Electron Capture vs Transfer Dissociation for Site Determination of Tryptic Peptide Tyrosine Sulfation: Direct Detection of Fibrinogen Sulfation Sites and Identification of Novel Isobaric Interferences-Reference-Cited by-同舟云学术

Electron Capture vs Transfer Dissociation for Site Determination of Tryptic Peptide Tyrosine Sulfation: Direct Detection of Fibrinogen Sulfation Sites and Identification of Novel Isobaric Interferences

Published:2024-06-20 Issue:7 Volume:23 Page:2386-2396
ISSN:1535-3893
Container-title:Journal of Proteome Research
language:en
Short-container-title:J. Proteome Res.

Author:

Youssef Menatallah M.¹²,Szot Carson W.¹,Folz Jeff³^ORCID,Collier Luke M.¹^ORCID,Kweon Hye Kyong¹,DeFiglia Steven A.¹,Ayad Miriam F.²,Hussein Lobna A.²,Abdel-Ghany Maha F.²,Hakansson Kristina¹^ORCID

Affiliation:

1. Department of Chemistry, University of Michigan, Ann Arbor, Michigan 48109-1055, United States

2. Department of Pharmaceutical Analytical Chemistry, Faculty of Pharmacy, Ain Shams University, Cairo 11566, Egypt

3. Department of Biomedical Engineering, University of Michigan, Ann Arbor, Michigan 48109-1055, United States

Funder

Office of Research Infrastructure Programs

Ministry of Higher Education

National Institute of General Medical Sciences

Agilent Technologies

Publisher

American Chemical Society (ACS)

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.jproteome.4c00072

Reference50 articles.

1. Tyrosine-O-sulfated proteins of PC12 pheochromocytoma cells and their sulfation by a tyrosylprotein sulfotransferase.

2. (Glu62, Ala30, Tyr8)n serves as high-affinity substrate for tyrosylprotein sulfotransferase: a Golgi enzyme.

3. Toward a framework for sulfoproteomics: Synthesis and characterization of sulfotyrosine-containing peptides

4. Sulfoproteomics Workflow with Precursor Ion Accurate Mass Shift Analysis Reveals Novel Tyrosine Sulfoproteins in the Golgi

5. Custom Workflow for the Confident Identification of Sulfotyrosine-Containing Peptides and Their Discrimination from Phosphopeptides