Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Jazmine P. Hallinan"'
Autor:
Jazmine P. Hallinan, Lindsey A. Doyle, Betty W. Shen, Mesfin M. Gewe, Brittany Takushi, Madison A. Kennedy, Della Friend, James M. Roberts, Philip Bradley, Barry L. Stoddard
Publikováno v:
Communications Biology, Vol 4, Iss 1, Pp 1-14 (2021)
Jazmine Hallinan et al. report the development of a new generation of circular tandem repeat proteins with enhanced self-assembly. Functionalisation of these constructs with SARS CoV-2 VHH domains resulted in sub-nanomolar binding affinity to the vir
Externí odkaz:
https://doaj.org/article/11aa8d39f41348bfa35c908901de8e41
Autor:
Brett K. Kaiser, Barry L. Stoddard, Betty W. Shen, Caley Ray Polkinghorn, Carla A. Jaeger-Ruckstuhl, Lindsey Doyle, Philip Bradley, Yuexin Xu, Colin Correnti, Jazmine P. Hallinan, Della Friend, Amanda Qu, Raymond O. Ruff, Ashok D. Bandaranayake, Stanley R. Riddell
Publikováno v:
Nat Struct Mol Biol
Protein engineering has enabled the design of molecular scaffolds that display a wide variety of sizes, shapes, symmetry and subunit composition. Symmetric protein-based nanoparticles that display multiple protein domains can exhibit enhanced functio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6a930d2f6cb098ad0048e78f05921b61
https://doi.org/10.1038/s41594-020-0397-5
https://doi.org/10.1038/s41594-020-0397-5
Publikováno v:
Structure
The redesign of a macromolecular binding interface and corresponding alteration of recognition specificity is a challenging endeavor that remains recalcitrant to computational approaches. This is particularly true for the redesign of DNA binding spec
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ef357ee0c507439a5aee3121636f36c8
https://europepmc.org/articles/PMC7347439/
https://europepmc.org/articles/PMC7347439/
Autor:
Rachel Werther, Tony Nolan, Barry L. Stoddard, Roberto Galizi, Andrea Crisanti, Jazmine P. Hallinan, Nikolai Windbichler, Abigail R. Lambert, Kyle Havens, Jordan Jarjour, Mark Pogson
Publikováno v:
Nucleic Acids Research
The retargeting of protein–DNA specificity, outside of extremely modular DNA binding proteins such as TAL effectors, has generally proved to be quite challenging. Here, we describe structural analyses of five different extensively retargeted varian
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::047027b61ad00720231769219f79046e
https://doi.org/10.1093/nar/gkx544
https://doi.org/10.1093/nar/gkx544
Autor:
Lori I. Robins, Betty W. Shen, Jill M. Bolduc, Kyle Havens, Abigail R. Lambert, Andrew M. Scharenberg, Jazmine P. Hallinan, Nadia Kulshina, Jennifer K. Chik, Barry L. Stoddard, Jordan Jarjour, Brett K. Kaiser
Publikováno v:
Structure. 24:862-873
LAGLIDADG meganucleases are DNA cleaving enzymes used for genome engineering. While their cleavage specificity can be altered using several protein engineering and selection strategies, their overall targetability is limited by highly specific indire
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1628fcd2c9afb5ac2a0e78b92e26dd27
https://doi.org/10.1016/j.str.2016.03.024
https://doi.org/10.1016/j.str.2016.03.024
Autor:
Lindsey Doyle, Philip Bradley, David Baker, Jazmine P. Hallinan, Fabio Parmeggiani, Barry L. Stoddard, Jill M. Bolduc
Publikováno v:
Nature
Tandem repeat proteins, which are formed by repetition of modular units of protein sequence and structure, play important biological roles as macromolecular binding and scaffolding domains, enzymes, and building blocks for the assembly of fibrous mat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8e2d8fa4ed834e82d15926f81a4a4243
https://doi.org/10.1038/nature16191
https://doi.org/10.1038/nature16191
Autor:
Barry L. Stoddard, Lindsey Doyle, Caley Ray Polkinghorn, Brett K. Kaiser, Jazmine P. Hallinan, Phil Bradley
Publikováno v:
The FASEB Journal. 32
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::49a33c5d531609b8f57abc4a12666d2a
https://doi.org/10.1096/fasebj.2018.32.1_supplement.798.20
https://doi.org/10.1096/fasebj.2018.32.1_supplement.798.20