메뉴 건너뛰기




Volumn 5, Issue 5, 2015, Pages

Structural constraints on the evolution of the collagen fibril: Convergence on a 1014-residue COL domain

Author keywords

Collagen; Cross links; D period; Exon structure

Indexed keywords

AMINO ACID; COLLAGEN;

EID: 84934914413     PISSN: None     EISSN: 20462441     Source Type: Journal    
DOI: 10.1098/rsob.140220     Document Type: Article
Times cited : (12)

References (33)
  • 1
    • 0025016078 scopus 로고
    • Characterization of a fibrillar collagen gene in sponges reveals the early evolutionary appearance of two collagen gene families
    • Exposito JY, Garrone R. 1990 Characterization of a fibrillar collagen gene in sponges reveals the early evolutionary appearance of two collagen gene families. Proc. Natl Acad. Sci. USA 87, 6669-6673. (doi:10.1073/pnas.87.17.6669)
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 6669-6673
    • Exposito, J.Y.1    Garrone, R.2
  • 2
    • 0027327007 scopus 로고
    • The complete intron/exon structure of Ephydatia mulleri fibrillar collagen gene suggests a mechanism for the evolution of an ancestral gene module
    • Exposito JY, van der Rest M, Garrone R. 1993 The complete intron/exon structure of Ephydatia mulleri fibrillar collagen gene suggests a mechanism for the evolution of an ancestral gene module. J. Mol. Evol. 37, 254-259. (doi:10.1007/BF00175502)
    • (1993) J. Mol. Evol. , vol.37 , pp. 254-259
    • Exposito, J.Y.1    Van Der Rest, M.2    Garrone, R.3
  • 3
    • 0024372722 scopus 로고
    • Structure and developmental expression of a sea urchin fibrillar collagen gene
    • D'Alessio M, Ramirez F, Suzuki HR, Solursh M, Gambino R. 1989 Structure and developmental expression of a sea urchin fibrillar collagen gene. Proc. Natl Acad. Sci. USA 86, 9303-9307. (doi:10. 1073/pnas.86.23.9303)
    • (1989) Proc. Natl Acad. Sci. USA , vol.86 , pp. 9303-9307
    • D'Alessio, M.1    Ramirez, F.2    Suzuki, H.R.3    Solursh, M.4    Gambino, R.5
  • 4
    • 9144240550 scopus 로고    scopus 로고
    • Invertebrate data predict an early emergence of vertebrate fibrillar collagen clades and an anti-incest model
    • Aouacheria A, Cluzel C, Lethias C, Gouy M, Garrone R, Exposito JY. 2004 Invertebrate data predict an early emergence of vertebrate fibrillar collagen clades and an anti-incest model. J. Biol. Chem. 279, 47 711-47 719. (doi:10.1074/jbc. M408950200)
    • (2004) J. Biol. Chem. , vol.279 , pp. 47711-47719
    • Aouacheria, A.1    Cluzel, C.2    Lethias, C.3    Gouy, M.4    Garrone, R.5    Exposito, J.Y.6
  • 6
    • 0037321822 scopus 로고    scopus 로고
    • Fibrillar collagen: The key to vertebrate evolution? A tale of molecular incest
    • Boot-Handford RP, Tuckwell DS. 2003 Fibrillar collagen: the key to vertebrate evolution? A tale of molecular incest. Bioessays 25, 142-151. (doi:10. 1002/bies.10230)
    • (2003) Bioessays , vol.25 , pp. 142-151
    • Boot-Handford, R.P.1    Tuckwell, D.S.2
  • 7
    • 0242290312 scopus 로고    scopus 로고
    • Collagen XXIV, a vertebrate fibrillar collagen with structural features of invertebrate collagens: Selective expression in developing cornea and bone
    • Koch M, Laub F, Zhou P, Hahn RA, Tanaka S, Burgeson RE, Gerecke DR, Ramirez F, Gordon MK. 2003 Collagen XXIV, a vertebrate fibrillar collagen with structural features of invertebrate collagens: selective expression in developing cornea and bone. J. Biol. Chem. 278, 43 236-43 244. (doi:10.1074/jbc. M302112200)
