Transport pathways of macromolecules between the nucleus and the cytoplasm

Current Opinion in Cell Biology

Volumn 11, Issue 3, 1999, Pages 402-406

  Adam, Stephen A ^a  

^a NORTHWESTERN UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

EXPORTIN; KARYOPHERIN; SMALL NUCLEAR RIBONUCLEOPROTEIN; UNCLASSIFIED DRUG;

CELL NUCLEUS; CELL TRANSPORT; CYTOPLASM; ENERGY; MACROMOLECULE; NUCLEAR LOCALIZATION SIGNAL; NUCLEAR PORE COMPLEX; PRIORITY JOURNAL; REVIEW; SIGNAL TRANSDUCTION;

EID: 0033152544     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-0674(99)80056-8     Document Type: Review

References (41)

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31. 3G-cap-binding protein called snurportin1 was identified. The protein enhances cap-dependent nuclear import of U snRNPs in permeabilized cells, functioning as an snRNP import receptor. The 45 kDa protein contains an IBB domain and interacts with importin β, but has no structural similarity to other transport factors. Snurportin1 can be thought of as an adapter like importin α.
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