Author

L. E. Miller-Vedam

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

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Research Focus:cell signaling & trafficking· 2 Assay:cryo-EM· 2 Organism:human· 2 Research Focus:protein folding & dynamics· 2 Research Focus:protein structure prediction· 2 Research Focus:chromatin & epigenetic regulation· 1 Approach:microscopy & imaging analysis· 1

Frequent Co-Authors

A. Frost· 3 shared A. A. Anand· 2 shared H. C. Nguyen· 2 shared J. C. Tsai· 2 shared P. Walter· 2 shared A. G. Myasnikov· 1 shared A. R. Renslo· 1 shared B. Bräuning· 1 shared

Activity by Year

2017-2020 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 29 mutual co-author links

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3 shared papersBiochemistry

A. Frost

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3 papers

Recent·Most cited

BiophysicsbioRxivSep 2, 2020

Structural and mechanistic basis of the EMC-dependent biogenesis of distinct transmembrane clients

L. E. Miller-Vedam, B. Bräuning, K. D. Popova…·J. S. Weissman

The paper reveals the structural and mechanistic basis of EMC's role in biogenesis of distinct transmembrane proteins through cryo-EM structures and functional studies.

DOI 10.7554/elife.62611

yeasthuman

𝕏 PostBluesky

BiochemistrybioRxivDec 22, 2018

Structural basis of eIF2B-catalyzed GDP exchange and phosphoregulation by the integrated stress response

A. A. Anand, L. R. Kenner, H. C. Nguyen…·A. Frost

The paper reports cryoEM structures of eIF2 bound to eIF2B, revealing the mechanism of GDP exchange and phosphoregulation in the integrated stress response.

DOI 10.1126/science.aaw2922

cryo-EMexperimental assay

𝕏 PostBluesky

BiochemistrybioRxivNov 24, 2017

Structure of the nucleotide exchange factor eIF2B reveals mechanism of memory-enhancing molecule

J. C. Tsai, L. E. Miller-Vedam, A. A. Anand…·P. Walter

The paper determines the structure of eIF2B bound to ISRIB, revealing how it promotes eIF2B assembly and reverses eIF2 phosphorylation effects.

DOI 10.1126/science.aaq0939

humanstructural biology

𝕏 PostBluesky