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A Functional Genomics Approach to Viral-Host Interactions for HIV [PDF]
Elledge, Stephen J.
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Charge of karyopherins and nuclear FG-Nups are key ingredients of nucleocytoplasmic transport. [PDF]
Mishra A, Van der Giessen E, Onck PR.
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Normal male fertility in a mouse model of KPNA2 deficiency. [PDF]
Rother F +3 more
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Directed stochasticity: Building biomolecular condensates in the right place. [PDF]
Geisler MS, Kemp JP, Duronio RJ.
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Exporting nuclear export inhibitors from hematologic to solid tumor malignancies. [PDF]
Chirino A, Maye A, Taylor J.
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Karyopherin-mediated nucleocytoplasmic transport
Nature Reviews Molecular Cell Biology, 2022Efficient and regulated nucleocytoplasmic trafficking of macromolecules to the correct subcellular compartment is critical for proper functions of the eukaryotic cell. The majority of the macromolecular traffic across the nuclear pores is mediated by the Karyopherin-β (or Kap) family of nuclear transport receptors.
Casey E. Wing +2 more
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Karyopherins and nuclear import
Current Opinion in Structural Biology, 2001Proteins of the karyopherin alpha and karyopherin beta families play a central role in nucleocytoplasmic transport. Recently, crystal structures of karyopherin alpha and its complexes with nuclear localization signal peptides, a karyopherin beta2-Ran complex and complexes of full-length and fragments of karyopherin beta1 with import substrates, Ran and
Y M, Chook, G, Blobel
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Karyopherins and kissing cousins
Trends in Cell Biology, 1998In eukaryotic cells, a regulated flux of molecules between the cytoplasm and the nucleus maintains two very different environments while allowing the controlled exchange of macromolecules necessary for their individual functions. Molecules entering or leaving the nucleus use nuclear localization signals or nuclear export signals to pass through ...
R W, Wozniak, M P, Rout, J D, Aitchison
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Karyopherin flexibility in nucleocytoplasmic transport
Current Opinion in Structural Biology, 2006Recent structural work on nuclear transport factors of the importin-beta superfamily of karyopherins has shown that these proteins are superhelices of HEAT repeats that are able to assume different conformations in different functional states. The inherent flexibility of these helicoids facilitates the accommodation of different binding partners by an ...
Elena, Conti +2 more
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