A new approach to the ferritin iron core growth: Influence of the H/L ratio on the core shape. Ĺopez-Castro, D, J., Delgado, J, J., Perez-Omil, A, J., Ǵalvez, N., Cuesta, R., Watt, K, R., Domínguez-Vera, & M, J. Dalton Transactions, 41(4):1320--1324, Departamento Ciencia de Materiales e Ingenieria Metalurgica y Quimica Inorganica, Universidad de Ćadiz, Campus Río San Pedro, 11510 Ćadiz, Spain, 2012.
Paper abstract bibtex 1 download An electron microscopy study, in combination with modeling and image simulation, of four different reconstituted ferritin samples: recombinant human H and L homopolymers, and H and L heteropolymers of native L-subunit-rich horse spleen and H-subunit-rich human heart ferritins, points out the existence of a correlation between iron core shape and protein shell. © 2012 The Royal Society of Chemistry.
@article{ Lopez-Castro2012,
abstract = {An electron microscopy study, in combination with modeling and image simulation, of four different reconstituted ferritin samples: recombinant human H and L homopolymers, and H and L heteropolymers of native L-subunit-rich horse spleen and H-subunit-rich human heart ferritins, points out the existence of a correlation between iron core shape and protein shell. © 2012 The Royal Society of Chemistry.},
address = {Departamento Ciencia de Materiales e Ingenieria Metalurgica y Quimica Inorganica, Universidad de Ć{a}diz, Campus Río San Pedro, 11510 Ć{a}diz, Spain},
annote = {Export Date: 15 January 2013
Source: Scopus
doi: 10.1039/c1dt11205h
PubMed ID: 22134157
Language of Original Document: English
Correspondence Address: Delgado, J.J.; Departamento Ciencia de Materiales e Ingenieria Metalurgica y Quimica Inorganica, Universidad de Ć{a}diz, Campus Río San Pedro, 11510 Ć{a}diz, Spain; email: juanjose.delgado@uca.es
Chemicals/CAS: ferritin, 9007-73-2; iron, 14093-02-8, 53858-86-9, 7439-89-6; Ferritins, 9007-73-2; Iron, 7439-89-6; Protein Subunits
References: Corbett, J.V., (1995) Am. J. Matern. Child. Nurs., 20, pp. 234-237;
Dever, J., Kowdley, K.V., (2010) Expert Opin. Med. Diagn., 4, pp. 67-77;
Chasteen, D.N., Harrison, P., (1999) J. Struct. Biol., 126, pp. 182-194;
Harrison, P.M., Arosio, P., (1996) Biochim. Biophys. Acta, Bioenerg., 1275, pp. 161-203;
Santambrogio, P., Levi, S., Cozzi, A., Corsi, B., Arosio, P., (1996) Biochem. J., 314, pp. 139-144;
Levi, S., Yewdall, S.J., Harrison, P.M., Santambrogio, P., Cozzi, A., Rovida, E., Albertini, A., Arosio, P., (1992) Biochem. J., 288, pp. 591-596;
Crichton, R.R., Herbas, A., Chavez-Alba, O., Roland, F., (1996) J. Biol. Inorg. Chem., 1, pp. 567-574;
Wade, V.J., Levi, S., Arosio, P., Treffry, A., Harrison, P.M., Mann, S., (1991) J. Mol. Biol., 221, pp. 1443-1452;
Le Brun, N.E., Crow, A., Murphy, M.E.P., Mauk, A.G., Moore, G.R., (2010) Biochim. Biophys. Acta, Gen. Subj., 1800, pp. 732-744;
Lewin, A., Moore, G.R., Le Brun, N.E., (2005) Dalton Trans., pp. 3597-3610;
Collingwood, J.F., Chong, R.K.K., Kasama, T., Cervera-Gontard, L., Dunin-Borkowski, P.E., Perry, G., Posfai, M., Dobson, J., (2008) J. Alzheimer's Dis., 14, pp. 235-245;
Pankhurst, Q., Hautot, D., Khan, N., Dobson, J., (2008) J. Alzheimer's Dis., 131, pp. 49-52;
