Analysis of defective protein ubiquitylation associated to adriamycin resistant cells-Reference-Cited by-同舟云学术

Analysis of defective protein ubiquitylation associated to adriamycin resistant cells

Published:2017-11-20 Issue:24 Volume:16 Page:2337-2344
ISSN:1538-4101
Container-title:Cell Cycle
language:en
Short-container-title:Cell Cycle

Author:

Lang Valérie¹,Aillet Fabienne¹,Xolalpa Wendy¹,Serna Sonia²,Ceccato Laurie³⁴,Lopez-Reyes Rosa G.³⁴,Lopez-Mato Maria Paz¹,Januchowski Radosław⁵,Reichardt Niels-Christian²⁶,Rodriguez Manuel S.¹³⁴

Affiliation:

1. Inbiomed, Mikeletegi Pasealekua, San Sebastian-Donostia, Spain

2. Glycotechnology Laboratory, CIC biomaGUNE, Miramon Pasealekua, San Sebastian-Donostia, Spain

3. Institut des Technologies Avancées en sciences du Vivant (ITAV) 1 Place Pierre Potier, Université de Toulouse, CNRS, UPS, Toulouse, France

4. Institut de Pharmacologie et de Biologie Structurale (IPBS), 205 Route de Narbonne,Université de Toulouse, CNRS, UPS, Toulouse, France

5. Department of Histology and Embryology, Poznan University of Medical Sciences, Swiecickiego 6 St., Poznan, Poland

6. CIBER de Bioingenierıa, Biomateriales y Nanomedicina (CIBER-BBN), San Sebastian-Donostia, Spain

Funder

Spanish Ministry of Economy and Competiveness

Government of the Basque Country

Polish National Science Centre

Publisher

Informa UK Limited

Subject

Cell Biology,Developmental Biology,Molecular Biology

Link

https://www.tandfonline.com/doi/pdf/10.1080/15384101.2017.1387694

Reference35 articles.

1. The complexity of recognition of ubiquitinated substrates by the 26S proteasome

2. The ubiquitin proteasome system — Implications for cell cycle control and the targeted treatment of cancer

3. The demographics of the ubiquitin system

4. Generation and physiological roles of linear ubiquitin chains

5. DUBs, the regulation of cell identity and disease

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