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

Proteomic Identification of in Vivo Interactors Reveals Novel Function of Skin Cornification Proteins

23 Apr 2012

Abstract excerpt

Protection against injurious external insults and loss of vital fluids is essential for life and is in all organisms, from bacteria to plants and humans, provided by some form of barrier. Members of the small proline-rich (SPRR) protein family are major components of the cornified cell envelope (CE), a structure responsible for the barrier properties of our skin. These proteins are efficient reactive oxygen...

Read the complete abstract on PubMed

Topics

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

Share to Dermatologic Treatments and Research
Share to Skin and Cellular Biology Research
Share to Wound Healing and Treatments

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 22519520
DOI: 10.1021/pr300310b

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 8 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Proteomic Identification of in Vivo Interactors Reveals Novel Function of Skin Cornification ProteinsPMID 22519520Read ↗

SPRR4, a novel cornified envelope precursor: UV-dependent epidermal expression and selective incorporation into fragile envelopesSemantic proximity Read ↗

Update on the epidermal differentiation complexSemantic proximity Read ↗

The Interactions of Small Proline-rich Proteins With Late Cornified Envelope Proteins Are Involved in the Pathogenesis of PsoriasisSemantic proximity Read ↗

The small proline-rich proteins constitute a multigene family of differentially regulated cornified cell envelope precursor proteins.Semantic proximity Read ↗

Epigenomic signature of the progeroid Cockayne syndrome exposes distinct and common features with physiological ageingSemantic proximity Read ↗

A review on protein–protein interaction network of APE1/Ref‐1 and its associated biological functionsSemantic proximity Read ↗

The Interactions of Small Proline-Rich Proteins with Late Cornified Envelope Proteins are Involved in the Pathogenesis of PsoriasisSemantic proximity Read ↗

Psoriasis-Associated Late Cornified Envelope (LCE) Proteins Have Antibacterial Activity.Semantic proximity Read ↗

Glyoxal induces DNA-Protein Crosslinking in CellsSemantic proximity Read ↗

The Enigma of UV Stress Granules: Research Challenges and New PerspectivesSemantic proximity Read ↗

Mapping the Human Proteome with Physical Access to DNASemantic proximity Read ↗

Plasma membrane integrity: implications for health and diseaseSemantic proximity Read ↗

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