In vivo homodimerisation of HTLV-1 Gag and MA gives clues to the retroviral capsid and TM envelope protein arrangement.
about
New insights into HTLV-1 particle structure, assembly, and Gag-Gag interactions in living cellsA unique spumavirus Gag N-terminal domain with functional properties of orthoretroviral matrix and capsidReconstruction and Function of Ancestral Center-of-Tree Human Immunodeficiency Virus Type 1 ProteinsQuantitative comparison of HTLV-1 and HIV-1 cell-to-cell infection with new replication dependent vectorsCharacterization of cytoplasmic Gag-gag interactions by dual-color z-scan fluorescence fluctuation spectroscopy.In situ quantification of protein binding to the plasma membrane.Electrostatic interactions drive membrane association of the human immunodeficiency virus type 1 Gag MA domainInterrelationship between cytoplasmic retroviral Gag concentration and Gag-membrane association.The retroviral capsid domain dictates virion size, morphology, and coassembly of gag into virus-like particles.
P2860
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P2860
In vivo homodimerisation of HTLV-1 Gag and MA gives clues to the retroviral capsid and TM envelope protein arrangement.
description
2004 nî lūn-bûn
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2004年の論文
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2004年学术文章
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2004年学术文章
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2004年学术文章
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name
In vivo homodimerisation of HT ...... envelope protein arrangement.
@en
In vivo homodimerisation of HT ...... envelope protein arrangement.
@nl
type
label
In vivo homodimerisation of HT ...... envelope protein arrangement.
@en
In vivo homodimerisation of HT ...... envelope protein arrangement.
@nl
prefLabel
In vivo homodimerisation of HT ...... envelope protein arrangement.
@en
In vivo homodimerisation of HT ...... envelope protein arrangement.
@nl
P2093
P1476
In vivo homodimerisation of HT ...... envelope protein arrangement.
@en
P2093
Andrey V Kajava
Fabienne Rayne
Jacqueline Lalanne
Robert Z Mamoun
P304
P356
10.1016/J.JMB.2004.09.013
P407
P577
2004-10-01T00:00:00Z