(Q44361735)

English

Deletion of N-terminal amino acids from human lecithin:cholesterol acyltransferase differentially affects enzyme activity toward alpha- and beta-substrate lipoproteins

scientific article published in March 2003

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

2 December 2017

Deletion of N-terminal amino acids from human lecithin:cholesterol acyltransferase differentially affects enzyme activity toward alpha- and beta-substrate lipoproteins (English)

1 reference

Europe PubMed Central

PubMed publication ID

2 December 2017

Roger S. McLeod

6

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PubMed publication ID

2 December 2017

author name string

Nicola K Vickaryous

1

1 reference

Europe PubMed Central

PubMed publication ID

2 December 2017

Evelyn M Teh

2

1 reference

Europe PubMed Central

PubMed publication ID

2 December 2017

Bruce Stewart

3

1 reference

Europe PubMed Central

PubMed publication ID

2 December 2017

Peter J Dolphin

4

1 reference

Europe PubMed Central

PubMed publication ID

2 December 2017

Catherine K L Too

5

1 reference

Europe PubMed Central

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2 December 2017

language of work or name

1 reference

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inferred from title

publication date

1 March 2003

1 reference

Europe PubMed Central

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2 December 2017

Biochimica et Biophysica Acta

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Europe PubMed Central

PubMed publication ID

2 December 2017

1646

1 reference

Europe PubMed Central

PubMed publication ID

2 December 2017

1-2

1 reference

Europe PubMed Central

PubMed publication ID

2 December 2017

164-172

1 reference

Europe PubMed Central

PubMed publication ID

2 December 2017

Lecithin cholesterol acyltransferase

1 reference

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Cloning and expression of human lecithin-cholesterol acyltransferase cDNA

1 reference

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Bacterial biocatalysts: molecular biology, three-dimensional structures, and biotechnological applications of lipases

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Structure as basis for understanding interfacial properties of lipases

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Characterization of functional residues in the interfacial recognition domain of lecithin cholesterol acyltransferase (LCAT).

1 reference

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Identification of a domain of lecithin-cholesterol acyltransferase that is involved in interfacial recognition

1 reference

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Surface plasmon resonance biosensor studies of human wild-type and mutant lecithin cholesterol acyltransferase interactions with lipoproteins

1 reference

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A proposed architecture for lecithin cholesterol acyl transferase (LCAT): identification of the catalytic triad and molecular modeling

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Chicken lecithin-cholesterol acyltransferase. Molecular characterization reveals unusual structure and expression pattern

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Organic extraction and preparative isoelectric focussing of rat serum apolipoproteins

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Analysis of human lecithin-cholesterol acyltransferase activity by carboxyl-terminal truncation

1 reference

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Determination of Lecithin: Cholesterol Acyltransfer in Human Blood Plasma

1 reference

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

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Machine learning approaches for the prediction of signal peptides and other protein sorting signals

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A molecular defect causing fish eye disease: an amino acid exchange in lecithin-cholesterol acyltransferase (LCAT) leads to the selective loss of alpha-LCAT activity

1 reference

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Fish eye syndrome: a molecular defect in the lecithin-cholesterol acyltransferase (LCAT) gene associated with normal alpha-LCAT-specific activity. Implications for classification and prognosis

1 reference

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Familial high-density-lipoprotein deficiency causing corneal opacities (fish eye disease) in a family of Dutch descent

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Two novel molecular defects in the LCAT gene are associated with fish eye disease

1 reference

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An amino acid exchange in exon I of the human lecithin: cholesterol acyltransferase (LCAT) gene is associated with fish eye disease

1 reference

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based on heuristic

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Binding affinity and reactivity of lecithin cholesterol acyltransferase with native lipoproteins

1 reference

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Interaction of N-methyl-anthraniloyl-labelled porcine apolipoprotein A-I with porcine lecithin: cholesterol acyltransferase: an energy transfer study

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Identifiers

10.1016/S1570-9639(03)00005-0

1 reference

Europe PubMed Central

PubMed publication ID

2 December 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

2 December 2017

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