Maturation-induced conformational changes of HIV-1 capsid protein and identification of two high affinity sites for cyclophilins in the C-terminal domain.

Maturation-induced conformational changes of HIV-1 capsid protein and identification of two high affinity sites for cyclophilins in the C-terminal domain.

Item
http://www.wikidata.org/entity/Q33852559
Time-Resolved Imaging of Single HIV-1 Uncoating In Vitro and in Living CellsThree isoforms of cyclophilin A associated with human immunodeficiency virus type 1 were found by proteomics by using two-dimensional gel electrophoresis and matrix-assisted laser desorption ionization-time of flight mass spectrometry.The intriguing cyclophilin A-HIV-1 Vpr interaction: prolyl cis/trans isomerisation catalysis and specific binding.Chimeric human immunodeficiency virus type 1 virions that contain the simian immunodeficiency virus nef gene are cyclosporin A resistant.Catalysis of cis/trans isomerization in native HIV-1 capsid by human cyclophilin ATripeptide interference with human immunodeficiency virus type 1 morphogenesis.The cysteine residues of HIV-1 capsid regulate oligomerization and cyclophilin A-induced changes.Microbial peptidyl-prolyl cis/trans isomerases (PPIases): virulence factors and potential alternative drug targets.trans-Complementation rescue of cyclophilin A-deficient viruses reveals that the requirement for cyclophilin A in human immunodeficiency virus type 1 replication is independent of its isomerase activityRetroviral proteomics and interactomes: intricate balances of cell survival and viral replication.Protein folding includes oligomerization - examples from the endoplasmic reticulum and cytosol.The capsid protein of human immunodeficiency virus: interactions of HIV-1 capsid with host protein factors.Structural consequences of cyclophilin A binding on maturational refolding in human immunodeficiency virus type 1 capsid protein.Interaction of human cyclophilin hCyp-18 with short peptides suggests the existence of two functionally independent subsites.Cyclophilin A binds to linear peptide motifs containing a consensus that is present in many human proteins.Peptidyl-prolyl isomerization targets rice Aux/IAAs for proteasomal degradation during auxin signalling.Probing contacts between the ribonuclease H domain of HIV-1 reverse transcriptase and nucleic acid by site-specific photocross-linking.
P2860

Maturation-induced conformational changes of HIV-1 capsid protein and identification of two high affinity sites for cyclophilins in the C-terminal domain.

Item
http://www.wikidata.org/entity/Q33852559
description
1999 nî lūn-bûn
@nan
1999 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年学术文章
@wuu
1999年学术文章
@zh-cn
1999年学术文章
@zh-hans
1999年学术文章
@zh-my
1999年学术文章
@zh-sg
1999年學術文章
@yue
name
Maturation-induced conformatio ...... lins in the C-terminal domain.
@ast
Maturation-induced conformatio ...... lins in the C-terminal domain.
@en
type
label
Maturation-induced conformatio ...... lins in the C-terminal domain.
@ast
Maturation-induced conformatio ...... lins in the C-terminal domain.
@en
prefLabel
Maturation-induced conformatio ...... lins in the C-terminal domain.
@ast
Maturation-induced conformatio ...... lins in the C-terminal domain.
@en
P1433
P1476
P2093
P2860
P304
P31
P356
P407
P433
P478
P577
P5875
P698
P356
P1433
P1476
Maturation-induced conformatio ...... lins in the C-terminal domain.
@en
P2093
P2860
P304
P31
P356
P407
P433
P478
P577
P5875
P698