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Jacomine Krijnse-Locker

Researcher at Heidelberg University

Publications -  33
Citations -  5796

Jacomine Krijnse-Locker is an academic researcher from Heidelberg University. The author has contributed to research in topics: Viral replication & Virus. The author has an hindex of 27, co-authored 32 publications receiving 5388 citations. Previous affiliations of Jacomine Krijnse-Locker include University Hospital Heidelberg & Utrecht University.

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Composition and three-dimensional architecture of the dengue virus replication and assembly sites.

TL;DR: Dengue virus (DENV) modifies ER membrane structure to promote replication and efficient encapsidation of the genome into progeny virus, which could explain the coordination of distinct steps of the flavivirus replication cycle.
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Modification of intracellular membrane structures for virus replication

TL;DR: How viruses modify intracellular membranes is described, similarities between the structures that are induced by viruses of different families are highlighted and how these structures could be formed are discussed.
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Essential role of domain III of nonstructural protein 5A for hepatitis C virus infectious particle assembly.

TL;DR: Novel insights are provided into the production of infectious HCV and NS5A is identified as a major determinant for HCV assembly, which suggests that viral isolates may differ in their level of virion production and thus in theirlevel of fitness and pathogenesis.
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Three-Dimensional Architecture and Biogenesis of Membrane Structures Associated with Hepatitis C Virus Replication

TL;DR: The morphology of the membranous rearrangements induced in HCV-infected cells resemble those of the unrelated picorna-, corona- and arteriviruses, but are clearly distinct from those from the closely related flavivirus.
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The non-structural protein 4A of dengue virus is an integral membrane protein inducing membrane alterations in a 2K-regulated manner.

TL;DR: It is demonstrated that NS4A associates with membranes via 4 internal hydrophobic regions, which are all able to mediate membrane targeting of a cytosolic reporter protein, and a model of how this protein induces membrane rearrangements and how this property may be regulated is provided.