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Volumn 88, Issue 6, 2010, Pages 917-925

Effect of FKBP65, a putative elastin chaperone, on the coacervation of tropoelastin in vitro

Author keywords

Circular dichroism; Coacervation; Elastin biosynthesis; Elastin model polypeptide; FKBP65; Molecular chaperone; Tropoelastin

Indexed keywords

CIRCULAR DICHROISM; COACERVATION; ELASTIN BIOSYNTHESIS; ELASTIN MODEL POLYPEPTIDE; FKBP65; MOLECULAR CHAPERONES; TROPOELASTIN;

EID: 78650400334     PISSN: 08298211     EISSN: 12086002     Source Type: Journal    
DOI: 10.1139/O10-137     Document Type: Article
Times cited : (11)

References (38)
  • 1
    • 0024380715 scopus 로고
    • Characterization of the complete human elastin gene. Delineation of unusual features in the 5′-flanking region
    • 2722804
    • Bashir, M.M., Indik, Z., Yeh, H., Ornstein-Goldstein, N., Rosenbloom, J.C., Abrams, W., et al. 1989. Characterization of the complete human elastin gene. Delineation of unusual features in the 5′-flanking region. J. Biol. Chem. 264 (15): 8887-8891. 2722804
    • (1989) J. Biol. Chem. , vol.264 , Issue.15 , pp. 8887-8891
    • Bashir, M.M.1    Indik, Z.2    Yeh, H.3    Ornstein-Goldstein, N.4    Rosenbloom, J.C.5    Abrams, W.6
  • 2
    • 0035956277 scopus 로고    scopus 로고
    • Self-aggregation characteristics of recombinantly expressed human elastin polypeptides
    • 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. 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
  • 3
    • 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
    • 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. 10.1016/0889-1605(86)90068-6 3805787 (Pubitemid 17066009)
    • (1986) Journal of Ultrastructure and Molecular Structure Research , vol.94 , Issue.3 , pp. 209-216
    • Bressan, G.M.1    Pasquali-Ronchetti, I.2    Fornieri, C.3
  • 4
    • 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
    • 10.1021/bi8005384 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. 10.1021/bi8005384 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
  • 5
    • 70249119255 scopus 로고    scopus 로고
    • Viscoelastic properties and gelation of an elastin-like polypeptide
    • Cirulis, J.T., Keeley, F.W., and James, D.F. 2009. Viscoelastic properties and gelation of an elastin-like polypeptide. J. Rheol. (N.Y.N.Y.), 53: 1215-1228.
    • (2009) J. Rheol. (N.Y.N.Y.) , vol.53 , pp. 1215-1228
    • Cirulis, J.T.1    Keeley, F.W.2    James, D.F.3
  • 6
    • 0028846571 scopus 로고
    • Molecular cloning, DNA sequence analysis, and biochemical characterization of a novel 65-kDa FK506-binding protein (FKBP65)
    • 10.1074/jbc.270.49.29336 7493967
    • Coss, M.C., Winterstein, D., Sowder, R.C. II, and Simek, S.L. 1995. Molecular cloning, DNA sequence analysis, and biochemical characterization of a novel 65-kDa FK506-binding protein (FKBP65). J. Biol. Chem. 270 (49): 29336-29341. 10.1074/jbc.270.49.29336 7493967
    • (1995) J. Biol. Chem. , vol.270 , Issue.49 , pp. 29336-29341
    • Coss, M.C.1    Winterstein, D.2    Sowder, R.C.I.I.3    Simek, S.L.4
  • 7
    • 0032567714 scopus 로고    scopus 로고
    • Identification of tropoelastin as a ligand for the 65-kD FK506-binding protein, FKBP65, in the secretory pathway
    • DOI 10.1083/jcb.140.2.295
    • Davis, E.C., Broekelmann, T.J., Ozawa, Y., and Mecham, R.P. 1998. Identification of tropoelastin as a ligand for the 65-kD FK506-binding protein, FKBP65, in the secretory pathway. J. Cell Biol. 140 (2): 295-303. 10.1083/jcb.140.2.295 9442105 (Pubitemid 28078393)
    • (1998) Journal of Cell Biology , vol.140 , Issue.2 , pp. 295-303
    • Davis, E.C.1    Broekelmann, T.J.2    Ozawa, Y.3    Mecham, R.P.4
  • 9
    • 33846627696 scopus 로고    scopus 로고
