메뉴 건너뛰기




Volumn 88, Issue 2, 2010, Pages 239-250

Structural disorder and dynamics of elastin

Author keywords

Conformational disorder; Elastin; Flexibility; Structure

Indexed keywords

CONFORMATIONAL DISORDERS; ELASTIC RECOIL; ENTROPY-DRIVEN MECHANISMS; EXTRACELLULAR MATRIX PROTEIN; SELF-ASSEMBLING; STRUCTURAL DISORDERS; STRUCTURAL ORGANIZATION; STRUCTURAL STUDIES; TISSUE ELASTICITY;

EID: 77950609823     PISSN: 08298211     EISSN: 12086002     Source Type: Journal    
DOI: 10.1139/O09-161     Document Type: Conference Paper
Times cited : (131)

References (149)
  • 1
    • 0019142643 scopus 로고
    • Optical properties of single elastin fibres indicate random protein conformation
    • doi:10.1038/287865a0. PMID:7432503
    • Aaron, B.B., and Gosline, J.M. 1980. Optical properties of single elastin fibres indicate random protein conformation. Nature, 287(5785): 865-867. doi:10.1038/287865a0. PMID:7432503.
    • (1980) Nature , vol.287 , Issue.5785 , pp. 865-867
    • Aaron, B.B.1    Gosline, J.M.2
  • 2
    • 0015411804 scopus 로고
    • Developing elastic tissue. An electron microscopic study
    • PMID:4117029
    • Albert, E.N. 1972. Developing elastic tissue. An electron microscopic study. Am. J. Pathol. 69(1): 89-102. PMID:4117029.
    • (1972) Am. J. Pathol. , vol.69 , Issue.1 , pp. 89-102
    • Albert, E.N.1
  • 3
    • 3142754280 scopus 로고    scopus 로고
    • UV Raman demonstrates that alpha-helical polyalanine peptides melt to polyproline II conformations
    • doi:10.1021/ja049518j. PMID:15238000
    • Asher, S.A., Mikhonin, A.V., and Bykov, S. 2004. UV Raman demonstrates that alpha-helical polyalanine peptides melt to polyproline II conformations. J. Am. Chem. Soc. 126(27): 8433-8440. doi:10.1021/ja049518j. PMID:15238000.
    • (2004) J. Am. Chem. Soc. , vol.126 , Issue.27 , pp. 8433-8440
    • Asher, S.A.1    Mikhonin, A.V.2    Bykov, S.3
  • 4
    • 0035956277 scopus 로고    scopus 로고
    • Self-aggregation characteristics of recombinantly expressed human elastin polypeptides
    • PMID:11738083
    • Bellingham, C.M., Woodhouse, K.A., Robson, P., Rothstein, S.J., and Keeley, F.W. 2001. Self-aggregation characteristics of recombinantly expressed human elastin polypeptides. Biochim. Biophys. Acta, 1550(1): 6-19. PMID:11738083.
    • (2001) Biochim. Biophys. Acta , vol.1550 , Issue.1 , pp. 6-19
    • Bellingham, C.M.1    Woodhouse, K.A.2    Robson, P.3    Rothstein, S.J.4    Keeley, F.W.5
  • 5
    • 0346850628 scopus 로고    scopus 로고
    • Recombinant human elastin polypeptides self-assemble into biomaterials with elastinlike properties
    • doi:10.1002/bip.10512. PMID:14648756
    • Bellingham, C.M., Lillie, M.A., Gosline, J.M., Wright, G.M., Starcher, B.C., Bailey, A.J., et al. 2003. Recombinant human elastin polypeptides self-assemble into biomaterials with elastinlike properties. Biopolymers, 70(4): 445-455. doi:10.1002/bip.10512. PMID:14648756.
    • (2003) Biopolymers , vol.70 , Issue.4 , pp. 445-455
    • Bellingham, C.M.1    Lillie, M.A.2    Gosline, J.M.3    Wright, G.M.4    Starcher, B.C.5    Bailey, A.J.6
  • 6
    • 0032483056 scopus 로고    scopus 로고
    • The amino acid sequence coded by the rarely expressed exon 26A of human elastin contains a stable beta-turn with chemotactic activity for monocytes
    • doi:10.1021/bi9802566. PMID:9693009
    • Bisaccia, F., Castiglione-Morelli, M.A., Spisani, S., Ostuni, A., Serafini-Fracassini, A., Bavoso, A., and Tamburro, A.M. 1998. The amino acid sequence coded by the rarely expressed exon 26A of human elastin contains a stable beta-turn with chemotactic activity for monocytes. Biochemistry, 37(31): 11128-11135. doi:10.1021/bi9802566. PMID:9693009.
    • (1998) Biochemistry , vol.37 , Issue.31 , pp. 11128-11135
    • Bisaccia, F.1    Castiglione-Morelli, M.A.2    Spisani, S.3    Ostuni, A.4    Serafini-Fracassini, A.5    Bavoso, A.6    Tamburro, A.M.7
  • 7
    • 0036035968 scopus 로고    scopus 로고
    • Polyproline II structure in proteins: Identification by chiroptical spectroscopies, stability, and functions
    • doi:10.1002/chir.10153. PMID:12395395
    • Bochicchio, B., and Tamburro, A.M. 2002. Polyproline II structure in proteins: identification by chiroptical spectroscopies, stability, and functions. Chirality, 14(10): 782-792. doi:10.1002/chir.10153. PMID:12395395.
    • (2002) Chirality , vol.14 , Issue.10 , pp. 782-792
    • Bochicchio, B.1    Tamburro, A.M.2
  • 8
    • 1542619619 scopus 로고    scopus 로고
    • Spectroscopic evidence revealing polyproline II structure in hydrophobic, putatively elastomeric sequences encoded by specific exons of human tropoelastin
    • doi:10.1002/bip.10552. PMID:14991666
    • Bochicchio, B., Aït-Ali, A., Tamburro, A.M., and Alix, A.J. 2004a. Spectroscopic evidence revealing polyproline II structure in hydrophobic, putatively elastomeric sequences encoded by specific exons of human tropoelastin. Biopolymers, 73(4): 484-493. doi:10.1002/bip.10552. PMID:14991666.
    • (2004) Biopolymers , vol.73 , Issue.4 , pp. 484-493
    • Bochicchio, B.1    Aït-Ali, A.2    Tamburro, A.M.3    Alix, A.J.4
  • 9
    • 3142687653 scopus 로고    scopus 로고
    • Dissection of human tropoelastin: Solution structure, dynamics and self-assembly of the exon 5 peptide
    • doi:10.1002/chem.200305661
    • Bochicchio, B., Floquet, N., Pepe, A., Alix, A.J., and Tamburro, A.M. 2004b. Dissection of human tropoelastin: solution structure, dynamics and self-assembly of the exon 5 peptide. Chem. Eur. J. 10(13): 3166-3176. doi:10.1002/chem.200305661.
    • (2004) Chem. Eur. J. , vol.10 , Issue.13 , pp. 3166-3176
    • Bochicchio, B.1    Floquet, N.2    Pepe, A.3    Alix, A.J.4    Tamburro, A.M.5
  • 10
    • 36649020438 scopus 로고    scopus 로고
    • Investigating the amyloidogenic nanostructured sequences of elastin: Sequence encoded by exon 28 of human tropoelastin gene
    • doi:10.1021/bm700636a. PMID:17929969
    • Bochicchio, B., Pepe, A., Flamia, R., Lorusso, M., and Tamburro, A.M. 2007. Investigating the amyloidogenic nanostructured sequences of elastin: sequence encoded by exon 28 of human tropoelastin gene. Biomacromolecules, 8(11): 3478-3486. doi:10.1021/bm700636a. PMID:17929969.
    • (2007) Biomacromolecules , vol.8 , Issue.11 , pp. 3478-3486
    • Bochicchio, B.1    Pepe, A.2    Flamia, R.3    Lorusso, M.4    Tamburro, A.M.5
  • 11
    • 58149242893 scopus 로고    scopus 로고
    • Investigating by CD the molecular mechanism of elasticity of elastomeric proteins
    • doi:10.1002/chir.20541. PMID:18293367
    • Bochicchio, B., Pepe, A., and Tamburro, A.M. 2008. Investigating by CD the molecular mechanism of elasticity of elastomeric proteins. Chirality, 20(9): 985-994. doi:10.1002/chir.20541. PMID:18293367.
    • (2008) Chirality , vol.20 , Issue.9 , pp. 985-994
    • Bochicchio, B.1    Pepe, A.2    Tamburro, A.M.3
  • 12
    • 0022965882 scopus 로고
    • Relevance of aggregation properties of tropoelastin to the assembly and structure of elastic fibers
    • doi:10.1016/0889-1605(86)90068-6. PMID:3805787
    • Bressan, G.M., Pasquali-Ronchetti, I., Fornieri, C., Mattioli, F., Castellani, I., and Volpin, D. 1986. Relevance of aggregation properties of tropoelastin to the assembly and structure of elastic fibers. J. Ultrastruct. Mol. Struct. Res. 94(3): 209-216. doi:10.1016/0889-1605(86)90068-6. PMID:3805787.
    • (1986) J. Ultrastruct. Mol. Struct. Res. , vol.94 , Issue.3 , pp. 209-216
    • Bressan, G.M.1    Pasquali-Ronchetti, I.2    Fornieri, C.3    Mattioli, F.4    Castellani, I.5    Volpin, D.6
  • 13
    • 0023663346 scopus 로고
    • Repeating structure of chick tropoelastin revealed by complementary DNA cloning
    • doi:10.1021/bi00380a001. PMID:3593675
    • Bressan, G.M., Argos, P., and Stanley, K.K. 1987. Repeating structure of chick tropoelastin revealed by complementary DNA cloning. Biochemistry, 26(6): 1497-1503. doi:10.1021/bi00380a001. PMID:3593675.
    • (1987) Biochemistry , vol.26 , Issue.6 , pp. 1497-1503
    • Bressan, G.M.1    Argos, P.2    Stanley, K.K.3
  • 14
    • 0029967225 scopus 로고    scopus 로고
    • Conformational and electrostatic properties of V-G-G-V-G, a typical sequence of the glycine-rich regions of elastin. An ab initio quantum molecular study
    • PMID:8791163
    • Broch, H., Moulabbi, M., Vasilescu, D., and Tamburro, A.M. 1996. Conformational and electrostatic properties of V-G-G-V-G, a typical sequence of the glycine-rich regions of elastin. An ab initio quantum molecular study. Int. J. Pept. Protein Res. 47(5): 394-404. PMID:8791163.
    • (1996) Int. J. Pept. Protein Res. , vol.47 , Issue.5 , pp. 394-404
    • Broch, H.1    Moulabbi, M.2    Vasilescu, D.3    Tamburro, A.M.4
  • 15
    • 28844489364 scopus 로고    scopus 로고
    • Tropoelastin interacts with cell-surface glycosaminoglycans via its COOHterminal domain
    • doi:10.1074/jbc.M507309200. PMID:16192266
    • Broekelmann, T.J., Kozel, B.A., Ishibashi, H., Werneck, C.C., Keeley, F.W., Zhang, L., and Mecham, R.P. 2005. Tropoelastin interacts with cell-surface glycosaminoglycans via its COOHterminal domain. J. Biol. Chem. 280(49): 40939-40947. doi:10.1074/jbc.M507309200. PMID:16192266.
    • (2005) J. Biol. Chem. , vol.280 , Issue.49 , pp. 40939-40947
    • Broekelmann, T.J.1    Kozel, B.A.2    Ishibashi, H.3    Werneck, C.C.4    Keeley, F.W.5    Zhang, L.6    Mecham, R.P.7
  • 16
    • 0026641004 scopus 로고
    • The cysteine residues in the carboxy terminal domain of tropoelastin form an intrachain disulfide bond that stabilizes a loop structure and positively charged pocket
    • doi:10.1016/S0006-291X(05)80843-5. PMID:1632791
    • Brown, P.L., Mecham, L., Tisdale, C., and Mecham, R.P. 1992. The cysteine residues in the carboxy terminal domain of tropoelastin form an intrachain disulfide bond that stabilizes a loop structure and positively charged pocket. Biochem. Biophys. Res. Commun. 186(1): 549-555. doi:10.1016/S0006-291X(05)80843- 5. PMID:1632791.
