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Items: 1 to 20 of 132

1.

The host proteins transportin SR2/TNPO3 and cyclophilin A exert opposing effects on HIV-1 uncoating.

Shah VB, Shi J, Hout DR, Oztop I, Krishnan L, Ahn J, Shotwell MS, Engelman A, Aiken C.

J Virol. 2013 Jan;87(1):422-32. doi: 10.1128/JVI.07177-11.

2.

Interplay between HIV entry and transportin-SR2 dependency.

Thys W, De Houwer S, Demeulemeester J, Taltynov O, Vancraenenbroeck R, Gérard M, De Rijck J, Gijsbers R, Christ F, Debyser Z.

Retrovirology. 2011 Jan 30;8:7. doi: 10.1186/1742-4690-8-7.

3.

The requirement for cellular transportin 3 (TNPO3 or TRN-SR2) during infection maps to human immunodeficiency virus type 1 capsid and not integrase.

Krishnan L, Matreyek KA, Oztop I, Lee K, Tipper CH, Li X, Dar MJ, Kewalramani VN, Engelman A.

J Virol. 2010 Jan;84(1):397-406. doi: 10.1128/JVI.01899-09.

4.

Transportin 3 and importin α are required for effective nuclear import of HIV-1 integrase in virus-infected cells.

Levin A, Hayouka Z, Friedler A, Loyter A.

Nucleus. 2010 Sep-Oct;1(5):422-31. doi: 10.4161/nucl.1.5.12903.

5.

A model for cofactor use during HIV-1 reverse transcription and nuclear entry.

Hilditch L, Towers GJ.

Curr Opin Virol. 2014 Feb;4:32-6. doi: 10.1016/j.coviro.2013.11.003. Review.

6.

TNPO3 protects HIV-1 replication from CPSF6-mediated capsid stabilization in the host cell cytoplasm.

De Iaco A, Santoni F, Vannier A, Guipponi M, Antonarakis S, Luban J.

Retrovirology. 2013 Feb 15;10:20. doi: 10.1186/1742-4690-10-20.

7.

Small-molecule inhibition of human immunodeficiency virus type 1 infection by virus capsid destabilization.

Shi J, Zhou J, Shah VB, Aiken C, Whitby K.

J Virol. 2011 Jan;85(1):542-9. doi: 10.1128/JVI.01406-10.

8.

Interaction of the HIV-1 intasome with transportin 3 protein (TNPO3 or TRN-SR2).

Larue R, Gupta K, Wuensch C, Shkriabai N, Kessl JJ, Danhart E, Feng L, Taltynov O, Christ F, Van Duyne GD, Debyser Z, Foster MP, Kvaratskhelia M.

J Biol Chem. 2012 Oct 5;287(41):34044-58. doi: 10.1074/jbc.M112.384669.

9.
10.

The ability of TNPO3-depleted cells to inhibit HIV-1 infection requires CPSF6.

Fricke T, Valle-Casuso JC, White TE, Brandariz-Nuñez A, Bosche WJ, Reszka N, Gorelick R, Diaz-Griffero F.

Retrovirology. 2013 Apr 26;10:46. doi: 10.1186/1742-4690-10-46.

11.

Complementary Assays Reveal a Low Level of CA Associated with Viral Complexes in the Nuclei of HIV-1-Infected Cells.

Hulme AE, Kelley Z, Foley D, Hope TJ.

J Virol. 2015 May;89(10):5350-61. doi: 10.1128/JVI.00476-15.

12.

HIV-1 Resistance to the Capsid-Targeting Inhibitor PF74 Results in Altered Dependence on Host Factors Required for Virus Nuclear Entry.

Zhou J, Price AJ, Halambage UD, James LC, Aiken C.

J Virol. 2015 Sep;89(17):9068-79. doi: 10.1128/JVI.00340-15.

13.

Interaction of transportin-SR2 with Ras-related nuclear protein (Ran) GTPase.

Taltynov O, Demeulemeester J, Christ F, De Houwer S, Tsirkone VG, Gerard M, Weeks SD, Strelkov SV, Debyser Z.

J Biol Chem. 2013 Aug 30;288(35):25603-13. doi: 10.1074/jbc.M113.484345.

14.

HIV-1 uncoating is facilitated by dynein and kinesin 1.

Lukic Z, Dharan A, Fricke T, Diaz-Griffero F, Campbell EM.

J Virol. 2014 Dec;88(23):13613-25. doi: 10.1128/JVI.02219-14.

15.
16.

The cargo-binding domain of transportin 3 is required for lentivirus nuclear import.

Logue EC, Taylor KT, Goff PH, Landau NR.

J Virol. 2011 Dec;85(24):12950-61. doi: 10.1128/JVI.05384-11.

17.

A new functional role of HIV-1 integrase during uncoating of the viral core.

Briones MS, Chow SA.

Immunol Res. 2010 Dec;48(1-3):14-26. doi: 10.1007/s12026-010-8164-z.

PMID:
20721640
18.

Role of human immunodeficiency virus type 1 integrase in uncoating of the viral core.

Briones MS, Dobard CW, Chow SA.

J Virol. 2010 May;84(10):5181-90. doi: 10.1128/JVI.02382-09.

19.

HIV-1 infection: going nuclear with TNPO3/Transportin-SR2 and integrase.

Luban J.

Curr Biol. 2008 Aug 26;18(16):R710-3. doi: 10.1016/j.cub.2008.07.037.

20.

Identification of capsid mutations that alter the rate of HIV-1 uncoating in infected cells.

Hulme AE, Kelley Z, Okocha EA, Hope TJ.

J Virol. 2015 Jan;89(1):643-51. doi: 10.1128/JVI.03043-14.

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