    • Domains 17-27 of tropoelastin contain key regions of contact for coacervation and contain an unusual turn-containing crosslinking domain
    • DOI 10.1016/j.matbio.2006.10.002, PII S0945053X06003921
    • 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 turn-containing crosslinking domain. Matrix Biol. 26 (2): 125-135. 10.1016/j.matbio.2006.10.002 17129717 (Pubitemid 46187042)
    • (2007) Matrix Biology , 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
  • 10
    • 21544455223 scopus 로고    scopus 로고
    • Posttranslational modification of recombinant Plasmodium falciparum apical membrane antigen 1: Impact on functional immune responses to a malaria vaccine candidate
    • DOI 10.1128/IAI.73.7.3963-3970.2005
    • Giersing, B., Miura, K., Shimp, R., Wang, J., Zhou, H., Orcutt, A., et al. 2005. Posttranslational modification of recombinant Plasmodium falciparum apical membrane antigen 1: impact on functional immune responses to a malaria vaccine candidate. Infect. Immun. 73 (7): 3963-3970. 10.1128/IAI.73.7.3963-3970. 2005 15972483 (Pubitemid 40923135)
    • (2005) Infection and Immunity , vol.73 , Issue.7 , pp. 3963-3970
    • Giersing, B.1    Miura, K.2    Shimp, R.3    Wang, J.4    Zhou, H.5    Orcutt, A.6    Stowers, A.7    Saul, A.8    Miller, L.H.9    Long, C.10    Singh, S.11
  • 11
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • 10.1016/0003-2697(89)90602-7 2610349
    • Gill, S.C., and von Hippel, P.H. 1989. Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem. 182 (2): 319-326. 10.1016/0003-2697(89)90602-7 2610349
    • (1989) Anal. Biochem. , vol.182 , Issue.2 , pp. 319-326
    • Gill, S.C.1    Von Hippel, P.H.2
  • 12
    • 58049145348 scopus 로고    scopus 로고
    • Conformational dynamics of minimal elastin-like polypeptides: The role of proline revealed by molecular dynamics and nuclear magnetic resonance
    • 10.1002/cphc.200800474 18972488
    • Glaves, R., Baer, M., Schreiner, E., Stoll, R., and Marx, D. 2008. Conformational dynamics of minimal elastin-like polypeptides: the role of proline revealed by molecular dynamics and nuclear magnetic resonance. ChemPhysChem, 9 (18): 2759-2765. 10.1002/cphc.200800474 18972488
    • (2008) ChemPhysChem , vol.9 , Issue.18 , pp. 2759-2765
    • Glaves, R.1    Baer, M.2    Schreiner, E.3    Stoll, R.4    Marx, D.5
  • 13
    • 66149128447 scopus 로고    scopus 로고
    • Loss-of-function mutations in ATP6V0A2 impair vesicular trafficking, tropoelastin secretion and cell survival
    • 10.1093/hmg/ddp148 19321599
    • Hucthagowder, V., Morava, E., Kornak, U., Lefeber, D.J., Fischer, B., Dimopoulou, A., et al. 2009. Loss-of-function mutations in ATP6V0A2 impair vesicular trafficking, tropoelastin secretion and cell survival. Hum. Mol. Genet. 18 (12): 2149-2165. 10.1093/hmg/ddp148 19321599
    • (2009) Hum. Mol. Genet. , vol.18 , Issue.12 , pp. 2149-2165
    • Hucthagowder, V.1    Morava, E.2    Kornak, U.3    Lefeber, D.J.4    Fischer, B.5    Dimopoulou, A.6
  • 14
    • 0034665987 scopus 로고    scopus 로고
    • Domain 26 of tropoelastin plays a dominant role in association by coacervation
    • 10.1074/jbc.M004265200 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. 10.1074/jbc.M004265200 10862774
    • (2000) J. Biol. Chem. , vol.275 , Issue.37 , pp. 28449-28454
    • Jensen, S.A.1    Vrhovski, B.2    Weiss, A.S.3
  • 15
    • 0002553444 scopus 로고
    • Elastic fibre structure and assembly
    • Edited by P.D. Yurchenko, D.E. Birk, and R.P. Mecham. Academic Press, San Diego
    • Mecham, R.P., and Davis, E.C. 1994. Elastic fibre structure and assembly. In Extracellular matrix assembly and structure. Edited by P.D. Yurchenko, D.E. Birk, and R.P. Mecham. Academic Press, San Diego. pp. 281-314.
