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Volumn 16, Issue 4, 2005, Pages 427-433

Protein fibers as performance proteins: New technologies and applications

Author keywords

[No Author keywords available]

Indexed keywords

FIBROUS PROTEINS; ORGANISMS; PERFORMANCE PROTEINS; PROTEIN FIBERS;

EID: 23444450224     PISSN: 09581669     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.copbio.2005.05.005     Document Type: Review
Times cited : (173)

References (54)
  • 1
    • 84889813074 scopus 로고    scopus 로고
    • Physical methods for studies of fibre formation and structure
    • J. Buchner T. Kiefhaber Wiley-VCH Weinheim
    • T. Scheibel, and L. Serpell Physical methods for studies of fibre formation and structure J. Buchner T. Kiefhaber Protein Folding Handbook Vol. 3 2005 Wiley-VCH Weinheim 197 253 This review provides a comprehensive and excellent overview of all known fiber morphologies and discusses how to detect fibrous structures and fiber assembly.
    • (2005) Protein Folding Handbook , vol.3 , pp. 197-253
    • Scheibel, T.1    Serpell, L.2
  • 3
    • 12144269871 scopus 로고    scopus 로고
    • The muscle ultrastructure: A structural perspective of the sarcomere
    • Y. Au The muscle ultrastructure: a structural perspective of the sarcomere Cell Mol Life Sci 61 2004 3016 3033
    • (2004) Cell Mol Life Sci , vol.61 , pp. 3016-3033
    • Au, Y.1
  • 5
    • 9944235461 scopus 로고    scopus 로고
    • Biomimetic actuators: Where technology and cell biology merge
    • M. Knoblauch, and W.S. Peters Biomimetic actuators: where technology and cell biology merge Cell Mol Life Sci 61 2004 2497 2509 The authors provide recent insight into how to use protein fibers as tracks for technological applications.
    • (2004) Cell Mol Life Sci , vol.61 , pp. 2497-2509
    • Knoblauch, M.1    Peters, W.S.2
  • 6
    • 33644568477 scopus 로고    scopus 로고
    • Biomolecular motors operating in engineered environments
    • C. Niemeyer C. Mirkin Wiley-VCH Weinheim
    • S. Diez, J.H. Helenius, and J. Howard Biomolecular motors operating in engineered environments C. Niemeyer C. Mirkin Nanobiotechnology 2004 Wiley-VCH Weinheim 185 199
    • (2004) Nanobiotechnology , pp. 185-199
    • Diez, S.1    Helenius, J.H.2    Howard, J.3
  • 8
    • 0036220495 scopus 로고    scopus 로고
    • Growth mechanism of the bacterial flagellar filament
    • K. Yonekura, S. Maki-Yonekura, and K. Namba Growth mechanism of the bacterial flagellar filament Res Microbiol 153 2002 191 197
    • (2002) Res Microbiol , vol.153 , pp. 191-197
    • Yonekura, K.1    Maki-Yonekura, S.2    Namba, K.3
  • 10
    • 0036527515 scopus 로고    scopus 로고
    • Recent progress on collagen triple helix structure, stability and assembly
    • R. Berisio, L. Vitagliano, L. Mazzarella, and A. Zagari Recent progress on collagen triple helix structure, stability and assembly Protein Pept Lett 9 2002 107 116
    • (2002) Protein Pept Lett , vol.9 , pp. 107-116
    • Berisio, R.1    Vitagliano, L.2    Mazzarella, L.3    Zagari, A.4
  • 11
    • 0037185950 scopus 로고    scopus 로고
    • Comparative structures and properties of elastic proteins
    • A.S. Tatham, and P.R. Shewry Comparative structures and properties of elastic proteins Philos Trans R Soc Lond B Biol Sci 357 2002 229 234 Within this review, structures and properties of elastic proteins are described in detail.
    • (2002) Philos Trans R Soc Lond B Biol Sci , vol.357 , pp. 229-234
    • Tatham, A.S.1    Shewry, P.R.2
  • 13
    • 0037335755 scopus 로고    scopus 로고
    • Molecular architecture of intermediate filaments
    • S.V. Strelkov, H. Herrmann, and U. Aebi Molecular architecture of intermediate filaments Bioessays 25 2003 243 251
    • (2003) Bioessays , vol.25 , pp. 243-251
    • Strelkov, S.V.1    Herrmann, H.2    Aebi, U.3
  • 14
    • 0036468732 scopus 로고    scopus 로고
    • 'Hard' and 'soft' principles defining the structure, function and regulation of keratin intermediate filaments
