The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Ubiquitin. Not just for proteasomes anymore
Abstract
Ubiquitin is a small protein that can be covalently linked to itself or other proteins, either as single ubiquitin molecules or as chains of polyubiquitin. Addition of ubiquitin to a target protein requires a series of enzymatic activities (by ubiquitin-activating, -conjugating and -ligating enzymes). The first function attributed to ubiquitin was the covalent modification of misfolded cytoplasmic proteins, thereby directing proteasome-dependent proteolysis. More recently, additional functions have been ascribed to ubiquitin and ubiquitin-related proteins. Ubiquitin directs specific proteins through the endocytic pathway by modifying cargo proteins, and possibly also components of the cytoplasmic protein trafficking machinery.
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“In neuronal cells pharmacological inhibition of proteosomal activity up-regulates lysosomal enzymes, whereas lysosomal disruptors inhibit both lysosomal and proteosomal degradation.”
From A Unique Carboxyl-terminal Insert Domain in the Hematopoietic-specific, GTPase-deficient Rho GTPase RhoH Regulates Post-translational Processing (2013) · cites this paper as [39]
In the citing paper
“In neuronal cells pharmacological inhibition of proteosomal activity up-regulates lysosomal enzymes, whereas lysosomal disruptors inhibit both lysosomal and proteosomal degradation.”
From A Unique Carboxyl-terminal Insert Domain in the Hematopoietic-specific, GTPase-deficient Rho GTPase RhoH Regulates Post-translational Processing (2013) · cites this paper as [39]
In the citing paper
“Furthermore, inhibition of lysosomal or proteosomal pathways both lead to up-regulation of Hsc70 levels and induced chaperone-mediated autophagy (39, 40, 54 -57).”
From A Unique Carboxyl-terminal Insert Domain in the Hematopoietic-specific, GTPase-deficient Rho GTPase RhoH Regulates Post-translational Processing (2013) · cites this paper as [39]
Citations
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Cited by
MDM2 Promotes Cell Motility and Invasiveness by Regulating E-Cadherin Degradation
Yang, J.-Y., Zong, C. S., Xia, W., Wei, Y., Ali-Seyed, M., Li, Z., Broglio, K., Berry, D. A., & Hung, M.-C. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.00172-06 · Cited by 211
Cellular proteins detected in HIV‐1
Ott, D. E. (2008) · Reviews in Medical Virology · doi:10.1002/rmv.570 · Cited by 141
Gao, Y., Colletti, K., & Pari, G. S. (2008) · Journal of Virology · doi:10.1128/jvi.01559-07 · Cited by 58
Troeger, A., Chae, H.-D., Senturk, M., Wood, J., & Williams, D. A. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.505727 · Cited by 15
Metadata
- Authors
- Aguilar, R. C., & Wendland, B.
- Venue
- Current Opinion in Cell Biology
- Publisher
- Elsevier BV
- Published
- 2003-04
- Volume
- 15
- Issue
- 2
- Pages
- 184-190
- ISSN
- 0955-0674
- Cited by
- 138
- References
- 1
- Language
- en
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