    • (1994) Extracellular matrix assembly and structure , pp. 281-314
    • Mecham, R.P.1    Davis, E.C.2
  • 16
    • 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
    • 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. 10.1074/jbc.M308465200 14500713 (Pubitemid 41079493)
    • (2003) Journal of Biological Chemistry , 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
  • 17
    • 0033783405 scopus 로고    scopus 로고
    • Genetic disorders of the elastic fiber system
    • 10.1016/S0945-053X(00)00099-8 11068201
    • Milewicz, D.M., Urbn, Z., and Boyd, C. 2000. Genetic disorders of the elastic fiber system. Matrix Biol. 19 (6): 471-480. 10.1016/S0945-053X(00)00099- 8 11068201
    • (2000) Matrix Biol. , vol.19 , Issue.6 , pp. 471-480
    • Milewicz, D.M.1    Urbn, Z.2    Boyd, C.3
  • 18
    • 34648850062 scopus 로고    scopus 로고
    • Molecular and supramolecular structural studies on human tropoelastin sequences
    • DOI 10.1529/biophysj.107.110809
    • 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. 10.1529/biophysj.107.110809 17693470 (Pubitemid 350190826)
    • (2007) Biophysical Journal , vol.93 , Issue.10 , pp. 3640-3651
    • Ostuni, A.1    Bochicchio, B.2    Armentano, M.F.3    Bisaccia, F.4    Tamburro, A.M.5
  • 19
    • 24944532876 scopus 로고    scopus 로고
    • Identification and comparative analysis of the peptidyl-prolyl cis/trans isomerase repertoires of H. sapiens, D. melanogaster, C. elegans, S. cerevisiae and Sz. pombe
    • DOI 10.1002/cfg.482
    • Pemberton, T.J., and Kay, J.E. 2005. Identification and comparative analysis of the peptidyl-prolyl cis/trans isomerase repertoires of H. sapiens, D. melanogaster, C. elegans, S. cerevisiae and Sz. pombe. Comp. Funct. Genomics, 6 (5-6): 277-300. 10.1002/cfg.482 18629211 (Pubitemid 41319900)
    • (2005) Comparative and Functional Genomics , vol.6 , Issue.5-6 , pp. 277-300
    • Pemberton, T.J.1    Kay, J.E.2
  • 20
    • 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, PII S0945053X0500020X
    • 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. 10.1016/j.matbio.2005.01.004 15890261 (Pubitemid 40693634)
    • (2005) Matrix Biology , 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
  • 21
    • 0019873820 scopus 로고
    • Estimation of globular protein secondary structure from circular dichroism
    • 10.1021/bi00504a006 7470476
    • Provencher, S.W., and Glckner, J. 1981. Estimation of globular protein secondary structure from circular dichroism. Biochemistry, 20 (1): 33-37. 10.1021/bi00504a006 7470476
    • (1981) Biochemistry , vol.20 , Issue.1 , pp. 33-37
    • Provencher, S.W.1    Glckner, J.2
  • 22
    • 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, PII S0969212606003947
    • 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. 10.1016/j.str.2006.09.008 17098192 (Pubitemid 46107274)
    • (2006) Structure , vol.14 , Issue.11 , pp. 1667-1676
    • Rauscher, S.1    Baud, S.2    Miao, M.3    Keeley, FredW.4    Pomes, R.5
  • 23
    • 0032538330 scopus 로고    scopus 로고
    • Short elastin-like peptides exhibit the same temperature-induced structural transitions as elastin polymers: Implications for protein engineering
    • DOI 10.1006/jmbi.1998.2067
    • Reiersen, H., Clarke, A.R., and Rees, A.R. 1998. Short elastin-like peptides exhibit the same temperature-induced structural transitions as elastin polymers: implications for protein engineering. J. Mol. Biol. 283 (1): 255-264. 10.1006/jmbi.1998.2067 9761688 (Pubitemid 28466654)
    • (1998) Journal of Molecular Biology , vol.283 , Issue.1 , pp. 255-264
