메뉴 건너뛰기




Volumn 49, Issue , 2016, Pages 106-119

Structure, evolution and expression of collagen XXVIII: Lessons from the zebrafish

Author keywords

Collagen XXVIII; Gene duplication; Kunitz domain; Ohnolog; VWA; Zebrafish

Indexed keywords

COLLAGEN DERIVATIVE; COLLAGEN XXVIII; UNCLASSIFIED DRUG; COLLAGEN; ZEBRAFISH PROTEIN;

EID: 84961138933     PISSN: 0945053X     EISSN: 15691802     Source Type: Journal    
DOI: 10.1016/j.matbio.2015.07.001     Document Type: Article
Times cited : (24)

References (29)
  • 2
    • 38649105499 scopus 로고    scopus 로고
    • Common interruptions in the repeating tripeptide sequence of non-fibrillar collagens: sequence analysis and structural studies on triple-helix peptide models
    • Thiagarajan G., Li Y., Mohs A., Strafaci C., Popiel M., et al. Common interruptions in the repeating tripeptide sequence of non-fibrillar collagens: sequence analysis and structural studies on triple-helix peptide models. J. Mol. Biol. 2008, 376:736-748.
    • (2008) J. Mol. Biol. , vol.376 , pp. 736-748
    • Thiagarajan, G.1    Li, Y.2    Mohs, A.3    Strafaci, C.4    Popiel, M.5
  • 3
    • 0036796740 scopus 로고    scopus 로고
    • Distribution and evolution of von Willebrand/integrin A domains: widely dispersed domains with roles in cell adhesion and elsewhere
    • Whittaker C.A., Hynes R.O. Distribution and evolution of von Willebrand/integrin A domains: widely dispersed domains with roles in cell adhesion and elsewhere. Mol. Biol. Cell 2002, 13:3369-3387.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 3369-3387
    • Whittaker, C.A.1    Hynes, R.O.2
  • 4
    • 33645645281 scopus 로고    scopus 로고
    • Collagen XXVIII, a novel von Willebrand factor A domain-containing protein with many imperfections in the collagenous domain
    • Veit G., Kobbe B., Keene D.R., Paulsson M., Koch M., Wagener R. Collagen XXVIII, a novel von Willebrand factor A domain-containing protein with many imperfections in the collagenous domain. J. Biol. Chem. 2006, 281:3494-3504.
    • (2006) J. Biol. Chem. , vol.281 , pp. 3494-3504
    • Veit, G.1    Kobbe, B.2    Keene, D.R.3    Paulsson, M.4    Koch, M.5    Wagener, R.6
  • 5
    • 78649420778 scopus 로고    scopus 로고
    • Collagen XXVIII is a distinctive component of the peripheral nervous system nodes of ranvier and surrounds nonmyelinating glial cells
    • Grimal S., Puech S., Wagener R., Ventéo S., Carroll P., Fichard-Carroll A. Collagen XXVIII is a distinctive component of the peripheral nervous system nodes of ranvier and surrounds nonmyelinating glial cells. Glia 2010, 58:1977-1987.
    • (2010) Glia , vol.58 , pp. 1977-1987
    • Grimal, S.1    Puech, S.2    Wagener, R.3    Ventéo, S.4    Carroll, P.5    Fichard-Carroll, A.6
  • 6
    • 80053345905 scopus 로고    scopus 로고
    • SignalP 4.0: discriminating signal peptides from transmembrane regions
    • Petersen T.N., Brunak S., von Heijne G., Nielsen H. SignalP 4.0: discriminating signal peptides from transmembrane regions. Nat. Methods 2011, 8:785-786.
    • (2011) Nat. Methods , vol.8 , pp. 785-786
    • Petersen, T.N.1    Brunak, S.2    von Heijne, G.3    Nielsen, H.4
  • 7
    • 21444453832 scopus 로고    scopus 로고
    • Prediction of collagen stability from amino acid sequence
    • Persikov A.V., Ramshaw J.A., Brodsky B. Prediction of collagen stability from amino acid sequence. J. Biol. Chem. 2005, 280:19343-19349.
    • (2005) J. Biol. Chem. , vol.280 , pp. 19343-19349
    • Persikov, A.V.1    Ramshaw, J.A.2    Brodsky, B.3
  • 8
    • 13644257223 scopus 로고    scopus 로고
    • Prediction, conservation analysis, and structural characterization of mammalian mucin-type O-glycosylation sites
    • Julenius K., Molgaard A., Gupta R., Brunak S. Prediction, conservation analysis, and structural characterization of mammalian mucin-type O-glycosylation sites. Glycobiology 2005, 15:153-164.
    • (2005) Glycobiology , vol.15 , pp. 153-164
    • Julenius, K.1    Molgaard, A.2    Gupta, R.3    Brunak, S.4
  • 9
