ArticleMatrix biology : journal of the International Society for Matrix Biology2017
Structural and functional analysis of two small leucine-rich repeat proteoglycans, fibromodulin and chondroadherin.
Article in Matrix biology : journal of the International Society for Matrix Biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed.
- Gold micro-particles for knee osteoarthritis.European journal of pain (London, England) · 2022Trial
- Reversible homodimerization of a small leucine-rich proteoglycan PRELP modulates the interactions with TGFβ1 and IGFI-R.The Journal of biological chemistry · 2026Article
- Fibromodulin-overexpressing fibroblast cells increase wound contraction, improve scar quality and enhance angiogenesis: an in-vivo study.BMC biotechnology · 2025Article
- Spatial gene expression in the adult rat patellar tendon.Matrix biology plus · 2023Article
- Small leucine rich proteoglycans: Biology, function and their therapeutic potential in the ocular surface.The ocular surface · 2023Review
- Fibromodulin, a Multifunctional Matricellular Modulator.Journal of dental research · 2023Review
- The role of fibromodulin in inflammatory responses and diseases associated with inflammation.Frontiers in immunology · 2023Review
- Crystal structures of FNIP/FGxxFN motif-containing leucine-rich repeat proteins.Scientific reports · 2022Article
- Sequence features, structure, ligand interaction, and diseases in small leucine rich repeat proteoglycans.Journal of cell communication and signaling · 2021Review
- The effects of maturation and aging on the rotator cuff tendon-to-bone interface.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2021Article
- Maternal protein restriction changes structural and metabolic gene expression in the skeletal muscle of aging offspring rats.Histology and histopathology · 2021Article
- Novel cell sources for bone regeneration.MedComm · 2021Review
- Constructing 3-Dimensional Atomic-Resolution Models of Nonsulfated Glycosaminoglycans with Arbitrary Lengths Using Conformations from Molecular Dynamics.International journal of molecular sciences · 2020Article
- The origins and developments of sulfation-prone tyrosine-rich and acidic N- and C-terminal extensions of class ll and lll small leucine-rich repeat proteins shed light on connective tissue evolution in vertebrates.BMC evolutionary biology · 2020Article
- Structural basis of the leukocyte integrin Mac-1 I-domain interactions with the platelet glycoprotein Ib.Blood advances · 2019Article
- Monoclonal and Polyclonal Antibodies Specific to Human Fibromodulin.Iranian journal of biotechnology · 2019Article
- Cartilage diseases.Matrix biology : journal of the International Society for Matrix Biology · 2018Review
- Glycosaminoglycan synthesis in the nucleus pulposus: Dysregulation and the pathogenesis of disc degeneration.Matrix biology : journal of the International Society for Matrix Biology · 2018Review
- A novel mouse model of intervertebral disc degeneration shows altered cell fate and matrix homeostasis.Matrix biology : journal of the International Society for Matrix Biology · 2018Article
- Super Secondary Structure Consisting of a Polyproline II Helix and a β-Turn in Leucine Rich Repeats in Bacterial Type III Secretion System Effectors.The protein journal · 2018Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
The small leucine-rich proteoglycans (SLRPs) are important regulators of extracellular matrix assembly and cell signalling. We have determined crystal structures at ~2.2Å resolution of human fibromodulin and chondroadherin, two collagen-binding SLRPs. Their overall fold is similar to that of the prototypical SLRP, decorin, but unlike decorin neither fibromodulin nor chondroadherin forms a stable dimer. A previously identified binding site for integrin α2β1 maps to an α-helix in the C-terminal cap region of chondroadherin. Interrogation of the Collagen Toolkits revealed a unique binding site for chondroadherin in collagen II, and no binding to collagen III. A triple-helical peptide containing the sequence GAOGPSGFQGLOGPOGPO (O is hydroxyproline) forms a stable complex with chondroadherin in solution. In fibrillar collagen I and II, this sequence is aligned with the collagen cross-linking site KGHR, suggesting a role for chondroadherin in cross-linking.
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Registered trials
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