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
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.
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“Phosphatidylinositol transfer protein membrane associated 2 (Piptnm24) plays a role in neurite elongation and synapse formation [85].”
Citations
Cites
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
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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
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1 of the 126 references couldn’t be matched to a known paper.
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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
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
Metadata
- Authors
- Schmidt, M. H. H., & Dikic, I.
- Affiliations
- Goethe University Frankfurt (DE)
- ORCID
- Schmidt, Mirko H.H.
- Venue
- Nature Reviews Molecular Cell Biology
- Published
- 2005-10-14
- Volume
- 6
- Issue
- 12
- Pages
- 907-919
- ISSN
- 1471-0072 (ISSN-L)
- 1471-0080
- 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
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