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ISSN 打印: 1045-4403

ISSN 在线: 2162-6502

The Impact Factor measures the average number of citations received in a particular year by papers published in the journal during the two preceding years. 2017 Journal Citation Reports (Clarivate Analytics, 2018) IF: 1.6 To calculate the five year Impact Factor, citations are counted in 2017 to the previous five years and divided by the source items published in the previous five years. 2017 Journal Citation Reports (Clarivate Analytics, 2018) 5-Year IF: 2.2 The Immediacy Index is the average number of times an article is cited in the year it is published. The journal Immediacy Index indicates how quickly articles in a journal are cited. Immediacy Index: 0.3 The Eigenfactor score, developed by Jevin West and Carl Bergstrom at the University of Washington, is a rating of the total importance of a scientific journal. Journals are rated according to the number of incoming citations, with citations from highly ranked journals weighted to make a larger contribution to the eigenfactor than those from poorly ranked journals. Eigenfactor: 0.00058 The Journal Citation Indicator (JCI) is a single measurement of the field-normalized citation impact of journals in the Web of Science Core Collection across disciplines. The key words here are that the metric is normalized and cross-disciplinary. JCI: 0.33 SJR: 0.345 SNIP: 0.46 CiteScore™:: 2.5 H-Index: 67

Indexed in

Molecular Mechanisms of Nuclear Protein Transport

卷 7, 册 1-2, 1997, pp. 61-72
DOI: 10.1615/CritRevEukarGeneExpr.v7.i1-2.40
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摘要

Transport of proteins into and out of the nucleus occurs through nuclear pore complexes (NPC). A heterodimeric protein complex, composed of karyopherin a and β (or importin α and β) functions to target proteins containing a nuclear localization sequence (NLS) to the NPCs. Two additional proteins, the GTPase Ran and p10, are required to translocate the docked NLS protein into the nucleus. The α subunit of karyopherin functions as the NLS receptor, whereas the β subunit mediates docking to nucleoporins that contain peptide repeats. During import the karyopherin heterodimer dissociates: karyopherin α and import substrates enter and accumulate in the nucleoplasm, whereas karyopherin β accumulates at the nuclear pore complex. Ran-GTP induces dissociation of karyopherin α from β by forming a complex with karyopherin β and promotes the release of both karyopherin subunits from a docking site. Protein transport across the NPC may occur via guided diffusion involving the karyopherin-mediated docking and undocking of import substrate to multiple binding sites that extend from the cytoplasmic to the nucleoplasmic ends of the NPC.

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