Lysosomal Pathways of Protein Degradation, Dice, J Fred

Автор: Friedman, Laurie
Название: Targeted Protein Degradation
ISBN: 1071616676 ISBN-13(EAN): 9781071616673
Издательство: Springer
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Описание: This detailed volume explores molecularly imprinted polymers (MIPs), which have attracted great interest both in fundamental research and for practical applications due to their selective molecular recognition capabilities, extraordinary stability, and ease of preparation.

Автор: Cacace Angela M., Hickey Christopher M., Bйkйs Miklуs
Название: Targeted Protein Degradation: Methods and Protocols
ISBN: 1071616641 ISBN-13(EAN): 9781071616642
Издательство: Springer
Цена: 15855.00 р.
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Описание: This detailed book aims to provide an overview of novel bioinformatics resources for exploring diverse aspects of RNA biology. This edition focuses on methods dealing with non-coding RNA (miRNAs, circRNAs or lncRNAs), RNA modifications (m6A or RNA editing), single cell RNA-seq and statistical models to handle count data from RNA-seq experiments.

Автор: Hochstrasser, Mark
Название: Hochstrasser-Ubiquitin-Dependent Protein Degradation V619
ISBN: 0128186674 ISBN-13(EAN): 9780128186671
Издательство: Elsevier Science
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Описание:

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.

Автор: De, Arnab
Название: Ubiquitin chains
ISBN: 3319149644 ISBN-13(EAN): 9783319149646
Издательство: Springer
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Описание: This thesis examines the evidence for regulatory ubiquitination by focusing on A20.