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 efficiency of dentin sialoprotein-phosphophoryn processing is affected by mutations both flanking and distant from the cleavage site.

The Journal of biological chemistry - 22 Feb 2013

Yang Robert T, Lim Glendale L, Dong Zhihong, Lee Arthur M, Yee Colin T, Fuller Robert S, Ritchie Helena H

Abstract excerpt

Normal dentin mineralization requires two highly acidic proteins, dentin sialoprotein (DSP) and phosphophoryn (PP). DSP and PP are synthesized as part of a single secreted precursor, DSP-PP, which is conserved in marsupial and placental mammals. Using a baculovirus expression system, we previously found that DSP-PP is accurately cleaved into DSP and PP after secretion into medium by an endogenous, secreted,...

Read the complete abstract on PubMed

Topics

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

Share to Baculoviridae
Share to Drosophila Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Electrophoresis, Polyacrylamide Gel

Share to Extracellular Matrix

Share to Extracellular Matrix Proteins

Share to Insecta

Share to Phosphoproteins

Share to Sialoglycoproteins

Source

Open in PubMed Open full text

Identifiers

PMID: 23297400
DOI: 10.1074/jbc.M112.382952
PMCID: PMC3581424

Genes

DSP
BMP1
TLR1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The efficiency of dentin sialoprotein-phosphophoryn processing is affected by mutations both flanking and distant from the cleavage site.PMID 23297400Read ↗

Dentin sialophosphoprotein in biomineralization.Semantic proximity Read ↗

Rough endoplasmic reticulum trafficking errors by different classes of mutant dentin sialophosphoprotein (DSPP) cause dominant negative effects in both dentinogenesis imperfecta and dentin dysplasia by entrapping normal DSPPSemantic proximity Read ↗

Key proteolytic cleavage site and full-length form of DSPP.Semantic proximity Read ↗

Dentin sialoprotein and dentin phosphoprotein have distinct roles in dentin mineralization.Semantic proximity Read ↗

A dentin sialophosphoprotein mutation that partially disrupts a splice acceptor site causes type II dentin dysplasia.Semantic proximity Read ↗

Dentin sialophosphoprotein and dentin matrix protein-1: Two highly phosphorylated proteins in mineralized tissues.Semantic proximity Read ↗

Molecular evolution of dentin phosphoprotein among toothed and toothless animalsSemantic proximity Read ↗

Dentin defects caused by a Dspp-1 frameshift mutation are associated with the activation of autophagy.Semantic proximity Read ↗

Porcine dentin sialophosphoprotein: length polymorphisms, glycosylation, phosphorylation, and stability.Semantic proximity Read ↗

Disulfide bonds are critical for tissue-nonspecific alkaline phosphatase function revealed by analysis of mutant proteins bearing a C(201)-Y or C(489)-S substitution associated with severe hypophosphatasia.Semantic proximity Read ↗

Efficient trafficking of acidic proteins out of the endoplasmic reticulum involves a conserved amino terminal IleProVal (IPV)-like tripeptide motif.Semantic proximity Read ↗

Functional splicing assay of DSPP mutations in hereditary dentin defects.Semantic proximity Read ↗

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