Structural basis of nectin-1 recognition by pseudorabies virus glycoprotein D - Wikidata - awgldk - TriplyDB

Structural basis of nectin-1 recognition by pseudorabies virus glycoprotein D

Structural basis of nectin-1 recognition by pseudorabies virus glycoprotein D

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Structure-function dissection of the Pseudorabies virus glycoprotein B fusion loops.Zinc in Wound Healing Modulation.Functional relevance of the transmembrane domain and cytoplasmic tail of the pseudorabies virus glycoprotein H for membrane fusion.Molecular basis of binding between the global post-transcriptional regulator CsrA and the T3SS chaperone CesT.

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Structural basis of nectin-1 recognition by pseudorabies virus glycoprotein D

http://www.wikidata.org/entity/Q33752109

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2017 nî lūn-bûn

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2017 թուականի Մայիսին հրատարակուած գիտական յօդուած

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2017 թվականի մայիսին հրատարակված գիտական հոդված

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2017年の論文

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2017年論文

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2017年論文

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2017年論文

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2017年論文

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2017年論文

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Structural basis of nectin-1 recognition by pseudorabies virus glycoprotein D

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Structural basis of nectin-1 recognition by pseudorabies virus glycoprotein D

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Structural basis of nectin-1 recognition by pseudorabies virus glycoprotein D

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Structural basis of nectin-1 recognition by pseudorabies virus glycoprotein D

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Structural basis of nectin-1 recognition by pseudorabies virus glycoprotein D

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Structural basis of nectin-1 recognition by pseudorabies virus glycoprotein D

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Structural basis of nectin-1 recognition by pseudorabies virus glycoprotein D

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An Li

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Guangwen Lu

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Jianxun Qi

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Jinghua Yan

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Kegong Tian

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Lili Wu

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Tingrong Luo

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P2860

Nectin/PRR: an immunoglobulin-like cell adhesion molecule recruited to cadherin-based adherens junctions through interaction with Afadin, a PDZ domain-containing protein

A cell surface protein with herpesvirus entry activity (HveB) confers susceptibility to infection by mutants of herpes simplex virus type 1, herpes simplex virus type 2, and pseudorabies virus

Mutations in the N-terminal domains of nectin-1 and nectin-2 reveal differences in requirements for entry of various alphaherpesviruses and for nectin-nectin interactions.

Entry of alphaherpesviruses mediated by poliovirus receptor-related protein 1 and poliovirus receptor

Processing of X-ray diffraction data collected in oscillation mode

Herpes simplex virus glycoprotein D bound to the human receptor HveA

The 2009 pandemic H1N1 neuraminidase N1 lacks the 150-cavity in its active site

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Nectin ectodomain structures reveal a canonical adhesive interface

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