Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Morgan B. Ludwicki"'
Autor:
Morgan B. Ludwicki, Jiahe Li, Erin A. Stephens, Richard W. Roberts, Shohei Koide, Paula T. Hammond, Matthew P. DeLisa
Publikováno v:
ACS Central Science, Vol 5, Iss 5, Pp 852-866 (2019)
Externí odkaz:
https://doaj.org/article/0192f621174940d7b673e9ba5021607e
Autor:
Bunyarit Meksiriporn, Morgan B. Ludwicki, Erin A. Stephens, Allen Jiang, Hyeon-Cheol Lee, Dujduan Waraho-Zhmayev, Lutz Kummer, Fabian Brandl, Andreas Plückthun, Matthew P. DeLisa
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-10 (2019)
Protein phosphorylation helps to control many important cellular activities. Here the authors describe a genetic selection strategy to isolate designed ankyrin repeat proteins that bind specifically to phosphomodified targets.
Externí odkaz:
https://doaj.org/article/f70795db157645a6a02bf6f3d05cdf0b
Autor:
Katherine J Forsythe, Bunyarit Meksiriporn, Erin A. Stephens, Pengbo Zhou, Connor Monticello, Matthew P. DeLisa, Morgan B. Ludwicki, Mingji Li, Andreas Plückthun, Tianzheng Ye, Lutz Kummer
Publikováno v:
ACS synthetic biology. 10(9)
Ubiquibodies (uAbs) are a customizable proteome editing technology that utilizes E3 ubiquitin ligases genetically fused to synthetic binding proteins to steer otherwise stable proteins of interest (POIs) to the 26S proteasome for degradation. The abi
Autor:
Richard W. Roberts, Shohei Koide, Morgan B. Ludwicki, Matthew P. DeLisa, Jiahe Li, Erin A. Stephens, Paula T. Hammond
Publikováno v:
ACS Central Science, Vol 5, Iss 5, Pp 852-866 (2019)
[Image: see text] Manipulation of the ubiquitin-proteasome pathway to achieve targeted silencing of cellular proteins has emerged as a reliable and customizable strategy for remodeling the mammalian proteome. One such approach involves engineering bi
Autor:
Erin A. Stephens, Lutz Kummer, Andreas Plückthun, Fabian Brandl, Dujduan Waraho-Zhmayev, Matthew P. DeLisa, Allen Jiang, Morgan B. Ludwicki, Bunyarit Meksiriporn, Hyeon-Cheol Lee
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-10 (2019)
Nature Communications
Nature Communications
There is an urgent need for affinity reagents that target phospho-modified sites on individual proteins; however, generating such reagents remains a significant challenge. Here, we describe a genetic selection strategy for routine laboratory isolatio
Autor:
Erin A. Stephens, T. Ye, Morgan B. Ludwicki, Bunyarit Meksiriporn, Mingji Li, K. J. Forsythe, C. Monticello, Andreas Plueckthun, Matthew P. DeLisa, Lutz Kummer
Ubiquibodies (uAbs) are a customizable proteome editing technology that utilizes E3 ubiquitin ligases genetically fused to synthetic binding proteins to steer otherwise stable proteins of interest (POIs) to the proteasome for degradation. The ability
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d4f4466137d09b4151d3e69214ae8619
https://doi.org/10.1101/2021.04.16.440242
https://doi.org/10.1101/2021.04.16.440242
Publikováno v:
AIChE Journal. 66