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

The unfolded-protein-response element discriminates misfolding induced by different mutant pro-sequences of yeast carboxypeptidase Y.

Biochemical and biophysical research communications - 6 Apr 1995

Chaudhuri B, Delany N S, Stephan C

Abstract excerpt

The C-terminal region of the chaperone-like pro-sequence (py) of yeast carboxypeptidase Y (CPY) is suggested to be crucial for the folding of mature CPY. In order to study the influence of hydrophobic residues in this domain, a set of mutations have been introduced in py. Unexpectedly, only small amounts of CPY precursors are expressed when Leu108, at the C-terminal end of py, is substituted for polar residues...

Read the complete abstract on PubMed

Topics

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

Share to Base Sequence
Share to DNA Primers
Share to Fungal Proteins

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

Share to Glycosylation

Share to Molecular Sequence Data

Share to Mutation

Share to Protein Folding

Share to Saccharomyces cerevisiae

Source

Identifiers

PMID: 7726851
DOI: 10.1006/bbrc.1995.1466

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

The unfolded-protein-response element discriminates misfolding induced by different mutant pro-sequences of yeast carboxypeptidase Y.PMID 7726851Read ↗

Use of CPY and its derivatives to study protein quality control in various cell compartments.Semantic proximity Read ↗

Requirement of the propeptide for in vivo formation of active yeast carboxypeptidase Y.Semantic proximity Read ↗

Stress tolerance of misfolded carboxypeptidase Y requires maintenance of protein trafficking and degradative pathways.Semantic proximity Read ↗

Re-entering the translocon from the lumenal side of the endoplasmic reticulum. Studies on mutated carboxypeptidase yscY species.Semantic proximity Read ↗

Endoplasmic reticulum-associated protein quality control and degradation: screen for ERAD mutants after ethylmethane sulfonate mutagenesis.Semantic proximity Read ↗

Retention of a co-translational translocated mutant protein of carboxypeptidase Y of Saccharomyces cerevisiae in endoplasmic reticulum.Semantic proximity Read ↗

Cytoplasmic peptide:N-glycanase cleaves N-glycans on a carboxypeptidase Y mutant during ERAD in Saccharomyces cerevisiae.Semantic proximity Read ↗

Yeast carboxypeptidase Y vacuolar targeting signal is defined by four propeptide amino acids.Semantic proximity Read ↗

N-Glycosylation affects endoplasmic reticulum degradation of a mutated derivative of carboxypeptidase yscY in yeast.Semantic proximity Read ↗

Der3p/Hrd1p is required for endoplasmic reticulum-associated degradation of misfolded lumenal and integral membrane proteins.Semantic proximity Read ↗

R73A and H144Q mutants of the yeast mitochondrial cyclophilin Cpr3 exhibit a low prolyl isomerase activity in both peptide and protein-folding assays.Semantic proximity Read ↗

Increased proteolytic susceptibility of carboxypeptidase Y caused by modification of the disulfide zipper.Semantic proximity Read ↗

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