A gene controlling variation in Arabidopsis glucosinolate composition is part of the methionine chain elongation pathway (Q28363897)

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English	A gene controlling variation in Arabidopsis glucosinolate composition is part of the methionine chain elongation pathway	scientific article

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title

A gene controlling variation in Arabidopsis glucosinolate composition is part of the methionine chain elongation pathway (English)

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author

Juergen Kroymann

object named as

J Kroymann

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1

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author name string

S Textor

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2

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J G Tokuhisa

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3

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K L Falk

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4

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S Bartram

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5

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J Gershenzon

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6

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T Mitchell-Olds

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7

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language of work or name

English

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publication date

November 2001

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published in

Plant Physiology

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volume

127

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issue

3

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page(s)

1077-88

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cites work

Genetic control of natural variation in Arabidopsis glucosinolate accumulation

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A major inducer of anticarcinogenic protective enzymes from broccoli: isolation and elucidation of structure

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ChloroP, a neural network-based method for predicting chloroplast transit peptides and their cleavage sites

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Developmental profile of sinalbin (p-hydroxybenzyl glucosinolate) in mustard seedlings,Sinapis alba L., and its relationship to insect resistance

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Toxicity of Glucosinolates and Their Enzymatic Decomposition Products to Caenorhabditis elegans.

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The methionine chain elongation pathway in the biosynthesis of glucosinolates in Eruca sativa (Brassicaceae)

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BIOSYNTHESIS OF MUSTARD OIL GLUCOSIDES. IV. THE ADMINISTRATION OF METHIONINE-C14 AND RELATED COMPOUNDS TO HORSERADISH

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Purification and Characterization of Methionine:Glyoxylate Aminotransferase from Brassica carinata and Brassica napus

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Biochemical Genetics of Plant Secondary Metabolites in Arabidopsis thaliana: The Glucosinolates

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Allylglucosinolate and herbivorous caterpillars: a contrast in toxicity and tolerance

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Domain structure of mitochondrial and chloroplast targeting peptides

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Confidence Limits on Phylogenies: an Approach using the Bootstrap

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Biosynthesis of Sinigrin. II

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Leucine synthesis in spinach chloroplasts: partial characterization of 2-isopropylmalate synthase

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Identifiers

DOI

10.1104/PP.127.3.1077

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

3149129

OpenCitations bibliographic resource ID

3149129

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

3149129

PMC publication ID

129277

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PubMed publication ID

11706188

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

3149129

ResearchGate publication ID

283376437

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