Double knockout mutants of Arabidopsis grown under normal conditions reveal that the plastidial phosphorylase isozyme participates in transitory starch metabolism (Q46963992)

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scientific article published on 3 December 2013

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English	Double knockout mutants of Arabidopsis grown under normal conditions reveal that the plastidial phosphorylase isozyme participates in transitory starch metabolism	scientific article published on 3 December 2013

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scholarly article

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Europe PubMed Central

PubMed publication ID

26 December 2017

http://europepmc.org/abstract/MED/24302650

Double knockout mutants of Arabidopsis grown under normal conditions reveal that the plastidial phosphorylase isozyme participates in transitory starch metabolism (English)

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Europe PubMed Central

PubMed publication ID

26 December 2017

http://europepmc.org/abstract/MED/24302650

Alisdair R Fernie

5

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Alisdair R Fernie

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Europe PubMed Central

PubMed publication ID

26 December 2017

author name string

Irina Malinova

1

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26 December 2017

http://europepmc.org/abstract/MED/24302650

Sebastian Mahlow

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26 December 2017

http://europepmc.org/abstract/MED/24302650

Saleh Alseekh

3

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26 December 2017

http://europepmc.org/abstract/MED/24302650

Tom Orawetz

4

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26 December 2017

http://europepmc.org/abstract/MED/24302650

Otto Baumann

6

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26 December 2017

http://europepmc.org/abstract/MED/24302650

Martin Steup

7

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26 December 2017

http://europepmc.org/abstract/MED/24302650

Joerg Fettke

8

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26 December 2017

http://europepmc.org/abstract/MED/24302650

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3 December 2013

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26 December 2017

http://europepmc.org/abstract/MED/24302650

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15

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Plant Physiology

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26 December 2017

http://europepmc.org/abstract/MED/24302650

164

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26 December 2017

http://europepmc.org/abstract/MED/24302650

2

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26 December 2017

http://europepmc.org/abstract/MED/24302650

907-921

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Europe PubMed Central

PubMed publication ID

26 December 2017

http://europepmc.org/abstract/MED/24302650

Loss of starch granule initiation has a deleterious effect on the growth of arabidopsis plants due to an accumulation of ADP-glucose

1 reference

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Arabidopsis plants perform arithmetic division to prevent starvation at night

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Neuromuscular disorders of glycogen metabolism

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The simultaneous abolition of three starch hydrolases blocks transient starch breakdown in Arabidopsis.

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Inferring transcriptional gene regulation network of starch metabolism in Arabidopsis thaliana leaves using graphical Gaussian model

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The role of plastidial glucose-6-phosphate/phosphate translocators in vegetative tissues of Arabidopsis thaliana mutants impaired in starch biosynthesis

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Regulation of glycogen metabolism in yeast and bacteria

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Glucose 1-phosphate is efficiently taken up by potato (Solanum tuberosum) tuber parenchyma cells and converted to reserve starch granules.

1 reference

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Blocking the metabolism of starch breakdown products in Arabidopsis leaves triggers chloroplast degradation.

1 reference

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The phenotype of soluble starch synthase IV defective mutants of Arabidopsis thaliana suggests a novel function of elongation enzymes in the control of starch granule formation.

1 reference

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The role of cytosolic alpha-glucan phosphorylase in maltose metabolism and the comparison of amylomaltase in Arabidopsis and Escherichia coli

1 reference

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Structural and enzymatic characterization of the isoamylase1 homo-oligomer and the isoamylase1-isoamylase2 hetero-oligomer from rice endosperm.

1 reference

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Glycogen phosphorylase, the product of the glgP Gene, catalyzes glycogen breakdown by removing glucose units from the nonreducing ends in Escherichia coli

1 reference

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Nature of the periplastidial pathway of starch synthesis in the cryptophyte Guillardia theta

1 reference

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1 reference

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COPPER ENZYMES IN ISOLATED CHLOROPLASTS. POLYPHENOLOXIDASE IN BETA VULGARIS

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1 reference

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alpha-Amylase is not required for breakdown of transitory starch in Arabidopsis leaves

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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Plastidial phosphorylase is required for normal starch synthesis inChlamydomonas reinhardtii

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

10.1104/PP.113.227843

1 reference

Europe PubMed Central

PubMed publication ID

26 December 2017

http://europepmc.org/abstract/MED/24302650

PMC publication ID

0 references

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

26 December 2017

http://europepmc.org/abstract/MED/24302650

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