Zobrazeno 1 - 10
of 38
pro vyhledávání: '"Kathy A. Suprenant"'
Autor:
Danielle R. Hamill, Susan A. Seipel, Marta Di Carlo, Danielle P. Romancino, Kathy A. Suprenant, Alexis Rodriguez, Edward M. Bonder
Publikováno v:
RNA. 11:646-656
The piwi/argonaute family of proteins is involved in key developmental processes such as stem cell maintenance and axis specification through molecular mechanisms that may involve RNA silencing. Here we report on the cloning and characterization of t
Autor:
Patrick A. Everley, Bernd Eichenmüller, Kathy A. Suprenant, Richard H. Himes, Elena Solovyeva, Nancy Kedersha, Jennifer Lang
Publikováno v:
Cell Motility and the Cytoskeleton. 56:225-236
Vaults are large (13 Mda) ribonucleoprotein particles that are especially abundant in multidrug resistant cancer cells and have been implicated in nucleocytoplasmic drug transport. To understand how these large barrel-shaped complexes are transported
Autor:
Chad G. Pearson, Mohan L. Gupta, Claudia J. Bode, Kerry Bloom, Kathy A. Suprenant, Richard H. Himes, Douglas A. Thrower
Publikováno v:
Molecular Biology of the Cell. 13:2919-2932
Microtubule dynamics are influenced by interactions of microtubules with cellular factors and by changes in the primary sequence of the tubulin molecule. Mutations of yeast β-tubulin C354, which is located near the binding site of some antimitotic c
Autor:
Mohan L. Gupta, Emily A. Reiff, Claudia J. Bode, Gunda I. Georg, Kathy A. Suprenant, Richard H. Himes
Publikováno v:
Biochemistry. 41:3870-3874
Paclitaxel (Taxol) and the epothilones are antimitotic agents that promote the assembly of mammalian tubulin and stabilization of microtubules. The epothilones competitively inhibit the binding of paclitaxel to mammalian brain tubulin, suggesting tha
Autor:
Patrick A. Everley, Bernd Eichenmüller, Denise M. Lepley, Kathy A. Suprenant, Jean M. Palange
Publikováno v:
Journal of Biological Chemistry. 277:1301-1309
In this report, we show that the echinoderm microtubule (MT)-associated protein (EMAP) and related EMAP-like proteins (ELPs) share a similar domain organization with a highly conserved hydrophobic ELP (HELP) domain and a large tryptophan-aspartic aci
Publikováno v:
Cell Motility and the Cytoskeleton. 50:161-172
The echinoderm microtubule-associated protein (EMAP) is a 75-kDa, WD-repeat protein associated with the mitotic spindle apparatus. To understand EMAP's biological role, it is important to determine its affinity for microtubules (MTs) and other cytosk
Autor:
Douglas P. Ahrens, J. M. Palange, Kathy A. Suprenant, A. Hostetler, Brian T. Livingston, M. A. F. Daggett, J. A. Tuxhorn, C. E. VanWinkle
Publikováno v:
Development, Genes and Evolution. 210:2-10
The echinoderm microtubule-associated protein (EMAP) is the most abundant microtubule-binding protein in the first cleavage mitotic apparatus in sea urchin embryos. The first goal of this study was to determine whether there is sufficient EMAP in the
Publikováno v:
Journal of Experimental Zoology. 283:258-269
Publikováno v:
Biochemical and Biophysical Research Communications. 250:502-505
Previous work has shown that the echinoderm microtubule-associated protein (EMAP) was a unique MAP with little sequence similarity with the brain MAPs. The purpose of this study was to determine whether there were any small domains within EMAP that w
Publikováno v:
Cell Motility and the Cytoskeleton. 41:57-67
The purpose of this study was to test whether any assembly-promoting microtubule-associated protein (MAP) would bundle microtubules and induce process formation in recombinant baculovirus-infected Sf9 cells, in particular, whether a non-neural MAP fr