| IRF5-TNOP3 polymorphisms are associated with elite control of HIV infection: A retrospective study. | IRF5-TNOP3 polymorphisms are associated with elite control of HIV infection: A retrospective study.
Sepúlveda-Crespo D, Jiménez-Sousa MA, Fernández-Rodíguez A, Muñoz-Fernández MA, Jiménez JL, Moreno S, Garcia F, Martínez I, Benito JM, Rallón N, Resino S. | 06/1/2023 |
| Transportin-3 Facilitates Uncoating of Influenza A Virus. | Transportin-3 Facilitates Uncoating of Influenza A Virus.
Zou J, Yu L, Zhu Y, Yang S, Zhao J, Zhao Y, Jiang M, Xie S, Liu H, Zhao C, Zhou H., Free PMC Article | 04/30/2022 |
| CRISPR/Cas9-Induced Mutagenesis Corroborates the Role of Transportin-SR2 in HIV-1 Nuclear Import. | CRISPR/Cas9-Induced Mutagenesis Corroborates the Role of Transportin-SR2 in HIV-1 Nuclear Import.
Janssens J, Blokken J, Lampi Y, De Wit F, Zurnic Bonisch I, Nombela I, Van de Velde P, Van Remoortel B, Gijsbers R, Christ F, Debyser Z., Free PMC Article | 02/5/2022 |
| TNPO3-Mediated Nuclear Entry of the Rous Sarcoma Virus Gag Protein Is Independent of the Cargo-Binding Domain. | TNPO3-Mediated Nuclear Entry of the Rous Sarcoma Virus Gag Protein Is Independent of the Cargo-Binding Domain.
Rice BL, Stake MS, Parent LJ., Free PMC Article | 12/5/2020 |
| An Allele-Specific Functional SNP Associated with Two Systemic Autoimmune Diseases Modulates IRF5 Expression by Long-Range Chromatin Loop Formation. | An Allele-Specific Functional SNP Associated with Two Systemic Autoimmune Diseases Modulates IRF5 Expression by Long-Range Chromatin Loop Formation.
Thynn HN, Chen XF, Hu WX, Duan YY, Zhu DL, Chen H, Wang NN, Chen HH, Rong Y, Lu BJ, Yang M, Jiang F, Dong SS, Guo Y, Yang TL. | 09/19/2020 |
| our results support a model in which miR-128 is expressed in primary HIV-1 target cells, is a type I IFN response gene, and functions as a novel antiviral defense mechanism during HIV-1 infection, partly by repressing the nuclear import factors TNPO3 and by inhibiting HIV-1 replication and viral spreading | Interferon-Inducible MicroRNA miR-128 Modulates HIV-1 Replication by Targeting TNPO3 mRNA.
Bochnakian A, Zhen A, Zisoulis DG, Idica A, KewalRamani VN, Neel N, Daugaard I, Hamdorf M, Kitchen S, Lee K, Pedersen IM., Free PMC Article | 06/13/2020 |
| TNPO3 mutant protein expressed in limb girdle muscular dystrophy 1F cells is the second genetic defect leading to strong HIV-1 restriction. | The mutation of Transportin 3 gene that causes limb girdle muscular dystrophy 1F induces protection against HIV-1 infection.
Rodríguez-Mora S, De Wit F, García-Perez J, Bermejo M, López-Huertas MR, Mateos E, Martí P, Rocha S, Vigón L, Christ F, Debyser Z, Vílchez JJ, Coiras M, Alcamí J., Free PMC Article | 01/18/2020 |
| The crystal structure of the RSLD-TNPO3 complex revealed potential CPSF6 interaction residues, which were confirmed to mediate TNPO3 binding and CPSF6 nuclear import. Both binding and nuclear import were independent of RSLD phosphorylation, though a hyperphosphorylated mimetic mutant failed to bind TNPO3 and mislocalized to the cell cytoplasm | Differential role for phosphorylation in alternative polyadenylation function versus nuclear import of SR-like protein CPSF6.