    • Reiersen, H.1    Clarke, A.R.2    Rees, A.R.3
  • 24
    • 0027422979 scopus 로고
    • Extracellular matrix 4: The elastic fiber
    • 8405806
    • Rosenbloom, J., Abrams, W.R., and Mecham, R. 1993. Extracellular matrix 4: the elastic fiber. FASEB J. 7 (13): 1208-1218. 8405806
    • (1993) FASEB J. , vol.7 , Issue.13 , pp. 1208-1218
    • Rosenbloom, J.1    Abrams, W.R.2    Mecham, R.3
  • 26
    • 0242499494 scopus 로고    scopus 로고
    • Dissection of Human Tropoelastin: Exon-By-Exon Chemical Synthesis and Related Conformational Studies
    • DOI 10.1021/bi034837t
    • 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. 10.1021/bi034837t 14609345 (Pubitemid 37420687)
    • (2003) Biochemistry , vol.42 , Issue.45 , pp. 13347-13362
    • Tamburro, A.M.1    Bochicchio, B.2    Pepe, A.3
  • 27
    • 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
    • Tamburro, A.M., Pepe, A., Bochicchio, B., Quaglino, D., and Ronchetti, I.P. 2005. Supramolecular amyloid-like assembly of the polypeptide sequence coded by exon 30 of human tropoelastin. J. Biol. Chem. 280 (4): 2682-2690. 10.1074/jbc.M411617200 15550396 (Pubitemid 40189373)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.4 , pp. 2682-2690
    • Tamburro, A.M.1    Pepe, A.2    Bochicchio, B.3    Quaglino, D.4    Ronchetti, I.P.5
  • 28
    • 0034254604 scopus 로고    scopus 로고
    • Structure-function studies on Hsp47: PH-dependent inhibition of collagen fibril formation in vitro
    • 10903151
    • Thomson, C.A., and Ananthanarayanan, V.S. 2000. Structure-function studies on Hsp47: pH-dependent inhibition of collagen fibril formation in vitro. Biochem. J. 349 (Pt 3): 877-883. 10903151
    • (2000) Biochem. J. , vol.349 , Issue.PART 3 , pp. 877-883
    • Thomson, C.A.1    Ananthanarayanan, V.S.2
  • 29
    • 0018345685 scopus 로고
    • Electron microscopic and cytochemical studies of rat aorta. Intracellular vesicles containing elastin-and collagen-like material
    • 10.1007/BF01041263 218909
    • Thyberg, J., Hinek, A., Nilsson, J., and Friberg, U. 1979. Electron microscopic and cytochemical studies of rat aorta. Intracellular vesicles containing elastin-and collagen-like material. Histochem. J. 11 (1): 1-17. 10.1007/BF01041263 218909
    • (1979) Histochem. J. , vol.11 , Issue.1 , pp. 1-17
    • Thyberg, J.1    Hinek, A.2    Nilsson, J.3    Friberg, U.4
  • 30
    • 0035977033 scopus 로고    scopus 로고
    • Hydrophobic domains of human tropoelastin interact in a context-dependent manner
    • 10.1074/jbc.M107920200 11564742
    • Toonkool, P., Jensen, S.A., Maxwell, A.L., and Weiss, A.S. 2001. Hydrophobic domains of human tropoelastin interact in a context-dependent manner. J. Biol. Chem. 276 (48): 44575-44580. 10.1074/jbc.M107920200 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
  • 31
    • 76549121556 scopus 로고    scopus 로고
    • Transient tropoelastin nanoparticles are early-stage intermediates in the coacervation of human tropoelastin whose aggregation is facilitated by heparan sulfate and heparin decasaccharides
    • 10.1016/j.matbio.2009.10.003 19895887
    • Tu, Y., and Weiss, A.S. 2010. Transient tropoelastin nanoparticles are early-stage intermediates in the coacervation of human tropoelastin whose aggregation is facilitated by heparan sulfate and heparin decasaccharides. Matrix Biol. 29 (2): 152-159. 10.1016/j.matbio.2009.10.003 19895887
    • (2010) Matrix Biol. , vol.29 , Issue.2 , pp. 152-159
    • Tu, Y.1    Weiss, A.S.2
  • 32
    • 75949088524 scopus 로고    scopus 로고
