Sequences in rotavirus glycoprotein VP7 that mediate delayed translocation and retention of the protein in the endoplasmic reticulum
about
Molecular interactions in rotavirus assembly and uncoating seen by high-resolution cryo-EMOn the effect of thermodynamic equilibrium on the assembly efficiency of complex multi-layered virus-like particles (VLP): the case of rotavirus VLP.Retention by the endoplasmic reticulum of rotavirus VP7 is controlled by three adjacent amino-terminal residues.Analysis of multiple mRNAs from pathogenic equine infectious anemia virus (EIAV) in an acutely infected horse reveals a novel protein, Ttm, derived from the carboxy terminus of the EIAV transmembrane protein.Membrane binding and endoplasmic reticulum retention sequences of rotavirus VP7 are distinct: role of carboxy-terminal and other residues in membrane binding.The cytoplasmic and N-terminal transmembrane domains of cytochrome P450 contain independent signals for retention in the endoplasmic reticulum.
P2860
Sequences in rotavirus glycoprotein VP7 that mediate delayed translocation and retention of the protein in the endoplasmic reticulum
description
1990 nî lūn-bûn
@nan
1990年の論文
@ja
1990年論文
@yue
1990年論文
@zh-hant
1990年論文
@zh-hk
1990年論文
@zh-mo
1990年論文
@zh-tw
1990年论文
@wuu
1990年论文
@zh
1990年论文
@zh-cn
name
Sequences in rotavirus glycopr ...... n in the endoplasmic reticulum
@ast
Sequences in rotavirus glycopr ...... n in the endoplasmic reticulum
@en
type
label
Sequences in rotavirus glycopr ...... n in the endoplasmic reticulum
@ast
Sequences in rotavirus glycopr ...... n in the endoplasmic reticulum
@en
prefLabel
Sequences in rotavirus glycopr ...... n in the endoplasmic reticulum
@ast
Sequences in rotavirus glycopr ...... n in the endoplasmic reticulum
@en
P2093
P2860
P356
P1476
Sequences in rotavirus glycopr ...... n in the endoplasmic reticulum
@en
P2093
P2860
P304
P356
10.1083/JCB.111.4.1343
P407
P577
1990-10-01T00:00:00Z