The tyrosine kinase Hck is an inhibitor of HIV-1 replication counteracted by the viral vif protein
about
Comprehensive analysis of interactions between the Src-associated protein in mitosis of 68 kDa and the human Src-homology 3 proteomeThe dimerization domain of HIV-1 viral infectivity factor Vif is required to block virion incorporation of APOBEC3GIdentification and biophysical assessment of the molecular recognition mechanisms between the human haemopoietic cell kinase Src homology domain 3 and ALG-2-interacting protein XRing finger protein ZIN interacts with human immunodeficiency virus type 1 VifProtein kinase C-delta regulates HIV-1 replication at an early post-entry step in macrophagesThe HIV-1 Vif PPLP motif is necessary for human APOBEC3G binding and degradationComprehensive investigation of the molecular defect in vif-deficient human immunodeficiency virus type 1 virionsHIV Genome-Wide Protein Associations: a Review of 30 Years of ResearchIsolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif proteinPartial cooperative unfolding in proteins as observed by hydrogen exchange mass spectrometry.Anti-CD45RO suppresses human immunodeficiency virus type 1 replication in microglia: role of Hck tyrosine kinase and implications for AIDS dementia.Activation of STAT3 by the Src family kinase Hck requires a functional SH3 domain.The human immunodeficiency virus type 1 Vif protein reduces intracellular expression and inhibits packaging of APOBEC3G (CEM15), a cellular inhibitor of virus infectivity.Identification of dominant negative human immunodeficiency virus type 1 Vif mutants that interfere with the functional inactivation of APOBEC3G by virus-encoded VifPotent suppression of viral infectivity by the peptides that inhibit multimerization of human immunodeficiency virus type 1 (HIV-1) Vif proteins.Characterization of producer cell-dependent restriction of murine leukemia virus replicationIntravirion processing of the human immunodeficiency virus type 1 Vif protein by the viral protease may be correlated with Vif function.On the solution conformation and dynamics of the HIV-1 viral infectivity factorAPOBEC3G impairs the multimerization of the HIV-1 Vif protein in living cells.HIV-1 Nef dimerization is required for Nef-mediated receptor downregulation and viral replication.Tumultuous relationship between the human immunodeficiency virus type 1 viral infectivity factor (Vif) and the human APOBEC-3G and APOBEC-3F restriction factors.Functional neutralization of HIV-1 Vif protein by intracellular immunization inhibits reverse transcription and viral replication.Towards Inhibition of Vif-APOBEC3G Interaction: Which Protein to Target?The Src kinase Lck facilitates assembly of HIV-1 at the plasma membrane.
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P2860
The tyrosine kinase Hck is an inhibitor of HIV-1 replication counteracted by the viral vif protein
description
2001 nî lūn-bûn
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2001 թուականի Մայիսին հրատարակուած գիտական յօդուած
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2001 թվականի մայիսին հրատարակված գիտական հոդված
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2001年の論文
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2001年学术文章
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2001年学术文章
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2001年学术文章
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2001年學術文章
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The tyrosine kinase Hck is an ...... acted by the viral vif protein
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The tyrosine kinase Hck is an ...... acted by the viral vif protein
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P2093
P2860
P356
P1476
The tyrosine kinase Hck is an ...... acted by the viral vif protein
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P2093
G Hassaïne
M Courcoul
Y Barthalay
P2860
P304
P356
10.1074/JBC.M009076200
P407
P577
2001-05-18T00:00:00Z