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Protein Termini Part A: Volume 718(Volume 718 Methods in Enzymology)

Protein Termini Part A: Volume 718(Volume 718 Methods in Enzymology)

          
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About the Book

Protein termini represent a major route to protein regulation. From the moment the very first amino acid of a polypeptide chain exits the ribosome there is potential for steering from the cellular environment. This volume of Methods in Enzymology Modifications and Targeting of Protein Termini focuses on Protein N-termini and C-termini and their modifications which include acetylation, arginylation, myristoylation and oxidation. Also, the impact of terminal modifications is covered, in particular the impact on protein turnover and the ubiquitin E3 ligases which specifically recognize protein N-termini (N-degrons) and C-termini (C-degrons). In addition to the detailed methods and laboratory protocols, the chapters include informative overviews and reviews of the different subfields.

Table of Contents:
1. In vitro acetyltransferase assays for NAT enzymes Ronen Marmorstein 2. A fluorescent CPM-based in vitro acetylation assay: a tool for assessing N-Terminal acetyltransferase activity and profiling compound activity Tanja Bange 3. Methods for Purification and Activity Analysis of N-Terminal Acetyltransferases Rong Huang 4. N-terminal acetylation of plastid precursor proteins Sacha Baginsky 5. Utilizing N-terminal acetylation specific antibodies Henriette Aksnes 6. Functional assessment of N-terminal acetyltransferase variants Nina McTiernan 7. Affinity purification-mass spectrometry to identify nuclear protein interactions of N-terminal acetyltransferase NAA40 Antonis Kirmizis 8. A pan-N-formylmethionine-specific antibody as a tool to for analyzing Nα︎-terminal formylation Cheol-Sang Hwang 9. Chemical proteomic approaches to investigate N-myristoylation Edward W. Tate 10. Analysis of the oxidation state of N-terminal methionines Sina Ghaemmaghami 11. A biophysical approach to studying N-terminal cysteine oxidase substrate preferences Mark White 12. Recombinant expression, purification, and characterization of human ATE1 arginyltransferase Yi Zhang 13. In-bacteria arginylation assay Yi Zhang 14. Identification of arginylated N-termini with specific antibodies Jasper Eising 15. Characterization of the autophagic N-degron pathway and monitoring its chemical modulation for therapeutic development Yong Tae Kwon 16. Developing a flow cytometric method to evaluate the stability of protein N-termini Aditya M. Kunjapur 17. Degronopedia: A practical guide to identifying and targeting protein degrons Wojciech Pokrzywa 18. Generation and usage of ubiquitin-reference technique (URT) plasmids to validate N-degrons Chang Hoon Ji 19. Quantitative Insights into Protein Turnover and Ubiquitination with HiBiT and NanoBRET Wojciech Pokrzywa 20. Characterization of the autophagy E3 ligase/N-recognin KCMF1 Chang Hoon Ji 21. Identification of Ac/N-degron-recognition domain within the MARCHF6 E3 ubiquitin ligase Cheol-Sang Hwang 22. TurboID technique for proximity labelling of interacting proteins Greta Jarck 23. Proteome analysis of nascent polypeptide chains using puromycin Koshi Imami 24. HUNTER-DIA: An updated protocol for enrichment and mass spectrometry-based identification of protein N-termini Pitter F. Huesgen 25. TERMINER - Bioinformatic detection and annotation of proteolytic protein termini in shotgun proteomics data Oliver Schilling 26. Chemical proteomic approaches to investigate S-prenylation Edward W. Tate 27. Quantitative analysis of C-terminal prenylated protein levels using tandem mass tagging Mark Distefano 28. Optimizing purification and FP-based binding assays for the E3 ligase FEM1C Rong Huang


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Product Details
  • ISBN-13: 9780443414831
  • Publisher: Elsevier Science Publishing Co Inc
  • Publisher Imprint: Academic Press Inc
  • Height: 229 mm
  • No of Pages: 412
  • Sub Title: Volume 718
  • Width: 152 mm
  • ISBN-10: 0443414831
  • Publisher Date: 01 Aug 2025
  • Binding: Hardback
  • Language: English
  • Series Title: Volume 718 Methods in Enzymology
  • Weight: 684 gr


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