Author

E. M. Lynch

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· 3 Cell Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Research Focus:cell signaling & trafficking· 3 Assay:cryo-EM· 2 Research Focus:metabolism & bioenergetics· 2 Organism:yeast· 2 Research Focus:chromatin & epigenetic regulation· 1 Organism:human· 1 Research Focus:protein folding & dynamics· 1

Frequent Co-Authors

J. M. Kollman· 3 shared D. P. Farrell· 2 shared F. DiMaio· 2 shared A. G. Cook· 1 shared A. Horowitz· 1 shared A. M. Dosey· 1 shared A. W. Murray· 1 shared E. C. Garner· 1 shared

Activity by Year

2019-2021 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 23 mutual co-author links

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3 shared papersBiochemistry

J. M. Kollman

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Author profile →

4 papers

Recent·Most cited

Cryo-EM Structures of CTP Synthase Filaments Reveal Mechanism of pH-Sensitive Assembly During Budding Yeast Starvation

J. M. Hansen, A. Horowitz, E. M. Lynch, D. P. Farrell, J. Quispe, F. DiMaio, J. M. Kollman

The paper uses cryo-EM to study CTP synthase filament assembly in yeast, revealing pH-sensitive mechanisms and their role in starvation response.

bioRxiv · Aug 25, 2021Biochemistry

Coupled structural transitions enable highly cooperative regulation of human CTPS2 filaments

E. M. Lynch, J. M. Kollman

The paper reveals how human CTPS2 filaments use coupled structural transitions to enable highly cooperative regulation through dynamic switching between active and inactive states.

bioRxiv · Sep 16, 2019Biochemistry

Architecture of the Mto1/2 microtubule nucleation complex

H. C. Thakur, E. M. Lynch, W. E. Borek, X. X. Bao, S. Ashraf, J. Zou, J. Rappsilber, A. G. Cook, K. E. Sawin

The paper investigates the structure and organization of the Mto1/2 complex, revealing its multimeric architecture and the role of specific domains in dimerization.

bioRxiv · Aug 31, 2019 · PreprintCell Biology

Independent evolution of polymerization in the Actin ATPase clan regulates hexokinase activity

P. R. Stoddard, E. M. Lynch, D. P. Farrell, Q. A. Justman, A. M. Dosey, F. DiMaio, T. A. Williams, J. M. Kollman, A. W. Murray, E. C. Garner

Yeast glucokinase activity is limited by its polymerization, which is critical for cell viability during glucose refeeding.

bioRxiv · Jul 2, 2019 · PreprintBiochemistry