메뉴 건너뛰기




Volumn 118, Issue , 2014, Pages 80-88

Corrigendum to "Anti-angiogenic effect of the basement membrane protein nidogen-1 in a mouse model of choroidal neovascularization" [Exp. Eye Res. 118C (2014) 80-88] DOI:10.1016/j.exer.2013.11.006.;Anti-angiogenic effect of the basement membrane protein nidogen-1 in a mouse model of choroidal neovascularization

Author keywords

Angiogenesis; Basement membrane; Choroidal neovascularization; Nidogen

Indexed keywords

COLLAGEN TYPE 4; ENTACTIN; ENTACTIN 1; ENTACTIN 2; LAMININ GAMMA1; MEMBRANE PROTEIN; MESSENGER RNA; PERLECAN; UNCLASSIFIED DRUG;

EID: 84890355682     PISSN: 00144835     EISSN: 10960007     Source Type: Journal    
DOI: 10.1016/j.exer.2015.05.015     Document Type: Erratum
Times cited : (13)

References (43)
  • 2
    • 34248141664 scopus 로고    scopus 로고
    • Retinal pigment epithelial cells synthesize laminins, including laminin 5, and adhere to them through alpha3- and alpha6-containing integrins
    • Aisenbrey S., Zhang M., Bacher D., Yee J., Brunken W.J., Hunter D.D. Retinal pigment epithelial cells synthesize laminins, including laminin 5, and adhere to them through alpha3- and alpha6-containing integrins. Invest. Ophthalmol. Vis. Sci. 2006, 47:5537-5544.
    • (2006) Invest. Ophthalmol. Vis. Sci. , vol.47 , pp. 5537-5544
    • Aisenbrey, S.1    Zhang, M.2    Bacher, D.3    Yee, J.4    Brunken, W.J.5    Hunter, D.D.6
  • 6
    • 84865762615 scopus 로고    scopus 로고
    • Different domains in nidogen-1 and nidogen-2 drive basement membrane formation in skin organotypic cocultures
    • Bechtel M., Keller M.V., Bloch W., Sasaki T., Boukamp P., Zaucke F., Paulsson M., Nischt R. Different domains in nidogen-1 and nidogen-2 drive basement membrane formation in skin organotypic cocultures. FASEB J. 2012, 26:3637-3648.
    • (2012) FASEB J. , vol.26 , pp. 3637-3648
    • Bechtel, M.1    Keller, M.V.2    Bloch, W.3    Sasaki, T.4    Boukamp, P.5    Zaucke, F.6    Paulsson, M.7    Nischt, R.8
  • 7
    • 0033519279 scopus 로고    scopus 로고
    • Laminin polymerization induces a receptor-cytoskeleton network
    • Colognato H., Winkelmann D.A., Yurchenco P.D. Laminin polymerization induces a receptor-cytoskeleton network. J.Cell Biol. 1999, 145:619-631.
    • (1999) J.Cell Biol. , vol.145 , pp. 619-631
    • Colognato, H.1    Winkelmann, D.A.2    Yurchenco, P.D.3
  • 8
    • 79956020106 scopus 로고    scopus 로고
    • Heat-sensitive TRPV channels in retinal pigment epithelial cells: regulation of VEGF-A secretion
    • Cordeiro S., Seyler S., Stindl J., Milenkovic V.M., Strauss O. Heat-sensitive TRPV channels in retinal pigment epithelial cells: regulation of VEGF-A secretion. Invest. Ophthalmol. Vis. Sci. 2010, 51:6001-6008.
    • (2010) Invest. Ophthalmol. Vis. Sci. , vol.51 , pp. 6001-6008
    • Cordeiro, S.1    Seyler, S.2    Stindl, J.3    Milenkovic, V.M.4    Strauss, O.5
  • 9
    • 0033695419 scopus 로고    scopus 로고
    • Quantitative image analysis of laser-induced choroidal neovascularization in rat
    • Edelman J.L., Castro M.R. Quantitative image analysis of laser-induced choroidal neovascularization in rat. Exp. Eye Res. 2000, 71:523-533.
    • (2000) Exp. Eye Res. , vol.71 , pp. 523-533
    • Edelman, J.L.1    Castro, M.R.2
  • 10
    • 0033808066 scopus 로고    scopus 로고
    • Still more complexity in mammalian basement membranes
    • Erickson A.C., Couchman J.R. Still more complexity in mammalian basement membranes. J.Histochem. Cytochem. 2000, 48:1291-1306.
    • (2000) J.Histochem. Cytochem. , vol.48 , pp. 1291-1306