    • 0032733930 scopus 로고    scopus 로고
    • Gene and genome duplications in vertebrates: the one-to-four (-to-eight in fish) rule and the evolution of novel gene functions
    • Meyer A., Schartl M. Gene and genome duplications in vertebrates: the one-to-four (-to-eight in fish) rule and the evolution of novel gene functions. Curr. Opin. Cell Biol. 1999, 11:699-704.
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 699-704
    • Meyer, A.1    Schartl, M.2
  • 10
    • 84876798186 scopus 로고    scopus 로고
    • The zebrafish reference genome sequence and its relationship to the human genome
    • Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., et al. The zebrafish reference genome sequence and its relationship to the human genome. Nature 2013, 496:498-503.
    • (2013) Nature , vol.496 , pp. 498-503
    • Howe, K.1    Clark, M.D.2    Torroja, C.F.3    Torrance, J.4    Berthelot, C.5
  • 11
    • 34948908604 scopus 로고    scopus 로고
    • The zebrafish genome in context: ohnologs gone missing
    • Postlethwait J.H. The zebrafish genome in context: ohnologs gone missing. J. Exp. Zool. B Mol. Dev. Evol. 2007, 308:563-577.
    • (2007) J. Exp. Zool. B Mol. Dev. Evol. , vol.308 , pp. 563-577
    • Postlethwait, J.H.1
  • 13
    • 0030729183 scopus 로고    scopus 로고
    • Expression and potential role of the extracellular matrix in hepatic ontogenesis: a review
    • Amenta P.S., Harrison D. Expression and potential role of the extracellular matrix in hepatic ontogenesis: a review. Microsc. Res. Tech. 1997, 39:372-386.
    • (1997) Microsc. Res. Tech. , vol.39 , pp. 372-386
    • Amenta, P.S.1    Harrison, D.2
  • 14
    • 33646786080 scopus 로고    scopus 로고
    • Characterization of a conduit system containing laminin-5 in the human thymus: a potential transport system for small molecules
    • Drumea-Mirancea M., Wessels J.T., Müller C.A., Essl M., Eble J.A., et al. Characterization of a conduit system containing laminin-5 in the human thymus: a potential transport system for small molecules. J. Cell Sci. 2006, 119:1396-1405.
    • (2006) J. Cell Sci. , vol.119 , pp. 1396-1405
    • Drumea-Mirancea, M.1    Wessels, J.T.2    Müller, C.A.3    Essl, M.4    Eble, J.A.5
  • 16
    • 79959826381 scopus 로고    scopus 로고
    • Extracellular matrix dynamics in hepatocarcinogenesis: a comparative proteomics study of PDGFC transgenic and Pten null mouse models
    • Lai K.K.Y., Shang S., Lohia N., Booth G.C., Masse D.J., et al. Extracellular matrix dynamics in hepatocarcinogenesis: a comparative proteomics study of PDGFC transgenic and Pten null mouse models. PLoS Genet. 2011, 7:e1002147.
    • (2011) PLoS Genet. , vol.7 , pp. e1002147
    • Lai, K.K.Y.1    Shang, S.2    Lohia, N.3    Booth, G.C.4    Masse, D.J.5
  • 17
    • 84938096093 scopus 로고    scopus 로고
    • Time- and compartment-resolved proteome profiling of the extracellular niche in lung injury and repair
    • Schiller H.B., Fernandez I.E., Burgstaller G., Schaab C., Scheltema R.A., et al. Time- and compartment-resolved proteome profiling of the extracellular niche in lung injury and repair. Mol. Syst. Biol. 2015, 11:819.
    • (2015) Mol. Syst. Biol. , vol.11 , pp. 819
    • Schiller, H.B.1    Fernandez, I.E.2    Burgstaller, G.3    Schaab, C.4    Scheltema, R.A.5
  • 18
    • 33747789133 scopus 로고    scopus 로고
    • Conformational effects of Gly-X-Gly interruptions in the collagen triple helix
    • Bella J., Liu J., Kramer R., Brodsky B., Berman H.M. Conformational effects of Gly-X-Gly interruptions in the collagen triple helix. J. Mol. Biol. 2006, 362:298-311.
    • (2006) J. Mol. Biol. , vol.362 , pp. 298-311
    • Bella, J.1    Liu, J.2    Kramer, R.3    Brodsky, B.4    Berman, H.M.5
  • 20
    • 0035877585 scopus 로고    scopus 로고
    • The carboxyl terminus of type VII collagen mediates antiparallel dimer formation and constitutes a new antigenic epitope for epidermolysis Bullosa acquisita autoantibodies