    • P.A. Coulombe, and M.B. Omary 'Hard' and 'soft' principles defining the structure, function and regulation of keratin intermediate filaments Curr Opin Cell Biol 14 2002 110 122
    • (2002) Curr Opin Cell Biol , vol.14 , pp. 110-122
    • Coulombe, P.A.1    Omary, M.B.2
  • 15
    • 0022961165 scopus 로고
    • Fibrinogen and fibrin: Biochemistry and pathophysiology
    • A.Z. Budzynski Fibrinogen and fibrin: biochemistry and pathophysiology Crit Rev Oncol Hematol 6 1986 97 146
    • (1986) Crit Rev Oncol Hematol , vol.6 , pp. 97-146
    • Budzynski, A.Z.1
  • 16
    • 0037102416 scopus 로고    scopus 로고
    • Surprising strength of silkworm silk
    • Z. Shao, and F. Vollrath Surprising strength of silkworm silk Nature 418 2002 741 The strength of natural silkworm silk can be exceeded by artificially wet-spun silkworm silk after optimizing the spinning conditions.
    • (2002) Nature , vol.418 , pp. 741
    • Shao, Z.1    Vollrath, F.2
  • 17
    • 0036897954 scopus 로고    scopus 로고
    • Comparative architecture of silks, fibrous proteins and their encoding genes in insects and spiders
    • C.L. Craig, and C. Riekel Comparative architecture of silks, fibrous proteins and their encoding genes in insects and spiders Comp Biochem Physiol B Biochem Mol Biol 133 2002 493 507
    • (2002) Comp Biochem Physiol B Biochem Mol Biol , vol.133 , pp. 493-507
    • Craig, C.L.1    Riekel, C.2
  • 19
    • 13644260108 scopus 로고    scopus 로고
    • Spider silks: Recombinant synthesis, assembly, spinning, and engineering of synthetic proteins
    • T. Scheibel Spider silks: recombinant synthesis, assembly, spinning, and engineering of synthetic proteins Microb Cell Fact 3 2004 14
    • (2004) Microb Cell Fact , vol.3 , pp. 14
    • Scheibel, T.1
  • 20
    • 0037117535 scopus 로고    scopus 로고
    • Molecular self-assembly of surfactant-like peptides to form nanotubes and nanovesicles
    • S. Vauthey, S. Santoso, H. Gong, N. Watson, and S. Zhang Molecular self-assembly of surfactant-like peptides to form nanotubes and nanovesicles Proc Natl Acad Sci USA 99 2002 5355 5360
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 5355-5360
    • Vauthey, S.1    Santoso, S.2    Gong, H.3    Watson, N.4    Zhang, S.5
  • 21
    • 2942630633 scopus 로고    scopus 로고
    • Fiber recruiting peptides: Noncovalent decoration of an engineered protein scaffold
    • M.G. Ryadnov, and D.N. Woolfson Fiber recruiting peptides: noncovalent decoration of an engineered protein scaffold J Am Chem Soc 126 2004 7454 7455
    • (2004) J Am Chem Soc , vol.126 , pp. 7454-7455
    • Ryadnov, M.G.1    Woolfson, D.N.2
  • 23
    • 0041305916 scopus 로고    scopus 로고
    • Introducing branches into a self-assembling peptide fiber
    • M.G. Ryadnov, and D.N. Woolfson Introducing branches into a self-assembling peptide fiber Angew Chem Int Ed Engl 42 2003 3021 3023
    • (2003) Angew Chem Int Ed Engl , vol.42 , pp. 3021-3023
    • Ryadnov, M.G.1    Woolfson, D.N.2
  • 24
    • 6344228390 scopus 로고    scopus 로고
    • Primary structure elements of spider dragline silks and their contribution to protein solubility
    • D. Huemmerich, C.W. Helsen, S. Quedzuweit, J. Oschmann, R. Rudolph, and T. Scheibel Primary structure elements of spider dragline silks and their contribution to protein solubility Biochemistry 43 2004 13604 13612
    • (2004) Biochemistry , vol.43 , pp. 13604-13612
    • Huemmerich, D.1    Helsen, C.W.2    Quedzuweit, S.3    Oschmann, J.4    Rudolph, R.5    Scheibel, T.6
  • 25
    • 9244235033 scopus 로고    scopus 로고
    • Novel assembly properties of recombinant spider dragline silk proteins
    • D. Huemmerich, T. Scheibel, F. Vollrath, S. Cohen, U. Gat, and I. Ittah Novel assembly properties of recombinant spider dragline silk proteins Curr Biol 14 2004 2070 2074
    • (2004) Curr Biol , vol.14 , pp. 2070-2074
    • Huemmerich, D.1    Scheibel, T.2    Vollrath, F.3    Cohen, S.4    Gat, U.5    Ittah, I.6
