Author

M. T. Stubbs

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 Assay:cryo-EM· 2 Research Focus:protein structure prediction· 2 Research Focus:cell type annotation· 1 Approach:microscopy & imaging analysis· 1 Organism:mouse· 1 Research Focus:protein folding & dynamics· 1 Assay:protein structure· 1

Frequent Co-Authors

A. Meister· 3 shared C. Tueting· 2 shared D. A. Semchonok· 2 shared F. Hamdi· 2 shared F. L. Kyrilis· 2 shared L. Schmidt· 2 shared P. L. Kastritis· 2 shared A. Sinz· 1 shared

Activity by Year

2019-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 31 mutual co-author links

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3 shared papersBiochemistry

A. Meister

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Author profile →

3 papers

Recent·Most cited

BiochemistrybioRxivPreprintJun 17, 2023

Self-assembly of Grb2 meshworks revealed by Grb2-Gab1497-528 complex structure

C. Breithaupt, T. Gruber, K. Mandel…·M. T. Stubbs

This paper presents the structure of Grb2 bound to a Gab1 peptide, revealing its ability to form two-dimensional meshworks and phase-separated condensates through SH2/cSH3 domain interactions.

DOI 10.1101/2023.06.17.545433

protein structureexperimental assay

𝕏 PostBluesky

BiochemistrybioRxivJul 15, 2022

Delineating organizational principles of the endogenous L-A virus by cryo-EM and computational analysis of native cell extracts

L. Schmidt, C. Tueting, F. L. Kyrilis…·P. L. Kastritis

The paper uses cryo-EM and computational analysis to study the structure and organization of the yeast L-A virus in native cell extracts, revealing capsid architecture and viral community dynamics.

DOI 10.1038/s42003-024-06204-7

yeastcryo-EM

𝕏 PostBluesky

BiophysicsbioRxivAug 31, 2019

2.7 A cryo-EM structure of vitrified M. musculus H-chain apoferritin from 200 keV \"screening microscope\"

F. Hamdi, C. Tueting, D. A. Semchonok…·P. L. Kastritis

The paper solves the 2.7 Å structure of mouse H-chain apoferritin using a 200 keV cryo-EM screening microscope without energy filters or aberration correctors.

DOI 10.1371/journal.pone.0232540

mousecryo-EM

𝕏 PostBluesky