Author

C.-S. Ang

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

Biology Disciplines

Click to filter author papers

Biochemistry· 7 Microbiology· 1

Signature Assays, Organisms & Methods

Click to filter · or open tag

Assay:proteomics· 8 Approach:experimental assay· 7 Research Focus:cell type annotation· 5 Research Focus:protein folding & dynamics· 5 Organism:human· 4 Research Focus:differential expression· 2 Organism:bacteria (other)· 1 Research Focus:cell-cell communication· 1

Frequent Co-Authors

D. M. Hatters· 3 shared N. A. Williamson· 3 shared D. Cox· 2 shared G. E. Reid· 2 shared M. Radwan· 2 shared N. E. Scott· 2 shared S. Nie· 2 shared A. Dhillon· 1 shared

Activity by Year

2019-2023 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 12 mutual co-author links

Click any collaborator node to inspect or filter shared papers

Focal author (center)Selected co-authorORCID co-authorUnlinked name

Curved chords = mutual co-authorship

3 shared papersBiochemistry

D. M. Hatters

Mutual co-authors in cluster

Author profile →

8 papers

Recent·Most cited

Variation of wine preference amongst consumers is influenced by the composition of salivary proteins

J. Luo, X. Ruan, C.-S. Ang, Y. Nolvachai, P. Marriott, P. Zhang, K. Howell

The study shows that differences in salivary protein composition between Western and Chinese wine tasters influence their perception and preference for wine flavors.

bioRxiv · Mar 27, 2023Biochemistry

Getting more out of FLAG-Tag co-immunoprecipitation mass spectrometry experiments using FAIMS.

C.-S. Ang, J. Sacharz, M. G. Leeming, S. Nie, S. Varshney, N. E. Scott, N. A. Williamson

This study shows that using FAIMS in FLAG-Tag co-immunoprecipitation improves protein coverage by reducing tag peptide interference in mass spectrometry.

bioRxiv · Jun 15, 2021Biochemistry

Hidden information on protein function in censuses of proteome foldedness

D. Cox, C.-S. Ang, N. B. Nillegoda, G. E. Reid, D. M. Hatters

The paper shows proteome folding stability censuses are unreliable due to hidden information on conformation and ligand binding.

bioRxiv · Feb 24, 2021Biochemistry

What are we missing by using hydrophilic enrichment? Improving bacterial glycoproteome coverage using total proteome and FAIMS analysis.

A. R. Ahmad Izaham, C.-S. Ang, S. Nie, L. E. Bird, N. A. Williamson, N. E. Scott

This study shows that FAIMS fractionation can enrich glycopeptides missed by HILIC, increasing glycoproteome coverage in bacteria by at least 30%.

bioRxiv · Jul 22, 2020Microbiology

An Atlas of Phosphorylation and Proteolytic Processing Events During Excitotoxic Neuronal Death Reveals New Therapeutic Opportunities

S. S. Ameen, A. Dufour, M. I. Hossain, A. Hoque, S. Sturgeon, H. Nandurkar, D. Draxler, R. Medcalf, M. A. Kamaruddin, I. Lucet, M. Leeming, D. Liu, A. Dhillon, J. P. Lim, H. Zhu, , H. C. Cheng

The paper uses proteomic approaches to identify proteins modified during excitotoxic neuronal death and shows that blocking Src kinase protects neurons in a rat model.

bioRxiv · Jun 15, 2020 · PreprintBiochemistry

Inclusion bodies formed by polyglutamine and poly(glycine-alanine) are enriched with distinct proteomes but converge in proteins that are risk factors for disease and involved in protein degradation

M. Radwan, J. Lilley, C.-S. Ang, G. Reid, D. M. Hatters

The paper compares proteomes enriched in polyGA and polyQ inclusion bodies, finding distinct protein sets but shared degradation-related proteins linked to neurodegenerative diseases.

bioRxiv · May 4, 2020Biochemistry

HIGD2A is required for assembly of the COX3 module of human mitochondrial complex IV

D. H. Hock, B. Reljic, C.-S. Ang, H. S. Mountford, A. G. Compton, M. T. Ryan, D. R. Thorburn, D. A. Stroud

This study shows HIGD2A is essential for assembling the COX3 module of human mitochondrial complex IV, leading to defects in complex IV activity and intermediate accumulation.

bioRxiv · Dec 19, 2019Biochemistry

Arginine valency in C9ORF72 dipolypeptides mediates promiscuous proteome binding that stalls ribosomes, disable actin cytoskeleton assembly and impairs arginine methylation of endogenous proteins

M. Radwan, C.-S. Ang, A. R. Ormsby, D. Cox, J. C. Daly, G. E. Reid, D. M. Hatters

This study shows that arginine valency in C9ORF72 DPRs causes promiscuous proteome binding, ribosome stalling, actin cytoskeleton disruption, and arginine hypomethylation.

bioRxiv · Aug 28, 2019 · PreprintBiochemistry