Author

M. O. Sheikh

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· 2 Microbiology· 1

Signature Assays, Organisms & Methods

Click to filter · or open tag

Approach:statistical model· 2 Research Focus:chromatin & epigenetic regulation· 1 Research Focus:clustering· 1 Approach:deep learning· 1 Approach:experimental assay· 1 Research Focus:host-pathogen & immune response· 1 Organism:human· 1 Approach:mechanistic / dynamical model· 1

Frequent Co-Authors

L. Wells· 3 shared C. J. Capicciotti· 1 shared C. M. West· 1 shared D. G. Mead· 1 shared D. Thieker· 1 shared E. Gas-Pascual· 1 shared G.-J. Boons· 1 shared H. van der Wel· 1 shared

Activity by Year

2020-2021 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 25 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

L. Wells

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Cell Surface Glycan Engineering Reveals that Matriglycan Alone can Recapitulate Dystroglycan Binding and Function

M. O. Sheikh, C. J. Capicciotti, L. Liu, J. L. Praissman, D. G. Mead, M. A. Brindley, T. Willer, K. P. Campbell, K. W. Moremen, L. Wells, G.-J. Boons

This study shows matriglycan can independently bind Laminin, viral proteins, and antibodies, and block viral infection, suggesting it acts as a tunable receptor.

bioRxiv · May 10, 2021Biochemistry

Separation and identification of permethylated glycan isomers by reversed phase nanoLC-NSI-MSn

S. Kurz, M. O. Sheikh, S. Lu, L. Wells, M. Tiemeyer

This paper develops an optimized LC-MSn workflow for separating and identifying permethylated glycan isomers without requiring glycan standards or high-resolution mass spectrometers.

bioRxiv · Aug 4, 2020Biochemistry

A glycogenin homolog controls Toxoplasma gondii growth via glycosylation of an E3 ubiquitin ligase

M. Mandalasi, H. W. Kim, D. Thieker, M. O. Sheikh, E. Gas-Pascual, K. Rahman, P. Zhao, N. G. Daniel, H. van der Wel, T. H. Ichikawa, J. N. Glushka, L. Wells, R. J. Woods, Z. A. Wood, C. M. West

This study identifies Gat1, a glycogenin homolog, as essential for adding the terminal sugar to Skp1 in Toxoplasma gondii, which is critical for parasite growth.

bioRxiv · Feb 2, 2020 · PreprintMicrobiology