Glycation by ascorbic acid causes loss of activity of ribulose-1,5-bisphosphate carboxylase/oxygenase and its increased susceptibility to proteases (Q44235844)

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scientific article published in November 2002

Language	Label	Description	Also known as
English	Glycation by ascorbic acid causes loss of activity of ribulose-1,5-bisphosphate carboxylase/oxygenase and its increased susceptibility to proteases	scientific article published in November 2002

Statements

scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

1 December 2017

Glycation by ascorbic acid causes loss of activity of ribulose-1,5-bisphosphate carboxylase/oxygenase and its increased susceptibility to proteases (English)

1 reference

Europe PubMed Central

PubMed publication ID

1 December 2017

author name string

Yasuo Yamauchi

1

1 reference

Europe PubMed Central

PubMed publication ID

1 December 2017

Yukinori Ejiri

2

1 reference

Europe PubMed Central

PubMed publication ID

1 December 2017

Kiyoshi Tanaka

3

1 reference

Europe PubMed Central

PubMed publication ID

1 December 2017

publication date

1 November 2002

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Europe PubMed Central

PubMed publication ID

1 December 2017

number of pages

8

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based on heuristic

inferred from page(s)

Plant and Cell Physiology

1 reference

Europe PubMed Central

PubMed publication ID

1 December 2017

43

1 reference

Europe PubMed Central

PubMed publication ID

1 December 2017

11

1 reference

Europe PubMed Central

PubMed publication ID

1 December 2017

1334-1341

1 reference

Europe PubMed Central

PubMed publication ID

1 December 2017

Crystal structure of the active site of ribulose-bisphosphate carboxylase

1 reference

https://api.crossref.org/works/10.1093%2FPCP%2FPCF162

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Aminoguanidine prevents diabetes-induced arterial wall protein cross-linking

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Recent Trends in Glutathione Biochemistry—Glutathione–Protein Interactions: A Molecular Link between Oxidative Stress and Cell Proliferation?

1 reference

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Reaction of ascorbate with lysine and protein under autoxidizing conditions: formation of N epsilon-(carboxymethyl)lysine by reaction between lysine and products of autoxidation of ascorbate

1 reference

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The biology and enzymology of protein N-myristoylation

1 reference

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Measurement of the ascorbate content of spinach leaf protoplasts and chloroplasts during illumination

1 reference

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21 January 2018

Redox regulation of enzymatic activity and proteolytic susceptibility of ribulose-1,5-bisphosphate carboxylase/oxygenase fromEuglena gracilis

1 reference

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21 January 2018

Amides are novel protein modifications formed by physiological sugars

1 reference

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21 January 2018

Post-translational modifications in the large subunit of ribulose bisphosphate carboxylase/oxygenase

1 reference

https://api.crossref.org/works/10.1093%2FPCP%2FPCF162

21 January 2018

Identification and characterization of DegP, a serine protease associated with the luminal side of the thylakoid membrane.

1 reference

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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

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Identification, characterization, and molecular cloning of a homologue of the bacterial FtsH protease in chloroplasts of higher plants.

1 reference

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High correlation between pentosidine protein crosslinks and pigmentation implicates ascorbate oxidation in human lens senescence and cataractogenesis

1 reference

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21 January 2018

Site-specific glycation of lens crystallins by ascorbic acid

1 reference

https://api.crossref.org/works/10.1093%2FPCP%2FPCF162

21 January 2018

Increased susceptibility of ribulose-1,5-bisphosphate carboxylase/oxygenase to proteolytic degradation caused by oxidative treatments.

1 reference

https://api.crossref.org/works/10.1093%2FPCP%2FPCF162

21 January 2018

Aging of proteins: isolation and identification of a fluorescent chromophore from the reaction of polypeptides with glucose

1 reference

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21 January 2018

Interaction of constituent subunits in ribulose 1,5-bisphosphate carboxylase from Aphanothece halophytica

1 reference

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Expression of spinach ascorbate peroxidase isoenzymes in response to oxidative stresses

1 reference

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A novel post-translational modification of yeast elongation factor 1A. Methylesterification at the C terminus

1 reference

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21 January 2018

Identifiers

10.1093/PCP/PCF162

1 reference

Europe PubMed Central

PubMed publication ID

1 December 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

1 December 2017

ResearchGate publication ID

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