메뉴 건너뛰기




Volumn 53, Issue 16, 2014, Pages 2739-2748

A nacre protein, n16.3, self-assembles to form protein oligomers that dimensionally limit and organize mineral deposits

Author keywords

[No Author keywords available]

Indexed keywords

AMORPHOUS FILMS; BIOLOGICAL MATERIALS; CALCIUM; CARBONATE MINERALS; GEMS; MINERAL RESOURCES; MOLLUSCS; OLIGOMERS;

EID: 84899639099     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi401721z     Document Type: Article
Times cited : (33)

References (50)
  • 3
    • 36549044954 scopus 로고    scopus 로고
    • Fine structure of nacre revealed by solid-state 13-C and 1-H NMR
    • Jäger, C. and Cölfen, H. (2007) Fine structure of nacre revealed by solid-state 13-C and 1-H NMR CrystEngComm 9, 1237-1244
    • (2007) CrystEngComm , vol.9 , pp. 1237-1244
    • Jäger, C.1    Cölfen, H.2
  • 5
    • 46649109608 scopus 로고    scopus 로고
    • The inner-shell film: An intermediate structure participating in pearl oyster shell formation
    • Yan, Z., Ma, Z., Zheng, G., Feng, Q., Wang, H., Xie, L., and Zhang, R. (2008) The inner-shell film: An intermediate structure participating in pearl oyster shell formation ChemBioChem 9, 1093-1099
    • (2008) ChemBioChem , vol.9 , pp. 1093-1099
    • Yan, Z.1    Ma, Z.2    Zheng, G.3    Feng, Q.4    Wang, H.5    Xie, L.6    Zhang, R.7
  • 6
    • 58549120760 scopus 로고    scopus 로고
    • The key role of the surface membrane in why gastropod nacre grows in towers
    • Checa, A. G., Cartwright, J. H. E., and Willinger, M. G. (2009) The key role of the surface membrane in why gastropod nacre grows in towers Proc. Natl. Acad. Sci. U.S.A. 106, 38-43
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 38-43
    • Checa, A.G.1    Cartwright, J.H.E.2    Willinger, M.G.3
  • 7
    • 0029667586 scopus 로고    scopus 로고
    • Control of aragonite or calcite polymorphism by mollusk shell macromolecules
    • Falini, G., Albeck, S., Weiner, S., and Addadi, L. (1996) Control of aragonite or calcite polymorphism by mollusk shell macromolecules Science 271, 67-69
    • (1996) Science , vol.271 , pp. 67-69
    • Falini, G.1    Albeck, S.2    Weiner, S.3    Addadi, L.4
  • 8
    • 79959426005 scopus 로고    scopus 로고
    • Deep sequencing of ESTs from nacreous and prismatic layer producing tissues and a screen for novel shell formation-related genes in the pearl oyster
    • Kinoshita, S., Wang, N., Inoue, H., Maeyama, K., Okamoto, K., Nagai, K., Kondo, H., Hirono, I., Asakawa, S., and Watabe, S. (2011) Deep sequencing of ESTs from nacreous and prismatic layer producing tissues and a screen for novel shell formation-related genes in the pearl oyster PLoS One 6, 1-19
    • (2011) PLoS One , vol.6 , pp. 1-19
    • Kinoshita, S.1    Wang, N.2    Inoue, H.3    Maeyama, K.4    Okamoto, K.5    Nagai, K.6    Kondo, H.7    Hirono, I.8    Asakawa, S.9    Watabe, S.10
  • 10
    • 84862337695 scopus 로고    scopus 로고
    • Genetic structure and polymorphisms of the N16 gene in Pinctada fucata
    • Nogawa, C., Baba, H., Masaoka, T., Aoki, H., and Samata, T. (2012) Genetic structure and polymorphisms of the N16 gene in Pinctada fucata Gene 504, 84-91
    • (2012) Gene , vol.504 , pp. 84-91
    • Nogawa, C.1    Baba, H.2    Masaoka, T.3    Aoki, H.4    Samata, T.5
  • 11
    • 80053173085 scopus 로고    scopus 로고
    • Spatial analysis of biomineralization associated gene expression from the mantle organ of the pearl oyster, Pinctada maxima
    • Gardner, L. D., Mills, D., Wiegand, A., Leavesley, D., and Elizur, A. (2011) Spatial analysis of biomineralization associated gene expression from the mantle organ of the pearl oyster, Pinctada maxima BMC Genomics 12, 455-470
    • (2011) BMC Genomics , vol.12 , pp. 455-470
    • Gardner, L.D.1    Mills, D.2    Wiegand, A.3    Leavesley, D.4    Elizur, A.5
  • 13
    • 79959806595 scopus 로고    scopus 로고
    • Identification of genes directly involved in shell formation and their functions in pearl oyster, Pinctada fucata
