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

Some, but not all, glycine substitution mutations in COL7A1 result in intracellular accumulation of collagen VII, loss of anchoring fibrils, and skin blistering.

The Journal of biological chemistry - 24 Jul 1998

Hammami-Hauasli N, Schumann H, Raghunath M, Kilgus O, Lüthi U, Luger T, Bruckner-Tuderman L

Abstract excerpt

COL7A1 gene mutations cause dystrophic epidermolysis bullosa, a skin blistering disorder. The phenotypes result from defects of collagen VII, the major component of the anchoring fibrils at the dermo-epidermal junction; however, the molecular mechanisms underlying the phenotypes remain elusive. We investigated naturally occurring COL7A1 mutations and showed that some, but not all, glycine substitutions in...

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 Child

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

Share to Genotype

Share to Molecular Sequence Data

Share to Mutation

Share to Pedigree

Share to Phenotype

Source

Identifiers

PMID: 9668111
DOI: 10.1074/jbc.273.30.19228

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

Some, but not all, glycine substitution mutations in COL7A1 result in intracellular accumulation of collagen VII, loss of anchoring fibrils, and skin blistering.PMID 9668111Read ↗

Glycine substitutions in the triple-helical region of type VII collagen result in a spectrum of dystrophic epidermolysis bullosa phenotypes and patterns of inheritance.Semantic proximity Read ↗

Characterization of 18 new mutations in COL7A1 in recessive dystrophic epidermolysis bullosa provides evidence for distinct molecular mechanisms underlying defective anchoring fibril formation.Semantic proximity Read ↗

Identical glycine substitution mutations in type VII collagen may underlie both dominant and recessive forms of dystrophic epidermolysis bullosa.Semantic proximity Read ↗

A recurrent 'hot spot' glycine substitution mutation, G2043R in COL7A1, induces dominant dystrophic epidermolysis bullosa associated with intracytoplasmic accumulation of pro-collagen VII.Semantic proximity Read ↗

Characterization of molecular mechanisms underlying mutations in dystrophic epidermolysis bullosa using site-directed mutagenesis.Semantic proximity Read ↗

Biology of anchoring fibrils: lessons from dystrophic epidermolysis bullosa.Semantic proximity Read ↗

Glycine substitution mutations by different amino acids at the same codon in COL7A1 cause different modes of dystrophic epidermolysis bullosa inheritance.Semantic proximity Read ↗

Single glycine deletion in COL7A1 acting as glycine substitution in dystrophic epidermolysis bullosa.Semantic proximity Read ↗

Single amino acid substitutions in procollagen VII affect early stages of assembly of anchoring fibrils.Semantic proximity Read ↗

In this issue: glycine substitution mutations in the COL7A1 gene: implications for inheritance of dystrophic epidermolysis bullosa - dominant vs. recessive.Semantic proximity Read ↗

Molecular basis of dystrophic epidermolysis bullosa: mutations in the type VII collagen gene (COL7A1).Semantic proximity Read ↗

Collagen VII plays a dual role in wound healingSemantic proximity Read ↗

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