Cloning and characterization of a low molecular weight prolyl 4-hydroxylase from Arabidopsis thaliana. Effective hydroxylation of proline-rich, collagen-like, and hypoxia-inducible transcription factor alpha-like peptides (Q42051705)

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scientific article published on 25 April 2002

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English	Cloning and characterization of a low molecular weight prolyl 4-hydroxylase from Arabidopsis thaliana. Effective hydroxylation of proline-rich, collagen-like, and hypoxia-inducible transcription factor alpha-like peptides	scientific article published on 25 April 2002

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

15 October 2017

Cloning and characterization of a low molecular weight prolyl 4-hydroxylase from Arabidopsis thaliana. Effective hydroxylation of proline-rich, collagen-like, and hypoxia-inducible transcription factor alpha-like peptides (English)

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Europe PubMed Central

PubMed publication ID

15 October 2017

Arabidopsis thaliana

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Johanna Myllyharju

2

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Johanna Myllyharju

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Europe PubMed Central

PubMed publication ID

15 October 2017

author name string

Reija Hieta

1

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Europe PubMed Central

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15 October 2017

language of work or name

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publication date

25 April 2002

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15 October 2017

Journal of Biological Chemistry

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15 October 2017

277

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PubMed publication ID

15 October 2017

26

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Europe PubMed Central

PubMed publication ID

15 October 2017

23965-23971

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Europe PubMed Central

PubMed publication ID

15 October 2017

Collagens: molecular biology, diseases, and potentials for therapy

1 reference

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Collagens and collagen-related diseases

1 reference

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Prolyl 4-hydroxylases and their protein disulfide isomerase subunit

1 reference

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Cloning, baculovirus expression, and characterization of a second mouse prolyl 4-hydroxylase alpha-subunit isoform: formation of an alpha 2 beta 2 tetramer with the protein disulfide-isomerase/beta subunit

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Cloning of the human prolyl 4-hydroxylase alpha subunit isoform alpha(II) and characterization of the type II enzyme tetramer. The alpha(I) and alpha(II) subunits do not form a mixed alpha(I)alpha(II)beta2 tetramer

1 reference

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Baculovirus expression of two protein disulphide isomerase isoforms from Caenorhabditis elegans and characterization of prolyl 4-hydroxylases containing one of these polypeptides as their beta subunit

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Prolyl 4-hydroxylase is an essential procollagen-modifying enzyme required for exoskeleton formation and the maintenance of body shape in the nematode Caenorhabditis elegans

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Prolyl 4-hydroxylase is required for viability and morphogenesis in Caenorhabditis elegans

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PLANT CELL WALL PROTEINS.

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Evidence for 4-hydroxyproline in viral proteins. Characterization of a viral prolyl 4-hydroxylase and its peptide substrates

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Molecular cloning of the alpha-subunit of human prolyl 4-hydroxylase: the complete cDNA-derived amino acid sequence and evidence for alternative splicing of RNA transcripts

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CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice

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Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites

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Characterization of the iron- and 2-oxoglutarate-binding sites of human prolyl 4-hydroxylase

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Site-directed mutagenesis of the alpha subunit of human prolyl 4-hydroxylase. Identification of three histidine residues critical for catalytic activity

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Identification of a novel proline-rich peptide-binding domain in prolyl 4-hydroxylase

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Site-directed mutagenesis of human lysyl hydroxylase expressed in insect cells. Identification of histidine residues and an aspartic acid residue critical for catalytic activity

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Biosynthesis of Arabinogalactan-Protein in Lolium multiflorum (Ryegrass) Endosperm Cells : III. Subcellular Distribution of Prolyl Hydroxylase

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Structure of a cephalosporin synthase

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Hydroxylation of (Pro-Pro-Gly)5and (Pro-Pro-Gly)10by prolyl hydroxylase. Evidence for an asymmetric active site in the enzyme

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Identification of arginine-700 as the residue that binds the C-5 carboxyl group of 2-oxoglutarate in human lysyl hydroxylase 1.

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Ultrastructural localisation and further biochemical characterisation of prolyl 4-hydroxylase from Phaseolus vulgaris: comparative analysis

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Identifiers

10.1074/JBC.M201865200

1 reference

Europe PubMed Central

PubMed publication ID

15 October 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

15 October 2017

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