Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Maturation cleavage within the ectodomain of Lassa virus glycoprotein relies on stabilization by the cytoplasmic tail.

FEBS letters - 5 Nov 2010

Schlie Katrin, Strecker Thomas, Garten Wolfgang

Abstract excerpt

The Lassa virus glycoprotein consists of an ectodomain, a transmembrane anchor, and a cytoplasmic domain. It is synthesized as an inactive precursor and cleaved within the ectodomain to yield the mature form. Here, we show that this maturation cleavage can be abolished by mutation of single conserved amino acids within the cytoplasmic domain at the carboxy-terminus of the glycoprotein. Moreover, substitutions and...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to CHO Cells
Share to Cricetinae
Share to Cricetulus

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Cytoplasm

Share to Glycoproteins

Share to Peptide Hydrolases

Share to Protein Stability

Share to Viral Proteins

Source

Identifiers

PMID: 20875414
DOI: 10.1016/j.febslet.2010.09.032

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Maturation cleavage within the ectodomain of Lassa virus glycoprotein relies on stabilization by the cytoplasmic tail.PMID 20875414Read ↗

The role of single N-glycans in proteolytic processing and cell surface transport of the Lassa virus glycoprotein GP-C.Semantic proximity Read ↗

Activation and maturation of SARS-CoV main proteaseSemantic proximity Read ↗

Structural criteria for regulation of membrane fusion and virion incorporation by the murine leukemia virus TM cytoplasmic domain.Semantic proximity Read ↗

Effects of N-linked glycan of Lassa Virus Envelope Glycoprotein on the Immune ResponseSemantic proximity Read ↗

Functional analysis of the cytoplasmic tail of Moloney murine leukemia virus envelope protein.Semantic proximity Read ↗

Transport of meprin subunits through the secretory pathway: role of the transmembrane and cytoplasmic domains and oligomerization.Semantic proximity Read ↗

Mutations altering the gammaretrovirus endoproteolytic motif affect glycosylation of the envelope glycoprotein and early events of the virus life cycle.Semantic proximity Read ↗

Characterization of full-length and cytoplasmic tail-truncated envelope glycoproteins incorporated into human immunodeficiency virus (HIV-1) virions and virus-like particlesSemantic proximity Read ↗

The cytoplasmic domain of Marburg virus GP modulates early steps of viral infection.Semantic proximity Read ↗

A tyrosine motif in the cytoplasmic domain of mason-pfizer monkey virus is essential for the incorporation of glycoprotein into virions.Semantic proximity Read ↗

Virus maturation targets the protein capsid to concerted disassembly and unfolding.Semantic proximity Read ↗

Effects of blocking individual maturation cleavages in murine leukemia virus gag.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.