Author

A. Fomenkov

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

Microbiology· 2 Plant Biology· 1

Signature Assays, Organisms & Methods

Click to filter · or open tag

Approach:experimental assay· 3 Organism:bacteria (other)· 1 Research Focus:cell signaling & trafficking· 1 Research Focus:cell type annotation· 1 Research Focus:development & morphogenesis· 1 Organism:E. coli· 1 Research Focus:genome assembly· 1 Organism:human· 1

Frequent Co-Authors

S.-y. Xu· 2 shared A. Glushkevich· 1 shared A. Kniazev· 1 shared A. Mamaeva· 1 shared A. Nosov· 1 shared D. Heiter· 1 shared D. Kharlampieva· 1 shared E. Yigit· 1 shared

Activity by Year

2021-2022 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 23 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

2 shared papersMicrobiology

S.-y. Xu

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Modification-Dependent Restriction Endonuclease-based sequencing method (EcoWI-seq) maps the genome-wide landscape of phosphorothioate modification at base resolution.

W. Yang, A. Fomenkov, D. Heiter, S.-y. Xu, L. Ettwiller

The paper introduces EcoWI-seq, a method to map phosphorothioate modifications at base resolution in bacterial genomes, showing systematic usage of target sites in modified clones.

bioRxiv · May 16, 2022 · PreprintMicrobiology

FAMOSS, a conserved 41-aa peptide involved in plant tip growth regulation

A. Mamaeva, A. Kniazev, I. Sedlov, N. Golub, D. Kharlampieva, V. Manuvera, V. Rakitin, A. Nosov, A. Fomenkov, M. Pavlyukov, S. Kovalchuk, R. Ziganshin, A. Glushkevich, V. Lazarev, I. Fesenko

The paper identifies and characterizes FAMOSS, a conserved 41-aa peptide from moss that regulates tip growth by interacting with Rab GTPases and modulating vesicular transport.

bioRxiv · Nov 24, 2021 · PreprintPlant Biology

Expression of human ACE2 N-terminal domain, part of the receptor for SARS-CoV-2, in fusion with maltose binding protein, E. coli ribonuclease I and human RNase A

S.-y. Xu, A. Fomenkov, T.-H. Chen, E. Yigit

This paper constructs and evaluates RNase fusion proteins with the human ACE2 N-terminal domain to degrade SARS-CoV-2 RNA in vitro.

bioRxiv · Jan 31, 2021 · PreprintMicrobiology