Author

O. von Loeffelholz

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· 2 Biochemistry· 1

Signature Assays, Organisms & Methods

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Assay:cryo-EM· 3 Approach:experimental assay· 3 Organism:human· 2 Research Focus:protein structure prediction· 2 Research Focus:cell type annotation· 1 Research Focus:protein folding & dynamics· 1 Assay:proteomics· 1 Approach:statistical model· 1

Frequent Co-Authors

A. Lechner· 1 shared A. Pena· 1 shared A. Purkiss· 1 shared B. P. Klaholz· 1 shared C. A. Moores· 1 shared C. Barchet· 1 shared C. Moores· 1 shared D. R. Drummond· 1 shared

Activity by Year

2018-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 12 mutual co-author links

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1 shared paperBiochemistry

A. Lechner

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

BiochemistrybioRxivPreprintNov 23, 2023

Structure of the human 80S ribosome at 1.9 A resolution - the molecular role of chemical modifications and ions in RNA

S. Holvec, C. Barchet, A. Lechner…·B. P. Klaholz

The paper presents a 1.9 Å cryo-EM structure of the human 80S ribosome, revealing new rRNA modifications and ions, and their roles in RNA architecture and function.

DOI 10.1101/2023.11.23.568509

humancryo-EM

𝕏 PostBluesky

BiophysicsBiology OpenPeer-reviewedJan 1, 2020

Cryo-EM of human Arp2/3 complexes provides structural insights into actin nucleation modulation by ARPC5 isoforms

O. von Loeffelholz, A. Purkiss, L. Cao…·C. A. Moores

The paper determines cryo-EM structures of human Arp2/3 complexes with different ARPC5 isoforms to show how isoform variation affects complex activity.

DOI 10.1242/bio.054304

humancryo-EM

𝕏 PostBluesky

BiophysicsbioRxivApr 16, 2018

Near-atomic cryo-EM structure of yeast kinesin 5-microtubule complex reveals a distinct binding footprint

O. von Loeffelholz, A. Pena, D. R. Drummond…·C. Moores

The paper determines the near-atomic structure of yeast kinesin-5 bound to microtubules, revealing conserved and distinct features of the motor-microtubule interface.

DOI 10.1016/j.jmb.2019.01.011

yeastcryo-EM

𝕏 PostBluesky