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

Molecular architecture of the ER translocase probed by chemical crosslinking of Sss1p to complementary fragments of Sec61p.

The EMBO journal - 1 Aug 1997

Wilkinson B M, Esnault Y, Craven R A, Skiba F, Fieschi J, K'epès F, Stirling C J

Abstract excerpt

The heterotrimeric Sec61p complex is a key component of the protein translocation apparatus of the endoplasmic reticulum membrane. The complex characterized from yeast includes Sec61p, a 10-transmembrane-domain membrane protein which has a direct interaction with Sss1p, a small C-terminal anchor protein. In order to gain some insight into the architecture of this complex we have functionally expressed Sec61p as...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Base Sequence

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

Share to DNA Primers

Share to Escherichia coli

Share to Fungal Proteins

Share to Molecular Sequence Data

Share to Mutation

Share to Saccharomyces cerevisiae

Source

Open in PubMed Open full text

Identifiers

PMID: 9303299
DOI: 10.1093/emboj/16.15.4549
PMCID: PMC1170081

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

Molecular architecture of the ER translocase probed by chemical crosslinking of Sss1p to complementary fragments of Sec61p.PMID 9303299Read ↗

Sss1p is required to complete protein translocon activation.Semantic proximity Read ↗

Stability and function of the Sec61 translocation complex depends on the Sss1p tail-anchor sequence.Semantic proximity Read ↗

Sec61p serves multiple roles in secretory precursor binding and translocation into the endoplasmic reticulum membrane.Semantic proximity Read ↗

Cancer associated mutations in Sec61γ alter the permeability of the ER translocase.Semantic proximity Read ↗

The conserved C-terminus of Sss1p is required to maintain the endoplasmic reticulum permeability barrier.Semantic proximity Read ↗

Distinct domains within yeast Sec61p involved in post-translational translocation and protein dislocation.Semantic proximity Read ↗

Interactions between Sec complex and prepro-alpha-factor during posttranslational protein transport into the endoplasmic reticulum.Semantic proximity Read ↗

SecY-SecY and SecY-SecG contacts revealed by site-specific crosslinking.Semantic proximity Read ↗

Two alternative binding mechanisms connect the protein translocation Sec71-Sec72 complex with heat shock proteins.Semantic proximity Read ↗

Cysteine cross-linking in native membranes establishes the transmembrane architecture of Ire1.Semantic proximity Read ↗

Bacterial protein translocation requires only one copy of the SecY complex in vivo.Semantic proximity Read ↗

Nearest neighbor analysis of the SecYEG complex. 1. Identification of a SecY-SecG interface.Semantic proximity Read ↗

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