    • Erickson, A.C.1    Couchman, J.R.2
  • 12
    • 0029805953 scopus 로고    scopus 로고
    • Domain-specific interactions between entactin and neutrophil integrins. G2 domain ligation of integrin alpha3beta1 and E domain ligation of the leukocyte response integrin signal for different responses
    • Gresham H.D., Graham I.L., Griffin G.L., Hsieh J.C., Dong L.J., Chung A.E., Senior R.M. Domain-specific interactions between entactin and neutrophil integrins. G2 domain ligation of integrin alpha3beta1 and E domain ligation of the leukocyte response integrin signal for different responses. J.Biol. Chem. 1996, 271:30587-30594.
    • (1996) J.Biol. Chem. , vol.271 , pp. 30587-30594
    • Gresham, H.D.1    Graham, I.L.2    Griffin, G.L.3    Hsieh, J.C.4    Dong, L.J.5    Chung, A.E.6    Senior, R.M.7
  • 13
    • 0033230621 scopus 로고    scopus 로고
    • Suppression of nidogen-1 translation by antisense targeting affects the adhesive properties of cultured astrocytes
    • Grimpe B., Probst J.C., Hager G. Suppression of nidogen-1 translation by antisense targeting affects the adhesive properties of cultured astrocytes. Glia 1999, 28:138-149.
    • (1999) Glia , vol.28 , pp. 138-149
    • Grimpe, B.1    Probst, J.C.2    Hager, G.3
  • 17
    • 1542297332 scopus 로고    scopus 로고
    • Pathogenesis of lesions in late age-related macular disease
    • Holz F.G., Pauleikhoff D., Klein R., Bird A.C. Pathogenesis of lesions in late age-related macular disease. Am. J. Ophthalmol. 2004, 137:504-510.
    • (2004) Am. J. Ophthalmol. , vol.137 , pp. 504-510
    • Holz, F.G.1    Pauleikhoff, D.2    Klein, R.3    Bird, A.C.4
  • 18
    • 0032508461 scopus 로고    scopus 로고
    • Nidogen-2: a new basement membrane protein with diverse binding properties
    • Kohfeldt E., Sasaki T., Gohring W., Timpl R. Nidogen-2: a new basement membrane protein with diverse binding properties. J.Mol. Biol. 1998, 282:99-109.
    • (1998) J.Mol. Biol. , vol.282 , pp. 99-109
    • Kohfeldt, E.1    Sasaki, T.2    Gohring, W.3    Timpl, R.4
  • 20
    • 70349893184 scopus 로고    scopus 로고
    • Deposition of nidogens and other basement membrane proteins in the young and aging mouse retina
    • Kunze A., Abari E., Semkova I., Paulsson M., Hartmann U. Deposition of nidogens and other basement membrane proteins in the young and aging mouse retina. Ophthalmic Res. 2010, 43:108-112.
    • (2010) Ophthalmic Res. , vol.43 , pp. 108-112
    • Kunze, A.1    Abari, E.2    Semkova, I.3    Paulsson, M.4    Hartmann, U.5
  • 21
    • 0034848340 scopus 로고    scopus 로고
    • The role of collagen-derived proteolytic fragments in angiogenesis
    • Marneros A.G., Olsen B.R. The role of collagen-derived proteolytic fragments in angiogenesis. Matrix Biol. 2001, 20:337-345.
    • (2001) Matrix Biol. , vol.20 , pp. 337-345
    • Marneros, A.G.1    Olsen, B.R.2
  • 23
    • 0036860601 scopus 로고    scopus 로고
    • Evidence of nidogen-2 compensation for nidogen-1 deficiency in transgenic mice
    • Miosge N., Sasaki T., Timpl R. Evidence of nidogen-2 compensation for nidogen-1 deficiency in transgenic mice. Matrix Biol. 2002, 21:611-621.
    • (2002) Matrix Biol. , vol.21 , pp. 611-621
    • Miosge, N.1    Sasaki, T.2    Timpl, R.3
  • 25
    • 0023377705 scopus 로고
    • Laminin-nidogen complex. Extraction with chelating agents and structural characterization
    • Paulsson M., Aumailley M., Deutzmann R., Timpl R., Beck K., Engel J. Laminin-nidogen complex. Extraction with chelating agents and structural characterization. Eur. J. Biochem. 1987, 166:11-19.