    • (2003) J. Biol. Chem. , vol.278 , pp. 43236-43244
    • Koch, M.1    Laub, F.2    Zhou, P.3    Hahn, R.A.4    Tanaka, S.5    Burgeson, R.E.6    Gerecke, D.R.7    Ramirez, F.8    Gordon, M.K.9
  • 8
    • 0019126260 scopus 로고
    • The collagen gene: Evidence for its evolutionary assembly by amplification of a DNA segment containing an exon of 54 bp
    • Yamada Y, Avvedimento VE, Mudryj M, Ohkubo H, Vogeli G, Irani M, Pastan I, de Crombrugghe B. 1980 The collagen gene: evidence for its evolutionary assembly by amplification of a DNA segment containing an exon of 54 bp. Cell 22, 887-892. (doi:10.1016/0092-8674 (80) 90565-6)
    • (1980) Cell , vol.22 , pp. 887-892
    • Yamada, Y.1    Avvedimento, V.E.2    Mudryj, M.3    Ohkubo, H.4    Vogeli, G.5    Irani, M.6    Pastan, I.7    De Crombrugghe, B.8
  • 10
    • 21444453832 scopus 로고    scopus 로고
    • Prediction of collagen stability from amino acid sequence
    • Persikov AV, Ramshaw JA, Brodsky B. 2005 Prediction of collagen stability from amino acid sequence. J. Biol. Chem. 280, 19 343-19 349. (doi:10.1074/jbc. M501657200)
    • (2005) J. Biol. Chem. , vol.280 , pp. 19343-19349
    • Persikov, A.V.1    Ramshaw, J.A.2    Brodsky, B.3
  • 12
    • 0034730390 scopus 로고    scopus 로고
    • Molecular adaptation to an extreme environment: Origin of the thermal stability of the pompeii worm collagen
    • Sicot FX, Mesnage M, Masselot M, Exposito JY, Garrone R, Deutsch J, Gaill F. 2000 Molecular adaptation to an extreme environment: origin of the thermal stability of the pompeii worm collagen. J. Mol. Biol. 302, 811-820. (doi:10.1006/jmbi. 2000.4505)
    • (2000) J. Mol. Biol. , vol.302 , pp. 811-820
    • Sicot, F.X.1    Mesnage, M.2    Masselot, M.3    Exposito, J.Y.4    Garrone, R.5    Deutsch, J.6    Gaill, F.7
  • 13
    • 33845959679 scopus 로고    scopus 로고
    • Self-association of collagen triple helic peptides into higher order structures
    • Kar K, Amin P, Bryan MA, Persikov AV, Mohs A, Wang YH, Brodsky B. 2006 Self-association of collagen triple helic peptides into higher order structures. J. Biol. Chem. 281, 33 283-33 290. (doi:10.1074/jbc. M605747200)
    • (2006) J. Biol. Chem. , vol.281 , pp. 33283-33290
    • Kar, K.1    Amin, P.2    Bryan, M.A.3    Persikov, A.V.4    Mohs, A.5    Wang, Y.H.6    Brodsky, B.7
  • 14
    • 78650472828 scopus 로고    scopus 로고
    • Comparative vertebrate evolutionary analyses of type I collagen: Potential of COL1a1 gene structure and intron variation for common bone-related diseases
    • Stover DA, Verrelli BC. 2011 Comparative vertebrate evolutionary analyses of type I collagen: potential of COL1a1 gene structure and intron variation for common bone-related diseases. Mol. Biol. Evol. 28, 533-542. (doi:10.1093/molbev/msq221)
    • (2011) Mol. Biol. Evol. , vol.28 , pp. 533-542
    • Stover, D.A.1    Verrelli, B.C.2
  • 15
    • 0017255740 scopus 로고
    • Chemistry of the collagen cross-links. Nature of the cross-links in the polymorphic forms of dermal collagen during development
    • Bailey AJ, Sims TJ. 1976 Chemistry of the collagen cross-links. Nature of the cross-links in the polymorphic forms of dermal collagen during development. Biochem. J. 153, 211-215.