    • (1992) Biochem. Biophys. Res. Commun. , vol.186 , Issue.1 , pp. 549-555
    • Brown, P.L.1    Mecham, L.2    Tisdale, C.3    Mecham, R.P.4
  • 17
    • 0029051024 scopus 로고
    • Identification of an elastin cross-linking domain that joins three peptide chains. Possible role in nucleated assembly
    • doi:10.1074/jbc.270.30.17778. PMID:7629078
    • Brown-Augsburger, P., Tisdale, C., Broekelmann, T., Sloan, C., and Mecham, R.P. 1995. Identification of an elastin cross-linking domain that joins three peptide chains. Possible role in nucleated assembly. J. Biol. Chem. 270(30): 17778-17783. doi:10.1074/jbc.270.30.17778. PMID:7629078.
    • (1995) J. Biol. Chem. , vol.270 , Issue.30 , pp. 17778-17783
    • Brown-Augsburger, P.1    Tisdale, C.2    Broekelmann, T.3    Sloan, C.4    Mecham, R.P.5
  • 18
    • 0025650857 scopus 로고
    • Spectroscopic studies on elastin-like synthetic polypeptides
    • doi:10.1016/0141-8130(90)90044-B. PMID:2088493
    • Castiglione-Morelli, A., Scopa, A., Tamburro, A.M., and Guantieri, V. 1990. Spectroscopic studies on elastin-like synthetic polypeptides. Int. J. Biol. Macromol. 12(6): 363-368. doi:10.1016/0141-8130(90)90044-B. PMID:2088493.
    • (1990) Int. J. Biol. Macromol. , vol.12 , Issue.6 , pp. 363-368
    • Castiglione-Morelli, A.1    Scopa, A.2    Tamburro, A.M.3    Guantieri, V.4
  • 19
    • 2442522724 scopus 로고    scopus 로고
    • Short sequences of nonproline residues can adopt the polyproline II helical conformation
    • doi:10.1021/bi049922v. PMID:15134460
    • Chellgren, B.W., and Creamer, T.P. 2004. Short sequences of nonproline residues can adopt the polyproline II helical conformation. Biochemistry, 43(19): 5864-5869. doi:10.1021/bi049922v. PMID:15134460.
    • (2004) Biochemistry , vol.43 , Issue.19 , pp. 5864-5869
    • Chellgren, B.W.1    Creamer, T.P.2
  • 20
    • 63149131483 scopus 로고    scopus 로고
    • Modulation of elastin exon 26A mRNA and protein expression in human skin in vivo
    • doi:10.1111/j.1600-0625.2008.00799.x. PMID:19054052
    • Chen, Z., Shin, M.H., Moon, Y.J., Lee, S.R., Kim, Y.K., Seo, J.E., et al. 2009. Modulation of elastin exon 26A mRNA and protein expression in human skin in vivo. Exp. Dermatol. 18(4): 378-386. doi:10.1111/j.1600-0625.2008.00799.x. PMID:19054052.
    • (2009) Exp. Dermatol. , vol.18 , Issue.4 , pp. 378-386
    • Chen, Z.1    Shin, M.H.2    Moon, Y.J.3    Lee, S.R.4    Kim, Y.K.5    Seo, J.E.6
  • 21
    • 33751009077 scopus 로고    scopus 로고
    • Sequences and domain structures of mammalian, avian, amphibian and teleost tropoelastins: Clues to the evolutionary history of elastins
    • doi:10.1016/j.matbio.2006.08.258. PMID:16982180
    • Chung, M.I., Miao, M., Stahl, R.J., Chan, E., Parkinson, J., and Keeley, F.W. 2006. Sequences and domain structures of mammalian, avian, amphibian and teleost tropoelastins: Clues to the evolutionary history of elastins. Matrix Biol. 25(8): 492-504. doi:10.1016/j.matbio.2006.08.258. PMID:16982180.
    • (2006) Matrix Biol. , vol.25 , Issue.8 , pp. 492-504
    • Chung, M.I.1    Miao, M.2    Stahl, R.J.3    Chan, E.4    Parkinson, J.5    Keeley, F.W.6
  • 22
    • 0022428435 scopus 로고
    • Structure of the 3' portion of the bovine elastin gene
    • doi:10.1021/bi00334a001. PMID:2992576
    • Cicila, G., May, M., Ornstein-Goldstein, N., Indik, Z., Morrow, S.D., Yeh, H.S., et al. 1985. Structure of the 3' portion of the bovine elastin gene. Biochemistry, 24(13): 3075-3080. doi:10.1021/bi00334a001. PMID:2992576.
    • (1985) Biochemistry , vol.24 , Issue.13 , pp. 3075-3080
    • Cicila, G.1    May, M.2    Ornstein-Goldstein, N.3    Indik, Z.4    Morrow, S.D.5    Yeh, H.S.6
  • 23
    • 56749130152 scopus 로고    scopus 로고
    • Fibrillins, fibulins, and matrix-associated glycoprotein modulate the kinetics and morphology of in vitro self-assembly of a recombinant elastin-like polypeptide
    • doi:10.1021/bi8005384. PMID:18973305
    • Cirulis, J.T., Bellingham, C.M., Davis, E.C., Hubmacher, D., Reinhardt, D.P., Mecham, R.P., and Keeley, F.W. 2008. Fibrillins, fibulins, and matrix-associated glycoprotein modulate the kinetics and morphology of in vitro self-assembly of a recombinant elastin-like polypeptide. Biochemistry, 47(47): 12601-12613. doi:10.1021/bi8005384. PMID:18973305.
    • (2008) Biochemistry , vol.47 , Issue.47 , pp. 12601-12613
    • Cirulis, J.T.1    Bellingham, C.M.2    Davis, E.C.3    Hubmacher, D.4    Reinhardt, D.P.5    Mecham, R.P.6    Keeley, F.W.7
  • 24
    • 33747510080 scopus 로고    scopus 로고
    • Tropoelastin massively associates during coacervation to form quantized protein spheres
    • doi:10.1021/bi0610092. PMID:16906757
    • Clarke, A.W., Arnspang, E.C., Mithieux, S.M., Korkmaz, E., Braet, F., and Weiss, A.S. 2006. Tropoelastin massively associates during coacervation to form quantized protein spheres. Biochemistry, 45(33): 9989-9996. doi:10.1021/bi0610092. PMID:16906757.
    • (2006) Biochemistry , vol.45 , Issue.33 , pp. 9989-9996
    • Clarke, A.W.1    Arnspang, E.C.2    Mithieux, S.M.3    Korkmaz, E.4    Braet, F.5    Weiss, A.S.6
  • 26
    • 0021868803 scopus 로고
    • Crystal structure and conformation of the cyclic tetramer of a repeat tripeptide of elastin, cyclo(L-valyl-L-prolylglycyl)4
    • PMID:4019029
    • Cook, W.J., Trapane, T.L., and Prasad, K.U. 1985. Crystal structure and conformation of the cyclic tetramer of a repeat tripeptide of elastin, cyclo(L-valyl-L-prolylglycyl)4. Int. J. Pept. Protein Res. 25(5): 481-486. PMID:4019029.
    • (1985) Int. J. Pept. Protein Res. , vol.25 , Issue.5 , pp. 481-486
    • Cook, W.J.1    Trapane, T.L.2    Prasad, K.U.3
  • 27
    • 0015967414 scopus 로고
    • Communication: Coacervation of tropoelastin results in fiber formation
    • PMID:4359779
    • Cox, B.A., Starcher, B.C., and Urry, D.W. 1974. Communication: Coacervation of tropoelastin results in fiber formation. J. Biol. Chem. 249(3): 997-998. PMID:4359779.
    • (1974) J. Biol. Chem. , vol.249 , Issue.3 , pp. 997-998
    • Cox, B.A.1    Starcher, B.C.2    Urry, D.W.3
  • 28
    • 0034988430 scopus 로고    scopus 로고
    • Comparison of five procedures for the purification of insoluble elastin
    • doi:10.1016/S0142-9612(00)00383-5. PMID:11426877
    • Daamen, W.F., Hafmans, T., Veerkamp, J.H., and Van Kuppevelt, T.H. 2001. Comparison of five procedures for the purification of insoluble elastin. Biomaterials, 22(14): 1997-2005. doi:10.1016/S0142-9612(00)00383-5. PMID:11426877.
    • (2001) Biomaterials , vol.22 , Issue.14 , pp. 1997-2005
    • Daamen, W.F.1    Hafmans, T.2    Veerkamp, J.H.3    Van Kuppevelt, T.H.4
  • 29
    • 0001676342 scopus 로고
    • Optical spectroscopic determination of bovine tropoelastin molecular model
    • doi:10.1016/0022-2860(95)08653-D
    • Debelle, L., and Alix, A.J. 1995. Optical spectroscopic determination of bovine tropoelastin molecular model. J. Mol. Struct. 348:321-324. doi:10.1016/0022-2860(95)08653-D.
    • (1995) J. Mol. Struct. , vol.348 , pp. 321-324
    • Debelle, L.1    Alix, A.J.2
  • 30
    • 0032751580 scopus 로고    scopus 로고
    • The structures of elastins and their function
    • doi:10.1016/S0300-9084(99)00221-7. PMID:10575352
    • Debelle, L., and Alix, A.J. 1999. The structures of elastins and their function. Biochimie, 81(10): 981-994. doi:10.1016/S0300-9084(99)00221-7. PMID:10575352.
    • (1999) Biochimie , vol.81 , Issue.10 , pp. 981-994
    • Debelle, L.1    Alix, A.J.2
  • 31
    • 0033006918 scopus 로고    scopus 로고
    • Elastin: Molecular description and function
    • doi:10.1016/S1357-2725(98)00098-3. PMID:10216959
    • Debelle, L., and Tamburro, A.M. 1999. Elastin: molecular description and function. Int. J. Biochem. Cell Biol. 31(2): 261-272. doi:10.1016/S1357-2725(98) 00098-3. PMID:10216959.
    • (1999) Int. J. Biochem. Cell Biol. , vol.31 , Issue.2 , pp. 261-272
    • Debelle, L.1    Tamburro, A.M.2
  • 32
    • 0026690128 scopus 로고
    • Predictions of the secondary structure and antigenicity of human and bovine tropoelastins
    • doi:10.1007/BF00188344. PMID:1282881
    • Debelle, L., Wei, S.M., Jacob, M.P., Hornebeck, W., and Alix, A.J. 1992. Predictions of the secondary structure and antigenicity of human and bovine tropoelastins. Eur. Biophys. J. 21(5): 321-329. doi:10.1007/BF00188344. PMID:1282881.
    • (1992) Eur. Biophys. J. , vol.21 , Issue.5 , pp. 321-329
    • Debelle, L.1    Wei, S.M.2    Jacob, M.P.3    Hornebeck, W.4    Alix, A.J.5
  • 33
    • 0028874868 scopus 로고
    • Bovine elastin and kappaelastin secondary structure determination by optical spectroscopies
    • doi:10.1074/jbc.270.44.26099. PMID:7592811
    • Debelle, L., Alix, A.J., Jacob, M.P., Huvenne, J.P., Berjot, M., Sombret, B., and Legrand, P. 1995. Bovine elastin and kappaelastin secondary structure determination by optical spectroscopies. J. Biol. Chem. 270(44): 26099-26103. doi:10.1074/jbc.270.44.26099. PMID:7592811.
    • (1995) J. Biol. Chem. , vol.270 , Issue.44 , pp. 26099-26103
    • Debelle, L.1    Alix, A.J.2    Jacob, M.P.3    Huvenne, J.P.4    Berjot, M.5    Sombret, B.6    Legrand, P.7
  • 34
    • 0032401649 scopus 로고    scopus 로고
    • The secondary structure and architecture of human elastin
    • doi:10.1046/j.1432-1327.1998.2580533.x. PMID:9874220
    • Debelle, L., Alix, A.J., Wei, S.M., Jacob, M.P., Huvenne, J.P., Berjot, M., and Legrand, P. 1998. The secondary structure and architecture of human elastin. Eur. J. Biochem. 258(2): 533-539. doi:10.1046/j.1432-1327.1998.2580533. x. PMID:9874220.
