Zobrazeno 1 - 10
of 28
pro vyhledávání: '"Cheryl H. Arrowsmith"'
Publikováno v:
Journal of Biomolecular NMR. 66:209-219
HLTF is a SWI2/SNF2-family ATP-dependent chromatin remodeling enzyme that acts in the error-free branch of DNA damage tolerance (DDT), a cellular mechanism that enables replication of damaged DNA while leaving damage repair for a later time. Human HL
Publikováno v:
Journal of Biomolecular NMR. 51:185-190
Ube3A (also referred to as E6AP for E6 Associated Protein) is a E3 ubiquitin-protein ligase implicated in the development of Angelman syndrome by controlling degradation of synaptic protein Arc and oncogenic papilloma virus infection by controlling d
Autor:
Christophe Farès, Aleksandras Gutmanas, Alexander Lemak, Cheryl H. Arrowsmith, Maria Sunnerhagen, M. Karra, Seth Chitayat
Publikováno v:
Journal of Biomolecular NMR. 49:27-38
The quality of protein structures determined by nuclear magnetic resonance (NMR) spectroscopy is contingent on the number and quality of experimentally-derived resonance assignments, distance and angular restraints. Two key features of protein NMR da
Autor:
Fang Tian, Adelinda Yee, Xu Wang, Alexander Lemak, Cheryl H. Arrowsmith, James H. Prestegard, S. Srisailam
Publikováno v:
Journal of Biomolecular NMR. 39:53-61
In recent years paramagnetic NMR derived structural constraints have become increasingly popular for the study of biomolecules. Some of these are based on the distance and angular dependences of pseudo contact shifts (PCSs). When modulated by interna
Publikováno v:
Journal of Biomolecular NMR. 35:295-300
Autor:
Olivier Julien, Anna Hutton, Adelinda Yee, Isabelle Gignac, Cheryl H. Arrowsmith, Stéphane M. Gagné
Publikováno v:
Journal of Biomolecular NMR. 35:149-154
With the completion of genome sequencing projects, there are a large number of proteins for which we have little or no functional information. Since protein function is closely related to three-dimensional conformation, structural proteomics is one a
Autor:
Adelinda Yee, Ekaterina Kuznetsova, Cheryl H. Arrowsmith, Godwin Amegbey, Paul Stothard, David S. Wishart
Publikováno v:
Journal of Biomolecular NMR. 33:51-56
Godwin Amegbey, Paul Stothard, Ekaterina Kuznetsova, Adelinda Yee, Cheryl H. Arrowsmith & David S. Wishart* Departments of Computing Science and Biological Sciences, University of Alberta, Edmonton, Alberta, Canada T6G 2E8; Banting and Best Departmen
Publikováno v:
Journal of Biomolecular NMR. 28:81-84
Publikováno v:
Journal of Biomolecular NMR. 27:193-203
Simultaneous data acquisition in time-sharing (TS) multi-dimensional NMR experiments has been shown an effective means to reduce experimental time, and thus to accelerate structure determination of proteins. This has been accomplished by spin evoluti
Publikováno v:
Journal of Biomolecular NMR. 24:41-50
Here we present a novel suite of projected 4D triple-resonance NMR experiments for efficient sequential assignment of polypeptide backbone chemical shifts in 13C/15N doubly labeled proteins. In the 3D HNN[CAHA] and 3D HNN(CO)[CAHA] experiments, the 1