    • (1976) Biochem. J. , vol.153 , pp. 211-215
    • Bailey, A.J.1    Sims, T.J.2
  • 16
    • 0035374511 scopus 로고    scopus 로고
    • Structural characterization of pyrrolic cross-links in collagen using a biotinylated Ehrlich's reagent
    • Brady JD, Robins SP. 2001 Structural characterization of pyrrolic cross-links in collagen using a biotinylated Ehrlich's reagent. J. Biol. Chem. 276, 18 812-18 818. (doi:10.1074/jbc. M009506200)
    • (2001) J. Biol. Chem. , vol.276 , pp. 18812-18818
    • Brady, J.D.1    Robins, S.P.2
  • 17
    • 0015846875 scopus 로고
    • Analysis of a crosslinked peptide from calf bone collagen: Evidence that hydroxylysyl glycoside participates in the crosslink
    • Eyre DR, Glimcher MJ. 1973 Analysis of a crosslinked peptide from calf bone collagen: evidence that hydroxylysyl glycoside participates in the crosslink. Biochem. Biophys. Res. Commun. 52, 663-671. (doi:10.1016/0006-291X (73) 90764-X)
    • (1973) Biochem. Biophys. Res. Commun. , vol.52 , pp. 663-671
    • Eyre, D.R.1    Glimcher, M.J.2
  • 18
    • 0029987370 scopus 로고    scopus 로고
    • Molecular site specificity of pyridinoline and pyrrole cross-links in type I collagen of human bone
    • Hanson DA, Eyre DR. 1996 Molecular site specificity of pyridinoline and pyrrole cross-links in type I collagen of human bone. J. Biol. Chem. 271, 26 508-26 516. (doi:10.1074/jbc.271.26.15307)
    • (1996) J. Biol. Chem. , vol.271 , pp. 26508-26516
    • Hanson, D.A.1    Eyre, D.R.2
  • 19
    • 0026545182 scopus 로고
    • Identification of the loci of the collagenassociated Ehrlich chromogen in type I collagen confirms its role as a trivalent cross-link
    • Kuypers R, Tyler M, Kurth LB, Jenkins ID, Horgan DJ. 1992 Identification of the loci of the collagenassociated Ehrlich chromogen in type I collagen confirms its role as a trivalent cross-link. Biochem. J. 283, 129-136.
    • (1992) Biochem. J. , vol.283 , pp. 129-136
    • Kuypers, R.1    Tyler, M.2    Kurth, L.B.3    Jenkins, I.D.4    Horgan, D.J.5
  • 21
    • 0018400235 scopus 로고
    • Chain conformation in the collagen molecule
    • Fraser RD, MacRae TP, Suzuki E. 1979 Chain conformation in the collagen molecule. J. Mol. Biol. 129, 463-481. (doi:10.1016/0022-2836 (79) 90507-2)
    • (1979) J. Mol. Biol. , vol.129 , pp. 463-481
    • Fraser, R.D.1    MacRae, T.P.2    Suzuki, E.3
  • 22
    • 0034737296 scopus 로고    scopus 로고
    • Structural basis of collagen recognition by integrin alpha2beta1
    • Emsley J, Knight CG, Farndale RW, Barnes MJ, Liddington RC. 2000 Structural basis of collagen recognition by integrin alpha2beta1. Cell 101, 47-56. (doi:10.1016/S0092-8674 (00) 80622-4)
    • (2000) Cell , vol.101 , pp. 47-56
    • Emsley, J.1    Knight, C.G.2    Farndale, R.W.3    Barnes, M.J.4    Liddington, R.C.5
  • 23
    • 0032913989 scopus 로고    scopus 로고
    • Sequence dependent conformational variations of collagen triple-helical structure
    • Kramer RZ, Bella J, Mayville P, Brodsky B, Berman HM. 1999 Sequence dependent conformational variations of collagen triple-helical structure. Nat. Struct. Biol. 6, 454-457. (doi:10.1038/8259)
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 454-457
