The Primary Structure of a Basic Leucine-rich Repeat Protein, PRELP, Found in Connective Tissues
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference39 articles.
1. Primary structure of an extracellular matrix proteoglycan core protein deduced from cloned cDNA.
2. Detecting homology of distantly related proteins with consensus sequences
3. Deduced protein sequence of bone small proteoglycan I (biglycan) shows homology with proteoglycan II (decorin) and several nonconnective tissue proteins in a variety of species
4. A collagen-binding 59-kd protein (fibromodulin) is structurally related to the small interstitial proteoglycans PG-S1 and PG-S2 (decorin).
5. cDNA to chick lumican (corneal keratan sulfate proteoglycan) reveals homology to the small interstitial proteoglycan gene family and expression in muscle and intestine.
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1. Correlation of the tumor escape phenotype with loss of PRELP expression in melanoma;Journal of Translational Medicine;2023-09-20
2. The versatile roles of lumican in eye diseases: A review;The Ocular Surface;2023-07
3. Integrated analysis of WGCNA and machine learning identified diagnostic biomarkers in dilated cardiomyopathy with heart failure;Frontiers in Cell and Developmental Biology;2022-12-05
4. PRELP promotes myocardial fibrosis and ventricular remodelling after acute myocardial infarction by the wnt/β–catenin signalling pathway;Cardiovascular Journal of Africa;2022-11-02
5. Mechanistic interrogation of mutation-independent disease modulators of RDEB identifies the small leucine-rich proteoglycan PRELP as a TGF-β antagonist and inhibitor of fibrosis;Matrix Biology;2022-08
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