    • Stages in tropoelastin coalescence during synthetic elastin hydrogel formation
    • 10.1016/j.micron.2009.11.003 19969467
    • Tu, Y., Wise, S.G., and Weiss, A.S. 2010. Stages in tropoelastin coalescence during synthetic elastin hydrogel formation. Micron, 41 (3): 268-272. 10.1016/j.micron.2009.11.003 19969467
    • (2010) Micron , vol.41 , Issue.3 , pp. 268-272
    • Tu, Y.1    Wise, S.G.2    Weiss, A.S.3
  • 33
    • 0018256199 scopus 로고
    • Molecular perspectives of vascular wall structure and disease: The elastic component
    • 643517
    • Urry, D.W. 1978. Molecular perspectives of vascular wall structure and disease: the elastic component. Perspect. Biol. Med. 21 (2): 265-295. 643517
    • (1978) Perspect. Biol. Med. , vol.21 , Issue.2 , pp. 265-295
    • Urry, D.W.1
  • 34
    • 0014689359 scopus 로고
    • Coacervation of solubilized elastin effects a notable conformational change
    • 10.1038/222795a0 5786200
    • Urry, D.W., Starcher, B., and Partridge, S.M. 1969. Coacervation of solubilized elastin effects a notable conformational change. Nature, 222 (5195): 795-796. 10.1038/222795a0 5786200
    • (1969) Nature , vol.222 , Issue.5195 , pp. 795-796
    • Urry, D.W.1    Starcher, B.2    Partridge, S.M.3
  • 35
    • 0032533711 scopus 로고    scopus 로고
    • Biochemistry of tropoelastin
    • DOI 10.1046/j.1432-1327.1998.2580001.x
    • Vrhovski, B., and Weiss, A.S. 1998. Biochemistry of tropoelastin. Eur. J. Biochem. 258 (1): 1-18. 10.1046/j.1432-1327.1998.2580001.x 9851686 (Pubitemid 28538302)
    • (1998) European Journal of Biochemistry , vol.258 , Issue.1 , pp. 1-18
    • Vrhovski, B.1    Weiss, A.S.2
  • 36
    • 0030809954 scopus 로고    scopus 로고
    • Coacervation characteristics of recombinant human tropoelastin
    • 10.1111/j.1432-1033.1997.00092.x 9431995
    • Vrhovski, B., Jensen, S., and Weiss, A.S. 1997. Coacervation characteristics of recombinant human tropoelastin. Eur. J. Biochem. 250 (1): 92-98. 10.1111/j.1432-1033.1997.00092.x 9431995
    • (1997) Eur. J. Biochem. , vol.250 , Issue.1 , pp. 92-98
    • Vrhovski, B.1    Jensen, S.2    Weiss, A.S.3
  • 37
    • 2342424502 scopus 로고    scopus 로고
    • Investigation of recombinant human elastin polypeptides as non-thrombogenic coatings
    • DOI 10.1016/j.biomaterials.2003.11.043, PII S0142961203011086
    • Woodhouse, K.A., Klement, P., Chen, V., Gorbet, M.B., Keeley, F.W., Stahl, R., et al. 2004. Investigation of recombinant human elastin polypeptides as non-thrombogenic coatings. Biomaterials, 25 (19): 4543-4553. 10.1016/j.biomaterials.2003.11.043 15120499 (Pubitemid 38561141)
    • (2004) Biomaterials , vol.25 , Issue.19 , pp. 4543-4553
    • Woodhouse, K.A.1    Klement, P.2    Chen, V.3    Gorbet, M.B.4    Keeley, F.W.5    Stahl, R.6    Fromstein, J.D.7    Bellingham, C.M.8
  • 38
    • 0032520161 scopus 로고    scopus 로고
    • Chicken FK506- binding protein, FKBP65, a member of the FKBP family of peptidylprolyl cis - Trans isomerases, is only partially inhibited by FK506
    • 9461498
    • Zeng, B., MacDonald, J.R., Bann, J.G., Beck, K., Gambee, J.E., Boswell, B.A., and Bchinger, H.P. 1998. Chicken FK506-binding protein, FKBP65, a member of the FKBP family of peptidylprolyl cis-trans isomerases, is only partially inhibited by FK506. Biochem. J. 330 (Pt 1): 109-114. 9461498
    • (1998) Biochem. J. , vol.330 , Issue.PART 1 , pp. 109-114
    • Zeng, B.1    MacDonald, J.R.2    Bann, J.G.3    Beck, K.4    Gambee, J.E.5    Boswell, B.A.6    Bchinger, H.P.7


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