Author

C. H. Taron

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biochemistry· 4

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Assay:proteomics· 4 Research Focus:cell type annotation· 3 Organism:human· 2 Organism:mouse· 2 Research Focus:clustering· 1 Research Focus:differential expression· 1 Research Focus:gene regulatory network inference· 1

Frequent Co-Authors

C. Ruse· 2 shared S. Vainauskas· 2 shared B. Causey· 1 shared B. P. Anton· 1 shared C. H. Hokke· 1 shared C. M. McClung· 1 shared C. McClung· 1 shared D. M. Assis· 1 shared

Activity by Year

2021-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 13 mutual co-author links

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2 shared papersBiochemistry

C. Ruse

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

BiochemistrybioRxivJun 1, 2023

A novel family of sugar-specific phosphodiesterases that remove zwitterionic modifications of N-acetylglucosamine

S. L. Fossa, B. P. Anton, D. W. Kneller…·C. H. Taron

This study identifies and characterizes a novel phosphodiesterase, GlcNAc-PDase, that specifically removes zwitterionic modifications from GlcNAc-6-PC and GlcNAc-6-PE in parasitic nematodes.

DOI 10.1016/j.jbc.2023.105437

humanmouse

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BiochemistrybioRxivMay 16, 2023

The AMP deaminase of the mollusk Helix pomatia is an unexpected member of the adenosine deaminase-related growth factor (ADGF) family

G. Tzertzinis, M. B. Ganatra, C. Ruse…·I. Schildkraut

The paper identifies the AMP deaminase from Helix pomatia as a member of the ADGF family despite its preference for AMP over adenosine.

DOI 10.1371/journal.pone.0286435

mouseproteomics

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BiochemistrybioRxivPreprintJul 13, 2022

Comparative analyses of the N-glycoproteomes in HCT116 cancer cells and their non-tumorigenic DNMT1/3b double knockout (DKO1) cells and insight into the Mannose-6-phosphate pathway

M. Chen, D. M. Assis, M. Benet…·J. C. Samuelson

The paper compares N-glycoproteomes of HCT116 cancer cells and DKO1 non-tumorigenic cells, revealing hyper-M6P modification and its potential role in cancer biology.

DOI 10.1101/2022.07.13.499654

humanproteomics

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BiochemistrybioRxivSep 9, 2021

A broad-specificity O-glycoprotease that enables improved analysis of glycoproteins and glycopeptides containing intact complex O-glycans

S. Vainauskas, H. Guntz, E. McLeod…·C. H. Taron

This paper introduces IMPa, a broad-specificity O-glycoprotease that efficiently cleaves glycoproteins with sialylated and asialylated O-glycans, enabling improved O-glycoproteomics analysis.

DOI 10.1021/acs.analchem.1c04055

proteomicsexperimental assay

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