Jang S, Cook NJ, Pye VE, Bedwell GJ, Dudek AM, Singh PK, Cherepanov P, Engelman AN., Free PMC Article | 11/30/2019 |
| A novel pathogenic variant (Arg923AspfsTer17) in TNPO3 segregates with limb-girdle muscular dystrophy 1F in a Hungarian family. | A novel pathogenic variant in TNPO3 in a Hungarian family with limb-girdle muscular dystrophy 1F.
Pál E, Zima J, Hadzsiev K, Ito YA, Hartley T, Care4Rare Canada Consortium, Boycott KM, Melegh B. | 09/7/2019 |
| Combining these results with small-angle X-ray scattering data for the complex of TRN-SR2 with truncated integrase, we propose a molecular model of the complex. We speculate that nuclear import of the PIC may proceed concurrently with the normal nuclear transport. | N-terminal half of transportin SR2 interacts with HIV integrase.
Tsirkone VG, Blokken J, De Wit F, Breemans J, De Houwer S, Debyser Z, Christ F, Strelkov SV., Free PMC Article | 06/24/2017 |
| IRF5-TNPO3 genetic variation is associated systemic lupus erythematosus. | The IRF5-TNPO3 association with systemic lupus erythematosus has two components that other autoimmune disorders variably share.
Kottyan LC, Zoller EE, Bene J, Lu X, Kelly JA, Rupert AM, Lessard CJ, Vaughn SE, Marion M, Weirauch MT, Namjou B, Adler A, Rasmussen A, Glenn S, Montgomery CG, Hirschfield GM, Xie G, Coltescu C, Amos C, Li H, Ice JA, Nath SK, Mariette X, Bowman S, UK Primary Sjögren's Syndrome Registry, Rischmueller M, Lester S, Brun JG, Gøransson LG, Harboe E, Omdal R, Cunninghame-Graham DS, Vyse T, Miceli-Richard C, Brennan MT, Lessard JA, Wahren-Herlenius M, Kvarnström M, Illei GG, Witte T, Jonsson R, Eriksson P, Nordmark G, Ng WF, UK Primary Sjögren's Syndrome Registry, Anaya JM, Rhodus NL, Segal BM, Merrill JT, James JA, Guthridge JM, Scofield RH, Alarcon-Riquelme M, Bae SC, Boackle SA, Criswell LA, Gilkeson G, Kamen DL, Jacob CO, Kimberly R, Brown E, Edberg J, Alarcón GS, Reveille JD, Vilá LM, Petri M, Ramsey-Goldman R, Freedman BI, Niewold T, Stevens AM, Tsao BP, Ying J, Mayes MD, Gorlova OY, Wakeland W, Radstake T, Martin E, Martin J, Siminovitch K, Moser Sivils KL, Gaffney PM, Langefeld CD, Harley JB, Kaufman KM., Free PMC Article | 09/26/2015 |
| Data suggest that the HIV-1 integrase (IN)/transportin-SR2 (TRN-SR2) interaction interface is a potential target for antiviral therapy. | The HIV-1 integrase mutant R263A/K264A is 2-fold defective for TRN-SR2 binding and viral nuclear import.
De Houwer S, Demeulemeester J, Thys W, Rocha S, Dirix L, Gijsbers R, Christ F, Debyser Z., Free PMC Article | 01/31/2015 |
| Tnpo3 mutants that are not able to interact with cleavage and polyadenylation specificity factor 6 do not facilitate HIV-1 infectivity, suggesting a potential route of pharmacological intervention in the treatment of AIDS. | Structural basis for nuclear import of splicing factors by human Transportin 3.
Maertens GN, Cook NJ, Wang W, Hare S, Gupta SS, Öztop I, Lee K, Pye VE, Cosnefroy O, Snijders AP, KewalRamani VN, Fassati A, Engelman A, Cherepanov P., Free PMC Article | 04/19/2014 |
| TNPO3 mutation is the cause of limb-girdle muscular dystrophy 1F, expands knowledge of the molecular basis of muscular dystrophies and bolsters the importance of defects of nuclear envelope proteins as causes of inherited myopathies. | Limb-girdle muscular dystrophy 1F is caused by a microdeletion in the transportin 3 gene.