  • 28
    • 0033377495 scopus 로고    scopus 로고
    • The mechanical design of spider silks: From fibroin sequence to mechanical function
    • J.M. Gosline, P.A. Guerette, C.S. Ortlepp, and K.N. Savage The mechanical design of spider silks: from fibroin sequence to mechanical function J Exp Biol 202 1999 3295 3303
    • (1999) J Exp Biol , vol.202 , pp. 3295-3303
    • Gosline, J.M.1    Guerette, P.A.2    Ortlepp, C.S.3    Savage, K.N.4
  • 29
    • 2542579378 scopus 로고    scopus 로고
    • Phase behavior and hydration of silk fibroin
    • S. Sohn, H.H. Strey, and S.P. Gido Phase behavior and hydration of silk fibroin Biomacromolecules 5 2004 751 757
    • (2004) Biomacromolecules , vol.5 , pp. 751-757
    • Sohn, S.1    Strey, H.H.2    Gido, S.P.3
  • 30
    • 0038517813 scopus 로고    scopus 로고
    • Dissolution of Bombyx mori silk fibroin in the calcium nitrate tetrahydrate-methanol system and aspects of wet spinning of fibroin solution
    • S.W. Ha, Y.H. Park, and S.M. Hudson Dissolution of Bombyx mori silk fibroin in the calcium nitrate tetrahydrate-methanol system and aspects of wet spinning of fibroin solution Biomacromolecules 4 2003 488 496
    • (2003) Biomacromolecules , vol.4 , pp. 488-496
    • Ha, S.W.1    Park, Y.H.2    Hudson, S.M.3
  • 31
    • 2642520340 scopus 로고    scopus 로고
    • Wet spinning of silk polymer. I. Effect of coagulation conditions on the morphological feature of filament
    • I.C. Um, H. Kweon, K.G. Lee, D.W. Ihm, J.H. Lee, and Y.H. Park Wet spinning of silk polymer. I. Effect of coagulation conditions on the morphological feature of filament Int J Biol Macromol 34 2004 89 105
    • (2004) Int J Biol Macromol , vol.34 , pp. 89-105
    • Um, I.C.1    Kweon, H.2    Lee, K.G.3    Ihm, D.W.4    Lee, J.H.5    Park, Y.H.6
  • 32
    • 2542628135 scopus 로고    scopus 로고
    • Biomaterial films of Bombyx mori silk fibroin with poly(ethylene oxide)
    • H.J. Jin, J. Park, R. Valluzzi, P. Cebe, and D.L. Kaplan Biomaterial films of Bombyx mori silk fibroin with poly(ethylene oxide) Biomacromolecules 5 2004 711 717
    • (2004) Biomacromolecules , vol.5 , pp. 711-717
    • Jin, H.J.1    Park, J.2    Valluzzi, R.3    Cebe, P.4    Kaplan, D.L.5
  • 33
    • 0345688114 scopus 로고    scopus 로고
    • Electrospinning of silk fibroin nanofibers and its effect on the adhesion and spreading of normal human keratinocytes and fibroblasts in vitro
    • B.M. Min, G. Lee, S.H. Kim, Y.S. Nam, T.S. Lee, and W.H. Park Electrospinning of silk fibroin nanofibers and its effect on the adhesion and spreading of normal human keratinocytes and fibroblasts in vitro Biomaterials 25 2004 1289 1297
    • (2004) Biomaterials , vol.25 , pp. 1289-1297
    • Min, B.M.1    Lee, G.2    Kim, S.H.3    Nam, Y.S.4    Lee, T.S.5    Park, W.H.6
  • 34
    • 0036197050 scopus 로고    scopus 로고
    • Electrospinning of collagen nanofibers
    • J.A. Matthews, G.E. Wnek, D.G. Simpson, and G.L. Bowlin Electrospinning of collagen nanofibers Biomacromolecules 3 2002 232 238 Electrospinning of proteins lead to new fibrous materials with highly interesting properties. The electrospinning of collagen provided one landmark for this technology.
    • (2002) Biomacromolecules , vol.3 , pp. 232-238
    • Matthews, J.A.1    Wnek, G.E.2    Simpson, D.G.3    Bowlin, G.L.4
  • 36
    • 0038278084 scopus 로고    scopus 로고
    • Electrospinning of nanofiber fibrinogen structures
    • G.E. Wnek, M.E. Carr, D.G. Simpson, and G.L. Bowlin Electrospinning of nanofiber fibrinogen structures Nano Lett 3 2003 213 216
    • (2003) Nano Lett , vol.3 , pp. 213-216
    • Wnek, G.E.1    Carr, M.E.2    Simpson, D.G.3    Bowlin, G.L.4
  • 37
    • 1842484779 scopus 로고    scopus 로고
    • Designing materials for biology and medicine
    • R. Langer, and D.A. Tirrell Designing materials for biology and medicine Nature 428 2004 487 492
    • (2004) Nature , vol.428 , pp. 487-492
    • Langer, R.1    Tirrell, D.A.2
  • 38
    • 0001711774 scopus 로고    scopus 로고
