Genomic structure and cloned cDNAs predict that four variants in the kinase domain of serine/threonine kinase receptors arise by alternative splicing and poly(A) addition.

doi:10.1073/pnas.91.17.7957

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Article

Genomic structure and cloned cDNAs predict that four variants in the kinase domain of serine/threonine kinase receptors arise by alternative splicing and poly(A) addition.

Proceedings of the National Academy of Sciences of the United States of America - 16 Aug 1994

Xu J, Matsuzaki K, McKeehan K, Wang F, Kan M, McKeehan W L

Abstract excerpt

Heterodimers of types I and II serine/threonine kinase receptor monomers compose the active receptor complex for ligands of the transforming growth factor beta family. Here we show that the genomic organization of coding sequences for the intracellular domain of a widely expressed type I serine/threonine kinase receptor is similar to that of the activin type II receptor gene. The genomic structure and cDNA clones...

Topics

Alternative Splicing
Amino Acid Sequence
Base Sequence
Carcinoma, Hepatocellular
Cell Line
Cloning, Molecular
Conserved Sequence
DNA Primers
DNA, Complementary
Gene Expression

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Genetic Variation

Humans

Liver Neoplasms

Macromolecular Substances

Molecular Sequence Data

Poly A

Polymerase Chain Reaction

Protein Serine-Threonine Kinases

Source

Open in PubMed Open full text

Identifiers

PMID: 8058741
DOI: 10.1073/pnas.91.17.7957
PMCID: PMC44523

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-8058741-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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