    • Fang, D., Xu, G., Hu, Y., Pan, C., Xie, L., and Zhang, R. (2011) Identification of genes directly involved in shell formation and their functions in pearl oyster, Pinctada fucata PLoS One 6, 1-13
    • (2011) PLoS One , vol.6 , pp. 1-13
    • Fang, D.1    Xu, G.2    Hu, Y.3    Pan, C.4    Xie, L.5    Zhang, R.6
  • 14
    • 84867088834 scopus 로고    scopus 로고
    • The oyster genome reveals stress adaptation and complexity of shell formation
    • Zhang, G. 2012, The oyster genome reveals stress adaptation and complexity of shell formation Nature 490, 49-54
    • (2012) Nature , vol.490 , pp. 49-54
    • Zhang, G.1
  • 15
    • 0035782670 scopus 로고    scopus 로고
    • Structure of the nacreous organic matrix of a bivalve mollusk shell examined in the hydrated state using cryo-TEM
    • Levi-Kalisman, Y., Falini, G., Addadi, L., and Weiner, S. (2001) Structure of the nacreous organic matrix of a bivalve mollusk shell examined in the hydrated state using cryo-TEM J. Struct. Biol. 135, 8-17
    • (2001) J. Struct. Biol. , vol.135 , pp. 8-17
    • Levi-Kalisman, Y.1    Falini, G.2    Addadi, L.3    Weiner, S.4
  • 16
    • 42649145404 scopus 로고    scopus 로고
    • Forming nacreous layer of the shells of the bivalves Atrina rigida and Pinctada margaritifera: An environmental- and cryo-scanning electron microscopy study
    • Nudleman, F., Shimoni, E., Klein, E., Rousseau, M., Bourrat, X., Lopez, E., Addadi, L., and Weiner, S. (2008) Forming nacreous layer of the shells of the bivalves Atrina rigida and Pinctada margaritifera: An environmental- and cryo-scanning electron microscopy study J. Struct. Biol. 162, 290-300
    • (2008) J. Struct. Biol. , vol.162 , pp. 290-300
    • Nudleman, F.1    Shimoni, E.2    Klein, E.3    Rousseau, M.4    Bourrat, X.5    Lopez, E.6    Addadi, L.7    Weiner, S.8
  • 17
    • 78649938458 scopus 로고    scopus 로고
    • Silk fibroin hydrogels coupled with the n16N-β-chitin complex: An in vitro organic matrix for controlling calcium carbonate mineralization
    • Keene, E. C., Evans, J. S., and Estroff, L. A. (2010) Silk fibroin hydrogels coupled with the n16N-β-chitin complex: An in vitro organic matrix for controlling calcium carbonate mineralization Cryst. Growth Des. 10, 5169-5175
    • (2010) Cryst. Growth Des. , vol.10 , pp. 5169-5175
    • Keene, E.C.1    Evans, J.S.2    Estroff, L.A.3
  • 18
    • 0032712041 scopus 로고    scopus 로고
    • A new matrix protein family related to the nacreous layer formation of Pinctada fucata
    • Samata, T., Hayashi, N., Kono, M., Hasegawa, K., Horita, C., and Akera, S. (1999) A new matrix protein family related to the nacreous layer formation of Pinctada fucata FEBS Lett. 462, 225-232
    • (1999) FEBS Lett. , vol.462 , pp. 225-232
    • Samata, T.1    Hayashi, N.2    Kono, M.3    Hasegawa, K.4    Horita, C.5    Akera, S.6
  • 19
    • 80053461918 scopus 로고    scopus 로고
    • Polymorph crystal selection by n16, an intrinsically disordered nacre framework protein
    • Ponce, C. B. and Evans, J. S. (2011) Polymorph crystal selection by n16, an intrinsically disordered nacre framework protein Cryst. Growth Des. 11, 4690-4696
    • (2011) Cryst. Growth Des. , vol.11 , pp. 4690-4696
    • Ponce, C.B.1    Evans, J.S.2
  • 21
    • 84870838761 scopus 로고    scopus 로고
    • Identification of intrinsically disordered and aggregation: Promoting sequences within the aragonite-associated nacre proteome
    • Evans, J. S. (2012) Identification of intrinsically disordered and aggregation: Promoting sequences within the aragonite-associated nacre proteome Bioinformatics 28, 3182-3185
    • (2012) Bioinformatics , vol.28 , pp. 3182-3185
    • Evans, J.S.1
  • 22
    • 57849165523 scopus 로고    scopus 로고
    • Stable prenucleation of calcium carbonate clusters
    • Gebauer, D., Volkel, A., and Coelfen, H. (2008) Stable prenucleation of calcium carbonate clusters Science 322, 1819-1822
    • (2008) Science , vol.322 , pp. 1819-1822
    • Gebauer, D.1    Volkel, A.2    Coelfen, H.3
  • 23
