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

In vivo processing of the precursor of the major exoglucanase by KEX2 endoprotease in the Saccharomyces cerevisiae secretory pathway.

Biochimica et biophysica acta - 10 Jan 1996

Basco R D, Cueva R, Andaluz E, Larriba G

Abstract excerpt

We have established the main post-translational modification of the major exoglucanase of Saccharomyces cerevisiae as the enzyme progresses through the secretory pathway. The protein portion of the enzyme accumulated by sec18 cells was about 2 kDa larger than that of the secreted enzyme. This precursor (form A) was stable when maintained in the endoplasmic reticulum but was processed to the mature form (form B)...

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 Biological Transport

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

Share to Fungal Proteins

Share to Isoenzymes

Share to Molecular Sequence Data

Share to Mutation

Share to Saccharomyces cerevisiae

Share to Saccharomyces cerevisiae Proteins

Source

Identifiers

PMID: 9244183
DOI: 10.1016/0167-4889(95)00156-5

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

In vivo processing of the precursor of the major exoglucanase by KEX2 endoprotease in the Saccharomyces cerevisiae secretory pathway.PMID 9244183Read ↗

Introduction of Kex2 cleavage sites in fusion proteins for monitoring localization and transport in yeast secretory pathway.Semantic proximity Read ↗

Immunolocalization of Kex2 protease identifies a putative late Golgi compartment in the yeast Saccharomyces cerevisiae.Semantic proximity Read ↗

Molecular biology of yeast exoglucanases.Semantic proximity Read ↗

Immunoisolation of Kex2p-containing organelles from yeast demonstrates colocalisation of three processing proteinases to a single Golgi compartment.Semantic proximity Read ↗

The major exoglucanase secreted by Saccharomyces cerevisiae as a model to study protein glycosylation.Semantic proximity Read ↗

Activity of Kex2 dibasic endoprotease is localized throughout the secretory pathway in Saccharomyces cerevisiae. An ultracytochemical study.Semantic proximity Read ↗

A novel Kex2 enzyme can process the proregion of the yeast alpha-factor leader in the endoplasmic reticulum instead of in the Golgi.Semantic proximity Read ↗

Identification of the essential EPE1 gene involved in retention of secreted proteins on the cell surface of Saccharomyces cerevisiae cells.Semantic proximity Read ↗

Compartmental organization of Golgi-specific protein modification and vacuolar protein sorting events defined in a yeast sec18 (NSF) mutant.Semantic proximity Read ↗

Processing and trafficking of a prohormone convertase 2 active site mutant.Semantic proximity Read ↗

Mutational analysis of K28 preprotoxin processing in the yeast Saccharomyces cerevisiae.Semantic proximity Read ↗

Functional analysis of a Golgi-localized Kex2p-like protease in tobacco suspension culture cells.Semantic proximity Read ↗

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