Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Peter Michener"'
Autor:
Clare M. Adams, Ramkrishna Mitra, Youcai Xiao, Peter Michener, Juan Palazzo, Allen Chao, Jitendra Gour, Joel Cassel, Joseph M. Salvino, Christine M. Eischen
Publikováno v:
Cancer Discovery. 13:1210-1229
Triple-negative breast cancers (TNBC) frequently inactivate p53, increasing their aggressiveness and therapy resistance. We identified an unexpected protein vulnerability in p53-inactivated TNBC and designed a new PROteolysis TArgeting Chimera (PROTA
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::338c7ee0c9e0ddc7bdd6d7d8dd59e922
https://doi.org/10.1158/2159-8290.cd-22-1131
https://doi.org/10.1158/2159-8290.cd-22-1131
Autor:
Christine M. Eischen, Joseph M. Salvino, Joel Cassel, Jitendra Gour, Allen Chao, Juan Palazzo, Peter Michener, Youcai Xiao, Ramkrishna Mitra, Clare M. Adams
Supplementary Materials and Methods, Tables S1-S3, Figures S1-S7
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::043cd934e2ca32673c5b428cdf5854a4
https://doi.org/10.1158/2159-8290.22788849.v1
https://doi.org/10.1158/2159-8290.22788849.v1
Autor:
Christine M. Eischen, Joseph M. Salvino, Joel Cassel, Jitendra Gour, Allen Chao, Juan Palazzo, Peter Michener, Youcai Xiao, Ramkrishna Mitra, Clare M. Adams
Triple-negative breast cancers (TNBC) frequently inactivate p53, increasing their aggressiveness and therapy resistance. We identified an unexpected protein vulnerability in p53-inactivated TNBC and designed a new PROteolysis TArgeting Chimera (PROTA
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0035f0d07414b32dde4d95351c0ab2d7
https://doi.org/10.1158/2159-8290.c.6515061.v1
https://doi.org/10.1158/2159-8290.c.6515061.v1
Autor:
Justin M. Kollman, Peter Michener, Matthew C. Johnson, Yin-Ming Kuo, Anika L. Burrell, Jeffrey R. Peterson, Andrew J. Andrews, Krisna C. Duong-Ly, Sajitha Anthony
Several metabolic enzymes undergo reversible polymerization into macromolecular assemblies. The function of these assemblies is often unclear but in some cases they regulate enzyme activity and metabolic homeostasis. The guanine nucleotide biosynthet
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::17819870bf5114db25d67b37f47c9c1b
https://doi.org/10.1101/152173
https://doi.org/10.1101/152173
Autor:
Jeffrey R. Peterson, Peter Michener, Anika L. Burrell, Andrew J. Andrews, Sajitha Anthony, Jacqueline C. Simonet, Justin M. Kollman, Matthew C. Johnson, Yin-Ming Kuo, Krisna C. Duong-Ly
Publikováno v:
Molecular Biology of the Cell
The metabolic enzyme IMPDH assembles into octamers that can polymerize and form micron-scale structures in cells. Octamers can adopt active, expanded or inactive, compressed conformations driven by allosteric nucleotide and substrate binding. Both fo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::42407cbb68b24dbaf9c870c815b6fde5
https://pubmed.ncbi.nlm.nih.gov/28794265
https://pubmed.ncbi.nlm.nih.gov/28794265