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

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

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

http://www.wikidata.org/entity/Q39462609

about

Next-generation sequencing identifies transportin 3 as the causative gene for LGMD1F Interaction of the HIV-1 intasome with transportin 3 protein (TNPO3 or TRN-SR2)A model for cofactor use during HIV-1 reverse transcription and nuclear entry CPSF6 Defines a Conserved Capsid Interface that Modulates HIV-1 Replication Lv4 Is a Capsid-Specific Antiviral Activity in Human Blood Cells That Restricts Viruses of the SIVMAC/SIVSM/HIV-2 Lineage Prior to Integration Efficient transduction of myeloid cells by an HIV-1-derived lentiviral vector that packages the Vpx accessory protein The HIV-1 integrase mutant R263A/K264A is 2-fold defective for TRN-SR2 binding and viral nuclear import.TNPO3 is required for HIV-1 replication after nuclear import but prior to integration and binds the HIV-1 core.The Role of TNPO3 in HIV-1 Replication.Virus-producing cells determine the host protein profiles of HIV-1 virion cores.Identification of residues in the C-terminal domain of HIV-1 integrase that mediate binding to the transportin-SR2 protein.Analysis of the functional compatibility of SIV capsid sequences in the context of the FIV gag precursor TNPO3 protects HIV-1 replication from CPSF6-mediated capsid stabilization in the host cell cytoplasm.The ability of TNPO3-depleted cells to inhibit HIV-1 infection requires CPSF6.The HIV-1 passage from cytoplasm to nucleus: the process involving a complex exchange between the components of HIV-1 and cellular machinery to access nucleus and successful integration.Viral and cellular requirements for the nuclear entry of retroviral preintegration nucleoprotein complexes.Knockdown of the host cellular protein transportin 3 attenuates prototype foamy virus infection.The host proteins transportin SR2/TNPO3 and cyclophilin A exert opposing effects on HIV-1 uncoating.Capsid-Dependent Host Factors in HIV-1 Infection.Capsid-CPSF6 Interaction Is Dispensable for HIV-1 Replication in Primary Cells but Is Selected during Virus Passage In Vivo.In vivo functions of CPSF6 for HIV-1 as revealed by HIV-1 capsid evolution in HLA-B27-positive subjects.Cellular cofactors of lentiviral integrase: from target validation to drug discovery.Interaction of transportin-SR2 with Ras-related nuclear protein (Ran) GTPase

P2860

Q21133534-2D251FE8-1F22-4F34-94FA-B435B0D3E7DA Q24295223-FE83A94C-3172-4B3C-8B1F-3781D9D8A04F Q26859218-BD1EE538-4628-42EE-8E18-1402614573B7 Q27672646-0A532B56-CA55-49FE-BB07-BC76E50DFBC5 Q28546614-A724BB47-640B-4392-8118-E2126CF9161C Q33926275-40147319-886B-4FD9-B729-8B503032455E Q34139212-3C09352B-82A8-4809-B274-FF42BAEF77B2 Q35943450-7C41B127-A606-47AC-9234-D53D25571F76 Q36131846-8485F6B0-B939-4608-932D-522DDB0034D6 Q36204700-D541F092-F045-4A83-96F2-A5B4280211AE Q36298318-67649A56-C1E7-4B9A-9F6B-CA31D999F197 Q36364277-27FD572A-E940-46CC-B78B-235B922ABCE7 Q36689568-6F39CFCC-21F4-4B09-BF82-B7C1588A1E4C Q36964335-0163D193-1DF6-468F-B1ED-5A4423EAF09C Q38003158-4E8D5D93-2557-4F47-B432-3A3AF11FD655 Q38150610-5F3D8326-8E5F-4EE1-A575-4C67ADD927BA Q38911973-13359617-BADF-4994-9AA9-BB9AEE4CAE6C Q39253660-6A58AEDC-1B69-4794-A42D-E69630ED165B Q39320682-BFB36C27-1F2E-4123-9C9C-BCCD251284E0 Q40698862-DDAE71CF-759B-4B85-AE25-D9C4B3381AEB Q41863178-37A6A5CF-0105-4D79-8F4A-2EABC92203EA Q42277905-950946CF-D50B-462A-9C08-03F049F8E81A Q42282078-BB09928C-A4AA-434A-89CC-F5A1A18F022A

