Author

R. W. Baker

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· 2 Biophysics· 1 Cell Biology· 1 Microbiology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 5 Research Focus:cell signaling & trafficking· 4 Assay:cryo-EM· 2 Organism:bacteria (other)· 1 Organism:C. elegans· 1 Research Focus:cell type annotation· 1 Research Focus:development & morphogenesis· 1 Organism:human· 1

Frequent Co-Authors

A. E. Leschziner· 2 shared A. Mychack· 1 shared D. Z. Rudner· 1 shared E. A. Partlow· 1 shared F. M. Hughson· 1 shared G. Hollopeter· 1 shared G. M. Beacham· 1 shared H. Jin· 1 shared

Activity by Year

2018-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 13 mutual co-author links

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2 shared papersCell Biology

A. E. Leschziner

Mutual co-authors in cluster

Author profile →

5 papers

Recent·Most cited

Identification of FacZ as a division site placement factor in Staphylococcus aureus

T. M. Bartlett, T. A. Sisley, A. Mychack, S. Walker, R. W. Baker, D. Z. Rudner, T. G. Bernhardt

The paper identifies FacZ as a novel factor involved in controlling division site placement in Staphylococcus aureus and other Firmicutes by interacting with GpsB.

bioRxiv · Apr 24, 2023 · PreprintMicrobiology

Lipid nanodiscs as a template for high-resolution cryo-EM structures of peripheral membrane proteins

K. Cannon, R. Sarsam, T. Tedamrongwanish, K. Zhang, R. W. Baker

The paper demonstrates that lipid nanodiscs can be used to obtain high-resolution cryo-EM structures of peripheral membrane proteins, exemplified by a 3.3 Å structure of the AP2 clathrin adaptor complex.

bioRxiv · Mar 7, 2023Biochemistry

A structural mechanism for phosphorylation-dependent inactivation of the AP2 complex

E. A. Partlow, R. W. Baker, G. M. Beacham, J. S. Chappie, A. E. Leschziner, G. Hollopeter

The paper reports cryo-EM structures of NECAP bound to phosphorylated AP2 and shows how phosphorylation marks AP2 for inactivation by NECAP.

bioRxiv · Jul 13, 2019Cell Biology

Lis1 promotes the formation of maximally activated cytoplasmic dynein-1 complexes

Z. M. Htet, J. P. Gillies, R. W. Baker, A. E. Leschziner, M. E. DeSantis, S. L. Reck-Peterson

This paper identifies Lis1's role in forming maximally activated dynein complexes by binding to dynein's motor domain, enhancing microtubule binding and velocity.

bioRxiv · Jun 27, 2019Biochemistry

Munc18-1 catalyzes neuronal SNARE assembly by templating SNARE association

J. Jiao, M. He, S. A. Port, R. W. Baker, Y. Xu, H. Qu, Y. Xiong, Y. Wang, H. Jin, T. J. Eisemann, F. M. Hughson, Y. Zhang

This study shows Munc18-1 facilitates SNARE assembly by forming a template complex, and similar mechanisms are used by other SM proteins.

bioRxiv · Sep 10, 2018Biophysics