about
The host protein Staufen1 interacts with the Pr55Gag zinc fingers and regulates HIV-1 assembly via its N-terminusComplex interactions of HIV-1 nucleocapsid protein with oligonucleotidesIdentification of Staufen in the human immunodeficiency virus type 1 Gag ribonucleoprotein complex and a role in generating infectious viral particlesEfficient production of HIV-1 virus-like particles from a mammalian expression vector requires the N-terminal capsid domainAssociation of human immunodeficiency virus type 1 gag with membrane does not require highly basic sequences in the nucleocapsid: use of a novel Gag multimerization assayAnalysis of the initiating events in HIV-1 particle assembly and genome packagingAnx2 interacts with HIV-1 Gag at phosphatidylinositol (4,5) bisphosphate-containing lipid rafts and increases viral production in 293T cellsRedundant roles for nucleocapsid and matrix RNA-binding sequences in human immunodeficiency virus type 1 assembly.A large extension to HIV-1 Gag, like Pol, has negative impacts on virion assemblyThe cellular source for APOBEC3G's incorporation into HIV-1.Rapid localization of Gag/GagPol complexes to detergent-resistant membrane during the assembly of human immunodeficiency virus type 1.Quantitative fluorescence resonance energy transfer microscopy analysis of the human immunodeficiency virus type 1 Gag-Gag interaction: relative contributions of the CA and NC domains and membrane binding.The roles of APOBEC3G complexes in the incorporation of APOBEC3G into HIV-1.Gag induces the coalescence of clustered lipid rafts and tetraspanin-enriched microdomains at HIV-1 assembly sites on the plasma membrane.Interactions between HIV-1 Gag molecules in solution: an inositol phosphate-mediated switchSelective and nonselective packaging of cellular RNAs in retrovirus particles.Dynamic Association between HIV-1 Gag and Membrane Domains.Characterization of staufen1 ribonucleoproteins by mass spectrometry and biochemical analyses reveal the presence of diverse host proteins associated with human immunodeficiency virus type 1.Incorporation of pol into human immunodeficiency virus type 1 Gag virus-like particles occurs independently of the upstream Gag domain in Gag-polFormation of the tRNALys packaging complex in HIV-1.Structural dynamics of retroviral genome and the packagingNew insights into retroviral Gag-Gag and Gag-membrane interactions.A structurally disordered region at the C terminus of capsid plays essential roles in multimerization and membrane binding of the gag protein of human immunodeficiency virus type 1.Reovirus sigma NS protein localizes to inclusions through an association requiring the mu NS amino terminus.Human immunodeficiency virus type 1 matrix inhibits and confers cooperativity on gag precursor-membrane interactions.Perturbation of Human T-Cell Leukemia Virus Type 1 Particle Morphology by Differential Gag Co-Packaging.Inhibition of cellular HIV-1 protease activity by lysyl-tRNA synthetase.The interaction between HIV-1 Gag and APOBEC3G.Mutation of the SP1 sequence impairs both multimerization and membrane-binding activities of human immunodeficiency virus type 1 Gag.Elucidating the in vivo interactome of HIV-1 RNA by hybridization capture and mass spectrometry.
P2860
Q24315925-24E74DC8-352E-4CBF-9D88-BB303C84D569Q24539163-144AC9B3-1FF4-421F-A6AB-842C61099E8CQ24599767-D274D467-09C4-4056-A6DE-F82292436B6AQ28478202-991C588A-80D3-4D9D-9D31-72662D41E175Q30447057-7D04ECA3-3708-47FC-8301-68CBB63D9955Q30992792-A87B655A-387E-498D-AB56-AF284AE0DA36Q33422993-D2059A68-7100-452B-9FC4-4BE4DEA0B10AQ34123957-B7362DB7-9365-4088-8419-0083F57C9CB5Q34460625-D51D4F70-B54F-46D1-82B7-BE8423F6F45AQ34506802-EEDA4253-4927-4EF0-BA6B-820E038BA17BQ34781698-2FEB0808-0FF9-4B43-8781-F96DCE938BBBQ34978433-80DE36B6-232E-4713-99D0-1AE74A99C423Q35009019-A0073FF3-BA28-422E-8377-49831CE691CDQ35382894-9CC07498-9374-4379-BFAB-759E76F3976AQ35691189-369B83A9-C527-4D24-9317-E3769D77D66AQ35857245-ECA33C61-B06F-42E2-8A6D-1B58A38AFBB5Q36102200-F117085F-E21B-4D68-A66C-0F5F6CF1C342Q36364322-6511A6B6-5CD3-46C1-A345-2D1D9E68B566Q36942505-FDB31CFD-12AC-42F6-B6BF-CCE41E596411Q37633035-F3F0CFE4-568C-44A3-BD3A-BA6CC5E60941Q37974642-78745B36-829A-4A0A-A00D-DB79230D2774Q38227869-67E8495E-8D63-43BD-8E37-35047F1E192CQ39699793-8B997837-4A54-4D7D-8D6E-A2EBA35B4DFCQ39741994-BFDB49B0-DFAE-4FFD-AA22-DF6EBB3E9BA0Q39755256-A92ED0DA-774A-481A-930B-5A4429828781Q40103935-C69BFD73-A8A6-4261-A406-A22FC545A498Q40423828-1B972E8E-3B5E-40C8-ABA1-8B2C54740E99Q40552660-86BD0650-273E-43B8-9D76-70FC722308F9Q40894533-389EAD92-4AB9-42AB-8B33-78B2FC2E874FQ47094347-F30881C6-2381-4F77-960E-F9C093699DAD
P2860
description
2002 nî lūn-bûn
@nan
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
2002年论文
@zh
2002年论文
@zh-cn
name
Role of RNA in facilitating Gag/Gag-Pol interaction.
@en
Role of RNA in facilitating Gag/Gag-Pol interaction.
@nl
type
label
Role of RNA in facilitating Gag/Gag-Pol interaction.
@en
Role of RNA in facilitating Gag/Gag-Pol interaction.
@nl
prefLabel
Role of RNA in facilitating Gag/Gag-Pol interaction.
@en
Role of RNA in facilitating Gag/Gag-Pol interaction.
@nl
P2093
P2860
P1433
P1476
Role of RNA in facilitating Gag/Gag-Pol interaction.
@en
P2093
Ahmad Khorchid
Mark A Wainberg
Rabih Halwani
P2860
P304
P356
10.1128/JVI.76.8.4131-4137.2002
P407
P577
2002-04-01T00:00:00Z