    • (1998) Eur. J. Biochem. , vol.258 , Issue.2 , pp. 533-539
    • Debelle, L.1    Alix, A.J.2    Wei, S.M.3    Jacob, M.P.4    Huvenne, J.P.5    Berjot, M.6    Legrand, P.7
  • 35
    • 41949108642 scopus 로고    scopus 로고
    • Amyloidlike fibrils in elastin-related polypeptides: Structural characterization and elastic properties
    • doi:10.1021/bm7010104. PMID:18257556
    • del Mercato, L.L., Maruccio, G., Pompa, P.P., Bochicchio, B., Tamburro, A.M., Cingolani, R., and Rinaldi, R. 2008. Amyloidlike fibrils in elastin-related polypeptides: structural characterization and elastic properties. Biomacromolecules, 9(3): 796-803. doi:10.1021/bm7010104. PMID:18257556.
    • (2008) Biomacromolecules , vol.9 , Issue.3 , pp. 796-803
    • Del Mercato, L.L.1    Maruccio, G.2    Pompa, P.P.3    Bochicchio, B.4    Tamburro, A.M.5    Cingolani, R.6    Rinaldi, R.7
  • 36
    • 62749172818 scopus 로고    scopus 로고
    • Insights into a putative hinge region in elastin using molecular dynamics simulations
    • doi:10.1016/j.matbio.2008.12.001. PMID:19135150
    • Djajamuliadi, J., Kagawa, T.F., Ohgo, K., and Kumashiro, K.K. 2009. Insights into a putative hinge region in elastin using molecular dynamics simulations. Matrix Biol. 28(2): 92-100. doi:10.1016/j.matbio.2008.12.001. PMID:19135150.
    • (2009) Matrix Biol. , vol.28 , Issue.2 , pp. 92-100
    • Djajamuliadi, J.1    Kagawa, T.F.2    Ohgo, K.3    Kumashiro, K.K.4
  • 37
    • 0017392275 scopus 로고
    • Elastin as a rubber
    • doi:10.1002/bip.1977.360160604. PMID:880350
    • Dorrington, K.L., and McCrum, N.G. 1977. Elastin as a rubber. Biopolymers, 16(6): 1201-1222. doi:10.1002/bip.1977.360160604. PMID:880350.
    • (1977) Biopolymers , vol.16 , Issue.6 , pp. 1201-1222
    • Dorrington, K.L.1    McCrum, N.G.2
  • 38
    • 33846627696 scopus 로고    scopus 로고
    • Domains 17-27 of tropoelastin contain key regions of contact for coacervation and contain an unusual turncontaining crosslinking domain
    • doi:10.1016/j.matbio.2006.10.002. PMID:17129717
    • Dyksterhuis, L.B., Baldock, C., Lammie, D., Wess, T.J., and Weiss, A.S. 2007. Domains 17-27 of tropoelastin contain key regions of contact for coacervation and contain an unusual turncontaining crosslinking domain. Matrix Biol. 26(2): 125-135. doi:10.1016/j.matbio.2006.10.002. PMID:17129717.
    • (2007) Matrix Biol. , vol.26 , Issue.2 , pp. 125-135
    • Dyksterhuis, L.B.1    Baldock, C.2    Lammie, D.3    Wess, T.J.4    Weiss, A.S.5
  • 39
    • 67649804607 scopus 로고    scopus 로고
    • Tropoelastin as a thermodynamically unfolded premolten globule protein: The effect of trimethylamine N-oxide on structure and coacervation
    • doi:10.1016/j.abb.2009.06.001. PMID:19501564
    • Dyksterhuis, L.B., Carter, E.A., Mithieux, S.M., and Weiss, A.S. 2009. Tropoelastin as a thermodynamically unfolded premolten globule protein: The effect of trimethylamine N-oxide on structure and coacervation. Arch. Biochem. Biophys. 487(2): 79-84. doi:10.1016/j.abb.2009.06.001. PMID:19501564.
    • (2009) Arch. Biochem. Biophys. , vol.487 , Issue.2 , pp. 79-84
    • Dyksterhuis, L.B.1    Carter, E.A.2    Mithieux, S.M.3    Weiss, A.S.4
  • 40
    • 33846444691 scopus 로고    scopus 로고
    • Transformation of amyloid-like fibers, formed from an elastin-based biopolymer, into a hydrogel: An X-ray photoelectron spectroscopy and atomic force microscopy study
    • doi:10.1021/bm060764s. PMID:17206798
    • Flamia, R., Salvi, A.M., D'Alessio, L., Castle, J.E., and Tamburro, A.M. 2007. Transformation of amyloid-like fibers, formed from an elastin-based biopolymer, into a hydrogel: an X-ray photoelectron spectroscopy and atomic force microscopy study. Biomacromolecules, 8(1): 128-138. doi:10.1021/bm060764s. PMID:17206798.
    • (2007) Biomacromolecules , vol.8 , Issue.1 , pp. 128-138
    • Flamia, R.1    Salvi, A.M.2    D'Alessio, L.3    Castle, J.E.4    Tamburro, A.M.5
  • 41
    • 2642542700 scopus 로고    scopus 로고
    • Structural characterization of VGVAPG, an elastin-derived peptide
    • doi:10.1002/bip.20029. PMID:15148686
    • Floquet, N., Héry-Huynh, S., Dauchez, M., Derreumaux, P., Tamburro, A.M., and Alix, A.J. 2004. Structural characterization of VGVAPG, an elastin-derived peptide. Biopolymers, 76(3): 266-280. doi:10.1002/bip.20029. PMID:15148686.
    • (2004) Biopolymers , vol.76 , Issue.3 , pp. 266-280
    • Floquet, N.1    Héry-Huynh, S.2    Dauchez, M.3    Derreumaux, P.4    Tamburro, A.M.5    Alix, A.J.6
  • 42
    • 20744434889 scopus 로고    scopus 로고
    • Structure and modeling studies of the carboxy-terminus region of human tropoelastin
    • doi:10.1016/j.matbio.2005.03.002. PMID:15961300
    • Floquet, N., Pepe, A., Dauchez, M., Bochicchio, B., Tamburro, A.M., and Alix, A.J. 2005. Structure and modeling studies of the carboxy-terminus region of human tropoelastin. Matrix Biol. 24(4): 271-282. doi:10.1016/j.matbio.2005. 03.002. PMID:15961300.
    • (2005) Matrix Biol. , vol.24 , Issue.4 , pp. 271-282
    • Floquet, N.1    Pepe, A.2    Dauchez, M.3    Bochicchio, B.4    Tamburro, A.M.5    Alix, A.J.6
  • 43
    • 0020327009 scopus 로고
    • Contribution of cryotechniques to the study of elastin ultrastructure
    • PMID:7069796
    • Fornieri, C., Ronchetti, I.P., Edman, A.C., and Sjöström, M. 1982. Contribution of cryotechniques to the study of elastin ultrastructure. J. Microsc. 126(Pt 1): 87-93. PMID:7069796.
    • (1982) J. Microsc. , vol.126 , Issue.PART 1 , pp. 87-93
    • Fornieri, C.1    Ronchetti, I.P.2    Edman, A.C.3    Sjöström, M.4
  • 44
    • 0015935408 scopus 로고
    • Isolation and amino acid sequences of tropoelastin peptides
    • PMID:4697396
    • Foster, J.A., Bruenger, E., Gray, W.R., and Sandberg, L.B. 1973. Isolation and amino acid sequences of tropoelastin peptides. J. Biol. Chem. 248(8): 2876-2879. PMID:4697396.
    • (1973) J. Biol. Chem. , vol.248 , Issue.8 , pp. 2876-2879
    • Foster, J.A.1    Bruenger, E.2    Gray, W.R.3    Sandberg, L.B.4
  • 45
    • 0017161281 scopus 로고
    • Circular dichroism studies of an elastin crosslinked peptide
    • doi:10.1002/bip.1976.360150503. PMID:1260106
    • Foster, J.A., Bruenger, E., Rubin, L., Imberman, M., Kagan, H., Mecham, R., and Franzblau, C. 1976. Circular dichroism studies of an elastin crosslinked peptide. Biopolymers, 15(5): 833-841. doi:10.1002/bip.1976.360150503. PMID:1260106.
    • (1976) Biopolymers , vol.15 , Issue.5 , pp. 833-841
    • Foster, J.A.1    Bruenger, E.2    Rubin, L.3    Imberman, M.4    Kagan, H.5    Mecham, R.6    Franzblau, C.7
  • 46
    • 0016630191 scopus 로고
    • Raman scattering of collagen, gelatin, and elastin
    • doi:10.1002/bip.1975.360140211. PMID:1174668
    • Frushour, B.G., and Koenig, J.L. 1975. Raman scattering of collagen, gelatin, and elastin. Biopolymers, 14(2): 379-391. doi:10.1002/bip.1975. 360140211. PMID:1174668.
    • (1975) Biopolymers , vol.14 , Issue.2 , pp. 379-391
    • Frushour, B.G.1    Koenig, J.L.2
  • 47
    • 14644423319 scopus 로고    scopus 로고
    • Heparan sulphate interacts with tropoelastin, with some tropoelastin peptides and is present in human dermis elastic fibers
    • PMID:15748998
    • Gheduzzi, D., Guerra, D., Bochicchio, B., Pepe, A., Tamburro, A.M., Quaglino, D., et al. 2005. Heparan sulphate interacts with tropoelastin, with some tropoelastin peptides and is present in human dermis elastic fibers. Matrix Biol. 24(1): 15-25. PMID:15748998.
    • (2005) Matrix Biol. , vol.24 , Issue.1 , pp. 15-25
    • Gheduzzi, D.1    Guerra, D.2    Bochicchio, B.3    Pepe, A.4    Tamburro, A.M.5    Quaglino, D.6
  • 48
    • 0017849526 scopus 로고
    • Hydrophobic interaction and a model for the elasticity of elastin
    • doi:10.1002/bip.1978.360170311. PMID:638230
    • Gosline, J.M. 1978a. Hydrophobic interaction and a model for the elasticity of elastin. Biopolymers, 17(3): 677-695. doi:10.1002/bip.1978. 360170311. PMID:638230.
    • (1978) Biopolymers , vol.17 , Issue.3 , pp. 677-695
    • Gosline, J.M.1
  • 49
    • 0017818044 scopus 로고
    • The temperature-dependent swelling of elastin
    • doi:10.1002/bip.1978.360170312. PMID:638231
    • Gosline, J.M. 1978b. The temperature-dependent swelling of elastin. Biopolymers, 17(3): 697-707. doi:10.1002/bip.1978.360170312. PMID:638231.
    • (1978) Biopolymers , vol.17 , Issue.3 , pp. 697-707
    • Gosline, J.M.1
  • 50
    • 0016718521 scopus 로고
    • Reversible structural changes in a hydrophobic protein, elastin, as indicated by fluorescence probe analysis
    • doi:10.1002/bip.1975.360140904
    • Gosline, J.M., Yew, F.F., and Weis-Fogh, T. 1975. Reversible structural changes in a hydrophobic protein, elastin, as indicated by fluorescence probe analysis. Biopolymers, 14(9): 1811-1826. doi:10.1002/bip.1975.360140904.
    • (1975) Biopolymers , vol.14 , Issue.9 , pp. 1811-1826
    • Gosline, J.M.1    Yew, F.F.2    Weis-Fogh, T.3
  • 51
    • 0002293396 scopus 로고
    • Scanning electron microscope observations on elastin
    • doi:10.3109/03008207209152057
    • Gotte, L., Mammi, M., and Pezzin, G. 1972. Scanning electron microscope observations on elastin. Connect. Tissue Res. 1(1): 61-67. doi:10.3109/ 03008207209152057.
    • (1972) Connect. Tissue Res. , vol.1 , Issue.1 , pp. 61-67
    • Gotte, L.1    Mammi, M.2    Pezzin, G.3
  • 52
    • 0015987463 scopus 로고
    • The ultrastructural organization of elastin
    • doi:10.1016/S0022-5320(74)80019-5. PMID:4813268
    • Gotte, L., Giro, M.G., Volpin, D., and Horne, R.W. 1974. The ultrastructural organization of elastin. J. Ultrastruct. Res. 46(1): 23-33. doi:10.1016/S0022-5320(74)80019-5. PMID:4813268.
