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

STT3B-dependent posttranslational N-glycosylation as a surveillance system for secretory protein.

Molecular cell - 13 Jul 2012

Sato Takashi, Sako Yasuhiro, Sho Misato, Momohara Mamiko, Suico Mary Ann, Shuto Tsuyoshi, Nishitoh Hideki, Okiyoneda Tsukasa, Kokame Koichi, Kaneko Masayuki, Taura Manabu, Miyata Masanori, Chosa Keisuke, Koga Tomoaki, Morino-Koga Saori, Wada Ikuo, Kai Hirofumi

Abstract excerpt

Nascent secretory proteins are extensively scrutinized at the endoplasmic reticulum (ER). Various signatures of client proteins, including exposure of hydrophobic patches or unpaired sulfhydryls, are coordinately utilized to reduce nonnative proteins in the ER. We report here the cryptic N-glycosylation site as a recognition signal for unfolding of a natively nonglycosylated protein, transthyretin (TTR), involved...

Read the complete abstract on PubMed

Topics

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

Share to Calcium-Binding Proteins
Share to Hexosyltransferases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mannosidases

Share to Polysaccharides

Share to Prealbumin

Share to Protein Unfolding

Share to Secretory Pathway

Share to Ubiquitin-Conjugating Enzymes

Source

Identifiers

PMID: 22607976
DOI: 10.1016/j.molcel.2012.04.015

Genes

TTR
EDEM3

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 3 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

STT3B-dependent posttranslational N-glycosylation as a surveillance system for secretory protein.PMID 22607976Read ↗

ATF6 Activation Reduces Amyloidogenic Transthyretin Secretion Through Increased Interactions with Endoplasmic Reticulum Proteostasis FactorsSemantic proximity Read ↗

PERK Signaling Regulates Extracellular Proteostasis of an Amyloidogenic Protein During Endoplasmic Reticulum StressSemantic proximity Read ↗

Endoplasmic reticulum quality control regulates the fate of transthyretin variants in the cell.Semantic proximity Read ↗

Cellular secretion and cytotoxicity of transthyretin mutant proteins underlie late-onset amyloidosis and neurodegeneration.Semantic proximity Read ↗

Proteomic characterization of amyloid deposits in transthyretin amyloidosis associated with various mutations.Semantic proximity Read ↗

Presence of N-glycosylated transthyretin in plasma of V30M carriers in familial amyloidotic polyneuropathy: an escape from ERAD.Semantic proximity Read ↗

ER-associated degradation relying on protein O-mannosylationSemantic proximity Read ↗

The importance of a gatekeeper residue on the aggregation of transthyretin: implications for transthyretin-related amyloidoses.Semantic proximity Read ↗

Spatial proteomics reveals secretory pathway disturbances caused by neuropathy-associated TECPR2Semantic proximity Read ↗

Core glycan in the yeast multicopper ferroxidase, Fet3p: a case study of N-linked glycosylation, protein maturation, and stability.Semantic proximity Read ↗

Rescue of secretion of rare-disease-associated misfolded mutant glycoproteins in UGGT1 knock-out mammalian cells.Semantic proximity Read ↗

AUTOTAC-mediated targeted degradation of transthyretin aggregates ameliorates hereditary transthyretin amyloidosisSemantic proximity Read ↗

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