Zobrazeno 1 - 10
of 19
pro vyhledávání: '"Huay-Keng Loke"'
Autor:
Melissa Gallery, Julie Zhang, Daniel P Bradley, Pamela Brauer, Donna Cvet, Jose Estevam, Hadi Danaee, Edward Greenfield, Ping Li, Mark Manfredi, Huay-Keng Loke, Claudia Rabino, Brad Stringer, Mark Williamson, Tim Wyant, Johnny Yang, Qing Zhu, Adnan Abu-Yousif, O Petter Veiby
Publikováno v:
PLoS ONE, Vol 13, Iss 1, p e0191046 (2018)
Guanylyl cyclase C (GCC) is a cell-surface protein that is expressed by normal intestinal epithelial cells, more than 95% of metastatic colorectal cancers (mCRC), and the majority of gastric and pancreatic cancers. Due to strict apical localization,
Externí odkaz:
https://doaj.org/article/a7f83c04c46d4ef7a8377d00d5a34370
Autor:
Tim Wyant, Melissa Gallery, Daniel Bradley, Adnan O. Abu-Yousif, Mark Williamson, Jose Estevam, Qing Zhu, Ping Li, Johnny J. Yang, Mark Manfredi, Claudia Rabino, Huay-Keng Loke, Edward A. Greenfield, O. Petter Veiby, Julie Zhang, Brad Stringer, Hadi Danaee, Donna Cvet, Pamela Brauer
Publikováno v:
PLoS ONE, Vol 13, Iss 1, p e0191046 (2018)
PLoS ONE
PLoS ONE
Guanylyl cyclase C (GCC) is a cell-surface protein that is expressed by normal intestinal epithelial cells, more than 95% of metastatic colorectal cancers (mCRC), and the majority of gastric and pancreatic cancers. Due to strict apical localization,
Autor:
Pam Brauer, Qing Xu, Jingya Ma, Michael E. Bembenek, Jesse Chen, Zhong-Hua Yan, Lawrence R. Dick, Yafang Lin, Khris Garcia, Huay-Keng Loke, Anne L. Burkhardt
Publikováno v:
Analytical Biochemistry. 439:109-115
Cellular effects of a Nedd8-activating enzyme (NAE) inhibitor, MLN4924, using the AlphaScreen format were explored. MLN4924 acts as a substrate-assisted inhibitor of NAE by forming a tight binding Nedd8–MLN4924 adduct. The inhibited enzyme can no l
Autor:
Lawrence R. Dick, Hua Liao, Neil Rollins, Xiaofeng Yang, William D. Mallender, Qing Xu, James E. Brownell, James M. Gavin, Jingyang Chen, Alexandra E. Gould, Huay-Keng Loke, Jingya Ma, Trupti Lingaraj, Benjamin S. Amidon
Publikováno v:
Journal of Biological Chemistry. 287:15512-15522
Uba6 is a homolog of the ubiquitin-activating enzyme, Uba1, and activates two ubiquitin-like proteins (UBLs), ubiquitin and FAT10. In this study, biochemical and biophysical experiments were performed to understand the mechanisms of how Uba6 recogniz
Autor:
Dongyun Wu, Zhi Li, Qing Xu, Huay-Keng Loke, Anne L. Burkhardt, Liying Xie, Michael E. Bembenek, Ping Li, Li Li, Jingya Ma, Olga Tayber
Publikováno v:
Analytical Biochemistry. 408:321-327
The utility of antibody reagents for the detection of specific cellular targets for both research and diagnostic applications is widespread and continually expanding. Often it is useful to develop specific antibodies as reagent pairs that distinguish
Publikováno v:
Journal of the American Chemical Society. 127:5833-5839
The effect of [CO] on acetyl-CoA synthesis activity of the isolated alpha subunit of acetyl-coenzyme A synthase/carbon monoxide dehydrogenase from Moorella thermoacetica was determined. In contrast to the complete alpha(2)beta(2) enzyme where multipl
Autor:
Paul A. Lindahl, Huay-Keng Loke
Publikováno v:
Journal of Inorganic Biochemistry. 93:33-40
The acs ABCDE genes in the Clostridium thermoaceticum genome are used for autotrophic acetyl-CoA synthesis using the Wood–Ljungdahl pathway. A 2.8-kb region between acs C and acs D was cloned and sequenced. Two open reading frames, orf 7 (∼1.9 kb
Publikováno v:
Journal of the American Chemical Society. 124:8667-8672
In this study, a genetics-based method is used to truncate acetyl-coenzyme A synthase from Clostridium thermoaceticum (ACS), an alpha(2)beta(2) tetrameric 310 kDa bifunctional enzyme. ACS catalyzes the reversible reduction of CO(2) to CO and the synt
Publikováno v:
Proceedings of the National Academy of Sciences. 97:12530-12535
Acetyl-CoA synthase from Clostridium thermoaceticum (ACS Ct ) is an α 2 β 2 tetramer containing two novel Ni-X-Fe 4 S 4 active sites (the A and C clusters) and a standard Fe 4 S 4 cluster (the B cluster). The acsA and acsB genes encoding the enzyme
Absolute quantification of E1, ubiquitin-like proteins and Nedd8-MLN4924 adduct by mass spectrometry
Autor:
Teresa A. Soucy, Michael P. Thomas, Xiaofeng Yang, Hua Liao, Qing Xu, Huay-Keng Loke, Ping Li, Neil Rollins, William D. Mallender, Fengying Zhu, Jingya Ma, Lawrence R. Dick, James J. Minissale, James E. Brownell
Publikováno v:
Cell biochemistry and biophysics. 67(1)
Ubiquitin (Ub) and ubiquitin-like (Ubl) proteins regulate a variety of important cellular processes by forming covalent conjugates with target proteins or lipids. Ubl conjugation is catalyzed by a cascade of proteins including activating enzymes (E1)