Kringle-dependent structural and functional polymorphism of apolipoprotein (a)
Author:
Publisher
Elsevier BV
Subject
Endocrinology,Biochemistry,Biophysics
Reference124 articles.
1. Proposed mechanisms for binding of apo[a] kringle type 9 to apo B-100 in human lipoprotein[a]
2. Identification of the cysteine residue in apolipoprotein(a) that mediates extracellular coupling with apolipoprotein B-100.
3. Analysis of strneture–fonction relationships in human apolipoprotein(a)
4. Lipoprotein (a). Heterogeneity and biological relevance.
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1. Antiangiogenic kringles derived from human plasminogen and apolipoprotein(a) inhibit fibrinolysis through a mechanism that requires a functional lysine-binding site;Biological Chemistry;2011-04-01
2. Naturally occurring human plasminogen, like genetically related apolipoprotein(a), contains oxidized phosphatidylcholine adducts;Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids;2010-07
3. Glycoprotein nonmetastatic melanoma protein b, a melanocytic cell marker, is a melanosome‐specific and proteolytically released protein;The FASEB Journal;2010-01-07
4. The secreted form of a melanocyte membrane‐bound glycoprotein (Pmel17/gp100) is released by ectodomain shedding;The FASEB Journal;2009-11-02
5. 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
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