ArticleAmerican journal of human genetics1990
Cloning and sequencing of a processed pseudogene derived from a human class III alcohol dehydrogenase gene.
Article in American journal of human genetics, 1990. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 27 citations in OpenAlex.
- The Role of Alcohol Dehydrogenase in Drug Metabolism: Beyond Ethanol Oxidation.The AAPS journal · 2021Review
- Why rodent pseudogenes refuse to retire.Genome biology · 2012Article
- Caenorhabditis elegans contains genes encoding two new members of the Zn-containing alcohol dehydrogenase family.Journal of molecular evolution · 1995Article
- Alcohol dehydrogenase genes: restriction fragment length polymorphisms for ADH4 (pi-ADH) and ADH5 (chi-ADH) and construction of haplotypes among different ADH classes.Human genetics · 1992Article
- Human class III alcohol dehydrogenase/glutathione-dependent formaldehyde dehydrogenase.Journal of protein chemistry · 1991Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Current information on the molecular structure of human alcohol dehydrogenase (ADH) genes is fragmentary. To characterize all ADH genes, we have isolated 63 ADH clones from human genomic libraries made from one individual. Fifty-nine clones have been classified into five previously known loci: ADH1 (18 clones), ADH2 (20 clones), and ADH3 class I (16 clones), ADH4 class II (4 clones), and ADH5 class III (1 clone). Sequencing of one of the remaining four unclassified clones, SY lambda ADHE38, about 1.1 kb in length, shows no introns and three frameshift mutations in the coding region, with a total of 10 internal termination codons. When its deduced amino acid sequence was compared with those of the class I, class II, and class III ADHs, the proportions of identical amino acids were 56.7%, 55.5%, and 88.7%, respectively, suggesting that the processed pseudogene was derived from an ADH5 gene. The duplication event seems to have occurred about 3.5 million years ago, and the pseudogene has undergone a rapid change since then.
Indexed as
Identifiers
2294756PMC1683552W345738570What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.