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

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Author profile →

4 papers

Recent·Most cited

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

S. L. Fossa, B. P. Anton, D. W. Kneller, L. M. C. Petralia, M. L. Boisvert, S. Vainauskas, C. H. Hokke, J. M. Foster, 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.

bioRxiv · Jun 1, 2023Biochemistry

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, C. H. Taron, B. Causey, L. Wang, 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.

bioRxiv · May 16, 2023Biochemistry

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, C. M. McClung, E. Gordon, S. Ghose, S. J. Dupard, M. Willetts, C. H. Taron, 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.

bioRxiv · Jul 13, 2022 · PreprintBiochemistry

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. McClung, C. Ruse, X. Shi, 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.

bioRxiv · Sep 9, 2021Biochemistry