    • (1987) Eur. J. Biochem. , vol.166 , pp. 11-19
    • Paulsson, M.1    Aumailley, M.2    Deutzmann, R.3    Timpl, R.4    Beck, K.5    Engel, J.6
  • 26
    • 0028074247 scopus 로고
    • Two non-contiguous regions contribute to nidogen binding to a single EGF-like motif of the laminin gamma 1 chain
    • Poschl E., Fox J.W., Block D., Mayer U., Timpl R. Two non-contiguous regions contribute to nidogen binding to a single EGF-like motif of the laminin gamma 1 chain. EMBO J. 1994, 13:3741-3747.
    • (1994) EMBO J. , vol.13 , pp. 3741-3747
    • Poschl, E.1    Fox, J.W.2    Block, D.3    Mayer, U.4    Timpl, R.5
  • 27
    • 0027258592 scopus 로고
    • Mapping of nidogen binding sites for collagen type IV, heparan sulfate proteoglycan, and zinc
    • Reinhardt D., Mann K., Nischt R., Fox J.W., Chu M.L., Krieg T., Timpl R. Mapping of nidogen binding sites for collagen type IV, heparan sulfate proteoglycan, and zinc. J.Biol. Chem. 1993, 268:10881-10887.
    • (1993) J.Biol. Chem. , vol.268 , pp. 10881-10887
    • Reinhardt, D.1    Mann, K.2    Nischt, R.3    Fox, J.W.4    Chu, M.L.5    Krieg, T.6    Timpl, R.7
  • 29
    • 0036405396 scopus 로고    scopus 로고
    • Binding of mouse nidogen-2 to basement membrane components and cells and its expression in embryonic and adult tissues suggest complementary functions of the two nidogens
    • Salmivirta K., Talts J.F., Olsson M., Sasaki T., Timpl R., Ekblom P. Binding of mouse nidogen-2 to basement membrane components and cells and its expression in embryonic and adult tissues suggest complementary functions of the two nidogens. Exp. Cell Res. 2002, 279:188-201.
    • (2002) Exp. Cell Res. , vol.279 , pp. 188-201
    • Salmivirta, K.1    Talts, J.F.2    Olsson, M.3    Sasaki, T.4    Timpl, R.5    Ekblom, P.6
  • 30
    • 0036785584 scopus 로고    scopus 로고
    • Gene structure and functional analysis of the mouse nidogen-2 gene: nidogen-2 is not essential for basement membrane formation in mice
    • Schymeinsky J., Nedbal S., Miosge N., Poschl E., Rao C., Beier D.R., Skarnes W.C., Timpl R., Bader B.L. Gene structure and functional analysis of the mouse nidogen-2 gene: nidogen-2 is not essential for basement membrane formation in mice. Mol. Cell Biol. 2002, 22:6820-6830.
    • (2002) Mol. Cell Biol. , vol.22 , pp. 6820-6830
    • Schymeinsky, J.1    Nedbal, S.2    Miosge, N.3    Poschl, E.4    Rao, C.5    Beier, D.R.6    Skarnes, W.C.7    Timpl, R.8    Bader, B.L.9
  • 32
    • 0027102384 scopus 로고
    • Entactin stimulates neutrophil adhesion and chemotaxis through interactions between its Arg-Gly-Asp (RGD) domain and the leukocyte response integrin
    • Senior R.M., Gresham H.D., Griffin G.L., Brown E.J., Chung A.E. Entactin stimulates neutrophil adhesion and chemotaxis through interactions between its Arg-Gly-Asp (RGD) domain and the leukocyte response integrin. J.Clin. Invest. 1992, 90:2251-2257.
    • (1992) J.Clin. Invest. , vol.90 , pp. 2251-2257
    • Senior, R.M.1    Gresham, H.D.2    Griffin, G.L.3    Brown, E.J.4    Chung, A.E.5
  • 34
    • 0029023713 scopus 로고
    • Capturing genes encoding membrane and secreted proteins important for mouse development
    • Skarnes W.C., Moss J.E., Hurtley S.M., Beddington R.S. Capturing genes encoding membrane and secreted proteins important for mouse development. Proc. Natl. Acad. Sci. U.S.A. 1995, 92:6592-6596.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 6592-6596
    • Skarnes, W.C.1    Moss, J.E.2    Hurtley, S.M.3    Beddington, R.S.4
  • 35
    • 0033545239 scopus 로고    scopus 로고
