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

Biosynthesis and enzymology of the Caenorhabditis elegans cuticle: identification and characterization of a novel serine protease inhibitor.

International journal for parasitology - 31 May 2006

Page Antony P, McCormack Gillian, Birnie Andrew J

Abstract excerpt

Caenorhabditis elegans represents an excellent model in which to dissect the biosynthesis and assembly of the nematode cuticle. A sequenced genome, straightforward transgenesis, available mutants and practical genome-wide RNAi approaches provide an invaluable toolkit in the characterization of cuticle components. We have performed a targeted RNAi screen in an attempt to identify components of the cuticle collagen...

Read the complete abstract on PubMed

Topics

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

Share to Caenorhabditis elegans
Share to Caenorhabditis elegans Proteins

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

Share to Collagen

Share to DNA, Helminth

Share to Microscopy, Electron

Share to RNA Interference

Share to Serine Proteinase Inhibitors

Share to Serpins

Source

Identifiers

PMID: 16500660
DOI: 10.1016/j.ijpara.2006.01.004

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

Biosynthesis and enzymology of the Caenorhabditis elegans cuticle: identification and characterization of a novel serine protease inhibitor.PMID 16500660Read ↗

Structures and functions of collagens in Caenorhabditis elegans.Semantic proximity Read ↗

The astacin metalloprotease moulting enzyme NAS-36 is required for normal cuticle ecdysis in free-living and parasitic nematodesSemantic proximity Read ↗

Collagens, modifying enzymes and their mutations in humans, flies and worms.Semantic proximity Read ↗

Prolyl 4-hydroxlase activity is essential for development and cuticle formation in the human infective parasitic nematode Brugia malayi.Semantic proximity Read ↗

The let-268 locus of Caenorhabditis elegans encodes a procollagen lysyl hydroxylase that is essential for type IV collagen secretion.Semantic proximity Read ↗

Prolyl 4-hydroxylase is an essential procollagen-modifying enzyme required for exoskeleton formation and the maintenance of body shape in the nematode Caenorhabditis elegans.Semantic proximity Read ↗

Structural and physiological functions of Caenorhabditis elegans epidermisSemantic proximity Read ↗

MLT-11 is necessary for <i>C. elegans</i> embryogenesis and conserved sequences play distinct roles in cuticle structureSemantic proximity Read ↗

Specific collagens maintain the cuticle permeability barrier in Caenorhabditis elegans.Semantic proximity Read ↗

Collagen processing and cuticle formation is catalysed by the astacin metalloprotease DPY-31 in free-living and parasitic nematodesSemantic proximity Read ↗

A novel zinc-carboxypeptidase SURO-1 regulates cuticle formation and body morphogenesis in Caenorhabditis elegans.Semantic proximity Read ↗

A mutation in the Bombyx mori BmSPI51 gene results in alterations protein abundance in cocoon and unveils compensatory mechanism of silk gland proteinase inhibitors.Semantic proximity Read ↗

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