    • (1974) J. Ultrastruct. Res. , vol.46 , Issue.1 , pp. 23-33
    • Gotte, L.1    Giro, M.G.2    Volpin, D.3    Horne, R.W.4
  • 53
    • 0011333288 scopus 로고
    • Electron microscopy and optical diffraction of elastin
    • Gotte, L., Volpin, D., Horne, R.W., and Mammi, M. 1976. Electron microscopy and optical diffraction of elastin. Micron, 7: 95-102.
    • (1976) Micron , vol.7 , pp. 95-102
    • Gotte, L.1    Volpin, D.2    Horne, R.W.3    Mammi, M.4
  • 54
    • 0015932437 scopus 로고
    • Molecular model for elastin structure and function
    • doi:10.1038/246461a0. PMID:4762195
    • Gray, W.R., Sandberg, L.B., and Foster, J.A. 1973. Molecular model for elastin structure and function. Nature, 246(5434): 461-466. doi:10.1038/ 246461a0. PMID:4762195.
    • (1973) Nature , vol.246 , Issue.5434 , pp. 461-466
    • Gray, W.R.1    Sandberg, L.B.2    Foster, J.A.3
  • 55
    • 35348904595 scopus 로고    scopus 로고
    • Comparative genomics of elastin: Sequence analysis of a highly repetitive protein
    • doi:10.1016/j.matbio.2007.05.005. PMID:17628459
    • He, D., Chung, M., Chan, E., Alleyne, T., Ha, K.C., Miao, M., et al. 2007. Comparative genomics of elastin: Sequence analysis of a highly repetitive protein. Matrix Biol. 26(7): 524-540. doi:10.1016/j.matbio.2007.05.005. PMID:17628459.
    • (2007) Matrix Biol. , vol.26 , Issue.7 , pp. 524-540
    • He, D.1    Chung, M.2    Chan, E.3    Alleyne, T.4    Ha, K.C.5    Miao, M.6
  • 56
    • 0016168148 scopus 로고
    • The elastic properties of elastin
    • doi:10.1002/bip.1974.360130404. PMID:4847581
    • Hoeve, C.A., and Flory, P.J. 1974. The elastic properties of elastin. Biopolymers, 13(4): 677-686. doi:10.1002/bip.1974.360130404. PMID:4847581.
    • (1974) Biopolymers , vol.13 , Issue.4 , pp. 677-686
    • Hoeve, C.A.1    Flory, P.J.2
  • 57
    • 0000263731 scopus 로고
    • Alternative splicing of human elastin mRNA indicated by sequence analysis of cloned genomic and complementary DNA
    • doi:10.1073/pnas.84.16.5680. PMID:3039501
    • Indik, Z., Yeh, H., Ornstein-Goldstein, N., Sheppard, P., Anderson, N., Rosenbloom, J.C., et al. 1987a. Alternative splicing of human elastin mRNA indicated by sequence analysis of cloned genomic and complementary DNA. Proc. Natl. Acad. Sci. U.S.A. 84(16): 5680-5684. doi:10.1073/pnas.84.16.5680. PMID:3039501.
    • (1987) Proc. Natl. Acad. Sci. U.S.A. , vol.84 , Issue.16 , pp. 5680-5684
    • Indik, Z.1    Yeh, H.2    Ornstein-Goldstein, N.3    Sheppard, P.4    Anderson, N.5    Rosenbloom, J.C.6
  • 58
    • 0023062132 scopus 로고
    • Structure of the 3′ region of the human elastin gene: Great abundance of Alu repetitive sequences and few coding sequences
    • doi:10.3109/03008208709006976. PMID:3038460
    • Indik, Z., Yoon, K., Morrow, S.D., Cicila, G., Rosenbloom, J., Rosenbloom, J., and Ornstein-Goldstein, N. 1987b. Structure of the 3′ region of the human elastin gene: great abundance of Alu repetitive sequences and few coding sequences. Connect. Tissue Res. 16(3): 197-211. doi:10.3109/03008208709006976. PMID:3038460.
    • (1987) Connect. Tissue Res. , vol.16 , Issue.3 , pp. 197-211
    • Indik, Z.1    Yoon, K.2    Morrow, S.D.3    Cicila, G.4    Rosenbloom, J.5    Rosenbloom, J.6    Ornstein-Goldstein, N.7
  • 59
    • 0025322996 scopus 로고
    • Production of recombinant human tropoelastin: Characterization and demonstration of immunologic and chemotactic activity
    • doi:10.1016/0003-9861(90)90521-Y. PMID:2191629
    • Indik, Z., Abrams, W.R., Kucich, U., Gibson, C.W., Mecham, R.P., and Rosenbloom, J. 1990. Production of recombinant human tropoelastin: characterization and demonstration of immunologic and chemotactic activity. Arch. Biochem. Biophys. 280(1): 80-86. doi:10.1016/0003-9861(90)90521-Y. PMID:2191629.
    • (1990) Arch. Biochem. Biophys. , vol.280 , Issue.1 , pp. 80-86
    • Indik, Z.1    Abrams, W.R.2    Kucich, U.3    Gibson, C.W.4    Mecham, R.P.5    Rosenbloom, J.6
  • 60
    • 0034665987 scopus 로고    scopus 로고
    • Domain 26 of tropoelastin plays a dominant role in association by coacervation
    • doi:10.1074/jbc.M004265200. PMID:10862774
    • Jensen, S.A., Vrhovski, B., and Weiss, A.S. 2000. Domain 26 of tropoelastin plays a dominant role in association by coacervation. J. Biol. Chem. 275(37): 28449-28454. doi:10.1074/jbc.M004265200. PMID:10862774.
    • (2000) J. Biol. Chem. , vol.275 , Issue.37 , pp. 28449-28454
    • Jensen, S.A.1    Vrhovski, B.2    Weiss, A.S.3
  • 61
    • 0020018910 scopus 로고
    • Lysyl oxidase: Preparation and role in elastin biosynthesis
    • doi:10.1016/0076-6879(82)82092-2. PMID:6123066
    • Kagan, H.M., and Sullivan, K.A. 1982. Lysyl oxidase: preparation and role in elastin biosynthesis. Methods Enzymol. 82(Pt A): 637-650. doi:10.1016/0076-6879(82)82092-2. PMID:6123066.
    • (1982) Methods Enzymol. , vol.82 , Issue.PART A , pp. 637-650
    • Kagan, H.M.1    Sullivan, K.A.2
  • 62
    • 0003266746 scopus 로고
    • The glass point of elastin
    • doi:10.1073/pnas.72.9.3505. PMID:1059138
    • Kakivaya, S.R., and Hoeve, C.A. 1975. The glass point of elastin. Proc. Natl. Acad. Sci. U.S.A. 72(9): 3505-3507. doi:10.1073/pnas.72.9.3505. PMID:1059138.
    • (1975) Proc. Natl. Acad. Sci. U.S.A. , vol.72 , Issue.9 , pp. 3505-3507
    • Kakivaya, S.R.1    Hoeve, C.A.2
  • 63
    • 0037705394 scopus 로고    scopus 로고
    • Domains in tropoelastin that mediate elastin deposition in vitro and in vivo
    • doi:10.1074/jbc.M212715200. PMID:12626514
    • Kozel, B.A., Wachi, H., Davis, E.C., and Mecham, R.P. 2003. Domains in tropoelastin that mediate elastin deposition in vitro and in vivo. J. Biol. Chem. 278(20): 18491-18498. doi:10.1074/jbc.M212715200. PMID:12626514.
    • (2003) J. Biol. Chem. , vol.278 , Issue.20 , pp. 18491-18498
    • Kozel, B.A.1    Wachi, H.2    Davis, E.C.3    Mecham, R.P.4
  • 64
    • 0141891811 scopus 로고    scopus 로고
    • 13C CPMAS NMR studies of the elastin-like polypeptide (LGGVG)n
    • doi:10.1002/bip.10470. PMID:14517910
    • Kumashiro, K.K., Kurano, T.L., Niemczura, W.P., Martino, M., and Tamburro, A.M. 2003. 13C CPMAS NMR studies of the elastin-like polypeptide (LGGVG)n. Biopolymers, 70(2): 221-226. doi:10.1002/bip.10470. PMID:14517910.
    • (2003) Biopolymers , vol.70 , Issue.2 , pp. 221-226
    • Kumashiro, K.K.1    Kurano, T.L.2    Niemczura, W.P.3    Martino, M.4    Tamburro, A.M.5
  • 65
    • 33747704224 scopus 로고    scopus 로고
    • Cooperativity between the hydrophobic and cross-linking domains of elastin
    • doi:10.1074/jbc.M510833200. PMID:16777851
    • Kumashiro, K.K., Ho, J.P., Niemczura, W.P., and Keeley, F.W. 2006. Cooperativity between the hydrophobic and cross-linking domains of elastin. J. Biol. Chem. 281(33): 23757-23765. doi:10.1074/jbc.M510833200. PMID:16777851.
    • (2006) J. Biol. Chem. , vol.281 , Issue.33 , pp. 23757-23765
    • Kumashiro, K.K.1    Ho, J.P.2    Niemczura, W.P.3    Keeley, F.W.4
  • 66
    • 52049125449 scopus 로고    scopus 로고
    • Structural insights into the elastin mimetic (LGGVG)6 using solid-state 13C NMR experiments and statistical analysis of the PDB
    • doi:10.1002/bip.20984. PMID:18335424
    • Kumashiro, K.K., Ohgo, K., Niemczura, W.P., Onizuka, A.K., and Asakura, T. 2008. Structural insights into the elastin mimetic (LGGVG)6 using solid-state 13C NMR experiments and statistical analysis of the PDB. Biopolymers, 89(8): 668-679. doi:10.1002/bip.20984. PMID:18335424.
    • (2008) Biopolymers , vol.89 , Issue.8 , pp. 668-679
    • Kumashiro, K.K.1    Ohgo, K.2    Niemczura, W.P.3    Onizuka, A.K.4    Asakura, T.5
  • 67
    • 2642579315 scopus 로고    scopus 로고
    • AMID: Autonomous modeler of intragenic duplication
    • PMID:15130804
    • Kummerfeld, S.K., Weiss, A.S., Fekete, A., and Jermiin, L.S. 2003. AMID: autonomous modeler of intragenic duplication. Appl. Bioinformatics, 2(3): 169-176. PMID:15130804.
    • (2003) Appl. Bioinformatics , vol.2 , Issue.3 , pp. 169-176
    • Kummerfeld, S.K.1    Weiss, A.S.2    Fekete, A.3    Jermiin, L.S.4
  • 68
    • 0037569589 scopus 로고    scopus 로고
    • Molecular basis for the extensibility of elastin
    • doi:10.1023/A:1023474909980. PMID:12785105
    • Li, B., and Daggett, V. 2002. Molecular basis for the extensibility of elastin. J. Muscle Res. Cell Motil. 23(5-6): 561-573. doi:10.1023/A: 1023474909980. PMID:12785105.
    • (2002) J. Muscle Res. Cell Motil. , vol.23 , Issue.5-6 , pp. 561-573
    • Li, B.1    Daggett, V.2
  • 69
    • 0035910282 scopus 로고    scopus 로고
    • The molecular basis for the inverse temperature transition of elastin
    • doi:10.1006/jmbi.2000.4306. PMID:11152614
    • Li, B., Alonso, D.O.V., and Daggett, V. 2001. The molecular basis for the inverse temperature transition of elastin. J. Mol. Biol. 305(3): 581-592. doi:10.1006/jmbi.2000.4306. PMID:11152614.
    • (2001) J. Mol. Biol. , vol.305 , Issue.3 , pp. 581-592
    • Li, B.1    Alonso, D.O.V.2    Daggett, V.3
  • 70
    • 0242458482 scopus 로고    scopus 로고
    • Protein disorder prediction: Implications for structural proteomics
    • [see comment.] doi:10.1016/j.str.2003.10.002. PMID:14604535
    • Linding, R., Jensen, L.J., Diella, F., Bork, P., Gibson, T.J., and Russell, R.B. 2003a. Protein disorder prediction: implications for structural proteomics. Structure, 11(11): 1453-1459 . [see comment.] doi:10.1016/j.str. 2003.10.002. PMID:14604535.