    • Chen M., Keene D.R., Costa F.K., Tahk S.H., Woodley D.T. The carboxyl terminus of type VII collagen mediates antiparallel dimer formation and constitutes a new antigenic epitope for epidermolysis Bullosa acquisita autoantibodies. J. Biol. Chem. 2001, 276:21649-21655.
    • (2001) J. Biol. Chem. , vol.276 , pp. 21649-21655
    • Chen, M.1    Keene, D.R.2    Costa, F.K.3    Tahk, S.H.4    Woodley, D.T.5
  • 21
    • 0141594873 scopus 로고    scopus 로고
    • Procollagen VII self-assembly depends on site-specific interactions and is promoted by cleavage of the NC2 domain with procollagen C-proteinase
    • Colombo M., Brittingham R.J., Klement J.F., Majsterek I., Birk D.E., et al. Procollagen VII self-assembly depends on site-specific interactions and is promoted by cleavage of the NC2 domain with procollagen C-proteinase. Biochemistry 2003, 42:11434-11442.
    • (2003) Biochemistry , vol.42 , pp. 11434-11442
    • Colombo, M.1    Brittingham, R.J.2    Klement, J.F.3    Majsterek, I.4    Birk, D.E.5
  • 22
    • 84894442790 scopus 로고    scopus 로고
    • The cysteine-rich region of type VII collagen is a cystine knot with a new topology
    • Wegener H., Paulsen H., Seeger K. The cysteine-rich region of type VII collagen is a cystine knot with a new topology. J. Biol. Chem. 2014, 289:4861-4869.
    • (2014) J. Biol. Chem. , vol.289 , pp. 4861-4869
    • Wegener, H.1    Paulsen, H.2    Seeger, K.3
  • 23
    • 33745225191 scopus 로고    scopus 로고
    • The C5 domain of the collagen VI alpha3(VI) chain is critical for extracellular microfibril formation and is present in the extracellular matrix of cultured cells
    • Lamandé S.R., Mörgelin M., Adams N.E., Selan C., Allen J.M. The C5 domain of the collagen VI alpha3(VI) chain is critical for extracellular microfibril formation and is present in the extracellular matrix of cultured cells. J. Biol. Chem. 2006, 281:16607-16614.
    • (2006) J. Biol. Chem. , vol.281 , pp. 16607-16614
    • Lamandé, S.R.1    Mörgelin, M.2    Adams, N.E.3    Selan, C.4    Allen, J.M.5
  • 26
    • 34249854025 scopus 로고    scopus 로고
    • Cleavage and oligomerization of gliomedin, a transmembrane collagen required for node of ranvier formation
    • Maertens B., Hopkins D., Franzke C.-W., Keene D.R., Bruckner-Tuderman L., et al. Cleavage and oligomerization of gliomedin, a transmembrane collagen required for node of ranvier formation. J. Biol. Chem. 2007, 282:10647-10659.
    • (2007) J. Biol. Chem. , vol.282 , pp. 10647-10659
    • Maertens, B.1    Hopkins, D.2    Franzke, C.-W.3    Keene, D.R.4    Bruckner-Tuderman, L.5
  • 27
    • 77954611767 scopus 로고    scopus 로고
    • Human intestinal TFF3 forms disulfide-linked heteromers with the mucus-associated FCGBP protein and is released by hydrogen sulfide
    • Albert T.K., Laubinger W., Müller S., Hanisch F.-G., Kalinski T., et al. Human intestinal TFF3 forms disulfide-linked heteromers with the mucus-associated FCGBP protein and is released by hydrogen sulfide. J. Proteome Res. 2010, 9:3108-3117.
    • (2010) J. Proteome Res. , vol.9 , pp. 3108-3117
    • Albert, T.K.1    Laubinger, W.2    Müller, S.3    Hanisch, F.-G.4    Kalinski, T.5
  • 28
    • 84897360331 scopus 로고    scopus 로고
    • Porcine gastric TFF2 is a mucus constituent and differs from pancreatic TFF2
    • Stürmer R., Müller S., Hanisch F.-G., Hoffmann W. Porcine gastric TFF2 is a mucus constituent and differs from pancreatic TFF2. Cell. Physiol. Biochem. 2014, 33:895-904.
    • (2014) Cell. Physiol. Biochem. , vol.33 , pp. 895-904
    • Stürmer, R.1    Müller, S.2    Hanisch, F.-G.3    Hoffmann, W.4
  • 29
    • 0014252443 scopus 로고
    • Molecular weight estimation and separation of ribonucleic acid by electrophoresis in agarose-acrylamide composite gels
    • Peacock A.C., Dingman C.W. Molecular weight estimation and separation of ribonucleic acid by electrophoresis in agarose-acrylamide composite gels. Biochemistry 1968, 7:668-674.
    • (1968) Biochemistry , vol.7 , pp. 668-674
    • Peacock, A.C.1    Dingman, C.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.