Aspartyl beta-hydroxylase: in vitro hydroxylation of a synthetic peptide based on the structure of the first growth factor-like domain of human factor IX. (Q33856789)

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English	Aspartyl beta-hydroxylase: in vitro hydroxylation of a synthetic peptide based on the structure of the first growth factor-like domain of human factor IX.	scientific article

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

29 July 2017

Aspartyl beta-hydroxylase: in vitro hydroxylation of a synthetic peptide based on the structure of the first growth factor-like domain of human factor IX. (English)

1 reference

Europe PubMed Central

PubMed publication ID

29 July 2017

author name string

R S Gronke

1

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Europe PubMed Central

PubMed publication ID

29 July 2017

W J VanDusen

2

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Europe PubMed Central

PubMed publication ID

29 July 2017

V M Garsky

3

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Europe PubMed Central

PubMed publication ID

29 July 2017

J W Jacobs

4

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Europe PubMed Central

PubMed publication ID

29 July 2017

M K Sardana

5

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Europe PubMed Central

PubMed publication ID

29 July 2017

A M Stern

6

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29 July 2017

P A Friedman

7

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Europe PubMed Central

PubMed publication ID

29 July 2017

language of work or name

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publication date

1 May 1989

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Europe PubMed Central

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29 July 2017

Proceedings of the National Academy of Sciences of the United States of America

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Europe PubMed Central

PubMed publication ID

29 July 2017

86

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Europe PubMed Central

PubMed publication ID

29 July 2017

10

1 reference

Europe PubMed Central

PubMed publication ID

29 July 2017

3609-3613

1 reference

Europe PubMed Central

PubMed publication ID

29 July 2017

Complete amino acid sequence of the light chain of human blood coagulation factor X: evidence for identification of residue 63 as beta-hydroxyaspartic acid

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=287187

5 July 2018

The occurrence of beta-hydroxyaspartic acid in the vitamin K-dependent blood coagulation zymogens

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=287187

5 July 2018

Calcium-binding properties of bovine factor X lacking the gamma-carboxyglutamic acid-containing region.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=287187

5 July 2018

Epidermal growth factor. Location of disulfide bonds

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=287187

5 July 2018

Prolyl hydroxylase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=287187

5 July 2018

Affinity column purification of protocollagen proline hydroxylase from chick embryos and further characterization of the enzyme

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=287187

5 July 2018

Vitamin K-dependent carboxylase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=287187

5 July 2018

Disulphide bridges of bovine factor X.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=287187

5 July 2018

The role of beta-hydroxyaspartate and adjacent carboxylate residues in the first EGF domain of human factor IX

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=287187

5 July 2018

Vitamin K-dependent carboxylation

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=287187

5 July 2018

beta-Hydroxyasparagine in domains homologous to the epidermal growth factor precursor in vitamin K-dependent protein S

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=287187

5 July 2018

Primary structure of bovine vitamin K-dependent protein S

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=287187

5 July 2018

Vitamin K-dependent carboxylation of glutamyl residues in proteins

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=287187

5 July 2018

Occurrence of beta-hydroxylated asparagine residues in non-vitamin K-dependent proteins containing epidermal growth factor-like domains

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=287187

5 July 2018

Beta-hydroxyaspartic acid in the first epidermal growth factor-like domain of protein C. Its role in Ca2+ binding and biological activity.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=287187

5 July 2018

Some characteristics of a vitamin K-dependent carboxylating system from rat liver microsomes

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=287187

5 July 2018

Vitamin K-Dependent Formation of γ-Carboxyglutamic Acid

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=287187

5 July 2018

Ascorbate increases the synthesis of procollagen hydroxyproline by cultured fibroblasts from chick embryo tendons without activation or prolyl hydroxylase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=287187

5 July 2018

Beta-hydroxyaspartic acid in vitamin K-dependent proteins

1 reference

https://pubmed.ncbi.nlm.nih.gov/2726737

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

The 2-oxoglutarate binding site of prolyl 4-hydroxylase. Identification of distinct subsites and evidence for 2-oxoglutarate decarboxylation in a ligand reaction at the enzyme-bound ferrous ion

1 reference

https://pubmed.ncbi.nlm.nih.gov/2726737

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Derivatives of blood coagulation factor IX contain a high affinity Ca2+-binding site that lacks gamma-carboxyglutamic acid

1 reference

https://pubmed.ncbi.nlm.nih.gov/2726737

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1073/PNAS.86.10.3609

1 reference

Europe PubMed Central

PubMed publication ID

29 July 2017

1989PNAS...86.3609G

0 references

PMC publication ID

1 reference

Europe PubMed Central

PubMed publication ID

29 July 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

29 July 2017

ResearchGate publication ID

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