    • (2003) Structure , vol.11 , Issue.11 , pp. 1453-1459
    • Linding, R.1    Jensen, L.J.2    Diella, F.3    Bork, P.4    Gibson, T.J.5    Russell, R.B.6
  • 71
    • 0042622240 scopus 로고    scopus 로고
    • GlobPlot: Exploring protein sequences for globularity and disorder
    • doi:10.1093/nar/gkg519. PMID:12824398
    • Linding, R., Russell, R.B., Neduva, V., and Gibson, T.J. 2003b. GlobPlot: Exploring protein sequences for globularity and disorder. Nucleic Acids Res. 31(13): 3701-3708. doi:10.1093/nar/gkg519. PMID:12824398.
    • (2003) Nucleic Acids Res. , vol.31 , Issue.13 , pp. 3701-3708
    • Linding, R.1    Russell, R.B.2    Neduva, V.3    Gibson, T.J.4
  • 72
    • 0842310831 scopus 로고    scopus 로고
    • Elastic fiber homeostasis requires lysyl oxidase-like 1 protein
    • doi:10.1038/ng1297. PMID:14745449
    • Liu, X., Zhao, Y., Gao, J., Pawlyk, B., Starcher, B., Spencer, J.A., et al. 2004. Elastic fiber homeostasis requires lysyl oxidase-like 1 protein. Nat. Genet. 36(2): 178-182. doi:10.1038/ng1297. PMID:14745449.
    • (2004) Nat. Genet. , vol.36 , Issue.2 , pp. 178-182
    • Liu, X.1    Zhao, Y.2    Gao, J.3    Pawlyk, B.4    Starcher, B.5    Spencer, J.A.6
  • 73
    • 0000754558 scopus 로고
    • The determination of collagen and elsatin in tissues, with results obtained in various normal tissues from different species
    • Lowry, O.H., Gilligan, D.R., and Katersky, E.M. 1941. The determination of collagen and elsatin in tissues, with results obtained in various normal tissues from different species. J. Biol. Chem. 139: 795-804.
    • (1941) J. Biol. Chem. , vol.139 , pp. 795-804
    • Lowry, O.H.1    Gilligan, D.R.2    Katersky, E.M.3
  • 74
    • 0016724586 scopus 로고
    • Molecular mobility and structure of elastin deduced from the solvent and temperature dependence of 13C magnetic resonance relaxation data
    • doi:10.1021/bi00694a024. PMID:1191633
    • Lyerla, J.R., Jr., and Torchia, D.A. 1975. Molecular mobility and structure of elastin deduced from the solvent and temperature dependence of 13C magnetic resonance relaxation data. Biochemistry, 14(23): 5175-5183. doi:10.1021/bi00694a024. PMID:1191633.
    • (1975) Biochemistry , vol.14 , Issue.23 , pp. 5175-5183
    • Lyerla Jr., J.R.1    Torchia, D.A.2
  • 75
    • 18144374871 scopus 로고    scopus 로고
    • The hydrophobic domain 26 of human tropoelastin is unstructured in solution
    • doi:10.1016/j.jsb.2005.02.005. PMID:15866738
    • Mackay, J.P., Muiznieks, L.D., Toonkool, P., and Weiss, A.S. 2005. The hydrophobic domain 26 of human tropoelastin is unstructured in solution. J. Struct. Biol. 150(2): 154-162. doi:10.1016/j.jsb.2005.02.005. PMID:15866738.
    • (2005) J. Struct. Biol. , vol.150 , Issue.2 , pp. 154-162
    • Mackay, J.P.1    Muiznieks, L.D.2    Toonkool, P.3    Weiss, A.S.4
  • 76
    • 0014431328 scopus 로고
    • Evidence for order in the structure of alpha-elastin
    • doi:10.1038/220371b0. PMID:5684878
    • Mammi, M., Gotte, L., and Pezzin, G. 1968. Evidence for order in the structure of alpha-elastin. Nature, 220(5165): 371-373. doi:10.1038/220371b0. PMID:5684878.
    • (1968) Nature , vol.220 , Issue.5165 , pp. 371-373
    • Mammi, M.1    Gotte, L.2    Pezzin, G.3
  • 77
    • 0014960152 scopus 로고
    • Comparison of soluble and native elastin conformations by far-ultraviolet circular dichroism
    • doi:10.1038/225380a0. PMID:5410519
    • Mammi, M., Gotte, L., and Pezzin, G. 1970. Comparison of soluble and native elastin conformations by far-ultraviolet circular dichroism. Nature, 225(5230): 380-381. doi:10.1038/225380a0. PMID:5410519.
    • (1970) Nature , vol.225 , Issue.5230 , pp. 380-381
    • Mammi, M.1    Gotte, L.2    Pezzin, G.3
  • 78
    • 0028945002 scopus 로고
    • Total synthesis and expression in Escherichia coli of a gene encoding human tropoelastin
    • doi:10.1016/0378-1119(94) 00848-M. PMID:7890158
    • Martin, S.L., Vrhovski, B., and Weiss, A.S. 1995. Total synthesis and expression in Escherichia coli of a gene encoding human tropoelastin. Gene, 154(2): 159-166. doi:10.1016/0378-1119(94) 00848-M. PMID:7890158.
    • (1995) Gene , vol.154 , Issue.2 , pp. 159-166
    • Martin, S.L.1    Vrhovski, B.2    Weiss, A.S.3
  • 79
    • 0034728484 scopus 로고    scopus 로고
    • On the occurrence of polyproline II structure in elastin
    • doi:10.1016/S0022-2860(99)00299-9
    • Martino, M., Bavoso, A., Guantieri, V., Coviello, A., and Tamburro, A.M. 2000. On the occurrence of polyproline II structure in elastin. J. Mol. Struct. 519(1-3): 173-189. doi:10.1016/S0022-2860(99)00299-9.
    • (2000) J. Mol. Struct. , vol.519 , Issue.1-3 , pp. 173-189
    • Martino, M.1    Bavoso, A.2    Guantieri, V.3    Coviello, A.4    Tamburro, A.M.5
  • 80
    • 42649141958 scopus 로고    scopus 로고
    • Methods in elastic tissue biology: Elastin isolation and purification
    • doi:10.1016/j.ymeth.2008.01.007. PMID:18442703
    • Mecham, R.P. 2008. Methods in elastic tissue biology: elastin isolation and purification. Methods, 45(1): 32-41. doi:10.1016/j.ymeth.2008.01.007. PMID:18442703.
    • (2008) Methods , vol.45 , Issue.1 , pp. 32-41
    • Mecham, R.P.1
  • 81
    • 1542281813 scopus 로고    scopus 로고
    • Sequence and structure determinants for the self-aggregation of recombinant polypeptides modeled after human elastin
    • doi:10.1074/jbc.M308465200. PMID:14500713
    • Miao, M., Bellingham, C.M., Stahl, R.J., Sitarz, E.E., Lane, C.J., and Keeley, F.W. 2003. Sequence and structure determinants for the self-aggregation of recombinant polypeptides modeled after human elastin. J. Biol. Chem. 278(49): 48553-48562. doi:10.1074/jbc.M308465200. PMID:14500713.
    • (2003) J. Biol. Chem. , vol.278 , Issue.49 , pp. 48553-48562
    • Miao, M.1    Bellingham, C.M.2    Stahl, R.J.3    Sitarz, E.E.4    Lane, C.J.5    Keeley, F.W.6
  • 82
    • 27444442269 scopus 로고    scopus 로고
    • Structural determinants of cross-linking and hydrophobic domains for selfassembly of elastin-like polypeptides
    • doi:10.1021/bi0510173. PMID:16245953
    • Miao, M., Cirulis, J.T., Lee, S., and Keeley, F.W. 2005. Structural determinants of cross-linking and hydrophobic domains for selfassembly of elastin-like polypeptides. Biochemistry, 44(43): 14367-14375. doi:10.1021/bi0510173. PMID:16245953.
    • (2005) Biochemistry , vol.44 , Issue.43 , pp. 14367-14375
    • Miao, M.1    Cirulis, J.T.2    Lee, S.3    Keeley, F.W.4
  • 83
    • 70350397609 scopus 로고    scopus 로고
    • Characterization of an unusual tropoelastin with truncated C-terminus in the frog
    • doi:10.1016/j.matbio.2009.07.003. PMID:19638308
    • Miao, M., Stahl, R.J., Petersen, L.F., Reintsch, W.E., Davis, E.C., and Keeley, F.W. 2009. Characterization of an unusual tropoelastin with truncated C-terminus in the frog. Matrix Biol. 28(7): 432-441. doi:10.1016/j.matbio.2009. 07.003. PMID:19638308.
    • (2009) Matrix Biol. , vol.28 , Issue.7 , pp. 432-441
    • Miao, M.1    Stahl, R.J.2    Petersen, L.F.3    Reintsch, W.E.4    Davis, E.C.5    Keeley, F.W.6
  • 84
    • 17444380093 scopus 로고    scopus 로고
    • Elastin
    • doi:10.1016/S0065-3233(05)70013-9. PMID:15837523
    • Mithieux, S.M., and Weiss, A.S. 2005. Elastin. Adv. Protein Chem. 70: 437-461. doi:10.1016/S0065-3233(05)70013-9. PMID:15837523.
    • (2005) Adv. Protein Chem. , vol.70 , pp. 437-461
    • Mithieux, S.M.1    Weiss, A.S.2
  • 85
    • 33846913510 scopus 로고    scopus 로고
    • Atomic-level characterization of disordered protein ensembles
    • doi:10.1016/j.sbi.2007.01.009. PMID:17250999
    • Mittag, T., and Forman-Kay, J.D. 2007. Atomic-level characterization of disordered protein ensembles. Curr. Opin. Struct. Biol. 17(1): 3-14. doi:10.1016/j.sbi.2007.01.009. PMID:17250999.
    • (2007) Curr. Opin. Struct. Biol. , vol.17 , Issue.1 , pp. 3-14
    • Mittag, T.1    Forman-Kay, J.D.2
  • 86
    • 34447333924 scopus 로고    scopus 로고
    • Flexibility in the solution structure of human tropoelastin
    • doi:10.1021/bi700139k. PMID:17567153
    • Muiznieks, L.D., and Weiss, A.S. 2007. Flexibility in the solution structure of human tropoelastin. Biochemistry, 46(27): 8196-8205. doi:10.1021/bi700139k. PMID:17567153.
    • (2007) Biochemistry , vol.46 , Issue.27 , pp. 8196-8205
    • Muiznieks, L.D.1    Weiss, A.S.2
  • 87
    • 0037442549 scopus 로고    scopus 로고
    • Structural changes and facilitated association of tropoelastin
    • doi:10.1016/S0003-9861(02)00719-1. PMID:12573292
    • Muiznieks, L.D., Jensen, S.A., and Weiss, A.S. 2003. Structural changes and facilitated association of tropoelastin. Arch. Biochem. Biophys. 410(2): 317-323. doi:10.1016/S0003-9861(02)00719-1. PMID:12573292.
    • (2003) Arch. Biochem. Biophys. , vol.410 , Issue.2 , pp. 317-323
    • Muiznieks, L.D.1    Jensen, S.A.2    Weiss, A.S.3
  • 88
    • 1842639461 scopus 로고    scopus 로고
    • Lysyl oxidase-like and lysyl oxidase are present in the dermis and epidermis of a skin equivalent and in human skin and are associated to elastic fibers
    • doi:10.1111/j.0022-202X.2004.22330.x. PMID:15086544
    • Noblesse, E., Cenizo, V., Bouez, C., Borel, A., Gleyzal, C., Peyrol, S., et al. 2004. Lysyl oxidase-like and lysyl oxidase are present in the dermis and epidermis of a skin equivalent and in human skin and are associated to elastic fibers. J. Invest. Dermatol. 122(3): 621-630. doi:10.1111/j.0022-202X.2004. 22330.x. PMID:15086544.