    • Absence of basement membranes after targeting the LAMC1 gene results in embryonic lethality due to failure of endoderm differentiation
    • Smyth N., Vatansever H.S., Murray P., Meyer M., Frie C., Paulsson M., Edgar D. Absence of basement membranes after targeting the LAMC1 gene results in embryonic lethality due to failure of endoderm differentiation. J.Cell Biol. 1999, 144:151-160.
    • (1999) J.Cell Biol. , vol.144 , pp. 151-160
    • Smyth, N.1    Vatansever, H.S.2    Murray, P.3    Meyer, M.4    Frie, C.5    Paulsson, M.6    Edgar, D.7
  • 36
    • 0030271572 scopus 로고    scopus 로고
    • Macromolecular organization of basement membranes
    • Timpl R. Macromolecular organization of basement membranes. Curr. Opin. Cell Biol. 1996, 8:618-624.
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 618-624
    • Timpl, R.1
  • 37
    • 0030087944 scopus 로고    scopus 로고
    • Supramolecular assembly of basement membranes
    • Timpl R., Brown J.C. Supramolecular assembly of basement membranes. Bioessays 1996, 18:123-132.
    • (1996) Bioessays , vol.18 , pp. 123-132
    • Timpl, R.1    Brown, J.C.2
  • 38
    • 0019781637 scopus 로고
    • Anetwork model for the organization of type IV collagen molecules in basement membranes
    • Timpl R., Wiedemann H., van D.V., Furthmayr H., Kuhn K. Anetwork model for the organization of type IV collagen molecules in basement membranes. Eur. J. Biochem. 1981, 120:203-211.
    • (1981) Eur. J. Biochem. , vol.120 , pp. 203-211
    • Timpl, R.1    Wiedemann, H.2    van, D.V.3    Furthmayr, H.4    Kuhn, K.5
  • 40
    • 0036333442 scopus 로고    scopus 로고
    • Specific ablation of the nidogen-binding site in the laminin gamma1 chain interferes with kidney and lung development
    • Willem M., Miosge N., Halfter W., Smyth N., Jannetti I., Burghart E., Timpl R., Mayer U. Specific ablation of the nidogen-binding site in the laminin gamma1 chain interferes with kidney and lung development. Development 2002, 129:2711-2722.
    • (2002) Development , vol.129 , pp. 2711-2722
    • Willem, M.1    Miosge, N.2    Halfter, W.3    Smyth, N.4    Jannetti, I.5    Burghart, E.6    Timpl, R.7    Mayer, U.8
  • 41
    • 0023600043 scopus 로고
    • Basement membrane structure in situ: evidence for lateral associations in the type IV collagen network
    • Yurchenco P.D., Ruben G.C. Basement membrane structure in situ: evidence for lateral associations in the type IV collagen network. J.Cell Biol. 1987, 105:2559-2568.
    • (1987) J.Cell Biol. , vol.105 , pp. 2559-2568
    • Yurchenco, P.D.1    Ruben, G.C.2
  • 42
    • 1842478123 scopus 로고    scopus 로고
    • Current concepts in the pathogenesis of age-related macular degeneration
    • Zarbin M.A. Current concepts in the pathogenesis of age-related macular degeneration. Arch. Ophthalmol. 2004, 122:598-614.
    • (2004) Arch. Ophthalmol. , vol.122 , pp. 598-614
    • Zarbin, M.A.1
  • 43
    • 84876825364 scopus 로고    scopus 로고
    • Biochemical and biophysical changes underlie the mechanisms of basement membrane disruptions in a mouse model of dystroglycanopathy
    • Zhang P., Yang Y., Candiello J., Thorn T.L., Gray N., Halfter W.M., Hu H. Biochemical and biophysical changes underlie the mechanisms of basement membrane disruptions in a mouse model of dystroglycanopathy. Matrix Biol. 2013, 32:196-207.
    • (2013) Matrix Biol. , vol.32 , pp. 196-207
    • Zhang, P.1    Yang, Y.2    Candiello, J.3    Thorn, T.L.4    Gray, N.5    Halfter, W.M.6    Hu, H.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.