Relation between tolerance to ethanol and alcohol dehydrogenase (ADH) activity in Drosophila melanogaster: selection, genotype and sex effects. (Q52458978)

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scientific article published in June 1987

Language	Label	Description	Also known as
English	Relation between tolerance to ethanol and alcohol dehydrogenase (ADH) activity in Drosophila melanogaster: selection, genotype and sex effects.	scientific article published in June 1987

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scholarly article

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Europe PubMed Central

2 May 2018

http://europepmc.org/abstract/MED/3110111

Relation between tolerance to ethanol and alcohol dehydrogenase (ADH) activity in Drosophila melanogaster: selection, genotype and sex effects. (English)

1 reference

Europe PubMed Central

2 May 2018

http://europepmc.org/abstract/MED/3110111

Drosophila melanogaster

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author name string

Barbancho M

1

1 reference

Europe PubMed Central

2 May 2018

http://europepmc.org/abstract/MED/3110111

Sánchez-Cañete FJ

2

1 reference

Europe PubMed Central

2 May 2018

http://europepmc.org/abstract/MED/3110111

Dorado G

3

1 reference

Europe PubMed Central

2 May 2018

http://europepmc.org/abstract/MED/3110111

Pineda M

4

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Europe PubMed Central

2 May 2018

http://europepmc.org/abstract/MED/3110111

language of work or name

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publication date

1 June 1987

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Europe PubMed Central

2 May 2018

http://europepmc.org/abstract/MED/3110111

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Europe PubMed Central

2 May 2018

http://europepmc.org/abstract/MED/3110111

58 ( Pt 3)

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Europe PubMed Central

2 May 2018

http://europepmc.org/abstract/MED/3110111

443-450

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Europe PubMed Central

2 May 2018

http://europepmc.org/abstract/MED/3110111

https://scigraph.springernature.com/pub.10.1038/hdy.1987.73

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Intra- and interpopulation selection concerning the alcohol dehydrogenase locus in Drosophila melanogaster.

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Genetical variation for enzyme activity in a population of Drosophila melanogaster. VI. Molecular variation in the control of alcohol dehydrogenase (ADH) activity.

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A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

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Dominance at Adh locus in response of adult Drosophila melanogaster to environmental alcohol

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Alcohol-oxidizing enzymes in 13 Drosophila species

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Biological role of alcohol dehydrogenase in the tolerance of Drosophila melanogaster to aliphatic alochols: utilization of an ADH-null mutant

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Drosophila alcohol dehydrogenase: detoxification of isopropanol and acetone, substances not used in energy metabolism.

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Properties of genetically polymorphic isozymes of alcohol dehydrogenase in Drosophila melanogaster.

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Selection at the alcoholdehydrogenase locus in Drosophila melanogaster

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Ethanol metabolism inDrosophila melanogaster

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Enzyme flexibility in Drosophila melanogaster.

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Modes of variation in alcohol dehydrogenase inDrosophila melanogaster

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Selection for ethanol tolerance and Adh allozymes in natural populations of Drosophila melanogaster

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Alcohol dehydrogenase polymorphism in populations of Drosophila melanogaster. II. Relation between ADH activity and adult mortality

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Wineries, drosophila, alcohol, and Adh.

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Adaptive response due to changes in gene regulation: a study with Drosophila

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Ethanol tolerance and the Adh polymorphism in a natural population of Drosophila melanogaster

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Selection acting directly on an enzyme polymorphism.

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Genetic variation in natural populations: Patterns and theory

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Selection at the alcohol dehydrogenase locus in Drosophila melanogaster imposed by environmental ethanol

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Biochemical Differences Between Alcohol Debydrogenases of Drosophila Melanogaster

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Selection affecting enzyme polymorphisms in laboratory populations of Drosophila melanogaster.

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Selective effects of the genetic background and ethanol on the alcohol dehydrogenase polymorphism in Drosophila melanogaster.

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New studies of the alcohol dehydrogenase cline in D. melanogaster from Mexico

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Alcohol dehydrogenase thermostability variants in Drosophila melanogaster: comparison of activity ratios and enzyme levels.

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Selection acting upon slow-migrating ADH alleles differing in enzyme activity

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Alcohol dehydrogenases: a polymorphism in Drosophila melanogaster.

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Isozyme variability in species of the genus Drosophila. VI. Frequency-property-environment relationships of allelic alcohol dehydrogenases in D. melanogaster.

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Selection at the alcohol dehydrogenase locus of Drosophila melanogaster: effects of ethanol and temperature.

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Alcohol dehydrogenase in Drosophila melanogaster: activity variation in natural populations

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Alcohol dehydrogenase activity in Drosophila melanogaster: a quantitative character

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Identifiers

10.1038/HDY.1987.73

1 reference

Europe PubMed Central

2 May 2018

http://europepmc.org/abstract/MED/3110111

release_aoqov4llxzh6lda5ql6sarhrq4

1 reference

https://api.fatcat.wiki/v0/release/aoqov4llxzh6lda5ql6sarhrq4

24 November 2022

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mapped directly with Wikidata item

1 reference

Europe PubMed Central

2 May 2018

http://europepmc.org/abstract/MED/3110111

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