You, S., Archacki, S.R., Angheloiu, G., Moravec, C.S., Rao, S., Kinter, M., Topol, E.J., Wang, Q., (2003) Physiol. Genomics, 13, pp. 25-30;
Levi, S., Santambrogio, P., Cozzi, A., Rovida, E., Corsi, B., Tamborini, E., Spada, S., Arosio, P., (1994) J. Mol. Biol., 238, pp. 649-654;
Tosha, T., Ng, H.-L., Bhattasali, O., Alber, T., Theil, E.C., (2010) J. Am. Chem. Soc., 132, pp. 14562-14569;
Turano, P., Lalli, D., Felli, I.C., Theil, E.C., Bertini, I., (2010) Proc. Natl. Acad. Sci. U. S. A., 107, pp. 545-550;
Wade, V.J., Levi, S., Arosio, P., Treffry, A., Harrison, P.M., Mann, S., (1991) J. Mol. Biol., 221, pp. 1443-1452;
Harrison, P.M., (1959) J. Mol. Biol., 1, pp. 69-80;
Massover, W.H., (1993) Micron, 24, pp. 389-437;
Pan, Y.-H., Sader, K., Powell, J.J., Bleloch, A., Gass, M., Trinick, J., Warley, A., Brown, A., (2009) J. Struct. Biol., 166, pp. 22-31;
Trikha, J., Theil, E.C., Allewell, N.M., (1995) J. Mol. Biol., 248, pp. 949-967;
Granier, T., D'Estaintot, B.L., Gallois, B., Chevalier, J.M., Precigoux, G., Santambrogio, P., Arosio, P., (2003) J. Biol. Inorg. Chem., 8, pp. 105-111;
Toussaint, L., Bertrand, L., Hue, L., Crichton, R.R., Declercq, J.P., (2007) J. Mol. Biol., 365, pp. 440-452;
Kim, J.-W., Choi, S.H., Lillehei, P.T., Chu, S.-H., King, G.C., Watt, G.D., (2005) Chem. Commun., pp. 4101-4103;
Luscieti, S., Santambrogio, P., Langlois, B., Granier, T., Cozzi, A., Poli, M., Gallois, B., Arosio, P., (2010) J. Mol. Biol. Chem., 285, p. 11948;
Lopez-Castro, J.D., Maraloiu, A.V., Delgado, J.J., Calvino, J.J., Blanchin, M.-G., Galvez, N., Domíinguez-Vera, J.M., (2011) Nanoscale, 3, p. 4597;
Santambrogio, P., Cozzi, A., Levi, S., Rovida, E., Magni, F., Albertini, A., Arosio, P., (2000) Protein Expression Purif., 19, pp. 212-218},
author = {Ĺ{o}pez-Castro, J D and Delgado, J J and Perez-Omil, J A and Ǵ{a}lvez, N and Cuesta, R and Watt, R K and Domínguez-Vera, J M},
issn = {14779226 (ISSN) },
journal = {Dalton Transactions},
keywords = {Chemistry,Ferritin iron,Ferritins,Heteropolymers,Human heart,Humans,Image simulations,Inorganic compounds,Iron,Iron cores,Microscopy, Electron,Models, Molecular,Protein Multimerization,Protein Structure, Quaternary,Protein Subunits,article,chemical structure,chemistry,electron microscopy,ferritin,human,iron,protein multimerization,protein quaternary structure,protein subunit},
number = {4},
pages = {1320--1324},
title = {{A new approach to the ferritin iron core growth: Influence of the H/L ratio on the core shape}},
url = {https://www.scopus.com/inward/record.url?eid=2-s2.0-84855827234\&partnerID=40\&md5=d8a09445fa5eb03a7566adb65db754a4},
volume = {41},
year = {2012}
}
Downloads: 1
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J. Matern. Child. Nurs., 20, pp. 234-237; \nDever, J., Kowdley, K.V., (2010) Expert Opin. Med. Diagn., 4, pp. 67-77; \nChasteen, D.N., Harrison, P., (1999) J. Struct. Biol., 126, pp. 182-194; \nHarrison, P.M., Arosio, P., (1996) Biochim. Biophys. Acta, Bioenerg., 1275, pp. 161-203; \nSantambrogio, P., Levi, S., Cozzi, A., Corsi, B., Arosio, P., (1996) Biochem. J., 314, pp. 139-144; \nLevi, S., Yewdall, S.J., Harrison, P.M., Santambrogio, P., Cozzi, A., Rovida, E., Albertini, A., Arosio, P., (1992) Biochem. J., 