Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

The functional and clinical significance of the Met-->Thr substitution in Kringle IV type 10 of apolipoprotein(a).

Thrombosis research - 1 May 1998

Prins J, van der Hoek Y Y, Biesheuvel T H, Leus F R, van Rijn H J, Kastelein J J

Abstract excerpt

Lipoprotein(a) [Lp(a)], an independent risk factor for the development of atherosclerosis, contains an apolipoprotein(a) [apo(a)] moiety covalently linked to a LDL moiety. Apo(a) is a glycoprotein homologous to plasminogen as it contains multiple repeats of a lysine binding domain resembling plasminogen kringle IV (K.IV). The multiple K.IV repeats can be differentiated in ten types that show a variation in their...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Alleles
Share to Amino Acid Substitution

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Arteriosclerosis

Share to Case-Control Studies

Share to Cholesterol

Share to Lysine

Share to Methionine

Share to Polymorphism, Genetic

Source

Identifiers

PMID: 9684731
DOI: 10.1016/s0049-3848(98)00041-3

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The functional and clinical significance of the Met-->Thr substitution in Kringle IV type 10 of apolipoprotein(a).PMID 9684731Read ↗

The identification and significance of a Thr-->Pro polymorphism in kringle IV type 8 of apolipoprotein(a).Semantic proximity Read ↗

Apolipoprotein(a): structural and functional consequences of mutations in kringle type 10 (or kringle 4-37).Semantic proximity Read ↗

Polymorphisms in human apolipoprotein(a) kringle IV-10 and coronary artery disease: relationship to allele size, plasma lipoprotein(a) concentration, and lysine binding site activity.Semantic proximity Read ↗

Structural and functional polymorphism of lipoprotein(a): biological and clinical implications.Semantic proximity Read ↗

Lys and fibrinogen binding of wild-type (Trp72) and mutant (Arg72) human apo(a) kringle IV-10 expressed in E coli and CHO cells.Semantic proximity Read ↗

The apolipoprotein(a) kringle IV repeats which differ from the major repeat kringle are present in variably-sized isoforms.Semantic proximity Read ↗

Molecular cloning of the cDNA encoding the carboxy-terminal domain of chimpanzee apolipoprotein(a): an Asp57 --> Asn mutation in kringle IV-10 is associated with poor fibrin binding.Semantic proximity Read ↗

Specificity determinants in the interaction of apolipoprotein(a) kringles with tetranectin and LDL.Semantic proximity Read ↗

Single nucleotide polymorphisms in exons of the apo(a) kringles IV types 6 to 10 domain affect Lp(a) plasma concentrations and have different patterns in Africans and Caucasians.Semantic proximity Read ↗

The number of kringle IV repeats 3-10 is invariable in the human apo(a) gene.Semantic proximity Read ↗

Identification of mutations in human apolipoprotein(a) kringle 4-37 from the study of the DNA of peripheral blood lymphocytes: relevance to the role of lipoprotein(a) in atherothrombosis.Semantic proximity Read ↗

Evidence that the conformation of unliganded human plasminogen is maintained via an intramolecular interaction between the lysine-binding site of kringle 5 and the N-terminal peptideSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.