    • (2004) J. Invest. Dermatol. , vol.122 , Issue.3 , pp. 621-630
    • Noblesse, E.1    Cenizo, V.2    Bouez, C.3    Borel, A.4    Gleyzal, C.5    Peyrol, S.6
  • 89
    • 33846288342 scopus 로고    scopus 로고
    • Heterogeneity in the conformation of valine in the elastin mimetic (LGGVG)6 as shown by solidstate 13C NMR SPEctroscopy
    • doi:10.1021/bm0607168. PMID:17154456
    • Ohgo, K., Niemczura, W.P., Ashida, J., Okonogi, M., Asakura, T., and Kumashiro, K.K. 2006. Heterogeneity in the conformation of valine in the elastin mimetic (LGGVG)6 as shown by solidstate 13C NMR SPEctroscopy. Biomacromolecules, 7(12): 3306-3310. doi:10.1021/bm0607168. PMID:17154456.
    • (2006) Biomacromolecules , vol.7 , Issue.12 , pp. 3306-3310
    • Ohgo, K.1    Niemczura, W.P.2    Ashida, J.3    Okonogi, M.4    Asakura, T.5    Kumashiro, K.K.6
  • 90
    • 34648850062 scopus 로고    scopus 로고
    • Molecular and supramolecular structural studies on human tropoelastin sequences
    • doi:10.1529/biophysj.107.110809. PMID:17693470
    • Ostuni, A., Bochicchio, B., Armentano, M.F., Bisaccia, F., and Tamburro, A.M. 2007. Molecular and supramolecular structural studies on human tropoelastin sequences. Biophys. J. 93(10): 3640-3651. doi:10.1529/biophysj.107.110809. PMID:17693470.
    • (2007) Biophys. J. , vol.93 , Issue.10 , pp. 3640-3651
    • Ostuni, A.1    Bochicchio, B.2    Armentano, M.F.3    Bisaccia, F.4    Tamburro, A.M.5
  • 91
    • 77049239749 scopus 로고
    • The chemistry of connective tissues. 2. Soluble proteins derived from partial hydrolysis of elastin
    • PMID:13260170
    • Partridge, S.M., Davis, H.F., and Adair, G.S. 1955. The chemistry of connective tissues. 2. Soluble proteins derived from partial hydrolysis of elastin. Biochem. J. 61(1): 11-21. PMID:13260170.
    • (1955) Biochem. J. , vol.61 , Issue.1 , pp. 11-21
    • Partridge, S.M.1    Davis, H.F.2    Adair, G.S.3
  • 92
    • 0018424687 scopus 로고
    • The ultrastructure of elastin revealed by freezefracture electron microscopy
    • Pasquali-Ronchetti, I., Fornieri, C., Baccarani-Contri, M., and Volpin, D. 1979. The ultrastructure of elastin revealed by freezefracture electron microscopy. Micron, 10: 89-99.
    • (1979) Micron , vol.10 , pp. 89-99
    • Pasquali-Ronchetti, I.1    Fornieri, C.2    Baccarani-Contri, M.3    Volpin, D.4
  • 95
    • 0017104272 scopus 로고
    • Isolation, purification, and cross-linking profiles of elastin from lung and aorta
    • doi:10.1021/bi00667a025. PMID:990252
    • Paz, M.A., Keith, D.A., Traverso, H.P., and Gallop, P.M. 1976. Isolation, purification, and cross-linking profiles of elastin from lung and aorta. Biochemistry, 15(22): 4912-4918. doi:10.1021/bi00667a025. PMID:990252.
    • (1976) Biochemistry , vol.15 , Issue.22 , pp. 4912-4918
    • Paz, M.A.1    Keith, D.A.2    Traverso, H.P.3    Gallop, P.M.4
  • 96
    • 14644431361 scopus 로고    scopus 로고
    • Dissection of human tropoelastin: Supramolecular organization of polypeptide sequences coded by particular exons
    • doi:10.1016/j.matbio.2005.01.004. PMID:15890261
    • Pepe, A., Guerra, D., Bochicchio, B., Quaglino, D., Gheduzzi, D., Pasquali Ronchetti, I., and Tamburro, A.M. 2005. Dissection of human tropoelastin: supramolecular organization of polypeptide sequences coded by particular exons. Matrix Biol. 24(2): 96-109. doi:10.1016/j.matbio.2005.01.004. PMID:15890261.
    • (2005) Matrix Biol. , vol.24 , Issue.2 , pp. 96-109
    • Pepe, A.1    Guerra, D.2    Bochicchio, B.3    Quaglino, D.4    Gheduzzi, D.5    Pasquali Ronchetti, I.6    Tamburro, A.M.7
  • 97
    • 34249829242 scopus 로고    scopus 로고
    • Supramolecular organization of elastin and elastin-related nanostructured biopolymers
    • doi:10.2217/17435889.2.2.203. PMID:17716121
    • Pepe, A., Bochicchio, B., and Tamburro, A.M. 2007. Supramolecular organization of elastin and elastin-related nanostructured biopolymers. Nanomed, 2(2): 203-218. doi:10.2217/17435889.2.2.203. PMID:17716121.
    • (2007) Nanomed , vol.2 , Issue.2 , pp. 203-218
    • Pepe, A.1    Bochicchio, B.2    Tamburro, A.M.3
  • 98
    • 0037134876 scopus 로고    scopus 로고
    • Observation of the glycines in elastin using (13)C and (15)N solid-state NMR spectroscopy and isotopic labeling
    • doi:10.1021/ja017711x. PMID:12059197
    • Perry, A., Stypa, M.P., Foster, J.A., and Kumashiro, K.K. 2002. Observation of the glycines in elastin using (13)C and (15)N solid-state NMR spectroscopy and isotopic labeling. J. Am. Chem. Soc. 124(24): 6832-6833. doi:10.1021/ja017711x. PMID:12059197.
    • (2002) J. Am. Chem. Soc. , vol.124 , Issue.24 , pp. 6832-6833
    • Perry, A.1    Stypa, M.P.2    Foster, J.A.3    Kumashiro, K.K.4
  • 99
    • 1542319866 scopus 로고    scopus 로고
    • Quantitative observation of backbone disorder in native elastin
    • doi:10.1074/jbc.M310948200. PMID:14625282
    • Pometun, M.S., Chekmenev, E.Y., and Wittebort, R.J. 2004. Quantitative observation of backbone disorder in native elastin. J. Biol. Chem. 279(9): 7982-7987. doi:10.1074/jbc.M310948200. PMID:14625282.
    • (2004) J. Biol. Chem. , vol.279 , Issue.9 , pp. 7982-7987
    • Pometun, M.S.1    Chekmenev, E.Y.2    Wittebort, R.J.3
  • 100
    • 0023353716 scopus 로고
    • Raman spectrum and structure of elastin in relation to type-II beta-turns
    • doi:10.1002/bip.360260612. PMID:3607250
    • Prescott, B., Renugopalakrishnan, V., and Thomas, G.J., Jr. 1987. Raman spectrum and structure of elastin in relation to type-II beta-turns. Biopolymers, 26(6): 934-936. doi:10.1002/bip.360260612. PMID:3607250.
    • (1987) Biopolymers , vol.26 , Issue.6 , pp. 934-936
    • Prescott, B.1    Renugopalakrishnan, V.2    Thomas Jr., G.J.3
  • 101
    • 0023664380 scopus 로고
    • Primary structures of bovine elastin a, b, and c deduced from the sequences of cDNA clones
    • PMID:3032943
    • Raju, K., and Anwar, R.A. 1987. Primary structures of bovine elastin a, b, and c deduced from the sequences of cDNA clones. J. Biol. Chem. 262(12): 5755-5762. PMID:3032943.
    • (1987) J. Biol. Chem. , vol.262 , Issue.12 , pp. 5755-5762
    • Raju, K.1    Anwar, R.A.2
  • 102
    • 77950618150 scopus 로고    scopus 로고
    • Molecular simulations of protein disorder
    • Rauscher, S., and Pomès, R. 2010. Molecular simulations of protein disorder. Biochem. Cell Biol.88: this issue.
    • (2010) Biochem. Cell Biol. , vol.88 , Issue.THIS ISSUE
    • Rauscher, S.1    Pomès, R.2
  • 103
    • 33846250450 scopus 로고    scopus 로고
    • Proline and glycine control protein self-organization into elastomeric or amyloid fibrils
    • doi:10.1016/j.str.2006.09.008. PMID:17098192
    • Rauscher, S., Baud, S., Miao, M., Keeley, F.W., and Pomès, R. 2006. Proline and glycine control protein self-organization into elastomeric or amyloid fibrils. Structure, 14(11): 1667-1676. doi:10.1016/j.str.2006.09.008. PMID:17098192.
    • (2006) Structure , vol.14 , Issue.11 , pp. 1667-1676
    • Rauscher, S.1    Baud, S.2    Miao, M.3    Keeley, F.W.4    Pomès, R.5
  • 105
    • 0027422979 scopus 로고
    • Extracellular matrix 4: The elastic fiber
    • PMID:8405806
    • Rosenbloom, J., Abrams, W.R., and Mecham, R. 1993. Extracellular matrix 4: the elastic fiber. FASEB J. 7(13): 1208-1218. PMID:8405806.
    • (1993) FASEB J. , vol.7 , Issue.13 , pp. 1208-1218
    • Rosenbloom, J.1    Abrams, W.R.2    Mecham, R.3
  • 106
    • 0014465980 scopus 로고
    • The elastic fiber. I. The separation and partial characterization of its macromolecular components
    • doi:10.1083/jcb.40.2.366. PMID:5812469
    • Ross, R., and Bornstein, P. 1969. The elastic fiber. I. The separation and partial characterization of its macromolecular components. J. Cell Biol. 40(2): 366-381. doi:10.1083/jcb.40.2.366. PMID:5812469.
    • (1969) J. Cell Biol. , vol.40 , Issue.2 , pp. 366-381
    • Ross, R.1    Bornstein, P.2
  • 107
    • 0015210990 scopus 로고
    • Structural features of tropoelastin related to the sites of cross-links in aortic elastin
    • doi:10.1021/bi00777a008. PMID:5538610
    • Sandberg, L.B., Weissman, N., and Gray, W.R. 1971. Structural features of tropoelastin related to the sites of cross-links in aortic elastin. Biochemistry, 10(1): 52-56. doi:10.1021/bi00777a008. PMID:5538610.
    • (1971) Biochemistry , vol.10 , Issue.1 , pp. 52-56
    • Sandberg, L.B.1    Weissman, N.2    Gray, W.R.3
  • 108
    • 0022530366 scopus 로고
    • Quantitation of elastin through measurement of its pentapeptide content
    • doi:10.1016/0006-291X(86)90493-6. PMID:3707587
    • Sandberg, L.B., Wolt, T.B., and Leslie, J.G. 1986. Quantitation of elastin through measurement of its pentapeptide content. Biochem. Biophys. Res. Commun. 136(2): 672-678. doi:10.1016/0006-291X(86)90493-6. PMID:3707587.
    • (1986) Biochem. Biophys. Res. Commun. , vol.136 , Issue.2 , pp. 672-678
    • Sandberg, L.B.1    Wolt, T.B.2    Leslie, J.G.3
  • 109
    • 0017419856 scopus 로고
    • Evidence that tropoelastin exists as a random coil
    • PMID:17275
    • Schein, J., Carpousis, A., and Rosenbloom, J. 1977. Evidence that tropoelastin exists as a random coil. Adv. Exp. Med. Biol. 79: 727-740. PMID:17275.
    • (1977) Adv. Exp. Med. Biol. , vol.79 , pp. 727-740
    • Schein, J.1    Carpousis, A.2    Rosenbloom, J.3
  • 110
    • 0016893216 scopus 로고
    • The macromolecular organization of the elastin fibril
    • doi:10.1016/S0022-2836(76)80035-6. PMID:175164
    • Serafini-Fracassini, A., Field, J.M., Spina, M., Stephens, W.G.S., and Delf, B. 1976. The macromolecular organization of the elastin fibril. J. Mol. Biol. 100(1): 73-84. doi:10.1016/S0022-2836(76)80035-6. PMID:175164.
