(Q50199805)

English

Utilization of sulfometuron methyl, an acetolactate synthase inhibitor, in molecular biological and metabolic studies of plants and microbes.

scientific article published in January 1988

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

27 February 2018

http://europepmc.org/abstract/MED/3071726

Utilization of sulfometuron methyl, an acetolactate synthase inhibitor, in molecular biological and metabolic studies of plants and microbes. (English)

1 reference

Europe PubMed Central

PubMed publication ID

27 February 2018

http://europepmc.org/abstract/MED/3071726

author name string

LaRossa RA

1

1 reference

Europe PubMed Central

PubMed publication ID

27 February 2018

http://europepmc.org/abstract/MED/3071726

Van Dyk TK

2

1 reference

Europe PubMed Central

PubMed publication ID

27 February 2018

http://europepmc.org/abstract/MED/3071726

language of work or name

0 references

publication date

1 January 1988

1 reference

Europe PubMed Central

PubMed publication ID

27 February 2018

http://europepmc.org/abstract/MED/3071726

Methods in Enzymology

1 reference

Europe PubMed Central

PubMed publication ID

27 February 2018

http://europepmc.org/abstract/MED/3071726

166

1 reference

Europe PubMed Central

PubMed publication ID

27 February 2018

http://europepmc.org/abstract/MED/3071726

97-107

1 reference

Europe PubMed Central

PubMed publication ID

27 February 2018

http://europepmc.org/abstract/MED/3071726

Imidazolinones: potent inhibitors of acetohydroxyacid synthase

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Herbicide-resistant mutants from tobacco cell cultures.

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Cloning and expression of the ilvB gene of Escherichia coli K-12

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Nucleotide sequence of theilvB multivalent attenuator region ofEscherichia coliK12

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The nucleotide sequence preceding and including the beginning of the ilvE gene of the ilvGEDA operon of Escherichia coli K12

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Isolation and characterization of plant genes coding for acetolactate synthase, the target enzyme for two classes of herbicides

1 reference

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2-Ketobutyrate: a putative alarmone of Escherichia coli

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Defect in alpha-ketobutyrate metabolism: a new inborn error

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A survey of inborn errors of amino acid metabolism and transport in man.

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Origin of the herbicide binding site of acetolactate synthase

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Genetic engineering in vivo using translocatable drug-resistance elements. New methods in bacterial genetics

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A restriction enzyme cleavage map of Tn5 and location of a region encoding neomycin resistance

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Acetolactate synthase is the site of action of two sulfonylurea herbicides in higher plants.

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Involvement of ack-pta operon products in alpha-ketobutyrate metabolism by Salmonella typhimurium.

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Toxic accumulation of alpha-ketobutyrate caused by inhibition of the branched-chain amino acid biosynthetic enzyme acetolactate synthase in Salmonella typhimurium

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Molecular cloning and expression of the ilvGEDAY genes from Salmonella typhimurium

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Pleiotropic effects of poxA regulatory mutations of Escherichia coli and Salmonella typhimurium, mutations conferring sulfometuron methyl and alpha-ketobutyrate hypersensitivity

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Identifiers

10.1016/S0076-6879(88)66015-0

1 reference

Europe PubMed Central

PubMed publication ID

27 February 2018

http://europepmc.org/abstract/MED/3071726

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

27 February 2018

http://europepmc.org/abstract/MED/3071726

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