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Ke Ding

Researcher at University of California, Los Angeles

Publications -  15
Citations -  385

Ke Ding is an academic researcher from University of California, Los Angeles. The author has contributed to research in topics: RNA polymerase & RNA. The author has an hindex of 8, co-authored 15 publications receiving 255 citations. Previous affiliations of Ke Ding include Stanford University & Queen's University.

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In situ structures of the segmented genome and RNA polymerase complex inside a dsRNA virus

TL;DR: These findings establish the link between sensing of environmental cues by the external proteins and activation of endogenous RNA transcription by the TEC inside the virus.
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In situ structures of rotavirus polymerase in action and mechanism of mRNA transcription and release

TL;DR: In situ cryo-electron microscopy structures of rotavirus dsRNA-dependent RNA polymerase (RdRp) in two states pertaining to transcription are presented, providing insights into the mechanism of viral mRNA transcription by determining the in situ Cryo-EM structures of a working rotav virus’ RNA-dependent-RNA polymerase, which is of interest for antiviral drug design.
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Structures and stabilization of kinetoplastid-specific split rRNAs revealed by comparing leishmanial and human ribosomes.

TL;DR: The structure of the leishmanial ribosome elucidates the organization of the six fragments of its large subunit rRNA and reveals atomic details of a unique 20 amino acid extension of the uL13 protein that pins down the ends of three of the rRNA fragments.
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Action of a minimal contractile bactericidal nanomachine.

TL;DR: The authors report near-atomic resolution structures of the R-type bacteriocin from Pseudomonas aeruginosa in the pre-contracted and post-contraction states, and these structures provide insight into the mechanism of action of molecular syringes.
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In situ structures of RNA-dependent RNA polymerase inside bluetongue virus before and after uncoating

TL;DR: The structural changes of RdRp VP1 and associated capsid shell proteins between BTV virions and cores suggest that the detachment of the outer capsid proteins VP2 and VP5 during viral entry induces both global movements of the inner Capsid shell and local conformational changes of the N-terminal latch helix.