    • 82955163290 scopus 로고    scopus 로고
    • Prenucleation clusters and non-classical nucleation
    • Gebauer, D. and Cölfen, H. (2011) Prenucleation clusters and non-classical nucleation Nano Today 6, 564-584
    • (2011) Nano Today , vol.6 , pp. 564-584
    • Gebauer, D.1    Cölfen, H.2
  • 27
    • 79953694799 scopus 로고    scopus 로고
    • Early stages of crystallization of calcium carbonate revealed in picoliter droplets
    • Stephens, C. J., Kim, Y. Y., Evans, S. D., Meldrum, F. C., and Christenson, H. K. (2011) Early stages of crystallization of calcium carbonate revealed in picoliter droplets J. Am. Chem. Soc. 133, 5210-5213
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 5210-5213
    • Stephens, C.J.1    Kim, Y.Y.2    Evans, S.D.3    Meldrum, F.C.4    Christenson, H.K.5
  • 29
    • 84882594567 scopus 로고    scopus 로고
    • A pearl protein self-assembles to form protein complexes that amplify mineralization
    • Perovic, I., Mandal, T., and Evans, J. S. (2013) A pearl protein self-assembles to form protein complexes that amplify mineralization Biochemistry 52, 5696-5703
    • (2013) Biochemistry , vol.52 , pp. 5696-5703
    • Perovic, I.1    Mandal, T.2    Evans, J.S.3
  • 30
    • 82555168165 scopus 로고    scopus 로고
    • Gwyddion: An open-source software for SPM data analysis
    • Nečas, D. and Klapetek, P. (2012) Gwyddion: An open-source software for SPM data analysis Cent. Eur. J. Phys. 10, 181-188
    • (2012) Cent. Eur. J. Phys. , vol.10 , pp. 181-188
    • Nečas, D.1    Klapetek, P.2
  • 31
    • 15844395840 scopus 로고    scopus 로고
    • A simple method to adjust inconsistently referenced 13-C and 15-N chemical shift assignments of proteins
    • Wang, Y. and Wishart, D. S. (2005) A simple method to adjust inconsistently referenced 13-C and 15-N chemical shift assignments of proteins J. Biomol. NMR 31, 143-148
    • (2005) J. Biomol. NMR , vol.31 , pp. 143-148
    • Wang, Y.1    Wishart, D.S.2
  • 33
    • 0035028745 scopus 로고    scopus 로고
    • Mechanisms of tryptophan fluorescence shifts in proteins
    • Vivian, J. T. and Callis, P. R. (2001) Mechanisms of tryptophan fluorescence shifts in proteins Biophys. J. 80, 2093-2091
    • (2001) Biophys. J. , vol.80 , pp. 2093-2091
    • Vivian, J.T.1    Callis, P.R.2
  • 34
    • 0032516433 scopus 로고    scopus 로고
    • Towards understanding tryptophan fluorescence in proteins
    • Chen, Y. and Barkley, M. D. (1998) Towards understanding tryptophan fluorescence in proteins Biochemistry 37, 9976-9982
    • (1998) Biochemistry , vol.37 , pp. 9976-9982
    • Chen, Y.1    Barkley, M.D.2
  • 35
    • 64349115533 scopus 로고    scopus 로고
    • The tooth enamel protein, porcine amelogenin, is an intrinsically disordered protein with an extended molecular configuration in the monomeric form
    • Delak, K., Harcup, C., Lakshminarayanan, R., Zhi, S., Fan, Y., Moradian-Oldak, J., and Evans, J. S. (2009) The tooth enamel protein, porcine amelogenin, is an intrinsically disordered protein with an extended molecular configuration in the monomeric form Biochemistry 48, 2272-2281
    • (2009) Biochemistry , vol.48 , pp. 2272-2281
    • Delak, K.1    Harcup, C.2    Lakshminarayanan, R.3    Zhi, S.4    Fan, Y.5    Moradian-Oldak, J.6    Evans, J.S.7
  • 37
    • 84867949171 scopus 로고    scopus 로고
    • Oligomer formation, metalation, and the existence of aggregation-prone and mobile sequences within the intracrystalline protein family, Asprich
    • Ndao, M., Ponce, C. B., and Evans, J. S. (2012) Oligomer formation, metalation, and the existence of aggregation-prone and mobile sequences within the intracrystalline protein family, Asprich Faraday Discuss. 159, 449-462
    • (2012) Faraday Discuss. , vol.159 , pp. 449-462
    • Ndao, M.1    Ponce, C.B.2    Evans, J.S.3
  • 38
    • 0036128797 scopus 로고    scopus 로고
    • Natively unfolded proteins: A point where biology waits for physics
    • Uversky, V. N. (2002) Natively unfolded proteins: A point where biology waits for physics Protein Sci. 11, 739-756