P2860

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

http://www.wikidata.org/entity/Q39462609

description

2011 nî lūn-bûn

@nan

2011年の論文

@ja

2011年論文

@yue

2011年論文

@zh-hant

2011年論文

@zh-hk

2011年論文

@zh-mo

2011年論文

@zh-tw

2011年论文

@wuu

2011年论文

@zh

2011年论文

@zh-cn

name

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

@en

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

@nl

type

label

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

@en

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

@nl

prefLabel

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

@en

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

@nl

P1433

Q39462609-038C6240-8A20-4286-BB31-FCD1C5A9F402

P1476

Q39462609-59D6F474-C9E0-43AB-ADFB-1D2AC54ABA9D

P2093

Q39462609-0C2C6D9A-7F34-4CD0-B87F-90D8231A6C65

Q39462609-61E56313-2B6B-4430-862D-E83B7B3C3E58

Q39462609-6AB2DCFB-ED4E-43F1-8954-DCC4B7BC493A

Q39462609-A060863A-A296-4FAB-BFAE-9EE4CD42CF32

P2860

Q39462609-00E6FF35-C7CB-4FB8-8C4D-14615B2463FD

Q39462609-0BB0F9B9-3223-4EA9-A78E-3AF955E02287

Q39462609-11E07F99-1DCE-4B91-81FC-0822A33BF7E5

Q39462609-1512725E-64F0-4E5A-B7EA-05E25DF197C3

Q39462609-1846EEAC-4F7B-4E40-B563-D5F99B5F9903

Q39462609-2013883C-F318-44A2-951E-F61595EDC1DF

Q39462609-25110095-A3E3-4F87-A97C-F3F3F34853C3

Q39462609-27673092-7D5D-4D1B-9042-751283B7D70C

Q39462609-2A3597DA-CC92-454D-8446-8178AF101936

Q39462609-2BFDF552-F120-4875-BCCA-D35A182AEC85

P304

Q39462609-FC3CB7C3-8B71-41D6-B9DA-2B313E9720F8

P31

Q39462609-D981D0B9-AAA8-4D3B-B4AB-11381C7CAD08

P356

Q39462609-F43A4774-B16A-4B02-8B94-2F5F1842D485

P407

Q39462609-467CA1A3-3EC6-4666-900B-510C0F40B230

P433

Q39462609-372A0114-6AD1-41C1-A9C0-417B018A25D1

P478

Q39462609-19C5C01D-18DD-4272-88F1-D9BBC5B31A97

P577

Q39462609-1730C531-4089-431B-BB43-4CB0332DF6B2

P5875

Q39462609-3A148695-9509-4312-932C-F9D2FF1B8052

P698

Q39462609-B1F0C836-C954-41AF-B373-55DE19DDD7F0

P932

Q39462609-76BCAA4A-855D-435A-974D-C7FFC0AD8F53

P356

P1433

Journal of Virology

P1476

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

@en

P2093

Eric C Logue

http://www.w3.org/2001/XMLSchema#string

Kayleigh T Taylor

http://www.w3.org/2001/XMLSchema#string

Nathaniel R Landau

http://www.w3.org/2001/XMLSchema#string

Peter H Goff

http://www.w3.org/2001/XMLSchema#string

P2860

Structure of the nuclear transport complex karyopherin-beta2-Ran x GppNHp

Transportin-SR, a nuclear import receptor for SR proteins

Identification of host proteins required for HIV infection through a functional genomic screen

A conserved Drosophila transportin-serine/arginine-rich (SR) protein permits nuclear import of Drosophila SR protein splicing factors and their antagonist repressor splicing factor 1

Importin 13: a novel mediator of nuclear import and export.

Transportin-SR2 mediates nuclear import of phosphorylated SR proteins

Active nuclear import of human immunodeficiency virus type 1 preintegration complexes

HIV-1 Vpr interacts with the nuclear transport pathway to promote macrophage infection

Human immunodeficiency virus type 1 preintegration complexes: studies of organization and composition

Role of the basic domain of human immunodeficiency virus type 1 matrix in macrophage infection

P304

12950-12961

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1128/JVI.05384-11

http://www.w3.org/2001/XMLSchema#string

P407

P433

24

http://www.w3.org/2001/XMLSchema#string

P478

85

http://www.w3.org/2001/XMLSchema#string

P577

2011-10-05T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

51696699

http://www.w3.org/2001/XMLSchema#string

P698

21976643

http://www.w3.org/2001/XMLSchema#string

P932

3233122

http://www.w3.org/2001/XMLSchema#string