Article (Published version) (314 Kb) - 
Limited access to UNIGEOther version: http://www.sciencemag.org/cgi/doi/10.1126/science.1127085
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Scientific Article
unige:13118 
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Proteasome-Independent Functions of Ubiquitin in Endocytosis and Signaling |
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| Published in | Science. 2007, vol. 315, no. 5809, p. 201 - 205 | |
| Abstract | Ubiquitination is a reversible posttranslational modification of cellular proteins, in which a 76–amino acid polypeptide, ubiquitin, is primarily attached to the e-amino group of lysines in target proteins. Ubiquitination is a major player in regulating a broad host of cellular processes, including cell division, differentiation, signal transduction, protein trafficking, and quality control. Aberrations in the ubiquitination system are implicated in pathogenesis of some diseases, certain malignancies, neurodegenerative disorders, and pathologies of the inflammatory immune response. Here, we discuss the proteasome-independent roles of ubiquitination in signaling and endocytosis. | |
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Article (Published version) (314 Kb) - Limited access to UNIGE Other version: http://www.sciencemag.org/cgi/doi/10.1126/science.1127085 |
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| Structures | ||
| Citation (ISO format) | MUKHOPADHYAY, Debdyuti, RIEZMAN, Howard. Proteasome-Independent Functions of Ubiquitin in Endocytosis and Signaling. In: Science, 2007, vol. 315, n° 5809, p. 201 - 205. https://archive-ouverte.unige.ch/unige:13118 |
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