Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Anthony M. Ciancone"'
Autor:
Anthony M. Ciancone, Kyung W. Seo, Miaomiao Chen, Adam L. Borne, Adam H. Libby, Dina L. Bai, Ralph E. Kleiner, Ku-Lung Hsu
Publikováno v:
Journal of the American Chemical Society. 145:11056-11066
Publikováno v:
Israel Journal of Chemistry. 63
Autor:
Anthony M. Ciancone, Seyyedmohsen Hosseinibarkooie, Dina L. Bai, Adam L. Borne, Heather A. Ferris, Ku-Lung Hsu
Publikováno v:
Cell Chemical Biology. 29:1709-1720.e7
RNA granules are cytoplasmic condensates that organize biochemical and signaling complexes in response to cellular stress. Functional proteomic investigations under RNA-granule-inducing conditions are needed to identify protein sites involved in coup
Autor:
Jeffrey W. Brulet, Emmanuel K. Toroitich, Adam L. Borne, Ku-Lung Hsu, Adam H. Libby, Kun Yuan, Rebecca L. McCloud, Heung Sik Hahm, Anthony M. Ciancone, Timothy B. Ware
Publikováno v:
Nature chemical biology
Covalent probes serve as valuable tools for global investigation of protein function and ligand binding capacity. Despite efforts to expand coverage of residues available for chemical proteomics (e.g. cysteine and lysine), a large fraction of the pro
Autor:
Adam H. Libby, Ku-Lung Hsu, Emmanuel K. Toroitich, Anthony M. Ciancone, Skylar M Brodowski, Heung Sik Hahm
Publikováno v:
Chembiochem
Sulfonyl-triazoles have emerged as a new reactive group for covalent modification of tyrosine sites on proteins through sulfur-triazole exchange (SuTEx) chemistry. The extent to which this sulfur electrophile can be tuned for developing ligands with
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::99ccfe0154ab4cdebc465848c6b89eac
https://europepmc.org/articles/PMC8206015/
https://europepmc.org/articles/PMC8206015/
Autor:
Ku-Lung Hsu, Adam L Borne, Jeffrey W Brulet, Heung S Hahm, Emmanuel K Toroitich, Adam H Libby, Kun Yuan, Timothy B Ware, Rebecca L McCloud, Anthony M Ciancone
Publikováno v:
The Journal of Immunology. 204:159.44-159.44
Chemoproteomic probes serve as valuable tools to study and perturb protein function on a global scale. Despite advances in methodologies for cysteine and lysine profiling, a large fraction of the human proteome remains inaccessible with current activ