Zobrazeno 1 - 10
of 46
pro vyhledávání: '"Tinglu Guan"'
Autor:
Larry Gerace, Howard J. Worman, Eric C. Schirmer, Arthur P. Hays, Cecilia Östlund, Denise A. Figlewicz, Tinglu Guan
Publikováno v:
Ostlund, C, Guan, T, Figlewicz, D A, Hays, A P, Worman, H J, Gerace, L & Schirmer, E C 2009, ' Reduction of a 4q35-encoded nuclear envelope protein in muscle differentiation ', Biochemical and Biophysical Research Communications, vol. 389, no. 2, pp. 279-83 . https://doi.org/10.1016/j.bbrc.2009.08.133
Muscular dystrophy and peripheral neuropathy have been linked to mutations in genes encoding nuclear envelope proteins; however, the molecular mechanisms underlying these disorders remain unresolved. Nuclear envelope protein p19A is a protein of unkn
Publikováno v:
Molecular and Cellular Biology. 29:5800-5812
Recently, several transmembrane proteins of the nuclear envelope have been implicated in regulation of signaling and gene expression. Here we demonstrate that the nuclear lamina-associated nuclear envelope transmembrane protein NET39 (Ppapdc3) functi
Publikováno v:
Molecular and Cellular Biology. 29:5718-5728
Mutations in certain nuclear envelope (NE) proteins cause muscular dystrophies and other disorders, but the disease mechanisms remain unclear. The nuclear envelope transmembrane protein NET25 (Lem2) is a truncated paralog of MAN1, an NE component lin
Autor:
Maximiliano A. D'Angelo, Aurelia Cassany, Tinglu Guan, Larry Gerace, Glen R. Nemerow, Harald Wodrich
Publikováno v:
Journal of Virology. 80:9608-9618
Adenoviruses are nonenveloped viruses with an ∼36-kb double-stranded DNA genome that replicate in the nucleus. Protein VII, an abundant structural component of the adenovirus core that is strongly associated with adenovirus DNA, is imported into th
Publikováno v:
Journal of Biological Chemistry. 278:16216-16221
Molecular recognition of the importin beta-binding (IBB) domain of importin alpha by importin beta is critical for the nuclear import of protein cargoes containing a classical nuclear localization signal. We have studied the function of four conserve
Publikováno v:
The Journal of Cell Biology
Previous work has shown that the transport of some small protein cargoes through the nuclear pore complex (NPC) can occur in vitro in the absence of nucleoside triphosphate hydrolysis. We now demonstrate that in the importin α/β and transportin imp
Publikováno v:
The Journal of Cell Biology
Tpr is a coiled-coil protein found near the nucleoplasmic side of the pore complex. Since neither the precise localization of Tpr nor its functions are well defined, we generated antibodies to three regions of Tpr to clarify these issues. Using light
Autor:
Aurelia Cassany, Glen R. Nemerow, Michael Kann, Harald Wodrich, Jessica Ragues, Larry Gerace, Dominique Bégu, Tinglu Guan
Publikováno v:
Journal of virology. 89(3)
In this study, we characterized the molecular basis for binding of adenovirus (AdV) to the cytoplasmic face of the nuclear pore complex (NPC), a key step during delivery of the viral genome into the nucleus. We used RNA interference (RNAi) to deplete
Publikováno v:
Journal of Virology. 74:2731-2739
Adenovirus (Ad) cell entry involves sequential interactions with host cell receptors that mediate attachment (CAR), internalization (alphavbeta3 and alphavbeta5), and penetration (alphavbeta5) of the endosomal membrane. These events allow the virus t
Publikováno v:
The Journal of Cell Biology
We recently developed an assay in which nuclear export of the shuttling transcription factor NFAT (nuclear factor of activated T cells) can be reconstituted in permeabilized cells with the GTPase Ran and the nuclear export receptor CRM1. We have now