Protein Termini Part B

Specificaties
Gebonden, blz. | Engels
Elsevier Science | e druk, 2025
ISBN13: 9780443471926
Rubricering
Elsevier Science e druk, 2025 9780443471926
Onderdeel van serie Methods in Enzymology
€ 178,50
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Samenvatting

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.

Specificaties

ISBN13:9780443471926
Taal:Engels
Bindwijze:Gebonden

Inhoudsopgave

1. Proteome analysis of puromycin-labeled nascent polypeptides<br>Koshi Imami<br>2. HUNTER-DIA: An updated protocol for enrichment and mass spectrometry-based identification of protein N-termini<br>Pitter F. Huesgen<br>3. TERMINER - Bioinformatic detection and annotation of proteolytic protein termini in shotgun proteomics data<br>Oliver Schilling<br>4. Degronopedia: A practical guide to identifying and targeting protein degrons<br>Wojciech Pokrzywa<br>5. Quantitative Insights into Protein Turnover and Ubiquitination with HiBiT and NanoBRET<br>Wojciech Pokrzywa<br>6. Development of a flow cytometric method to evaluate the impact of N-terminal sequences on protein stability<br>Aditya M. Kunjapur<br>7. Generation and characterization of engineered N-degrons of the N-degron pathway using the ubiquitin-reference technique<br>Chang Hoon Ji<br>8. Characterization of the autophagic N-degron pathway and monitoring its chemical modulation for therapeutic development<br>Yong Tae Kwon<br>9. Characterization of the E3 ligase KCMF1 as a ZZ/N-recognin of the autophagic Arg/N-degron pathway<br>Chang Hoon Ji<br>10. Identification of Ac/N-degron-recognition domain within the MARCHF6 E3 ubiquitin ligase<br>Cheol-Sang Hwang<br>11. Affinity purification-mass spectrometry to identify nuclear protein interactions of N-terminal acetyltransferase NAA40<br>Antonis Kirmizis<br>12. TurboID technique for proximity labelling of interacting proteins<br>Greta Jarck<br>13. Chemical proteomic approaches to investigate S-prenylation<br>Edward W. Tate<br>14. Quantitative analysis of C-terminal prenylated protein levels using tandem mass tagging<br>Mark Distefano<br>15. Optimizing purification and FP-based binding assays for the E3 ligase FEM1C<br>Rong Huang
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        Protein Termini Part B