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 coiled coil of in vitro assembled keratin filaments is a heterodimer of type I and II keratins: use of site-specific mutagenesis and recombinant protein expression.

The Journal of cell biology - 1 Apr 1990

Hatzfeld M, Weber K

Abstract excerpt

Recombinant DNA technology has been used to analyze the first step in keratin intermediate filament (IF) assembly; i.e., the formation of the double stranded coiled coil. Keratins 8 and 18, lacking cysteine, were subjected to site specific in vitro mutagenesis to change one amino acid in the same relative position of the alpha-helical rod domain of both keratins to a cysteine. The mutations lie at position -36 of...

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 Escherichia coli

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

Share to Gene Expression

Share to Molecular Sequence Data

Share to Mutation

Share to Protein Conformation

Share to Recombinant Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 1691189
DOI: 10.1083/jcb.110.4.1199
PMCID: PMC2116092

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

The coiled coil of in vitro assembled keratin filaments is a heterodimer of type I and II keratins: use of site-specific mutagenesis and recombinant protein expression.PMID 1691189Read ↗

Intermediate filament structure and assembly.Semantic proximity Read ↗

Do the ends justify the mean? Proline mutations at the ends of the keratin coiled-coil rod segment are more disruptive than internal mutations.Semantic proximity Read ↗

Human keratin 8 mutations that disturb filament assembly observed in inflammatory bowel disease patients.Semantic proximity Read ↗

Deletions in epidermal keratins leading to alterations in filament organization in vivo and in intermediate filament assembly in vitro.Semantic proximity Read ↗

Structural features of keratin intermediate filaments.Semantic proximity Read ↗

Structure-Function Analyses of a Keratin Heterotypic Complex Identify Specific Keratin Regions Involved in Intermediate Filament Assembly.Semantic proximity Read ↗

Protein chains in hair and epidermal keratin IF: structural features and spatial arrangements.Semantic proximity Read ↗

Crystal Structure of Keratin 1/10(C401A) 2B Heterodimer Demonstrates a Proclivity for the C-Terminus of Helix 2B to Form Higher Order Molecular Contacts.Semantic proximity Read ↗

Structural characterization of human vimentin rod 1 and the sequencing of assembly steps in intermediate filament formation in vitro using site-directed spin labeling and electron paramagnetic resonance.Semantic proximity Read ↗

A conserved region in the tail domain of vimentin is involved in its assembly into intermediate filaments.Semantic proximity Read ↗

Central rod domain insertion and carboxy-terminal fusion mutants of human cytokeratin K19 are incorporated into endogenous keratin filaments.Semantic proximity Read ↗

Mutation of human keratin 18 in association with cryptogenic cirrhosis.Semantic proximity Read ↗

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