Evidence that the fibrinogen binding domain of Apo(a) is outside the lysine binding site of kringle IV-10: a study involving naturally occurring lysine binding defective lipoprotein(a) phenotypes.-Reference-Cited by-同舟云学术

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Evidence that the fibrinogen binding domain of Apo(a) is outside the lysine binding site of kringle IV-10: a study involving naturally occurring lysine binding defective lipoprotein(a) phenotypes.

Published:1996-07-01 Issue:1 Volume:98 Page:185-191
ISSN:0021-9738
Container-title:Journal of Clinical Investigation
language:en
Short-container-title:J. Clin. Invest.

Author:

Klezovitch O,Edelstein C,Scanu A M

Publisher

American Society for Clinical Investigation

Subject

General Medicine

Cited by 35 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Solution structure, dynamics and function investigation of Kringle domain of human receptor tyrosine kinase-like orphan receptor 1;Journal of Biomolecular Structure and Dynamics;2019-07-09

2. Characterization of the I4399M variant of apolipoprotein(a): implications for altered prothrombotic properties of lipoprotein(a);Journal of Thrombosis and Haemostasis;2017-07-31

3. Oxidation of apolipoprotein(a) inhibits kringle-associated lysine binding: The loss of intrinsic protein fluorescence suggests a role for tryptophan residues in the lysine binding site;Protein Science;2008-12-31

4. Lipoprotein(a): identification of subjects with a superbinding capacity for fibrinogen;Clinical Genetics;2008-04-23

5. Vascular accumulation of Lp(a): in vivo analysis of the role of lysine-binding sites using recombinant adenovirus;Clinical Genetics;2008-04-23

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