ライフサイエンスコーパス: beta karyopherin

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1 nto the nucleus using the cellular alpha and beta karyopherins.

2 e interaction between Ran and beta-importin /beta-karyopherin, a component of the docking complex for

3 7 kDa, which have been termed importin alpha/beta, karyopherin alpha/beta, or PTAC 58/ 97.

4 ytosolic, multiprotein complex that contains beta-karyopherin and another delta-DE Ran binding protei

5 stinct from the competition by importin-beta/beta-karyopherin and may be involved in the physiologica

6 n mutant of Ran, delta-DE Ran, also binds to beta-karyopherin and that delta-DE Ran can associate wit

7 Human NXF1 can be imported via importin beta, karyopherin beta2, importin 4, importin 11, and im

8 dicating that beta-catenin and importin-beta/beta-karyopherin both interact with common nuclear pore

9 related to karyopherin-alpha (Kap-alpha) and beta-karyopherin family members.

10 ve transport factors that are members of the beta-karyopherin family, which can bind cargo directly (

11 The flexible beta-karyopherin fold of Tnpo3 embraces the RNA recognit

12 erodimeric import receptor consisting of the beta-karyopherin importin beta, which mediates interacti

13 tin-alpha, SRP1 alpha) and a 97-kDa protein (beta-karyopherin, importin-beta).

14 ng is specifically competed by importin-beta/beta-karyopherin, indicating that beta-catenin and impor

15 The structural flexibility of beta-karyopherins is critical to mediate the interaction

16 clear import cargoes for the essential yeast beta-karyopherin, Kap121p.

17 diated by a previously uncharacterized yeast beta karyopherin Kap123p.

18 The alpha- and beta-karyopherins (Kaps), also called importins, mediate

19 Here we show that Yap1p is a target of the beta-karyopherin-like nuclear exporter, Crm1p.

20 ear pore machinery, similar to importin-beta/beta-karyopherin or other importin-beta-like import fact

21 n yeast there are at least 14 members of the beta-karyopherin protein family that govern the movement

22 Kap123p is a yeast beta-karyopherin that imports ribosomal proteins into th

23 binds with high affinity and specificity to beta-karyopherin to form a ternary complex.

24 selection may be a general mechanism used by beta-karyopherins to recognize transport substrates.

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