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Fibrous Proteins: Comparison
Please note this is a comparison between Version 1 by Yu Peng and Version 3 by Catherine Yang.

Fibrous proteins are elongated, structural proteins characterized by elongatedmacromolecules whose polypeptide conformations,hains adopt repetitive sequence organization,conformations and assemblye into ordered extracellularsupramolecular architectures, including fibrils, fibers, microfibrils, orand networks. In connective-tissue biology and the genetics of connective-tissue disordersWithin glycosylation and glycoprotein research, the term principally encompasses collagenextracellular-matrix proteins and the protein constituents of elastic fibers, including tropothat form or organize filamentous assemblies, particularly collagens, elastin and fibrillin-containing microfibrils. Collagens contain glycine-rich repeating sequences that support triple-helical-associated proteins, fibrillins, and selected adhesive glycoproteins. Their molecular organization and the formation of tissue-specific supra is determined by characteristic sequence motifs, intermolecular matrices [1][2]. Theassocir batiosynthesis includes intracellularns, covalent cross-links, and post-translational processing, secretion of procomodifications. Collagen, proteolytic maturation, fibril assembly, and covalent cross-link formations contain triple-helical domains composed of repeating Gly–X–Y sequences and assemble into tissue-specific fibrillar or networked structures [21]. Elastin is produc fibers contain a ed from soluble tropoelastin precursors that undergo cross-linkeding to generate elastin core formed from tropoelastin and ac-fiber cores, which associate with microfibrillar scaffold composedglycoproteins [2]. Glargelyycosylation of fibrillin and associatedous extracellular proteins [3]. Thincludes genecollagen hydroxylysine O-glycosylaticon and biochemical scope of fibrous glycan modifications of associated glycoproteins includes the encoding genes, domain architecture, post-translational modifications; these modifications contribute to protein folding, secretion, intermolecular interactionsassembly, and matrix assembly processes that determine connective-tissue strurchitecture [2][3][4].

  • collagen
  • elastin
  • protein glycosylation
  • extracellular matrix

 

 🔵 Glycosylation and Glycoproteins Research • 🟣 Molecular Biology • 🟡 Biochemistry, Genetics and Molecular Biology • 🔴 Life Sciences

References

  1. G. N. Ramachandran; G. Kartha; Structure of Collagen. NSylvie Ricard-Blum; The Collagen Family. Cold Spring Harb. Perspect. Biol. 201954, 174, 269-270. [CrossRef]0, 3, a004978-a004978. [CrossRef]
  2. Sylvie Ricard-Blum; The Collagen Family. Cold SpriSteven G. Wise; Anthony S. Weiss; Tropoelastin. Ingt. Harb. Perspect.J. Biochem. Cell Biol. 2010, 3, a004978-a004978. [CrossRef]9, 41, 494-497. [CrossRef]
  3. Steven G. Wise; Anthony S. Weiss; Tropoelastin. Lavinia Arseni; Anita Lombardi; Donata Orioli; From Structure to Phenotype: Impact of Collagen Alterations on Human Health. Int. J. BiMochem. Cell Bioll. Sci. 2009, 418, 1, 494-497. [CrossRef]9, 1407. [CrossRef]
  4. Jaroslava Halper; Michael Kjaer. Basic Components of Connective Tissues and Extracellular Matrix: Elastin, Fibrillin, Fibulins, Fibrinogen, Fibronectin, Laminin, Tenascins and Thrombospondins; Springer Nature: Durham, NC, United States, 2013; pp. 31-47. [CrossRef]Nikos K. Karamanos; Achilleas D. Theocharis; Zoi Piperigkou; Dimitra Manou; Alberto Passi; Spyros S. Skandalis; Demitrios H. Vynios; Véronique Orian‐Rousseau; Sylvie Ricard‐Blum; Christian E.H. Schmelzer; Laurent Duca; Madeleine Durbeej; Nikolaos A. Afratis; Linda Troeberg; Marco Franchi; Valentina Masola; Maurizio Onisto; A Guide to the Composition and Functions of the Extracellular Matrix. FEBS J. 2021, 288, 6850-6912. [CrossRef]
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