Author

R. Bower

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

Cell Biology· 4

Signature Assays, Organisms & Methods

Click to filter · or open tag

Approach:experimental assay· 4 Research Focus:cell type annotation· 3 Organism:chicken / avian· 2 Assay:proteomics· 2 Research Focus:cell signaling & trafficking· 1 Research Focus:clustering· 1 Assay:cryo-EM· 1 Organism:Drosophila· 1

Frequent Co-Authors

M. E. Porter· 4 shared D. Nicastro· 3 shared D. Tritschler· 3 shared G. Fu· 2 shared J. Sakizadeh· 2 shared K. Augspurger· 2 shared L. Gui· 2 shared A. Chien· 1 shared

Activity by Year

2017-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 30 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

4 shared papersCell Biology

M. E. Porter

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

The ciliary MBO2 complex targets assembly of inner arm dynein b and reveals additional doublet microtubule asymmetries

G. Fu, K. Augspurger, J. Sakizadeh, J. Reck, R. Bower, D. Tritschler, L. Gui, D. Nicastro, M. E. Porter

The paper identifies the MBO2 complex as a regulator of inner arm dynein b assembly in cilia and reveals its structural organization on doublet microtubules.

bioRxiv · Jul 31, 2023 · PreprintCell Biology

FAP57/WDR65 targets assembly of a subset of inner arm dyneins and connects to regulatory hubs in cilia

J. Lin, T. V. Le, K. Augspurger, D. Tritschler, R. Bower, G. Fu, C. Perrone, E. O'Toole, K. V. Mills, E. Dymek, E. F. Smith, D. Nicastro, M. E. Porter

This study identifies FAP57/WDR65 as a docking factor that targets specific inner dynein arms to the 96 nm axonemal repeat and connects to regulatory hubs in cilia.

bioRxiv · Jul 1, 2019Cell Biology

Scaffold subunits support associated subunit assembly in the Chlamydomonas ciliary nexin-dynein regulatory complex

L. Gui, K. Song, D. Tristchler, R. Bower, Y. Si, A. Dai, K. Augsperger, J. Sakizadeh, M. Grzemska, T. Ni, M. E. Porter, D. Nicastro

This study uses cryo-electron tomography to determine the structure of the N-DRC in Chlamydomonas flagella and identifies key subunit interactions and assembly requirements.

bioRxiv · Jun 27, 2019Cell Biology

Dynamics of the IFT Machinery at the Ciliary Tip

A. Chien, S. M. Shih, R. Bower, D. Tritschler, M. E. Porter, A. Yildiz

The paper visualizes IFT dynamics in Chlamydomonas flagella, revealing kinesin-II dissociation as a negative feedback mechanism for flagellar length control.

bioRxiv · Sep 15, 2017Cell Biology