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of 6
pro vyhledávání: '"Ashley M. Thelen"'
Autor:
Livia Wilz Brier, Goran Stjepanovic, Ashley M. Thelen, Randy Schekman, Liang Ge, James H. Hurley
Publikováno v:
Molecular Biology of the Cell
Molecular biology of the cell, vol 30, iss 9
Molecular biology of the cell, vol 30, iss 9
Autophagy is a conserved eukaryotic pathway critical for cellular adaptation to changes in nutrition levels and stress. The class III phosphatidylinositol (PI)3-kinase complexes I and II (PI3KC3-C1 and -C2) are essential for autophagosome initiation
Autor:
Roberto Zoncu, Ashley M. Thelen
Publikováno v:
Trends in cell biology, vol 27, iss 11
Precise regulation of lipid biosynthesis, transport, and storage is key to the homeostasis of cells and organisms. Cells rely on a sophisticated but poorly understood network of vesicular and non-vesicular transport mechanisms to ensure efficient del
Autor:
Xuntian Jiang, Roberto Zoncu, Daniel K. Nomura, Ofer Moldavski, Laurel Mydock-McGrane, Daniel S. Ory, McKenna Feltes, Oliver B. Davis, Robert J. van Eijkeren, Rushika M. Perera, Brian M. Castellano, Sharon M. Louie, Douglas F. Covey, Ashley M. Thelen, Reini E. N. van der Welle
Publikováno v:
Science (New York, N.Y.), vol 355, iss 6331
The mechanistic target of rapamycin complex 1 (mTORC1) protein kinase is a master growth regulator that becomes activated at the lysosome in response to nutrient cues. Here, we identify cholesterol, an essential building block for cellular growth, as
Autor:
Ashley M. Thelen, Avi J. Samelson, Adam L. Yokom, Chun-Yan Lim, Rosalie E. Lawrence, Simon A. Fromm, Yangxue Fu, James H. Hurley, Lindsey N. Young, Do Jin Kim, Roberto Zoncu
Publikováno v:
Science
Cellular response to nutrient status An intricate regulatory mechanism is taking shape around control of the mechanistic target of rapamycin complex 1 (mTORC1) protein kinase complex. Physiological responses of cells to nutrient abundance is regulate
Autor:
Jaleen Albers, Jiantao Guo, George Grady, Ashley M. Thelen, Melanie A. Simpson, Tong Ju, Joseph J. Barycki
The enzyme UDP-glucose dehydrogenase (UGDH) catalyzes the reaction of UDP-glucose to UDP-glucuronate through two successive NAD(+)-dependent oxidation steps. Human UGDH apoprotein is purified as a mixture of dimeric and hexameric species. Addition of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::026bc658280cee7601d64ffb5ee55640
https://europepmc.org/articles/PMC4955856/
https://europepmc.org/articles/PMC4955856/
Publikováno v:
The Journal of biological chemistry. 288(49)
UDP-glucose dehydrogenase (UGDH) provides precursors for steroid elimination, hyaluronan production, and glycosaminoglycan synthesis. The wild-type UGDH enzyme purifies in a hexamer-dimer equilibrium and transiently undergoes dynamic motion that expo