Taher TE, Tjin EP, Beuling EA, Borst J, Spaargaren M, Pals ST. | 01/21/2010 |