Secure CheckoutPersonal information is secured with SSL technology.
Free ShippingFree global shipping
No minimum order.
1. Assays for protein retrotranslocation in ERAD
Sonya Neal, Sascha H. Duttke and Randolph Y. Hampton
2. Methods for measuring misfolded protein clearance in the budding yeast Saccharomyces cerevisiae
Rahul S. Samant and Judith Frydman
3. Methodologies to monitor protein turnover at the inner nuclear membrane
Pei-Ling Tsai, Chenguang Zhao and Christian Schlieker
4. Assays for dissecting the in vitro enzymatic activity of yeast Ubc7
Bayan Mashahreh, Yuval Reiss, Reuven Wiener and Tommer Ravid
5. Methods for genetic analysis of mammalian ER-associated degradation
Dara E. Leto and Ron R. Kopito
6. A dual system to manipulate protein levels for DNA replication- and cell cycle-related studies
Néstor García-Rodríguez and Helle D. Ulrich
7. Engineered disulfide crosslinking to measure conformational changes in the 26S proteasome
Randi G. Reed and Robert J. Tomko Jr.
8. Assays for ubiquitin-like protein ligation and proteasome function in archaea
Xian Fu, Zachary Adams and Julie Maupin-Furlow
9. Structural mass spectrometry approaches to study the 20S proteasome
Gili Ben-Nissan, Shay Vimer, Mark Tarnavsky and Michal Sharon
10. Single-molecule methods for measuring ubiquitination and protein stability
Jason Hon and Ying Lu
11. In vitro analysis of proteasome-associated USP14 activity for substrate degradation and deubiquitylation
Srinivasan Muniyappan and Byung-Hoon Lee
12. Methods for studying the regulation of membrane traffic by ubiquitin and the ESCRT pathway
Evan L. Guiney, Lu Zhu, Richa Sardana, Scott D. Emr and Matthew G. Baile
13. Detection of ubiquitinated targets in mammalian and Drosophila models
Elena Maspero, Valentina Fajner, Janine Weber and Simona Polo
14. Western blot analysis of the autophagosomal membrane protein LGG-1/LC3 in Caenorhabditis elegans
Alexander Springhorn and Thorsten Hoppe
15. Monitoring stress-induced autophagic engulfment and degradation of the 26S proteasome in mammalian cells
Victoria Cohen-Kaplan, Ido Livneh, Yong Tae Kwon and Aaron Ciechanover
Ubiquitination and Protein Stability - Part B, Volume 619, the latest release in the Methods in Enzymology series, highlights new advances in the field, with this updated volume presenting interesting chapters written by an international board of authors. Topics of note include chapters on Assays of SUMO protease function in mammalian cells, In vitro analysis of proteasome-associated USP14 activity for substrate degradation and deubiquitylation, Methods to study proteasome regulatory particle assembly, Native mass spectrometry approaches to study the proteasome, Single-molecule methods to study the ubiquitin-proteasome system, Assays for the function of ubiquitin in the mammalian endocytic pathway, and much more.
- Provides the authority and expertise of leading contributors from an international board of authors
- Presents the latest release in this series on enzymology
Biochemists, chemists, microbiologists, microbiome specialists, marine scientists, protein chemists, biotechnology, chemical biologists, blue biotech experts, natural product chemists, drug discovery professionals.
- No. of pages:
- © Academic Press 2019
- 23rd March 2019
- Academic Press
- Hardcover ISBN:
- eBook ISBN:
Praise for the Series:
"Should be on the shelves of all libraries in the world as a whole collection." --CHEMISTRY IN INDUSTRY
"The work most often consulted in the lab." --ENZYMOLOGIA
"The Methods in Enzymology series represents the gold-standard." --NEUROSCIENCE
Dr. Mark W Hochstrasser is a Eugene Higgins Professor of Molecular Biophysics and Biochemistry and Professor of Molecular, Cellular, and Developmental Biology Yale University, USA.
Eugene Higgins Professor of Molecular Biophysics and Biochemistry and Professor of Molecular, Cellular, and Developmental Biology, Yale University, USA
Elsevier.com visitor survey
We are always looking for ways to improve customer experience on Elsevier.com.
We would like to ask you for a moment of your time to fill in a short questionnaire, at the end of your visit.
If you decide to participate, a new browser tab will open so you can complete the survey after you have completed your visit to this website.
Thanks in advance for your time.