    • (2002) Protein Sci. , vol.11 , pp. 739-756
    • Uversky, V.N.1
  • 39
    • 0036803243 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins
    • Tompa, P. (2002) Intrinsically unstructured proteins Trends Biochem. Sci. 27, 527-533
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 527-533
    • Tompa, P.1
  • 42
    • 84907436365 scopus 로고    scopus 로고
    • Sweet on biomineralization: Effect of carbohydrates on the early stages of calcium carbonate crystallization
    • Rao, A., Berg, J. K., Kellermeier, M., and Gebauer, D. (2013) Sweet on biomineralization: Effect of carbohydrates on the early stages of calcium carbonate crystallization. European Journal of Mineralization, DOI: 10.1127/0935-1221/2014/0026-2379.
    • (2013) European Journal of Mineralization , pp. 1011270935-1221201400262379
    • Rao, A.1    Berg, J.K.2    Kellermeier, M.3    Gebauer, D.4
  • 43
    • 80054753936 scopus 로고    scopus 로고
    • A C-RING-like domain participates in protein self-assembly and mineral nucleation
    • Amos, F. F., Ndao, M., Ponce, C. B., and Evans, J. S. (2011) A C-RING-like domain participates in protein self-assembly and mineral nucleation Biochemistry 50, 8880-8887
    • (2011) Biochemistry , vol.50 , pp. 8880-8887
    • Amos, F.F.1    Ndao, M.2    Ponce, C.B.3    Evans, J.S.4
  • 44
    • 0038155558 scopus 로고    scopus 로고
    • Characterization of two molluscan crystal-modulating biomineralization proteins and identification of putative mineral binding domains
    • Michenfelder, M., Fu, G., Lawrence, C., Weaver, J. C., Wustman, B. A., Taranto, L., and Evans, J. S. (2003) Characterization of two molluscan crystal-modulating biomineralization proteins and identification of putative mineral binding domains Biopolymers 70, 522-533
    • (2003) Biopolymers , vol.70 , pp. 522-533
    • Michenfelder, M.1    Fu, G.2    Lawrence, C.3    Weaver, J.C.4    Wustman, B.A.5    Taranto, L.6    Evans, J.S.7
  • 45
    • 84875053392 scopus 로고    scopus 로고
    • From colloidal nanoparticles to a single crystal: New insights in the formation of nacre's aragonite tablets
    • Zhang, G. and Xu, J. (2013) From colloidal nanoparticles to a single crystal: New insights in the formation of nacre's aragonite tablets J. Struct. Biol. 182, 36-43
    • (2013) J. Struct. Biol. , vol.182 , pp. 36-43
    • Zhang, G.1    Xu, J.2
  • 47
    • 84896732589 scopus 로고    scopus 로고
    • Structural adaptation of tooth enamel protein amelogenin in the presence of SDS micelles
    • Chandrababu, K. B., Dutta, K., Lokappa, S. B., Ndao, M., Evans, J. S., and Moradian-Oldak, J. (2014) Structural adaptation of tooth enamel protein amelogenin in the presence of SDS micelles Biopolymers 101, 525-535
    • (2014) Biopolymers , vol.101 , pp. 525-535
    • Chandrababu, K.B.1    Dutta, K.2    Lokappa, S.B.3    Ndao, M.4    Evans, J.S.5    Moradian-Oldak, J.6
  • 49
    • 31344456451 scopus 로고    scopus 로고
    • Mollusk shell formation: A source of new concepts for understanding biomineralization processes
    • Addadi, L., Joester, D., Nudleman, F., and Weiner, S. (2006) Mollusk shell formation: A source of new concepts for understanding biomineralization processes Chem.-Eur. J. 12, 980-987
    • (2006) Chem.-Eur. J. , vol.12 , pp. 980-987
    • Addadi, L.1    Joester, D.2    Nudleman, F.3    Weiner, S.4
  • 50
    • 84876514771 scopus 로고    scopus 로고
    • Calcite crystal growth by a solid-state transformation of stabilized amorphous calcium carbonate nanospheres in a hydrogel
    • Gal, A., Habraken, W., Gur, D., Fratzl, P., Weiner, S., and Addadi, L. (2013) Calcite crystal growth by a solid-state transformation of stabilized amorphous calcium carbonate nanospheres in a hydrogel Angew. Chem., Int. Ed. 52, 4867-4870
    • (2013) Angew. Chem., Int. Ed. , vol.52 , pp. 4867-4870
    • Gal, A.1    Habraken, W.2    Gur, D.3    Fratzl, P.4    Weiner, S.5    Addadi, L.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.