Author

E. J. Montemayor

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· 1 Biophysics· 1 Microbiology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Assay:structural biology· 3 Organism:bacteria (other)· 2 Research Focus:protein folding & dynamics· 2 Research Focus:cell type annotation· 1 Research Focus:host-pathogen & immune response· 1

Frequent Co-Authors

D. Parrell· 2 shared E. R. Wright· 2 shared J. C. Sanchez· 2 shared N. T. Ploscariu· 2 shared B. Sibert· 1 shared C. W. Shebelut· 1 shared D. A. Brow· 1 shared J. E. Yang· 1 shared

Activity by Year

2020-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 26 mutual co-author links

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2 shared papersBiophysics

D. Parrell

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

BiophysicsbioRxivPreprintJul 10, 2023

Atomic-level architecture of Caulobacter crescentus flagellar filaments provide evidence for multi-flagellin filament stabilization

J. C. Sanchez, E. J. Montemayor, N. T. Ploscariu…·E. R. Wright

The paper presents an atomic-level structure of Caulobacter crescentus flagellar filaments, revealing molecular interactions and glycosylation sites that contribute to multi-flagellin filament stability and motility.

DOI 10.1101/2023.07.10.548443

bacteria (other)structural biology

𝕏 PostBluesky

MicrobiologybioRxivJul 27, 2020

Flagellar structures from the bacterium Caulobacter crescentus and implications for phage {Phi}CbK predation of multi-flagellin bacteria

E. J. Montemayor, N. T. Ploscariu, J. C. Sanchez…·E. R. Wright

This study investigates how phage {phi}CbK recognizes flagellins in Caulobacter crescentus, showing that multiple flagellins contribute to adsorption and identifying structural features that may influence this interaction.

DOI 10.1128/jb.00399-20

bacteria (other)structural biology

𝕏 PostBluesky

BiochemistrybioRxivApr 22, 2020

Molecular basis for the distinct cellular functions of the Lsm1-7 and Lsm2-8 complexes

E. J. Montemayor, J. M. Virta, S. M. Hayes…·S. E. Butcher

This study identifies the molecular mechanisms by which Lsm1-7 and Lsm2-8 complexes bind RNA with distinct specificity, revealing structural determinants for their unique functions.

DOI 10.1261/rna.075879.120

structural biologyexperimental assay

𝕏 PostBluesky