(Q38330905)

English

Two naturally occurring mutations at the first and second bases of codon aspartic acid 156 in the proposed catalytic triad of human lipoprotein lipase. In vivo evidence that aspartic acid 156 is essential for catalysis

scientific article published on January 25, 1992

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scholarly article

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PubMed publication ID

2 September 2017

Two naturally occurring mutations at the first and second bases of codon aspartic acid 156 in the proposed catalytic triad of human lipoprotein lipase. In vivo evidence that aspartic acid 156 is essential for catalysis (English)

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2 September 2017

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10.1016/S0021-9258(18)46034-6

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10 November 2022

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10.1016/S0021-9258(18)46034-6

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10 November 2022

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Davignon J

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2 September 2017

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Y. H. Ma

1

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Europe PubMed Central

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10 November 2022

T. Bruin

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10 November 2022

S. Tuzgol

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10 November 2022

B. I. Wilson

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10 November 2022

G. Roederer

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10 November 2022

M. S. Liu

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10 November 2022

J. J. Kastelein

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10 November 2022

J. D. Brunzell

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10 November 2022

M. R. Hayden

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publication date

1 January 1992

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2 September 2017

25 January 1992

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National Center for Biotechnology Information

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10 November 2022

full work available at URL

http://intl.jbc.org/cgi/content/abstract/267/3/1918

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10 November 2022

https://api.elsevier.com/content/article/PII:S0021925818460346?httpAccept=text/xml

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10.1016/S0021-9258(18)46034-6

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10 November 2022

https://api.elsevier.com/content/article/PII:S0021925818460346?httpAccept=text/plain

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10.1016/S0021-9258(18)46034-6

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Journal of Biological Chemistry

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2 September 2017

267

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Europe PubMed Central

PubMed publication ID

2 September 2017

3

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Europe PubMed Central

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2 September 2017

1918-1923

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Europe PubMed Central

PubMed publication ID

2 September 2017

Organization of the human lipoprotein lipase gene and evolution of the lipase gene family

1

1 reference

10.1016/S0021-9258(18)46034-6

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Cloning of rat hepatic lipase cDNA: evidence for a lipase gene family

2

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Human lipoprotein lipase complementary DNA sequence.

3

1 reference

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Molecular cloning and sequence of a cDNA coding for bovine lipoprotein lipase

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Porcine pancreatic lipase. Completion of the primary structure

7

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Structure of human pancreatic lipase

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Familial chylomicronemia (type I hyperlipoproteinemia) due to a single missense mutation in the lipoprotein lipase gene

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Lipoprotein lipaseBethesda: a single amino acid substitution (Ala-176----Thr) leads to abnormal heparin binding and loss of enzymic activity

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A missense mutation at codon 188 of the human lipoprotein lipase gene is a frequent cause of lipoprotein lipase deficiency in persons of different ancestries

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Amino acid substitution (Ile194----Thr) in exon 5 of the lipoprotein lipase gene causes lipoprotein lipase deficiency in three unrelated probands. Support for a multicentric origin

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A mutation in the human lipoprotein lipase gene as the most common cause of familial chylomicronemia in French Canadians

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Detection and characterization of the heterozygote state for lipoprotein lipase deficiency

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American Journal of Physiology

22

249

E107

author name string

Iverius

publication date

1985

1 reference

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Trends in Genetics

23

5

391

author name string

Mullenbach

publication date

1989

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Two polymorphisms in the human lipoprotein lipase (LPL) gene

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Hind III RFLP in the lipoprotein lipase gene, (LPL).

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An LFA-3 cDNA encodes a phospholipid-linked membrane protein homologous to its receptor CD2

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Direct detection and automated sequencing of individual alleles after electrophoretic strand separation: identification of a common nonsense mutation in exon 9 of the human lipoprotein lipase gene

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Dissecting the catalytic triad of a serine protease

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The three-dimensional structure of Asn102 mutant of trypsin: role of Asp102 in serine protease catalysis

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The catalytic role of the active site aspartic acid in serine proteases

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A serine protease triad forms the catalytic centre of a triacylglycerol lipase

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Ser-His-Glu triad forms the catalytic site of the lipase from Geotrichum candidum

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PubMed publication ID

2 September 2017

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