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Bruno P. Klaholz

Researcher at University of Strasbourg

Publications -  89
Citations -  5916

Bruno P. Klaholz is an academic researcher from University of Strasbourg. The author has contributed to research in topics: Eukaryotic Ribosome & Initiation factor. The author has an hindex of 32, co-authored 82 publications receiving 4644 citations. Previous affiliations of Bruno P. Klaholz include Centre national de la recherche scientifique & French Institute of Health and Medical Research.

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The Crystal Structure of the Nuclear Receptor for Vitamin D Bound to Its Natural Ligand

TL;DR: The 1.8 A resolution crystal structure of the complex between a VDR ligand-binding domain (LBD) construct lacking the highly variable VDR-specific insertion domain and vitamin D shows that the N-terminal part of the LBD is essential for its structural and functional integrity while the large insertion peptide is dispensable.
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New tools for the analysis and validation of cryo-EM maps and atomic models

TL;DR: New methods and PHENIX tools for quality assessment of cryo-EM maps, atomic models and model-to-map fitting are presented and results of systematic application of these tools to high-resolution cryospecies maps and corresponding atomic models are analyzed and discussed.
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Structure of the human 80S ribosome

TL;DR: The near-atomic structure of the human ribosome derived from high-resolution single-particle cryo-electron microscopy and atomic model building is reported and reveals atomic details of the subunit interface, which is seen to remodel strongly upon rotational movements of the ribosomal subunits.
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N 6- Methyladenosine methyltransferase ZCCHC4 mediates ribosomal RNA methylation

TL;DR: A new m6A methyltransferase, ZCCHC4, is reported, which primarily methylates human 28S rRNA and also interacts with a subset of mRNAs, and was identified as a mammalian ribosome RNA (rRNA) N6-methyladenosine (m6A) writer protein that installs m 6A 4220 in 28s rRNA.
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Visualization of chemical modifications in the human 80S ribosome structure.

TL;DR: A high-resolution structure of the human 80S ribosome determined by cryo-electron microscopy is determined that has sufficient resolution to map more than 130 rRNA modifications, some of which were unknown, and suggests the possibility of designing more specific ribo-targeting drugs.