Ebola Viral Glycoprotein Bound to Its Endosomal Receptor Niemann-Pick C1 (Q27703618)

2

object named as

Yi Shi

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Jinghua Yan

6

object named as

Jinghua Yan

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10 June 2020

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Jianxun Qi

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10 June 2020

5

Guangwen Lu

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10 June 2020

author name string

Han Wang

1

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10 June 2020

Jian Song

3

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10 June 2020

Yi Shi

2

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10 June 2020

George F Gao

7

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language of work or name

English

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publication date

14 January 2016

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published in

Cell

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volume

164

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page(s)

258-268

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issue

1-2

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Ebola virus entry requires the host-programmed recognition of an intracellular receptor

10 June 2020

cites work

1 reference

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Ebola virus entry requires the cholesterol transporter Niemann-Pick C1

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TIM-family proteins promote infection of multiple enveloped viruses through virion-associated phosphatidylserine

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Ebolavirus is internalized into host cells via macropinocytosis in a viral glycoprotein-dependent manner

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Small molecule inhibitors reveal Niemann-Pick C1 is essential for Ebola virus infection

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Structure of N-Terminal Domain of NPC1 Reveals Distinct Subdomains for Binding and Transfer of Cholesterol

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Proteolytic processing of the Ebola virus glycoprotein is not critical for Ebola virus replication in nonhuman primates

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Human macrophage C-type lectin specific for galactose and N-acetylgalactosamine promotes filovirus entry

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Assembly of the Ebola Virus Nucleoprotein from a Chaperoned VP35 Complex

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Crystal structure of the swine-origin A (H1N1)-2009 influenza A virus hemagglutinin (HA) reveals similar antigenicity to that of the 1918 pandemic virus

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Role of endosomal cathepsins in entry mediated by the Ebola virus glycoprotein

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Endosomal proteolysis of the Ebola virus glycoprotein is necessary for infection

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Cathepsin cleavage potentiates the Ebola virus glycoprotein to undergo a subsequent fusion-relevant conformational change

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12 December 2020

DC-SIGN and DC-SIGNR bind ebola glycoproteins and enhance infection of macrophages and endothelial cells.

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12 December 2020

Cellular entry of ebola virus involves uptake by a macropinocytosis-like mechanism and subsequent trafficking through early and late endosomes

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12 December 2020

Tyrosine kinase receptor Axl enhances entry of Zaire ebolavirus without direct interactions with the viral glycoprotein

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An Intrinsically Disordered Peptide from Ebola Virus VP35 Controls Viral RNA Synthesis by Modulating Nucleoprotein-RNA Interactions

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Cell adhesion-dependent membrane trafficking of a binding partner for the ebolavirus glycoprotein is a determinant of viral entry

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10.1016/J.CELL.2015.12.044

Identifiers

DOI

2 references

Consolidated OpenCitations Corpus – April 2017

1624007

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1624007

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10 June 2020

2 references

Consolidated OpenCitations Corpus – April 2017

1624007