    • Light controlled molecular shuttles made from motor proteins carrying cargo on engineered surfaces
    • H. Hess, J. Clemmens, D. Qin, J. Howard, and V. Vogel Light controlled molecular shuttles made from motor proteins carrying cargo on engineered surfaces Nano Lett 1 2001 235 239
    • (2001) Nano Lett , vol.1 , pp. 235-239
    • Hess, H.1    Clemmens, J.2    Qin, D.3    Howard, J.4    Vogel, V.5
  • 39
    • 0344490335 scopus 로고    scopus 로고
    • Conducting nanowires built by controlled self assembly of amyloid fibers and selective metal deposition
    • T. Scheibel, R. Parthasarathy, G. Sawicki, X.-M. Lin, H. Jaeger, and S. Lindquist Conducting nanowires built by controlled self assembly of amyloid fibers and selective metal deposition Proc Natl Acad Sci USA 100 2003 4527 4532
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 4527-4532
    • Scheibel, T.1    Parthasarathy, R.2    Sawicki, G.3    Lin, X.-M.4    Jaeger, H.5    Lindquist, S.6
  • 40
    • 0141739727 scopus 로고    scopus 로고
    • Organization of metallic nanoparticles using tobacco mosaic virus templates
    • E. Dujardin, C. Peet, G. Stibbs, J.N. Culver, and S. Mann Organization of metallic nanoparticles using tobacco mosaic virus templates Nano Lett 3 2003 413 417
    • (2003) Nano Lett , vol.3 , pp. 413-417
    • Dujardin, E.1    Peet, C.2    Stibbs, G.3    Culver, J.N.4    Mann, S.5
  • 41
    • 0037466613 scopus 로고    scopus 로고
    • Casting metal nanowires within discrete self-assembled peptide nanotubes
    • M. Reches, and E. Gazit Casting metal nanowires within discrete self-assembled peptide nanotubes Science 300 2003 625 627
    • (2003) Science , vol.300 , pp. 625-627
    • Reches, M.1    Gazit, E.2
  • 42
    • 0037012921 scopus 로고    scopus 로고
    • Ordering of quantum dots using genetically engineered viruses
    • S.W. Lee, C. Mao, C.E. Flynn, and A.M. Belcher Ordering of quantum dots using genetically engineered viruses Science 296 2002 892 895 Using bacteriophages as templates, quantum dots could be precisely ordered giving rise to a new era of bio-inspired materials.
    • (2002) Science , vol.296 , pp. 892-895
    • Lee, S.W.1    Mao, C.2    Flynn, C.E.3    Belcher, A.M.4
  • 45
    • 1942542453 scopus 로고    scopus 로고
    • Novel porous aortic elastin and collagen scaffolds for tissue engineering
    • Q. Lu, K. Ganesan, D.T. Simionescu, and N.R. Vyavahare Novel porous aortic elastin and collagen scaffolds for tissue engineering Biomaterials 25 2004 5227 5237
    • (2004) Biomaterials , vol.25 , pp. 5227-5237
    • Lu, Q.1    Ganesan, K.2    Simionescu, D.T.3    Vyavahare, N.R.4
  • 47
    • 0348014768 scopus 로고    scopus 로고
    • The use of a novel PLGA fiber/collagen composite web as a scaffold for engineering of articular cartilage tissue with adjustable thickness
    • G. Chen, T. Sato, T. Ushida, R. Hirochika, Y. Shirasaki, N. Ochiai, and T. Tateishi The use of a novel PLGA fiber/collagen composite web as a scaffold for engineering of articular cartilage tissue with adjustable thickness J Biomed Mater Res A 67 2003 1170 1180
    • (2003) J Biomed Mater Res a , vol.67 , pp. 1170-1180
    • Chen, G.1    Sato, T.2    Ushida, T.3    Hirochika, R.4    Shirasaki, Y.5    Ochiai, N.6    Tateishi, T.7
  • 51
    • 4344701213 scopus 로고    scopus 로고
    • Amyloid formation of a yeast prion determinant
    • T. Scheibel Amyloid formation of a yeast prion determinant J Mol Neurosci 23 2004 13 22
    • (2004) J Mol Neurosci , vol.23 , pp. 13-22
    • Scheibel, T.1
  • 52
    • 0141453852 scopus 로고    scopus 로고
    • Collagen self-assembly and the development of tendon mechanical properties
    • F.H. Silver, J.W. Freeman, and G.P. Seehra Collagen self-assembly and the development of tendon mechanical properties J Biomech 36 2003 1529 1553
    • (2003) J Biomech , vol.36 , pp. 1529-1553
    • Silver, F.H.1    Freeman, J.W.2    Seehra, G.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.