Role of the HIV-1 envelope transmembrane domain in intracellular sorting.

about

Role of the HIV-1 envelope transmembrane domain in intracellular sorting.

Item

http://www.wikidata.org/entity/Q54946721

description

2018 nî lūn-bûn

@nan

2018年の論文

@ja

2018年学术文章

@wuu

2018年学术文章

@zh-cn

2018年学术文章

@zh-hans

2018年学术文章

@zh-my

2018年学术文章

@zh-sg

2018年學術文章

@yue

2018年學術文章

@zh

2018年學術文章

@zh-hant

name

Role of the HIV-1 envelope transmembrane domain in intracellular sorting.

@en

Role of the HIV-1 envelope transmembrane domain in intracellular sorting.

@nl

type

Item

label

Role of the HIV-1 envelope transmembrane domain in intracellular sorting.

@en

Role of the HIV-1 envelope transmembrane domain in intracellular sorting.

@nl

prefLabel

Role of the HIV-1 envelope transmembrane domain in intracellular sorting.

@en

Role of the HIV-1 envelope transmembrane domain in intracellular sorting.

@nl

P1476

Role of the HIV-1 envelope transmembrane domain in intracellular sorting

@en

P2093

Aurélie Bary

http://www.w3.org/2001/XMLSchema#string

Pierre Cosson

http://www.w3.org/2001/XMLSchema#string

P2860

Rer1p, a retrieval receptor for endoplasmic reticulum membrane proteins, is dynamically localized to the Golgi apparatus by coatomer

TM9 family proteins control surface targeting of glycine-rich transmembrane domains

The HIV-1 envelope transmembrane domain binds TLR2 through a distinct dimerization motif and inhibits TLR2-mediated responses

Mutations in the leucine zipper of the human immunodeficiency virus type 1 transmembrane glycoprotein affect fusion and infectivity

HIV-1 gp41 and TCRalpha trans-membrane domains share a motif exploited by the HIV virus to modulate T-cell proliferation

A systematic approach to pair secretory cargo receptors with their cargo suggests a mechanism for cargo selection by Erv14.

The membrane-spanning domain of gp41 plays a critical role in intracellular trafficking of the HIV envelope protein.

The dynamic organisation of the secretory pathway.

Interaction of endocytic signals from the HIV-1 envelope glycoprotein complex with members of the adaptor medium chain family.

Lateral sorting in model membranes by cholesterol-mediated hydrophobic matching.

P2888

s12860-018-0153-4

P304

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1186/S12860-018-0153-4

http://www.w3.org/2001/XMLSchema#string

P433

http://www.w3.org/2001/XMLSchema#string

P478

http://www.w3.org/2001/XMLSchema#string

P50

Alexandre Vernay

Jackie Perrin

P577

2018-03-15T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P6179

1101547380

http://www.w3.org/2001/XMLSchema#string

P698

29544440

http://www.w3.org/2001/XMLSchema#string

P921

transmembrane protein

P932

5856207

http://www.w3.org/2001/XMLSchema#string