    • Kramer, R.Z.1    Bella, J.2    Mayville, P.3    Brodsky, B.4    Berman, H.M.5
  • 27
    • 80053257163 scopus 로고    scopus 로고
    • Multi-hierarchical self-assembly of a collagen mimetic peptide from triple helix to nanofibre and hydrogel
    • O'Leary LE, Fallas JA, Bakota EL, Kang MK, Hartgerink JD. 2011 Multi-hierarchical self-assembly of a collagen mimetic peptide from triple helix to nanofibre and hydrogel. Nat. Chem. 3, 821-828. (doi:10.1038/nchem.1123)
    • (2011) Nat. Chem. , vol.3 , pp. 821-828
    • O'Leary, L.E.1    Fallas, J.A.2    Bakota, E.L.3    Kang, M.K.4    Hartgerink, J.D.5
  • 28
    • 42449113812 scopus 로고    scopus 로고
    • Cell-collagen interactions: The use of peptide Toolkits to investigate collagen-receptor interactions
    • Farndale RW et al. 2008 Cell-collagen interactions: the use of peptide Toolkits to investigate collagen-receptor interactions. Biochem. Soc. Trans. 36, 241-250. (doi:10.1042/BST0360241)
    • (2008) Biochem. Soc. Trans. , vol.36 , pp. 241-250
    • Farndale, R.W.1
  • 29
    • 80054036560 scopus 로고    scopus 로고
    • Transmembrane collagen receptors
    • Leitinger B. 2011 Transmembrane collagen receptors. Annu. Rev. Cell Dev. Biol. 27, 265-290. (10.1146/annurev-cellbio-092910-154013)
    • (2011) Annu. Rev. Cell Dev. Biol. , vol.27 , pp. 265-290
    • Leitinger, B.1
  • 30
    • 33847227672 scopus 로고    scopus 로고
    • Consortium for osteogenesis imperfecta mutations in the helical domain of type I collagen: Regions rich in lethal mutations align with collagen binding sites for integrins and proteoglycans
    • Marini JC et al. 2007 Consortium for osteogenesis imperfecta mutations in the helical domain of type I collagen: regions rich in lethal mutations align with collagen binding sites for integrins and proteoglycans. Hum. Mutat. 28, 209-221. (doi:10. 1002/humu.20429)
    • (2007) Hum. Mutat. , vol.28 , pp. 209-221
    • Marini, J.C.1
  • 31
    • 84912057983 scopus 로고    scopus 로고
    • Urochordate serpins are classified into six groups encoded by exon-intron structures, microsynteny and Bayesian phylogenetic analyses
    • Kumar A, Bhandari A. 2014 Urochordate serpins are classified into six groups encoded by exon-intron structures, microsynteny and Bayesian phylogenetic analyses. J. Genomics 2, 131-140. (doi:10.7150/jgen. 9437)
    • (2014) J. Genomics , vol.2 , pp. 131-140
    • Kumar, A.1    Bhandari, A.2
  • 32
    • 43349098885 scopus 로고    scopus 로고
    • Exalign: A new method for comparative analysis of exon-intron gene structures
    • Pavesi G, Zambelli F, Caggese C, Pesole G. 2008 Exalign: a new method for comparative analysis of exon-intron gene structures. Nucleic Acids Res. 36, e47. (doi:10.1093/nar/gkn153)
    • (2008) Nucleic Acids Res. , vol.36 , pp. e47
    • Pavesi, G.1    Zambelli, F.2    Caggese, C.3    Pesole, G.4
  • 33
    • 84895860854 scopus 로고    scopus 로고
    • Evolution, functional divergence and conserved exon-intron structure of bHLH/PAS gene family
    • Yan J, Ma Z, Xu X, Guo AY. 2014 Evolution, functional divergence and conserved exon-intron structure of bHLH/PAS gene family. Mol. Genet. Genomics 289, 25-36. (10.1007/s00438-013-0786-0)
    • (2014) Mol. Genet. Genomics , vol.289 , pp. 25-36
    • Yan, J.1    Ma, Z.2    Xu, X.3    Guo, A.Y.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.