Zobrazeno 1 - 10
of 30
pro vyhledávání: '"Young-Ok You"'
Publikováno v:
ACS Chemical Biology. 14:304-312
Nonelongating modules with condensation-incompetent ketosynthase (KS0) are frequently found in many trans-acyltransferase polyketide synthases (trans-AT PKS). KS0 catalyzes translocation of carbon chain without decarboxylative condensation. Unlike ty
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f37a84c77e147c8f359b4a015bed15cf
https://doi.org/10.1021/acschembio.8b01043
https://doi.org/10.1021/acschembio.8b01043
Abstract 1643: BTN1A1: a novel immune checkpoint for cancer immunotherapy beyond the PD-1/PD-L1 axis
Autor:
Young-Ok You, Yong-Sik Bong, Ezra M. Chung, Young-Joon Lee, Stephen S. Yoo, Andrew H. Park, Hyunjin Jung, Steven H. Lin, Young-Seung Kim, Amrish Sharma
Publikováno v:
Cancer Research. 81:1643-1643
Cancer immunotherapy is an effective treatment against individuals with late-stage cancer forms. The PD-1/PD-LI axis is a main therapeutic target used in clinical settings, but only 15-20% of cancer patients are responsive. Thus, there is an urgent u
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5597724238b7663363d7c5021f25afa7
https://doi.org/10.1158/1538-7445.am2021-1643
https://doi.org/10.1158/1538-7445.am2021-1643
Autor:
Hyun-Mo Jung, Young-Ok You
Publikováno v:
KOREAN JOURNAL OF PACKAGING SCIENCE AND TECHNOLOGY. 23:97-101
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::cefd063c1c290b19cb831d2b39be8297
https://doi.org/10.20909/kopast.2017.23.2.97
https://doi.org/10.20909/kopast.2017.23.2.97
Publikováno v:
Journal of the American Chemical Society. 139(40)
The dehydratase domain FosDH1 from module 1 of the fostriecin polyketide synthase (PKS) catalyzed the stereospecific interconversion of (3R)-3-hydroxybutyryl-FosACP1 (5) and (E)-2-butenoyl-FosACP1 (11), as established by a combination of direct LC-MS
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bb153d5ccc2f3c93522388e6ab1a6859
https://pubmed.ncbi.nlm.nih.gov/28902510
https://pubmed.ncbi.nlm.nih.gov/28902510
Autor:
Young Ok You, Wilfred A. van der Donk, Aaron K. Knowlton, Matthew R. Levengood, L. A. Furgerson Ihnken
Publikováno v:
ACS Chemical Biology
Methods that introduce posttranslational modifications in a general, mild, and non-sequence-specific manner using biologically produced peptides have great utility for investigation of the functions of these modifications. In this study, the substrat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::99f6d83cc248623c13f4f6397ff85f96
https://doi.org/10.1021/cb800309v
https://doi.org/10.1021/cb800309v
Autor:
Young Ok You, David E. Cane, Chiara R. Valenzano, Ashish Garg, Adrian T. Keatinge-Clay, Chaitan Khosla
Publikováno v:
Journal of the American Chemical Society. 132:14697-14699
The dehydratase (DH) domain of module 4 of the 6-deoxyerythronolide B synthase (DEBS) has been shown to catalyze an exclusive syn elimination/syn addition of water. Incubation of recombinant DH4 with chemoenzymatically prepared anti-(2R,3R)-2-methyl-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::40c96ce62b37000721a1584499f1d712
https://doi.org/10.1021/ja107344h
https://doi.org/10.1021/ja107344h
Publikováno v:
Biochemistry. 52(49)
RifDH10, the dehydratase domain from the terminal module of the rifamycin polyketide synthase, catalyzes the stereospecific syn dehydration of the model substrate (2S,3S)-2-methyl-3-hydroxypentanoyl-RifACP10, resulting in the exclusive formation of (
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0fb13540b8fd2c67a4d43e48c889824d
https://pubmed.ncbi.nlm.nih.gov/24274103
https://pubmed.ncbi.nlm.nih.gov/24274103
Autor:
M. Violet Lee, Leigh Anne Furgerson Ihnken, Amanda L. McClerren, Young Ok You, Neil L. Kelleher, Wilfred A. van der Donk
Publikováno v:
Journal of the American Chemical Society
The lantibiotic synthetases LctM and HalM2 are bifunctional enzymes that catalyze both the dehydration of serine and threonine residues and the Michael-type additions of cysteine residues to the resulting dehydroamino acids in their substrate peptide
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aae36a8b69f59122c4b7e035f667505c
https://pubmed.ncbi.nlm.nih.gov/19663480
https://pubmed.ncbi.nlm.nih.gov/19663480
Autor:
Young‐Ok You
Publikováno v:
The FASEB Journal. 22
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b07e2c7f69abd1e6a36ee22e76923f84
https://doi.org/10.1096/fasebj.22.1_supplement.611.20
https://doi.org/10.1096/fasebj.22.1_supplement.611.20
Autor:
Young Ok You, Wilfred A. van der Donk
Lantibiotic synthetases catalyze the dehydration of Ser and Thr residues in their peptide substrates to dehydroalanine (Dha) and dehydrobutyrine (Dha), respectively, followed by the conjugate addition of Cys residues to the Dha and Dhb residues to ge
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::29183dd25ad4d4033d1791dc07d5a7b9
https://europepmc.org/articles/PMC2517115/
https://europepmc.org/articles/PMC2517115/