    • (1976) J. Mol. Biol. , vol.100 , Issue.1 , pp. 73-84
    • Serafini-Fracassini, A.1    Field, J.M.2    Spina, M.3    Stephens, W.G.S.4    Delf, B.5
  • 111
    • 0037047134 scopus 로고    scopus 로고
    • Polyproline II structure in a sequence of seven alanine residues
    • doi:10.1073/pnas.112193999
    • Shi, Z., Olsen, C.A., Rose, G.D., Baldwin, R.L., and Kellenbach, N.R. 2002. Polyproline II structure in a sequence of seven alanine residues. Proc. Natl. Acad. Sci. U.S.A. 99(14): 9190-9195. doi:10.1073/pnas.112193999.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , Issue.14 , pp. 9190-9195
    • Shi, Z.1    Olsen, C.A.2    Rose, G.D.3    Baldwin, R.L.4    Kellenbach, N.R.5
  • 112
    • 0015522986 scopus 로고
    • Preparation and properties of salt-soluble elastin
    • PMID:5019956
    • Smith, D.W., Brown, D.M., and Carnes, W.H. 1972. Preparation and properties of salt-soluble elastin. J. Biol. Chem. 247(8): 2427-2432. PMID:5019956.
    • (1972) J. Biol. Chem. , vol.247 , Issue.8 , pp. 2427-2432
    • Smith, D.W.1    Brown, D.M.2    Carnes, W.H.3
  • 113
    • 0032980562 scopus 로고    scopus 로고
    • A survey of left-handed polyproline II helices
    • PMID:10091661
    • Stapley, B.J., and Creamer, T.P. 1999. A survey of left-handed polyproline II helices. Protein Sci. 8(3): 587-595. PMID:10091661.
    • (1999) Protein Sci. , vol.8 , Issue.3 , pp. 587-595
    • Stapley, B.J.1    Creamer, T.P.2
  • 114
    • 0017165234 scopus 로고
    • Purification and comparison of elastins from different animal species
    • doi:10.1016/0003-2697(76)90224-4. PMID:822746
    • Starcher, B.C., and Galione, M.J. 1976. Purification and comparison of elastins from different animal species. Anal. Biochem. 74(2): 441-447. doi:10.1016/0003-2697(76)90224-4. PMID:822746.
    • (1976) Anal. Biochem. , vol.74 , Issue.2 , pp. 441-447
    • Starcher, B.C.1    Galione, M.J.2
  • 115
    • 0016204698 scopus 로고
    • Salt-soluble elastin from lathyritic chicks
    • PMID:4455221
    • Sykes, B.C., and Partridge, S.M. 1974. Salt-soluble elastin from lathyritic chicks. Biochem. J. 141(2): 567-572. PMID:4455221.
    • (1974) Biochem. J. , vol.141 , Issue.2 , pp. 567-572
    • Sykes, B.C.1    Partridge, S.M.2
  • 116
    • 0025343528 scopus 로고
    • Synthetic fragments and analogues of elastin. II. Conformational studies
    • doi:10.1002/bip.360290419. PMID:2383648
    • Tamburro, A.M., Guantieri, V., Pandolfo, L., and Scopa, A. 1990. Synthetic fragments and analogues of elastin. II. Conformational studies. Biopolymers, 29(4-5): 855-870. doi:10.1002/bip.360290419. PMID:2383648.
    • (1990) Biopolymers , vol.29 , Issue.4-5 , pp. 855-870
    • Tamburro, A.M.1    Guantieri, V.2    Pandolfo, L.3    Scopa, A.4
  • 117
    • 0027068138 scopus 로고
    • Synthesis and structural studies of a pentapeptide sequence of elastin. Poly (Val-Gly-Gly-Leu-Gly)
    • PMID:1492919
    • Tamburro, A.M., Guantieri, V., and Gordini, D.D. 1992. Synthesis and structural studies of a pentapeptide sequence of elastin. Poly (Val-Gly-Gly-Leu-Gly). J. Biomol. Struct. Dyn. 10(3): 441-454. PMID:1492919.
    • (1992) J. Biomol. Struct. Dyn. , vol.10 , Issue.3 , pp. 441-454
    • Tamburro, A.M.1    Guantieri, V.2    Gordini, D.D.3
  • 118
    • 0242499494 scopus 로고    scopus 로고
    • Dissection of human tropoelastin: Exon-by-exon chemical synthesis and related conformational studies
    • doi:10.1021/bi034837t. PMID:14609345
    • Tamburro, A.M., Bochicchio, B., and Pepe, A. 2003. Dissection of human tropoelastin: exon-by-exon chemical synthesis and related conformational studies. Biochemistry, 42(45): 13347-13362. doi:10.1021/bi034837t. PMID:14609345.
    • (2003) Biochemistry , vol.42 , Issue.45 , pp. 13347-13362
    • Tamburro, A.M.1    Bochicchio, B.2    Pepe, A.3
  • 119
    • 22844438705 scopus 로고    scopus 로고
    • The dissection of human tropoelastin: From the molecular structure to the self-assembly to the elasticity mechanism
    • (Paris), PMID:16085114
    • Tamburro, A.M., Bochicchio, B., and Pepe, A. 2005a. The dissection of human tropoelastin: from the molecular structure to the self-assembly to the elasticity mechanism. Pathol. Biol. (Paris), 53(7): 383-389. PMID:16085114.
    • (2005) Pathol. Biol. , vol.53 , Issue.7 , pp. 383-389
    • Tamburro, A.M.1    Bochicchio, B.2    Pepe, A.3
  • 120
    • 13244275209 scopus 로고    scopus 로고
    • Supramolecular amyloid-like assembly of the polypeptide sequence coded by exon 30 of human tropoelastin
    • doi:10.1074/jbc.M411617200. PMID:15550396
    • Tamburro, A.M., Pepe, A., Bochicchio, B., Quaglino, D., and Ronchetti, I.P. 2005b. Supramolecular amyloid-like assembly of the polypeptide sequence coded by exon 30 of human tropoelastin. J. Biol. Chem. 280(4): 2682-2690. doi:10.1074/jbc.M411617200. PMID:15550396.
    • (2005) J. Biol. Chem. , vol.280 , Issue.4 , pp. 2682-2690
    • Tamburro, A.M.1    Pepe, A.2    Bochicchio, B.3    Quaglino, D.4    Ronchetti, I.P.5
  • 121
    • 33747084768 scopus 로고    scopus 로고
    • Localizing alpha-helices in human tropoelastin: Assembly of the elastin "puzzle"
    • doi:10.1021/bi060289i. PMID:16878986
    • Tamburro, A.M., Pepe, A., and Bochicchio, B. 2006. Localizing alpha-helices in human tropoelastin: assembly of the elastin "puzzle". Biochemistry, 45(31): 9518-9530. doi:10.1021/bi060289i. PMID:16878986.
    • (2006) Biochemistry , vol.45 , Issue.31 , pp. 9518-9530
    • Tamburro, A.M.1    Pepe, A.2    Bochicchio, B.3
  • 122
    • 0014227144 scopus 로고
    • New chain conformations of poly(glutamic acid) and polylysine
    • doi:10.1002/bip.1968.360060911. PMID:5669472
    • Tiffany, M.L., and Krimm, S. 1968. New chain conformations of poly(glutamic acid) and polylysine. Biopolymers, 6(9): 1379-1382. doi:10.1002/bip.1968.360060911. PMID:5669472.
    • (1968) Biopolymers , vol.6 , Issue.9 , pp. 1379-1382
    • Tiffany, M.L.1    Krimm, S.2
  • 123
    • 0036803243 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins
    • doi:10.1016/S0968-0004(02)02169-2. PMID:12368089
    • Tompa, P. 2002. Intrinsically unstructured proteins. Trends Biochem. Sci. 27(10): 527-533. doi:10.1016/S0968-0004(02)02169-2. PMID:12368089.
    • (2002) Trends Biochem. Sci. , vol.27 , Issue.10 , pp. 527-533
    • Tompa, P.1
  • 124
    • 65249102824 scopus 로고    scopus 로고
    • Close encounters of the third kind: Disordered domains and the interactions of proteins
    • doi:10.1002/bies.200800151. PMID:19260013
    • Tompa, P., Fuxreiter, M., Oldfield, C.J., Simon, I., Dunker, A.K., and Uversky, V.N. 2009. Close encounters of the third kind: disordered domains and the interactions of proteins. Bioessays, 31(3): 328-335. doi:10.1002/bies. 200800151. PMID:19260013.
    • (2009) Bioessays , vol.31 , Issue.3 , pp. 328-335
    • Tompa, P.1    Fuxreiter, M.2    Oldfield, C.J.3    Simon, I.4    Dunker, A.K.5    Uversky, V.N.6
  • 125
    • 0035977033 scopus 로고    scopus 로고
    • Hydrophobic domains of human tropoelastin interact in a context-dependent manner
    • doi:10.1074/jbc.M107920200. PMID:11564742
    • Toonkool, P., Jensen, S.A., Maxwell, A.L., and Weiss, A.S. 2001a. Hydrophobic domains of human tropoelastin interact in a context-dependent manner. J. Biol. Chem. 276(48): 44575-44580. doi:10.1074/jbc.M107920200. PMID:11564742.
    • (2001) J. Biol. Chem. , vol.276 , Issue.48 , pp. 44575-44580
    • Toonkool, P.1    Jensen, S.A.2    Maxwell, A.L.3    Weiss, A.S.4
  • 126
    • 0035958855 scopus 로고    scopus 로고
    • Thermodynamic and hydrodynamic properties of human tropoelastin. Analytical ultracentrifuge and pulsed field-gradient spin-echo NMR studies
    • doi:10.1074/jbc.M103391200. PMID:11371569
    • Toonkool, P., Regan, D.G., Kuchel, P.W., Morris, M.B., and Weiss, A.S. 2001b. Thermodynamic and hydrodynamic properties of human tropoelastin. Analytical ultracentrifuge and pulsed field-gradient spin-echo NMR studies. J. Biol. Chem. 276(30): 28042-28050. doi:10.1074/jbc.M103391200. PMID:11371569.
    • (2001) J. Biol. Chem. , vol.276 , Issue.30 , pp. 28042-28050
    • Toonkool, P.1    Regan, D.G.2    Kuchel, P.W.3    Morris, M.B.4    Weiss, A.S.5
  • 127
    • 0015935567 scopus 로고
    • Mobility of elastin chains as determined by 13C nuclear magnetic resonance
    • doi:10.1016/0022-2836(73)90514-7. PMID:4738731
    • Torchia, D.A., and Piez, K.A. 1973. Mobility of elastin chains as determined by 13C nuclear magnetic resonance. J. Mol. Biol. 76(3): 419-424. doi:10.1016/0022-2836(73)90514-7. PMID:4738731.
    • (1973) J. Mol. Biol. , vol.76 , Issue.3 , pp. 419-424
    • Torchia, D.A.1    Piez, K.A.2
  • 128
    • 0017430592 scopus 로고
    • A 13C magnetic resonance study of embryonic chick aorta
    • PMID:868664
    • Torchia, D.A., and Sullivan, C.E. 1977. A 13C magnetic resonance study of embryonic chick aorta. Adv. Exp. Med. Biol. 79: 655-661. PMID:868664.
    • (1977) Adv. Exp. Med. Biol. , vol.79 , pp. 655-661
    • Torchia, D.A.1    Sullivan, C.E.2
  • 129
    • 0018256199 scopus 로고
    • Molecular perspectives of vascular wall structure and disease: The elastic component
    • PMID:643517
    • Urry, D.W. 1978. Molecular perspectives of vascular wall structure and disease: the elastic component. Perspect. Biol. Med. 21(2): 265-295. PMID:643517.
    • (1978) Perspect. Biol. Med. , vol.21 , Issue.2 , pp. 265-295
    • Urry, D.W.1
  • 130
    • 0015994757 scopus 로고
    • Studies on the conformation and interactions of elastin. Proton magnetic resonance of the repeating pentapeptide
    • doi:10.1021/bi00700a032. PMID:4810070
    • Urry, D.W., Cunningham, W.D., and Ohnishi, T. 1974a. Studies on the conformation and interactions of elastin. Proton magnetic resonance of the repeating pentapeptide. Biochemistry, 13(3): 609-616. doi:10.1021/bi00700a032. PMID:4810070.
