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| - artículu científicu espublizáu en 1999 (ast)
- vědecký článek publikovaný v roce 1999 (cs)
- 1999 թվականի ապրիլին հրատարակված գիտական հոդված (hy)
- vedecký článok (publikovaný 1999/04/02) (sk)
- 1999 թուականի Ապրիլին հրատարակուած գիտական յօդուած (hyw)
- مقالة علمية (نشرت في 2-4-1999) (ar)
- наукова стаття, опублікована у квітні 1999 (uk)
- article publié dans la revue scientifique Journal of Biological Chemistry (fr)
- wetenschappelijk artikel (gepubliceerd op 1999/04/02) (nl)
- scientific journal article (en)
- im April 1999 veröffentlichter wissenschaftlicher Artikel (de)
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| - R. Fässler
- A. Oldberg
- D. Heinegård
- L. Svensson
- F. P. Reinholt
- A. Aszódi
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| - Fibromodulin-null mice have abnormal collagen fibrils, tissue organization, and altered lumican deposition in tendon (en)
- Fibromodulin-null mice have abnormal collagen fibrils, tissue organization, and altered lumican deposition in tendon (nl)
- Fibromodulin-null mice have abnormal collagen fibrils, tissue organization, and altered lumican deposition in tendon (ast)
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| - Fibromodulin-null mice have abnormal collagen fibrils, tissue organization, and altered lumican deposition in tendon (en)
- Fibromodulin-null mice have abnormal collagen fibrils, tissue organization, and altered lumican deposition in tendon (nl)
- Fibromodulin-null mice have abnormal collagen fibrils, tissue organization, and altered lumican deposition in tendon (ast)
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| name
| - Fibromodulin-null mice have abnormal collagen fibrils, tissue organization, and altered lumican deposition in tendon (en)
- Fibromodulin-null mice have abnormal collagen fibrils, tissue organization, and altered lumican deposition in tendon (nl)
- Fibromodulin-null mice have abnormal collagen fibrils, tissue organization, and altered lumican deposition in tendon (ast)
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| title
| - Fibromodulin-null mice have abnormal collagen fibrils, tissue organization, and altered lumican deposition in tendon (en)
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| is cites work
of | - Fourier-transform infrared anisotropy in cross and parallel sections of tendon and articular cartilage
- Collagen fibril form and function
- Structural macromolecules and supramolecular organisation of the vitreous gel.
- Effects of decorin proteoglycan on fibrillogenesis, ultrastructure, and mechanics of type I collagen gels
- Decorin deficiency leads to impaired angiogenesis in injured mouse cornea.
- Molecular regulation of tendon cell fate during development
- Functions of lumican and fibromodulin: lessons from knockout mice
- The atypical homeodomain transcription factor Mohawk controls tendon morphogenesis
- Spatial and temporal expression of molecular markers and cell signals during normal development of the mouse patellar tendon
- Modulation of small leucine-rich proteoglycans (SLRPs) expression in the mouse uterus by estradiol and progesterone
- The skeletal phenotype of chondroadherin deficient mice
- Biglycan organizes collagen VI into hexagonal-like networks resembling tissue structures
- Collagen fibril diameters increase and fibril densities decrease in skin subjected to repetitive compressive and shear stresses
- Novel insights into the function and dynamics of extracellular matrix in liver fibrosis
- The regulatory roles of small leucine-rich proteoglycans in extracellular matrix assembly
- Proteoglycan form and function: A comprehensive nomenclature of proteoglycans
- Extracellular matrix molecules: potential targets in pharmacotherapy.
- Dermatopontin, a novel player in the biology of the extracellular matrix
- Type XIV Collagen Regulates Fibrillogenesis: PREMATURE COLLAGEN FIBRIL GROWTH AND TISSUE DYSFUNCTION IN NULL MICE.
- Fibromodulin and lumican bind to the same region on collagen type I fibrils
- Corneal opacity in lumican-null mice: defects in collagen fibril structure and packing in the posterior stroma.
- PRELP, collagen, and a theory of Hutchinson-Gilford progeria
- Defects in tendon, ligament, and enthesis in response to genetic alterations in key proteoglycans and glycoproteins: a review
- Expression pattern and gene characterization of asporin. a newly discovered member of the leucine-rich repeat protein family
- Biglycan and decorin bind close to the n-terminal region of the collagen VI triple helix
- Tenomodulin is necessary for tenocyte proliferation and tendon maturation
- Differential expression of lumican and fibromodulin regulate collagen fibrillogenesis in developing mouse tendons
- Fibromodulin binds collagen type I via Glu-353 and Lys-355 in leucine-rich repeat 11.
- Biological functions of the small leucine-rich proteoglycans: from genetics to signal transduction.
- Genetic evidence for the coordinated regulation of collagen fibrillogenesis in the cornea by decorin and biglycan
- Potential roles for the small leucine-rich proteoglycans biglycan and fibromodulin in ectopic ossification of tendon induced by exercise and in modulating rotarod performance.
- Dermatan sulfate epimerase 1-deficient mice have reduced content and changed distribution of iduronic acids in dermatan sulfate and an altered collagen structure in skin.
- Murine fibromodulin: cDNA and genomic structure, and age-related expression and distribution in the knee joint
- Distinctive localization and function for lumican, fibromodulin and decorin to regulate collagen fibril organization in periodontal tissues
- Association of chondroadherin with collagen type II.
- Collagen fibrillogenesis: fibronectin, integrins, and minor collagens as organizers and nucleators
- Type V collagen: heterotypic type I/V collagen interactions in the regulation of fibril assembly
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