Author

D. Toso

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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Biophysics· 4 Biochemistry· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 5 Assay:cryo-EM· 4 Organism:human· 3 Research Focus:protein structure prediction· 3 Research Focus:chromatin & epigenetic regulation· 1 Research Focus:protein folding & dynamics· 1 Assay:structural biology· 1

Frequent Co-Authors

E. Nogales· 4 shared A. B. Patel· 1 shared A. Litvak· 1 shared B. Greber· 1 shared C. Beck· 1 shared D. Portran· 1 shared J. Fang· 1 shared J. Fraser· 1 shared

Activity by Year

2019-2021 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 12 mutual co-author links

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4 shared papersBiophysics

E. Nogales

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5 papers

Recent·Most cited

Structural basis for the ARF GAP activity and specificity of the C9orf72 complex

M.-Y. Su, S. H. Fromm, J. Remis, D. Toso, J. H. Hurley

The paper determines the cryo-EM structure of the C9orf72 complex bound to ARF1-GDP-BeF3, revealing its specific GAP activity toward ARF1 and lower efficiency toward RAB8A.

bioRxiv · Apr 13, 2021Biochemistry

Efficient graphene oxide coating improves cryo-EM sample preparation and data collection from tilted grids

A. B. Patel, D. Toso, A. Litvak, E. Nogales

This paper improves cryo-EM sample preparation by modifying graphene oxide coating to enhance particle density and reduce drift during tilted data collection.

bioRxiv · Mar 8, 2021 · PreprintBiophysics

JARID2 and AEBP2 regulate PRC2 activity in the presence of H2A ubiquitination or other histone modifications

V. Kasinath, C. Beck, P. Sauer, S. Poepsel, J. Kosmatka, M. Faini, D. Toso, R. Aebersold, E. Nogales

This paper reports the cryo-EM structure of human PRC2 with cofactors JARID2 and AEBP2 bound to a nucleosome containing H2AK119ub1, revealing their roles in PRC2 activity regulation and histone modification crosstalk.

Science · Jan 22, 2021Peer-reviewedBiophysics

Effects of α-tubulin acetylation on microtubule structure and stability

L. Eshun-Wilson, R. Zhang, D. Portran, M. Nachury, D. Toso, T. Lohr, M. Vendruscolo, M. Bonomi, J. Fraser, E. Nogales

This study uses cryo-EM and molecular dynamics to show that α-tubulin acetylation at K40 reduces loop disorder and may affect microtubule stability.

bioRxiv · Jan 9, 2019Biophysics

The complete structure of the human TFIIH core complex

B. Greber, D. Toso, J. Fang, E. Nogales

The paper presents the complete structure of the human TFIIH core complex using cryo-electron microscopy, revealing assembly mechanisms and disease mutation sites.

bioRxiv · Jan 5, 2019Biophysics