Melià MJ, Kubota A, Ortolano S, Vílchez JJ, Gámez J, Tanji K, Bonilla E, Palenzuela L, Fernández-Cadenas I, Pristoupilová A, García-Arumí E, Andreu AL, Navarro C, Hirano M, Martí R, Melià MJ, Kubota A, Ortolano S, Vílchez JJ, Gámez J, Tanji K, Bonilla E, Palenzuela L, Fernández-Cadenas I, Pristoupilová A, García-Arumí E, Andreu AL, Navarro C, Hirano M, Martí R., Free PMC Articles: PMC3634201, PMC3634201 | 02/8/2014 |
| The TNPO3 gene is mapped within the Limb-girdle muscular dystrophy 1F critical interval and its 923-amino acid human gene product is also expressed in skeletal muscle. | Next-generation sequencing identifies transportin 3 as the causative gene for LGMD1F.
Torella A, Fanin M, Mutarelli M, Peterle E, Del Vecchio Blanco F, Rispoli R, Savarese M, Garofalo A, Piluso G, Morandi L, Ricci G, Siciliano G, Angelini C, Nigro V., Free PMC Article | 12/21/2013 |
| a model wherein one monomer of TRN-SR2 is bound to one monomer of RanGTP. | 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., Free PMC Article | 12/14/2013 |
| These results suggested that inhibition of HIV-1 by TNPO3-depleted cells requires CPSF6. | 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., Free PMC Article | 09/21/2013 |
| TNPO3 promotes HIV-1 infectivity indirectly, by shifting the CA-binding protein CPSF6 to the nucleus, thus preventing the excessive HIV-1 CA stability that would otherwise result from cytoplasmic accumulation of CPSF6. | 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., Free PMC Article | 08/31/2013 |
| In skeletal muscle of limb-girdle muscular dystrophy 1F individuals, expression of transportin 3 indicates altered transportin 3 function. | Limb-girdle muscular dystrophy 1F is caused by a microdeletion in the transportin 3 gene.
Melià MJ, Kubota A, Ortolano S, Vílchez JJ, Gámez J, Tanji K, Bonilla E, Palenzuela L, Fernández-Cadenas I, Pristoupilová A, García-Arumí E, Andreu AL, Navarro C, Hirano M, Martí R, Melià MJ, Kubota A, Ortolano S, Vílchez JJ, Gámez J, Tanji K, Bonilla E, Palenzuela L, Fernández-Cadenas I, Pristoupilová A, García-Arumí E, Andreu AL, Navarro C, Hirano M, Martí R., Free PMC Articles: PMC3634201, PMC3634201 | 06/29/2013 |
| These results suggest that TNPO3 and cyclophilin A facilitate HIV-1 infection by coordinating proper uncoating of the core in target cells. | 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., Free PMC Article | 03/2/2013 |
| TNPO3 can directly engage the HIV-1 IN tetramer prebound to the cognate DNA. | 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., Free PMC Article | 01/5/2013 |
| Identification of residues in the C-terminal domain of HIV-1 integrase that mediate binding to the transportin-SR2 protein. | Identification of residues in the C-terminal domain of HIV-1 integrase that mediate binding to the transportin-SR2 protein.
De Houwer S, Demeulemeester J, Thys W, Taltynov O, Zmajkovicova K, Christ F, Debyser Z., Free PMC Article | 01/5/2013 |
| Transportin 3 and importin alpha act as receptors and are required for effective nuclear import of HIV-1 integrase in virus-infected cells. | 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., Free PMC Article | 07/7/2012 |
| TNPO3 interacts with HIV-1 gag in the cytoplasm to assist HIV-1 infection after nuclear import. | TNPO3 is required for HIV-1 replication after nuclear import but prior to integration and binds the HIV-1 core.
Valle-Casuso JC, Di Nunzio F, Yang Y, Reszka N, Lienlaf M, Arhel N, Perez P, Brass AL, Diaz-Griffero F., Free PMC Article | 06/23/2012 |
| TNPO3 promotes HIV-1 infectivity at a step in the virus life cycle that is detectable after the preintegration complex arrives in the nucleus and capsid is the viral determinant for TNPO3 dependence. | Inhibition of HIV-1 infection by TNPO3 depletion is determined by capsid and detectable after viral cDNA enters the nucleus.
De Iaco A, Luban J., Free PMC Article | 06/16/2012 |