(Q35114792)

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The small subunit 1 of the Arabidopsis isopropylmalate isomerase is required for normal growth and development and the early stages of glucosinolate formation

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scholarly article

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Europe PubMed Central

PubMed publication ID

6 August 2017

The small subunit 1 of the Arabidopsis isopropylmalate isomerase is required for normal growth and development and the early stages of glucosinolate formation (English)

1 reference

Europe PubMed Central

PubMed publication ID

6 August 2017

Jonathan Gershenzon

4

object named as

Jonathan Gershenzon

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Michael Reichelt

3

object named as

Michael Reichelt

1 reference

Europe PubMed Central

PubMed publication ID

6 August 2017

7

object named as

Stefan Binder

1 reference

Europe PubMed Central

PubMed publication ID

6 August 2017

1

object named as

Janet Imhof

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Europe PubMed Central

PubMed publication ID

6 August 2017

6

object named as

Kurt Lächler

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Europe PubMed Central

PubMed publication ID

6 August 2017

author name string

Florian Huber

2

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Europe PubMed Central

PubMed publication ID

6 August 2017

Christoph Wiegreffe

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Europe PubMed Central

PubMed publication ID

6 August 2017

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publication date

7 March 2014

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Europe PubMed Central

PubMed publication ID

6 August 2017

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Europe PubMed Central

PubMed publication ID

6 August 2017

9

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Europe PubMed Central

PubMed publication ID

6 August 2017

3

1 reference

Europe PubMed Central

PubMed publication ID

6 August 2017

e91071

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Europe PubMed Central

PubMed publication ID

6 August 2017

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Creative Commons Attribution 4.0 International

7 March 2014

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April 2022 Public Data File from Crossref

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Sugar metabolism and the plant target of rapamycin kinase: a sweet operaTOR?

1 reference

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Integrated proteomics and metabolomics of Arabidopsis acclimation to gene-dosage dependent perturbation of isopropylmalate dehydrogenases

1 reference

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Partial deficiency of isoleucine impairs root development and alters transcript levels of the genes involved in branched-chain amino acid and glucosinolate metabolism in Arabidopsis

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Structural and Functional Evolution of Isopropylmalate Dehydrogenases in the Leucine and Glucosinolate Pathways of Arabidopsis thaliana

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From amino acid to glucosinolate biosynthesis: protein sequence changes in the evolution of methylthioalkylmalate synthase in Arabidopsis

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Glucosinolate-accumulating S-cells in Arabidopsis leaves and flower stalks undergo programmed cell death at early stages of differentiation.

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Arabidopsis thaliana encodes a bacterial-type heterodimeric isopropylmalate isomerase involved in both Leu biosynthesis and the Met chain elongation pathway of glucosinolate formation

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1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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Identifiers

10.1371/JOURNAL.PONE.0091071

1 reference

Europe PubMed Central

PubMed publication ID

6 August 2017

2014PLoSO...991071I

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PMC publication ID

1 reference

Europe PubMed Central

PubMed publication ID

6 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

6 August 2017

ResearchGate publication ID

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