288, pp. 591-596; \nCrichton, R.R., Herbas, A., Chavez-Alba, O., Roland, F., (1996) J. Biol. Inorg. Chem., 1, pp. 567-574; \nWade, V.J., Levi, S., Arosio, P., Treffry, A., Harrison, P.M., Mann, S., (1991) J. Mol. Biol., 221, pp. 1443-1452; \nLe Brun, N.E., Crow, A., Murphy, M.E.P., Mauk, A.G., Moore, G.R., (2010) Biochim. Biophys. Acta, Gen. Subj., 1800, pp. 732-744; \nLewin, A., Moore, G.R., Le Brun, N.E., (2005) Dalton Trans., pp. 3597-3610; \nCollingwood, J.F., Chong, R.K.K., Kasama, T., Cervera-Gontard, L., Dunin-Borkowski, P.E., Perry, G., Posfai, M., Dobson, J., (2008) J. Alzheimer's Dis., 14, pp. 235-245; \nPankhurst, Q., Hautot, D., Khan, N., Dobson, J., (2008) J. Alzheimer's Dis., 131, pp. 49-52; \nYou, S., Archacki, S.R., Angheloiu, G., Moravec, C.S., Rao, S., Kinter, M., Topol, E.J., Wang, Q., (2003) Physiol. Genomics, 13, pp. 25-30; \nLevi, S., Santambrogio, P., Cozzi, A., Rovida, E., Corsi, B., Tamborini, E., Spada, S., Arosio, P., (1994) J. Mol. Biol., 238, pp. 649-654; \nTosha, T., Ng, H.-L., Bhattasali, O., Alber, T., Theil, E.C., (2010) J. Am. Chem. Soc., 132, pp. 14562-14569; \nTurano, P., Lalli, D., Felli, I.C., Theil, E.C., Bertini, I., (2010) Proc. Natl. Acad. Sci. U. S. A., 107, pp. 545-550; \nWade, V.J., Levi, S., Arosio, P., Treffry, A., Harrison, P.M., Mann, S., (1991) J. Mol. Biol., 221, pp. 1443-1452; \nHarrison, P.M., (1959) J. Mol. Biol., 1, pp. 69-80; \nMassover, W.H., (1993) Micron, 24, pp. 389-437; \nPan, Y.-H., Sader, K., Powell, J.J., Bleloch, A., Gass, M., Trinick, J., Warley, A., Brown, A., (2009) J. Struct. Biol., 166, pp. 22-31; \nTrikha, J., Theil, E.C., Allewell, N.M., (1995) J. Mol. Biol., 248, pp. 949-967; \nGranier, T., D'Estaintot, B.L., Gallois, B., Chevalier, J.M., Precigoux, G., Santambrogio, P., Arosio, P., (2003) J. Biol. Inorg. Chem., 8, pp. 105-111; \nToussaint, L., Bertrand, L., Hue, L., Crichton, R.R., Declercq, J.P., (2007) J. Mol. Biol., 365, pp. 440-452; \nKim, J.-W., Choi, S.H., Lillehei, P.T., Chu, S.-H., King, G.C., Watt, G.D., (2005) Chem. Commun., pp. 4101-4103; \nLuscieti, S., Santambrogio, P., Langlois, B., Granier, T., Cozzi, A., Poli, M., Gallois, B., Arosio, P., (2010) J. Mol. Biol. Chem., 285, p. 11948; \nLopez-Castro, J.D., Maraloiu, A.V., Delgado, J.J., Calvino, J.J., Blanchin, M.-G., Galvez, N., Domíinguez-Vera, J.M., (2011) Nanoscale, 3, p. 4597; \nSantambrogio, P., Cozzi, A., Levi, S., Rovida, E., Magni, F., Albertini, A., Arosio, P., (2000) Protein Expression Purif., 19, pp. 212-218},\n author = {Ĺ{o}pez-Castro, J D and Delgado, J J and Perez-Omil, J A and Ǵ{a}lvez, N and Cuesta, R and Watt, R K and Domínguez-Vera, J M},\n issn = {14779226 (ISSN) },\n journal = {Dalton Transactions},\n keywords = {Chemistry,Ferritin iron,Ferritins,Heteropolymers,Human heart,Humans,Image simulations,Inorganic compounds,Iron,Iron cores,Microscopy, Electron,Models, Molecular,Protein Multimerization,Protein Structure, Quaternary,Protein Subunits,article,chemical structure,chemistry,electron microscopy,ferritin,human,iron,protein multimerization,protein quaternary structure,protein subunit},\n number = {4},\n pages = {1320--1324},\n title = {{A new approach to the ferritin iron core growth: Influence of the H/L ratio on the core shape}},\n url = {https://www.scopus.com/inward/record.url?eid=2-s2.0-84855827234\\&partnerID=40\\&md5=d8a09445fa5eb03a7566adb65db754a4},\n volume = {41},\n year = {2012}\n}</pre>\n</div>\n\n\n<div class=\"well well-small bibbase\" id=\"abstract_Lopez_Castro2012\"\n style=\"display:none\">\n An electron microscopy study, in combination with modeling and image simulation, of four different reconstituted ferritin samples: recombinant human H and L homopolymers, and H and L heteropolymers of native L-subunit-rich horse spleen and H-subunit-rich human heart ferritins, points out the existence of a correlation between iron core shape and protein shell. © 2012 The Royal Society of Chemistry.\n</div>\n\n\n</div>\n","downloads":1,"keyword":["Chemistry","Ferritin iron","Ferritins","Heteropolymers","Human heart","Humans","Image simulations","Inorganic compounds","Iron","Iron cores","Microscopy","Electron","Models","Molecular","Protein Multimerization","Protein Structure","Quaternary","Protein Subunits","article","chemical structure","chemistry","electron microscopy","ferritin","human","iron","protein multimerization","protein quaternary structure","protein subunit"],"abstract":"An electron microscopy study, in combination with modeling and image simulation, of four different reconstituted ferritin samples: recombinant human H and L homopolymers, and H and L heteropolymers of native L-subunit-rich horse spleen and H-subunit-rich human heart ferritins, points out the existence of a correlation between iron core shape and protein shell. © 2012 The Royal Society of Chemistry.","address":"Departamento Ciencia de Materiales e Ingenieria Metalurgica y Quimica Inorganica, Universidad de Ćadiz, Campus Río San Pedro, 11510 Ćadiz, Spain","annote":"Export Date: 15 January 2013 Source: Scopus doi: 10.1039/c1dt11205h PubMed ID: 22134157 Language of Original Document: English Correspondence Address: Delgado, J.J.; Departamento Ciencia de Materiales e Ingenieria Metalurgica y Quimica Inorganica, Universidad de Ćadiz, Campus Río San Pedro, 11510 Ćadiz, Spain; email: juanjose.delgado@uca.es Chemicals/CAS: ferritin, 9007-73-2; iron, 14093-02-8, 53858-86-9, 7439-89-6; Ferritins, 9007-73-2; Iron, 7439-89-6; Protein Subunits References: Corbett, J.V., (1995) Am. J. Matern. Child. Nurs., 20, pp. 234-237; Dever, J., Kowdley, K.V., (2010) Expert Opin. Med. Diagn., 4, pp. 67-77; Chasteen, D.N., Harrison, P., (1999) J. Struct. Biol., 126, pp. 182-194; Harrison, P.M., Arosio, P., (1996) Biochim. Biophys. Acta, Bioenerg., 1275, pp. 161-203; Santambrogio, P., Levi, S., Cozzi, A., Corsi, B., Arosio, P., (1996) Biochem. J., 314, pp. 139-144; Levi, S., Yewdall, S.J., Harrison, P.M., Santambrogio, P., Cozzi, A., Rovida, E., Albertini, A., Arosio, P., (1992) Biochem. J., 288, pp. 591-596; Crichton, R.R., Herbas, A., Chavez-Alba, O., Roland, F., (1996) J. Biol. Inorg. Chem., 1, pp. 567-574; Wade, V.J., Levi, S., Arosio, P., Treffry, A., Harrison, P.M., Mann, S., (1991) J. Mol. Biol., 221, pp. 1443-1452; Le