ArticleProstaglandins & other lipid mediators2008
Novel isoforms of intracellular platelet activating factor acetylhydrolase (PAFAH1b2) in human testis; encoded by alternatively spliced mRNAs.
Article in Prostaglandins & other lipid mediators, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
4 citing papers in PubMed.
- Comparison of reproductive performance and functional analysis of spermatogenesis factors between domestic yak and semi-wild blood yak.BMC genomics · 2025Article
- Reovirus infection induces transcriptome-wide unique A-to-I editing changes in the murine fibroblasts.Virus research · 2024Article
- A multicopy Y-chromosomal SGNH hydrolase gene expressed in the testis of the platyfish has been captured and mobilized by a Helitron transposon.BMC genetics · 2014Article
- Identification of New SRF Binding Sites in Genes Modulated by SRF Over-Expression in Mouse Hearts.Gene regulation and systems biology · 2011Article
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Authors and funding
4 authors.
Funding
Abstract
Platelet activating factor acetylhydrolase (paf-ah), a potent regulator of platelet activating factor activity, plays an important role in various physiological and pathophysiological functions including development, reproduction, inflammation, hemostasis, and apoptosis. Intracellular paf-ah (paf-ah-Ib) is composed of a regulatory subunit, Pafah1b1, and two highly conserved but non-identical catalytic subunits, Pafah1b2 and Pafah1b3. The present study identifies new splice variants of the Pafah1b2 gene transcript. The splice variants retain exons 1-5 and replace exon 6 with alternative exons derived from genomic sequence 3' to exon 6. Splice variants encode two proteins with different novel carboxy termini. One of the isoforms is expressed exclusively in testis. These new isoforms of pafah1b2 retain the ability to form higher order complexes while replacing known key catalytic residues, which raises the possibility that they may alter the subunit composition and catalytic function of paf-ah-Ib.
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