Lan B. Van
Aarhus University
7 Papers
99 Citations
Lan B. Van is an academic researcher from Aarhus University. The author has contributed to research in topics: Protein subunit & Eukaryotic Ribosome. The author has an hindex of 4, co-authored 7 publications.
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Papers
Anti-CRISPR proteins encoded by archaeal lytic viruses inhibit subtype I-D immunity.
Fei He,Yuvaraj Bhoobalan-Chitty,Lan B. Van,Anders L. Kjeldsen,Matteo Dedola,Kira S. Makarova,Eugene V. Koonin,Ditlev E. Brodersen,Xu Peng +8 more
TL;DR: It is demonstrated that AcrID1 protein inhibits the CRISPR–Cas subtype I-D system by interacting directly with Cas10d protein, which is required for the interference stage, and belongs to a conserved family of compact, dimeric αβ-sandwich proteins characterized by extreme pH and temperature stability and a tendency to form protein fibres.
Structure of the nuclear exosome component Rrp6p reveals an interplay between the active site and the HRDC domain
Søren Flinch Midtgaard,Jannie Assenholt,Anette Thyssen Jonstrup,Lan B. Van,Torben Heick Jensen,Ditlev E. Brodersen +5 more
TL;DR: In vivo mutational studies show the importance of the domain contacts for the processing function of Rrp6p and highlight fundamental differences between the protein and its prokaryotic RNase D counterparts.
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Structural basis for inhibition of an archaeal CRISPR–Cas type I-D large subunit by an anti-CRISPR protein
M. Cemre Manav,M. Cemre Manav,Lan B. Van,Jinzhong Lin,Anders Fuglsang,Xu Peng,Ditlev E. Brodersen +6 more
TL;DR: The architecture of Cas10d suggests that the type I-D effector complex is similar to those found in type III CRISPR–Cas systems and that this feature is specifically exploited by phages for anti-CRISPR defence.
Publisher Correction: Anti-CRISPR proteins encoded by archaeal lytic viruses inhibit subtype I-D immunity.
Fei He,Yuvaraj Bhoobalan-Chitty,Lan B. Van,Anders L. Kjeldsen,Matteo Dedola,Kira S. Makarova,Eugene V. Koonin,Ditlev E. Brodersen,Xu Peng +8 more
TL;DR: In the original version of this Article, molecular weight markers in Figs 1c, 2c,d and 4d were displaced during the production process, so that they were not correctly aligned with the corresponding bands.
Structure and Function of the Bacterial Protein Toxin Phenomycin.
Bente Krogh Hansen,Camilla K. Larsen,Jakob Nielsen,Esben B. Svenningsen,Lan B. Van,Kristian M. Jacobsen,Morten Bjerring,Rasmus K. Flygaard,Lasse Jenner,Lene N. Nejsum,Ditlev E. Brodersen,Frans A. A. Mulder,Thomas Tørring,Thomas B. Poulsen +13 more
TL;DR: In this paper, the authors used morphological profiling to show that direct inhibition of translation underlies the toxicity of phenomycin in mammalian cells and solved a solution phase high-resolution structure of the protein using NMR spectroscopy.
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