    • (1974) Biochemistry , vol.13 , Issue.3 , pp. 609-616
    • Urry, D.W.1    Cunningham, W.D.2    Ohnishi, T.3
  • 131
    • 0016309331 scopus 로고
    • Circular dichroism and absorption of the polytetrapeptide of elastin: A polymer model for the beta-turn
    • doi:10.1016/S0006-291X(74) 80442-0. PMID:4455262
    • Urry, D.W., Long, M.M., Ohnishi, T., and Jacobs, M. 1974b. Circular dichroism and absorption of the polytetrapeptide of elastin: a polymer model for the beta-turn. Biochem. Biophys. Res. Commun. 61(4): 1427-1433. doi:10.1016/S0006-291X(74) 80442-0. PMID:4455262.
    • (1974) Biochem. Biophys. Res. Commun. , vol.61 , Issue.4 , pp. 1427-1433
    • Urry, D.W.1    Long, M.M.2    Ohnishi, T.3    Jacobs, M.4
  • 132
    • 0016698904 scopus 로고
    • Proton and carbon magnetic resonance studies of the synthetic polypentapeptide of elastin
    • doi:10.1016/0022-2836(75)90184-9. PMID:1159785
    • Urry, D.W., Mitchell, L.W., Ohnishi, T., and Long, M.M. 1975a. Proton and carbon magnetic resonance studies of the synthetic polypentapeptide of elastin. J. Mol. Biol. 96(1): 101-117. doi:10.1016/0022-2836(75)90184-9. PMID:1159785.
    • (1975) J. Mol. Biol. , vol.96 , Issue.1 , pp. 101-117
    • Urry, D.W.1    Mitchell, L.W.2    Ohnishi, T.3    Long, M.M.4
  • 133
    • 0016715707 scopus 로고
    • Studies on the conformation and interactions of elastin: Nuclear magnetic resonance of the polyhexapeptide
    • PMID:1184287
    • Urry, D.W., Onishi, T., Long, M.M., and Mitchell, L.W. 1975b. Studies on the conformation and interactions of elastin: nuclear magnetic resonance of the polyhexapeptide. Int. J. Pept. Protein Res. 7(5): 367-378. PMID:1184287.
    • (1975) Int. J. Pept. Protein Res. , vol.7 , Issue.5 , pp. 367-378
    • Urry, D.W.1    Onishi, T.2    Long, M.M.3    Mitchell, L.W.4
  • 134
    • 0016966143 scopus 로고
    • Conformations of the repeat peptides of elastin in solution: An application of proton and carbon-13 magnetic resonance to the determination of polypeptide secondary structure
    • doi:10.3109/10409237609102557. PMID:782788
    • Urry, D.W., Long, M.M., and Gross, E. 1976. Conformations of the repeat peptides of elastin in solution: an application of proton and carbon-13 magnetic resonance to the determination of polypeptide secondary structure. CRC Crit. Rev. Biochem. 4(1): 1-45. doi:10.3109/10409237609102557. PMID:782788.
    • (1976) CRC Crit. Rev. Biochem. , vol.4 , Issue.1 , pp. 1-45
    • Urry, D.W.1    Long, M.M.2    Gross, E.3
  • 135
    • 0034669882 scopus 로고    scopus 로고
    • Why are "natively unfolded" proteins unstructured under physiologic conditions?
    • doi:10.1002/1097- 0134(20001115)41:3〈415::AID-PROT130〉3.0.CO;2- 7. PMID:11025552
    • Uversky, V.N., Gillespie, J.R., and Fink, A.L. 2000. Why are "natively unfolded" proteins unstructured under physiologic conditions? Proteins, 41(3): 415-427. doi:10.1002/1097- 0134(20001115)41: 3〈415::AID-PROT130〉3.0.CO;2-7. PMID:11025552.
    • (2000) Proteins , vol.41 , Issue.3 , pp. 415-427
    • Uversky, V.N.1    Gillespie, J.R.2    Fink, A.L.3
  • 136
    • 0015402816 scopus 로고
    • Studies on the chemistry and fine structure of elastic fibers from normal adult skin
    • doi:10.1111/1523-1747.ep12627261. PMID:5055186
    • Varadi, D.P. 1972. Studies on the chemistry and fine structure of elastic fibers from normal adult skin. J. Invest. Dermatol. 59(3): 238-246. doi:10.1111/1523-1747.ep12627261. PMID:5055186.
    • (1972) J. Invest. Dermatol. , vol.59 , Issue.3 , pp. 238-246
    • Varadi, D.P.1
  • 137
    • 0001756543 scopus 로고
    • Development of a linear helical conformation from its cyclic correlate. beta-spiral model of the elastin poly(pentapeptide) (VPGVG)n
    • doi:10.1021/ma50006a017
    • Venkatachalam, C.M., and Urry, D.W. 1981. Development of a linear helical conformation from its cyclic correlate. beta-spiral model of the elastin poly(pentapeptide) (VPGVG)n. Macromolecules, 14(5): 1225-1229. doi:10.1021/ma50006a017.
    • (1981) Macromolecules , vol.14 , Issue.5 , pp. 1225-1229
    • Venkatachalam, C.M.1    Urry, D.W.2
  • 138
    • 0032796605 scopus 로고    scopus 로고
    • Conformational chaos of an elastin-related peptide in aqueous solution
    • doi:10.1111/j.1749-6632.1999.tb10433.x. PMID:10415841
    • Villani, V., and Tamburro, A.M. 1999. Conformational chaos of an elastin-related peptide in aqueous solution. Ann. N. Y. Acad. Sci. 879(1 TEMPOS IN SCI): 284-287. doi:10.1111/j.1749-6632.1999.tb10433.x. PMID:10415841.
    • (1999) Ann. N. Y. Acad. Sci. , vol.879 , Issue.1 TEMPOS IN SCI , pp. 284-287
    • Villani, V.1    Tamburro, A.M.2
  • 139
    • 0038024557 scopus 로고    scopus 로고
    • Codistribution analysis of elastin and related fibrillar proteins in early vertebrate development
    • doi:10.1016/S0945-053X(03)00014-3. PMID:12782138
    • Visconti, R.P., Barth, J.L., Keeley, F.W., and Little, C.D. 2003. Codistribution analysis of elastin and related fibrillar proteins in early vertebrate development. Matrix Biol. 22(2): 109-121. doi:10.1016/S0945-053X(03) 00014-3. PMID:12782138.
    • (2003) Matrix Biol. , vol.22 , Issue.2 , pp. 109-121
    • Visconti, R.P.1    Barth, J.L.2    Keeley, F.W.3    Little, C.D.4
  • 140
    • 36949043812 scopus 로고
    • Thermoelasticity of elastin
    • doi:10.1038/225382a0. PMID:5410520
    • Volpin, D., and Ciferri, A. 1970. Thermoelasticity of elastin. Nature, 225(5230): 382. doi:10.1038/225382a0. PMID:5410520.
    • (1970) Nature , vol.225 , Issue.5230 , pp. 382
    • Volpin, D.1    Ciferri, A.2
  • 141
    • 0017680428 scopus 로고
    • The ultrastruct of high-temperature coacervates from elastin
    • doi:10.1016/S0022-5320(77)80054-80063 PMID:563927
    • Volpin, D., and Pasquali-Ronchetti, I. 1977. The ultrastruct of high-temperature coacervates from elastin. J. Ultrastruct. Res. 61(3): 295-302. doi:10.1016/S0022-5320(77)80054-80063 PMID:563927.
    • (1977) J. Ultrastruct. Res. , vol.61 , Issue.3 , pp. 295-302
    • Volpin, D.1    Pasquali-Ronchetti, I.2
  • 142
    • 0017064531 scopus 로고
    • Optical diffraction of tropoelastin and alpha-elastin coacervates
    • PMID:952955
    • Volpin, D., Urry, D.W., Cox, B.A., and Gotte, L. 1976a. Optical diffraction of tropoelastin and alpha-elastin coacervates. Biochim. Biophys. Acta, 439(1): 253-258. PMID:952955.
    • (1976) Biochim. Biophys. Acta , vol.439 , Issue.1 , pp. 253-258
    • Volpin, D.1    Urry, D.W.2    Cox, B.A.3    Gotte, L.4
  • 143
    • 0000121210 scopus 로고
    • Studies by electron microscopy on the structure of coacervates of synthetic polypetides of tropoelastin
    • Volpin, D., Urry, D.W., Pasquali Ronchetti, I., and Gotte, L. 1976b. Studies by electron microscopy on the structure of coacervates of synthetic polypetides of tropoelastin. Micron, 7: 193-198.
    • (1976) Micron , vol.7 , pp. 193-198
    • Volpin, D.1    Urry, D.W.2    Pasquali Ronchetti, I.3    Gotte, L.4
  • 144
    • 0032533711 scopus 로고    scopus 로고
    • Biochemistry of tropoelastin
    • doi:10.1046/j.1432-1327.1998. 2580001.x. PMID:9851686
    • Vrhovski, B., and Weiss, A.S. 1998. Biochemistry of tropoelastin. Eur. J. Biochem. 258(1): 1-18. doi:10.1046/j.1432-1327.1998. 2580001.x. PMID:9851686.
    • (1998) Eur. J. Biochem. , vol.258 , Issue.1 , pp. 1-18
    • Vrhovski, B.1    Weiss, A.S.2
  • 145
    • 0030809954 scopus 로고    scopus 로고
    • Coacervation characteristics of recombinant human tropoelastin
    • doi:10.1111/j.1432-1033.1997.00092.x. PMID:9431995
    • Vrhovski, B., Jensen, S., and Weiss, A.S. 1997. Coacervation characteristics of recombinant human tropoelastin. Eur. J. Biochem. 250(1): 92-98. doi:10.1111/j.1432-1033.1997.00092.x. PMID:9431995.
    • (1997) Eur. J. Biochem. , vol.250 , Issue.1 , pp. 92-98
    • Vrhovski, B.1    Jensen, S.2    Weiss, A.S.3
  • 146
    • 0014949231 scopus 로고
    • New molecular model for the long-range elasticity of elastin
    • doi:10.1038/227718a0. PMID:5432073
    • Weis-Fogh, T., and Anderson, S.O. 1970. New molecular model for the long-range elasticity of elastin. Nature, 227(5259): 718-721. doi:10.1038/227718a0. PMID:5432073.
    • (1970) Nature , vol.227 , Issue.5259 , pp. 718-721
    • Weis-Fogh, T.1    Anderson, S.O.2
  • 147
    • 0032749078 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins: Re-assessing the protein structure-function paradigm
    • doi:10.1006/jmbi.1999.3110. PMID:10550212
    • Wright, P.E., and Dyson, H.J. 1999. Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm. J. Mol. Biol. 293(2): 321-331. doi:10.1006/jmbi.1999.3110. PMID:10550212.
    • (1999) J. Mol. Biol. , vol.293 , Issue.2 , pp. 321-331
    • Wright, P.E.1    Dyson, H.J.2
  • 148
    • 0033571740 scopus 로고    scopus 로고
    • Deficient coacervation of two forms of human tropoelastin associated with supravalvular aortic stenosis
    • doi:10.1046/j.1432-1327.1999.00891.x. PMID:10542079
    • Wu, W.J., and Weiss, A.S. 1999. Deficient coacervation of two forms of human tropoelastin associated with supravalvular aortic stenosis. Eur. J. Biochem. 266(1): 308-314. doi:10.1046/j.1432-1327.1999.00891.x. PMID:10542079.
    • (1999) Eur. J. Biochem. , vol.266 , Issue.1 , pp. 308-314
    • Wu, W.J.1    Weiss, A.S.2
  • 149
    • 0033618373 scopus 로고    scopus 로고
    • Glycosaminoglycans mediate the coacervation of human tropoelastin through dominant charge interactions involving lysine side chains
    • doi:10.1074/jbc.274.31. 21719. PMID:10419484
    • Wu, W.J., Vrhovski, B., and Weiss, A.S. 1999. Glycosaminoglycans mediate the coacervation of human tropoelastin through dominant charge interactions involving lysine side chains. J. Biol. Chem. 274(31): 21719-21724. doi:10.1074/jbc.274.31. 21719. PMID:10419484.
    • (1999) J. Biol. Chem. , vol.274 , Issue.31 , pp. 21719-21724
    • Wu, W.J.1    Vrhovski, B.2    Weiss, A.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.