N-Terminal Modifications of Ubiquitin via Methionine Excision, Deamination, and Arginylation Expand the Ubiquitin Code-Reference-Cited by-同舟云学术

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N-Terminal Modifications of Ubiquitin via Methionine Excision, Deamination, and Arginylation Expand the Ubiquitin Code

Published:2022-03-31 Issue:3 Volume:45 Page:158-167
ISSN:0219-1032
Container-title:Molecules and Cells
language:en
Short-container-title:Mol.Cells

Author:

Nguyen Kha The¹²^ORCID,Ju Shinyeong³²^ORCID,Kim Sang-Yoon¹^ORCID,Lee Chang-Seok¹^ORCID,Lee Cheolju³⁴^ORCID,Hwang Cheol-Sang¹^ORCID

Affiliation:

1. Department of Life Sciences, Pohang University of Science and Technology, Pohang 37673, Korea

2. These authors contributed equally to this work

3. Center for Theragnosis, Korea Institute of Science and Technology, Seoul 02792, Korea

4. Division of Bio-Medical Science & Technology, KIST School, Korea University of Science and Technology, Seoul 02792, Korea

Publisher

Korean Society for Molecular and Cellular Biology

Subject

Cell Biology,Molecular Biology,General Medicine

Link

http://pdf.medrang.co.kr/KSMCB/2022/045/KSMCB045-03-07.pdf

Reference40 articles.

1. In Vivo Half-Life of a Protein Is a Function of Its Amino-Terminal Residue

2. Interactive Peptide Spectral Annotator: A Versatile Web-based Tool for Proteomic Applications

3. An efficient system for high-level expression and easy purification of authentic recombinant proteins

4. Post-translational Modifications of the Protein Termini

5. Aminopeptidases trim Xaa-Pro proteins, initiating their degradation by the Pro/N-degron pathway

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