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

Identification of the major physiologic phosphorylation site of human keratin 18: potential kinases and a role in filament reorganization.

The Journal of cell biology - 1 Oct 1994

Ku N O, Omary M B

Abstract excerpt

There is ample in vitro evidence that phosphorylation of intermediate filaments, including keratins, plays an important role in filament reorganization. In order to gain a better understanding of the function of intermediate filament phosphorylation, we sought to identify the major phosphorylation site of human keratin polypeptide 18 (K18) and study its role in filament assembly or reorganization. We generated a...

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 Cell Line
Share to Mice

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

Share to Molecular Sequence Data

Share to Mutation

Share to Phosphorylation

Share to Protein Serine-Threonine Kinases

Share to Serine

Source

Open in PubMed Open full text

Identifiers

PMID: 7523419
DOI: 10.1083/jcb.127.1.161
PMCID: PMC2120194

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

Identification of the major physiologic phosphorylation site of human keratin 18: potential kinases and a role in filament reorganization.PMID 7523419Read ↗

Phosphorylation of human keratin 18 serine 33 regulates binding to 14-3-3 proteins.Semantic proximity Read ↗

Keratin 8 phosphorylation by p38 kinase regulates cellular keratin filament reorganization: modulation by a keratin 1-like disease causing mutation.Semantic proximity Read ↗

Mutation of a major keratin phosphorylation site predisposes to hepatotoxic injury in transgenic mice.Semantic proximity Read ↗

Type II Keratins Are Phosphorylated on a Unique Motif during Stress and Mitosis in Tissues and Cultured CellsSemantic proximity Read ↗

Quantitative phosphoproteomic analysis reveals system-wide signaling pathways regulated by site-specific phosphorylation of Keratin-8 in skin squamous cell carcinoma derived cell line.Semantic proximity Read ↗

Stress, Apoptosis, and Mitosis Induce Phosphorylation of Human Keratin 8 at Ser-73 in Tissues and Cultured CellsSemantic proximity Read ↗

Keratins turn over by ubiquitination in a phosphorylation-modulated fashion.Semantic proximity Read ↗

Generation of a tissue-specific transgenic model for K8 phosphomutants: A tool to investigate the role of K8 phosphorylation during skin carcinogenesis in vivo.Semantic proximity Read ↗

O-GlcNAcylation determines the solubility, filament organization, and stability of keratins 8 and 18.Semantic proximity Read ↗

Keratins in colorectal epithelial function and diseaseSemantic proximity Read ↗

PKC412 normalizes mutation-related keratin filament disruption and hepatic injury in mice by promoting keratin-myosin binding.Semantic proximity Read ↗

G2/M transition requires multisite phosphorylation of oncoprotein 18 by two distinct protein kinase systems.Semantic proximity Read ↗

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