Membrane-association of EMR2/ADGRE2-NTF is regulated by site-specific N-glycosylation

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Location: Deutsche Nationalbibliothek Frankfurt am Main

ISSN: 2045-2322

Extent: Online-Ressource

Language: Englisch

Notes: online resource.

Bibliographic citation: Membrane-association of EMR2/ADGRE2-NTF is regulated by site-specific N-glycosylation ; volume:8 ; number:1 ; day:14 ; month:3 ; year:2018 ; pages:1-11 ; date:12.2018
Scientific reports ; 8, Heft 1 (14.3.2018), 1-11, 12.2018

Classification: Biowissenschaften, Biologie

Creator: Huang, Yi-Shu

Contributor: Chiang, Nien-Yi
Chang, Gin-Wen
Lin, Hsi-Hsien
SpringerLink (Online service)

DOI: 10.1038/s41598-018-22849-x

URN: urn:nbn:de:1111-2018051322137

Rights: Der Zugriff auf das Objekt ist unbeschränkt möglich.

Last update: 14.08.2025, 10:47 AM CEST

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Huang, Yi-Shu
Chiang, Nien-Yi
Chang, Gin-Wen
Lin, Hsi-Hsien
SpringerLink (Online service)

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Membrane-association of EMR2/ADGRE2-NTF is regulated by site-specific N-glycosylation

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Other Objects (12)

Site-specific N-glycosylation analysis of soluble Fcγ receptor IIIb in human serum

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N-Glycosylation signatures of epithelial ovarian cancer

ACE2 N-glycosylation modulates interactions with SARS-CoV-2 spike protein in a site-specific manner

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Self‐Promoted N‐Glycosylation: Extended Substrate Scope and Substituent Effects

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ACE2 N-glycosylation modulates interactions with SARS-CoV-2 spike protein in a site-specific manner

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Self‐Promoted N‐Glycosylation: Extended Substrate Scope and Substituent Effects

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