Search Results - "Davis, Jessie R."

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  1. 1

    Search-and-replace genome editing without double-strand breaks or donor DNA by Anzalone, Andrew V., Randolph, Peyton B., Davis, Jessie R., Sousa, Alexander A., Koblan, Luke W., Levy, Jonathan M., Chen, Peter J., Wilson, Christopher, Newby, Gregory A., Raguram, Aditya, Liu, David R.

    Published in Nature (London) (01-12-2019)
    “…Most genetic variants that contribute to disease 1 are challenging to correct efficiently and without excess byproducts 2 – 5 . Here we describe prime editing,…”
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  2. 2

    Efficient prime editing in mouse brain, liver and heart with dual AAVs by Davis, Jessie R., Banskota, Samagya, Levy, Jonathan M., Newby, Gregory A., Wang, Xiao, Anzalone, Andrew V., Nelson, Andrew T., Chen, Peter J., Hennes, Andrew D., An, Meirui, Roh, Heejin, Randolph, Peyton B., Musunuru, Kiran, Liu, David R.

    Published in Nature biotechnology (01-02-2024)
    “…Realizing the promise of prime editing for the study and treatment of genetic disorders requires efficient methods for delivering prime editors (PEs) in vivo…”
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  3. 3

    Engineered virus-like particles for transient delivery of prime editor ribonucleoprotein complexes in vivo by An, Meirui, Raguram, Aditya, Du, Samuel W., Banskota, Samagya, Davis, Jessie R., Newby, Gregory A., Chen, Paul Z., Palczewski, Krzysztof, Liu, David R.

    Published in Nature biotechnology (08-01-2024)
    “…Prime editing enables precise installation of genomic substitutions, insertions and deletions in living systems. Efficient in vitro and in vivo delivery of…”
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  4. 4

    Phage-assisted evolution and protein engineering yield compact, efficient prime editors by Doman, Jordan L., Pandey, Smriti, Neugebauer, Monica E., An, Meirui, Davis, Jessie R., Randolph, Peyton B., McElroy, Amber, Gao, Xin D., Raguram, Aditya, Richter, Michelle F., Everette, Kelcee A., Banskota, Samagya, Tian, Kathryn, Tao, Y. Allen, Tolar, Jakub, Osborn, Mark J., Liu, David R.

    Published in Cell (31-08-2023)
    “…Prime editing enables a wide variety of precise genome edits in living cells. Here we use protein evolution and engineering to generate prime editors with…”
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  5. 5

    Cytosine and adenine base editing of the brain, liver, retina, heart and skeletal muscle of mice via adeno-associated viruses by Levy, Jonathan M., Yeh, Wei-Hsi, Pendse, Nachiket, Davis, Jessie R., Hennessey, Erin, Butcher, Rossano, Koblan, Luke W., Comander, Jason, Liu, Qin, Liu, David R.

    Published in Nature biomedical engineering (01-01-2020)
    “…The success of base editors for the study and treatment of genetic diseases depends on the ability to deliver them in vivo to the relevant cell types. Delivery…”
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  6. 6

    Efficient in vivo base editing via single adeno-associated viruses with size-optimized genomes encoding compact adenine base editors by Davis, Jessie R., Wang, Xiao, Witte, Isaac P., Huang, Tony P., Levy, Jonathan M., Raguram, Aditya, Banskota, Samagya, Seidah, Nabil G., Musunuru, Kiran, Liu, David R.

    Published in Nature biomedical engineering (01-11-2022)
    “…The viral delivery of base editors has been complicated by their size and by the limited packaging capacity of adeno-associated viruses (AAVs). Typically,…”
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    Engineered virus-like particles for efficient in vivo delivery of therapeutic proteins by Banskota, Samagya, Raguram, Aditya, Suh, Susie, Du, Samuel W., Davis, Jessie R., Choi, Elliot H., Wang, Xiao, Nielsen, Sarah C., Newby, Gregory A., Randolph, Peyton B., Osborn, Mark J., Musunuru, Kiran, Palczewski, Krzysztof, Liu, David R.

    Published in Cell (20-01-2022)
    “…Methods to deliver gene editing agents in vivo as ribonucleoproteins could offer safety advantages over nucleic acid delivery approaches. We report the…”
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  9. 9

    Dynamic Consequences of Mutation of Tryptophan 215 in Thrombin by Peacock, Riley B, Davis, Jessie R, Markwick, Phineus R. L, Komives, Elizabeth A

    Published in Biochemistry (Easton) (08-05-2018)
    “…Thrombin normally cleaves fibrinogen to promote coagulation; however, binding of thrombomodulin to thrombin switches the specificity of thrombin toward protein…”
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