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Leonie C. van Dinten

Researcher at Leiden University Medical Center

Publications -  10
Citations -  1128

Leonie C. van Dinten is an academic researcher from Leiden University Medical Center. The author has contributed to research in topics: RNA-dependent RNA polymerase & RNA virus. The author has an hindex of 10, co-authored 10 publications receiving 1097 citations. Previous affiliations of Leonie C. van Dinten include Leiden University.

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An infectious arterivirus cDNA clone: identification of a replicase point mutation that abolishes discontinuous mRNA transcription.

TL;DR: This mutant provides the first evidence that the requirements for arterivirus genome replication and discontinuous mRNA synthesis are, at least partially, different and that these processes may be separated experimentally.
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Proteolytic Processing of the Open Reading Frame 1b-Encoded Part of Arterivirus Replicase Is Mediated by nsp4 Serine Protease and Is Essential for Virus Replication

TL;DR: An analysis of mutants showed that the selective blockage of ORF1b protein processing affected different stages of EAV reproduction, and the mutant with the nsp10/11 cleavage site mutation Gln-2837→Pro displayed an unusual phenotype.
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A zinc finger-containing papain-like protease couples subgenomic mRNA synthesis to genome translation in a positive-stranded RNA virus.

TL;DR: It is shown that the N-terminal replicase subunit, nonstructural protein 1 (nsp1), of the nidovirus equine arteritis virus is in fact dispensable for replication but crucial for transcription, thereby coupling Replicase expression and subgenomic mRNA synthesis in an unprecedented manner.
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The Arterivirus Nsp4 Protease Is the Prototype of a Novel Group of Chymotrypsin-like Enzymes, the 3C-like Serine Proteases

TL;DR: The results support a replicase processing model in which the SP cleaves multiple Glu(Gly/Ser/Ala) sites, and characterize the arterivirus SP as a representative of a novel group of chymotrypsin-like enzymes, the 3C-like serine proteases.
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A complex zinc finger controls the enzymatic activities of nidovirus helicases.

TL;DR: The characterized ATPase and helicase activities of bacterially expressed mutant forms of nsp10 and its human coronavirus 229E ortholog, nsp13, and correlated these in vitro activities with specific virus phenotypes suggest that the ZBD is critically involved in nidovirus replication and transcription by modulating the enzymatic activities of the helicase domain and other, yet unknown, mechanisms.