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- Publications
- Influence
Structure of the Lassa virus nucleoprotein reveals a dsRNA-specific 3′ to 5′ exonuclease activity essential for immune suppression
- K. M. Hastie, C. R. Kimberlin, M. Zandonatti, I. MacRae, E. O. Saphire
- Biology, Medicine
- Proceedings of the National Academy of Sciences
- 24 January 2011
Lassa fever virus, a member of the family Arenaviridae, is a highly endemic category A pathogen that causes 300,000–500,000 infections per year in Western Africa. The arenaviral nucleoprotein NP has… Expand
Ebola Virus VP35 Protein Binds Double-Stranded RNA and Inhibits Alpha/Beta Interferon Production Induced by RIG-I Signaling
- W. Cárdenas, Y. Loo, +5 authors C. Basler
- Biology, Medicine
- Journal of Virology
- 1 June 2006
ABSTRACT The Ebola virus (EBOV) VP35 protein blocks the virus-induced phosphorylation and activation of interferon regulatory factor 3 (IRF-3), a transcription factor critical for the induction of… Expand
A glutamate switch controls voltage-sensitive phosphatase function
- L. Liu, S. Kohout, +4 authors D. Minor
- Biology, Medicine
- Nature Structural &Molecular Biology
- 11 April 2012
The Ciona intestinalis voltage-sensing phosphatase (Ci-VSP) couples a voltage-sensing domain (VSD) to a lipid phosphatase that is similar to the tumor suppressor PTEN. How the VSD controls enzyme… Expand
Ebolavirus VP35 uses a bimodal strategy to bind dsRNA for innate immune suppression
- C. R. Kimberlin, Z. Bornholdt, S. Li, V. Woods, I. MacRae, E. O. Saphire
- Biology, Medicine
- Proceedings of the National Academy of Sciences
- 29 December 2009
Ebolavirus causes a severe hemorrhagic fever and is divided into five distinct species, of which Reston ebolavirus is uniquely nonpathogenic to humans. Disease caused by ebolavirus is marked by early… Expand
Marburg Virus VP35 Can Both Fully Coat the Backbone and Cap the Ends of dsRNA for Interferon Antagonism
- Shridhar Bale, J. Julien, +9 authors E. O. Saphire
- Biology, Medicine
- PLoS pathogens
- 1 September 2012
Filoviruses, including Marburg virus (MARV) and Ebola virus (EBOV), cause fatal hemorrhagic fever in humans and non-human primates. All filoviruses encode a unique multi-functional protein termed… Expand
Hiding the evidence: two strategies for innate immune evasion by hemorrhagic fever viruses
- K. M. Hastie, Shridhar Bale, C. R. Kimberlin, E. O. Saphire
- Biology, Medicine
- Current Opinion in Virology
- 28 January 2012
The innate immune system is one of the first lines of defense against invading pathogens. Pathogens have, in turn, evolved different strategies to counteract these responses. Recent studies have… Expand
Structure of the 4-1BB/4-1BBL complex and distinct binding and functional properties of utomilumab and urelumab
- S. M. Chin, C. R. Kimberlin, +13 authors J. Chaparro-Riggers
- Medicine
- Nature Communications
- 8 November 2018
Abstract4-1BB (CD137, TNFRSF9) is an inducible costimulatory receptor expressed on activated T cells. Clinical trials of two agonist antibodies, utomilumab (PF-05082566) and urelumab (BMS-663513),… Expand
Ebola Virus VP 35 Protein Binds Double-Stranded RNA and Inhibits Alpha / Beta Interferon Production Induced by RIGI Signaling
- W. Cárdenas, Y. Loo, +5 authors C. Basler
- 2006
Department of Microbiology, Mount Sinai School of Medicine, New York, New York 10029; Department of Microbiology, University of Texas Southwestern Medical Center, Dallas, Texas; Special Pathogens… Expand
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Structure of the 4-1BB/4-1BBL complex and distinct binding and functional properties of utomilumab and urelumab
- S. M. Chin, C. R. Kimberlin, +15 authors J. Chaparro-Riggers
- Chemistry
- 8 November 2018
4-1BB (CD137, TNFRSF9) is an inducible costimulatory receptor expressed on activated T cells. Clinical trials of two agonist antibodies, utomilumab (PF-05082566) and urelumab (BMS-663513), are… Expand
SARAF Luminal Domain Structure Reveals a Novel Domain-Swapped β-Sandwich Fold Important for SOCE Modulation.
- C. R. Kimberlin, A. Meshcheriakova, +4 authors D. Minor
- Chemistry, Medicine
- Journal of molecular biology
- 12 July 2019
Store-Operated Calcium Entry (SOCE) plays key roles in cell proliferation, muscle contraction, immune responses, and memory formation. The coordinated interactions of a number of proteins from the… Expand