Christopher P. Lapointe
Stanford University
31 Papers
42 Citations
Christopher P. Lapointe is an academic researcher from Stanford University. The author has contributed to research in topics: RNA & Ribosome. The author has an hindex of 11, co-authored 27 publications. Previous affiliations of Christopher P. Lapointe include University of Wisconsin-Madison.
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Papers
Dynamic competition between SARS-CoV-2 NSP1 and mRNA on the human ribosome inhibits translation initiation.
Christopher P. Lapointe,Rosslyn Grosely,Alex G. Johnson,Jinfan Wang,Israel S. Fernández,Joseph D. Puglisi +5 more
TL;DR: In this article, the SARS-CoV-2 NSP1 was found to be a virulence factor that inhibits protein synthesis by directly binding the human ribosome.
168
Multi-omics Reveal Specific Targets of the RNA-Binding Protein Puf3p and Its Orchestration of Mitochondrial Biogenesis.
Christopher P. Lapointe,Jonathan A. Stefely,Adam Jochem,Paul D. Hutchins,Gary M. Wilson,Nicholas W. Kwiecien,Joshua J. Coon,Marvin Wickens,David J. Pagliarini,David J. Pagliarini +9 more
TL;DR: A mechanism for post-transcriptionally coordinating CoQ production with OxPhos biogenesis is revealed, and the power of multi-omics for defining genuine targets of RBPs is demonstrated.
88
Protein-RNA networks revealed through covalent RNA marks
TL;DR: The results showed that although RNA-binding proteins productively bind specific RNAs to control their function, they also 'sample' RNAs without exerting a regulatory effect.
eIF5B gates the transition from translation initiation to elongation.
Jinfan Wang,Alex G. Johnson,Christopher P. Lapointe,Junhong Choi,Arjun Prabhakar,Dong-Hua Chen,Alexey Petrov,Alexey Petrov,Joseph D. Puglisi +8 more
TL;DR: Single-molecule dynamics reveal that the GTPase activity of eukaryotic initiation factor eIF5B serves as a kinetic checkpoint for the transition from translation initiation to elongation, and how its release may be governed by a change in the conformation of the ribosome complex that triggers GTP hydrolysis.
79
Unbiased screen of RNA tailing activities reveals a poly(UG) polymerase
Melanie A. Preston,Melanie A. Preston,Douglas F. Porter,Douglas F. Porter,Fan Chen,Natascha Buter,Natascha Buter,Christopher P. Lapointe,Christopher P. Lapointe,Sunduz Keles,Judith Kimble,Marvin Wickens +11 more
TL;DR: TRAID-seq is developed, a screening strategy in Saccharomyces cerevisiae to identify sequences added to a reporter RNA at single-nucleotide resolution by overexpressed candidate enzymes from different organisms that proposes that MUT-2 poly(UG) polymerase activity is required to promote genome integrity and RNA silencing.