Zobrazeno 1 - 10
of 106
pro vyhledávání: '"John D York"'
Autor:
Niyas Kudukkil Pulloor, Sajith Nair, Kathleen McCaffrey, Aleksandar D Kostic, Pradeep Bist, Jeremy D Weaver, Andrew M Riley, Richa Tyagi, Pradeep D Uchil, John D York, Solomon H Snyder, Adolfo García-Sastre, Barry V L Potter, Rongtuan Lin, Stephen B Shears, Ramnik J Xavier, Manoj N Krishnan
Publikováno v:
PLoS Pathogens, Vol 10, Iss 2, p e1003981 (2014)
The pattern recognition receptor RIG-I is critical for Type-I interferon production. However, the global regulation of RIG-I signaling is only partially understood. Using a human genome-wide RNAi-screen, we identified 226 novel regulatory proteins of
Externí odkaz:
https://doaj.org/article/f96658edd07f4b1fb196fa2464f3ef81
Autor:
Kevin R. Bersell, Tao Yang, Jonathan D. Mosley, Andrew M. Glazer, Andrew T. Hale, Dmytro O. Kryshtal, Kyungsoo Kim, Jeffrey D. Steimle, Jonathan D. Brown, Joe-Elie Salem, Courtney C. Campbell, Charles C. Hong, Quinn S. Wells, Amanda N. Johnson, Laura Short, Marcia A. Blair, Elijah R. Behr, Evmorfia Petropoulou, Yalda Jamshidi, Mark D. Benson, Michelle J. Keyes, Debby Ngo, Ramachandran S. Vasan, Qiong Yang, Robert E. Gerszten, Christian Shaffer, Shan Parikh, Quanhu Sheng, Prince J. Kannankeril, Ivan P. Moskowitz, John D. York, Thomas J. Wang, Bjorn C. Knollmann, Dan M. Roden
Publikováno v:
Circulation. 147:824-840
Background: Brugada syndrome (BrS) is an inherited arrhythmia syndrome caused by loss-of-function variants in the cardiac sodium channel gene SCN5A (sodium voltage-gated channel alpha subunit 5) in ≈20% of subjects. We identified a family with 4 in
Autor:
D. Eric Dollins, Samuel G. Gattis, Peter C. Fridy, Kavi P.M. Mehta, John D. York, Julie Neubauer, James C. Otto, Wenli Bai
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America
Significance Our studies demonstrate that Vip1 represents a rare class of bifunctional enzyme capable of synthesizing and destroying signaling molecules important for nutrient adaptation, cellular architecture, and organelle morphology. We find that
Publikováno v:
Adv Biol Regul
Bisphosphate nucleotidase 2 (BPNT2) is a member of a family of phosphatases that are directly inhibited by lithium, the first-line medication for bipolar disorder. BPNT2 is localized to the Golgi, where it metabolizes the by-products of glycosaminogl
Golgi-resident bisphosphate nucleotidase 2 (BPNT2) is a member of a family of magnesium-dependent/lithium-inhibited phosphatases that share a three-dimensional structural motif that directly coordinates metal binding to effect phosphate hydrolysis. B
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::077a6fd14f4aa4ca128cf78294de26e3
https://doi.org/10.1101/2021.06.24.449779
https://doi.org/10.1101/2021.06.24.449779
Autor:
Pengfei Xu, Yue Xi, Pengcheng Wang, Zigmund Luka, Meishu Xu, Hung-Chun Tung, Jingyuan Wang, Songrong Ren, Dechun Feng, Bin Gao, Aatur D. Singhi, Satdarshan P. Monga, John D. York, Xiaochao Ma, Zhiying Huang, Wen Xie
Publikováno v:
Gastroenterology. 162(4)
Sulfoconjugation of small molecules or protein peptides is a key mechanism to ensure biochemical and functional homeostasis in mammals. The PAPS synthase 2 (PAPSS2) is the primary enzyme to synthesize the universal sulfonate donor 3'-phosphoadenosine
Autor:
Zhiying Huang, Zigmund Luka, Pengfei Xu, Donna B. Stolz, Da Yang, Yue Xi, Xinran Cai, Songrong Ren, Xiaochao Ma, John D. York, Yang Xie, Wen Xie, Min Zhang, Meishu Xu, Junjie Zhu
Publikováno v:
The FASEB Journal. 35
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America
Significance Regulation of iron homeostasis is perturbed in numerous pathologic states. Thus, identifications of mechanisms responsible for iron metabolism have broad implications for disease modification. Here, we link the sulfur assimilation pathwa
Publikováno v:
The Journal of Biological Chemistry
Golgi-resident bisphosphate nucleotidase 2 (BPNT2) is a member of a family of magnesium-dependent, lithium-inhibited phosphatases that share a three-dimensional structural motif that directly coordinates metal binding to effect phosphate hydrolysis.
Autor:
Galina I. Lepesheva, F. Peter Guengerich, Tatiana Y. Hargrove, Zdzislaw Wawrzak, Robert J. Schotzinger, William J. Hoekstra, John D. York, Laura Friggeri, Aidong Qi
Publikováno v:
Journal of Biological Chemistry. 292:6728-6743
With some advances in modern medicine (such as cancer chemotherapy, broad exposure to antibiotics, and immunosuppression), the incidence of opportunistic fungal pathogens such as Candida albicans has increased. Cases of drug resistance among these pa