Brun, N.E., Crow, A., Murphy, M.E.P., Mauk, A.G., Moore, G.R., (2010) Biochim. Biophys. Acta, Gen. Subj., 1800, pp. 732-744; Lewin, A., Moore, G.R., Le Brun, N.E., (2005) Dalton Trans., pp. 3597-3610; Collingwood, J.F., Chong, R.K.K., Kasama, T., Cervera-Gontard, L., Dunin-Borkowski, P.E., Perry, G., Posfai, M., Dobson, J., (2008) J. Alzheimer's Dis., 14, pp. 235-245; Pankhurst, Q., Hautot, D., Khan, N., Dobson, J., (2008) J. Alzheimer's Dis., 131, pp. 49-52; You, S., Archacki, S.R., Angheloiu, G., Moravec, C.S., Rao, S., Kinter, M., Topol, E.J., Wang, Q., (2003) Physiol. Genomics, 13, pp. 25-30; Levi, S., Santambrogio, P., Cozzi, A., Rovida, E., Corsi, B., Tamborini, E., Spada, S., Arosio, P., (1994) J. Mol. Biol., 238, pp. 649-654; Tosha, T., Ng, H.-L., Bhattasali, O., Alber, T., Theil, E.C., (2010) J. Am. Chem. Soc., 132, pp. 14562-14569; Turano, P., Lalli, D., Felli, I.C., Theil, E.C., Bertini, I., (2010) Proc. Natl. Acad. Sci. U. S. A., 107, pp. 545-550; Wade, V.J., Levi, S., Arosio, P., Treffry, A., Harrison, P.M., Mann, S., (1991) J. Mol. Biol., 221, pp. 1443-1452; Harrison, P.M., (1959) J. Mol. Biol., 1, pp. 69-80; Massover, W.H., (1993) Micron, 24, pp. 389-437; Pan, Y.-H., Sader, K., Powell, J.J., Bleloch, A., Gass, M., Trinick, J., Warley, A., Brown, A., (2009) J. Struct. Biol., 166, pp. 22-31; Trikha, J., Theil, E.C., Allewell, N.M., (1995) J. Mol. Biol., 248, pp. 949-967; Granier, T., D'Estaintot, B.L., Gallois, B., Chevalier, J.M., Precigoux, G., Santambrogio, P., Arosio, P., (2003) J. Biol. Inorg. Chem., 8, pp. 105-111; Toussaint, L., Bertrand, L., Hue, L., Crichton, R.R., Declercq, J.P., (2007) J. Mol. Biol., 365, pp. 440-452; Kim, J.-W., Choi, S.H., Lillehei, P.T., Chu, S.-H., King, G.C., Watt, G.D., (2005) Chem. Commun., pp. 4101-4103; Luscieti, S., Santambrogio, P., Langlois, B., Granier, T., Cozzi, A., Poli, M., Gallois, B., Arosio, P., (2010) J. Mol. Biol. Chem., 285, p. 11948; Lopez-Castro, J.D., Maraloiu, A.V., Delgado, J.J., Calvino, J.J., Blanchin, M.-G., Galvez, N., Domíinguez-Vera, J.M., (2011) Nanoscale, 3, p. 4597; Santambrogio, P., Cozzi, A., Levi, S., Rovida, E., Magni, F., Albertini, A., Arosio, P., (2000) Protein Expression Purif., 19, pp. 212-218","author":["Ĺopez-Castro","D, J","Delgado","J, J","Perez-Omil","A, J","Ǵalvez, N","Cuesta, R","Watt","K, R","Domínguez-Vera","M, J"],"author_short":["Ĺopez-Castro","D, J.","Delgado","J, J.","Perez-Omil","A, J.","Ǵalvez, N.","Cuesta, R.","Watt","K, R.","Domínguez-Vera","M, J."],"bibtex":"@article{ Lopez-Castro2012,\n abstract = {An electron microscopy study, in combination with modeling and image simulation, of four different reconstituted ferritin samples: recombinant human H and L homopolymers, and H and L heteropolymers of native L-subunit-rich horse spleen and H-subunit-rich human heart ferritins, points out the existence of a correlation between iron core shape and protein shell. © 2012 The Royal Society of Chemistry.},\n address = {Departamento Ciencia de Materiales e Ingenieria Metalurgica y Quimica Inorganica, Universidad de Ć{a}diz, Campus Río San Pedro, 11510 Ć{a}diz, Spain},\n annote = {Export Date: 15 January 2013\n\nSource: Scopus\n\ndoi: 10.1039/c1dt11205h\n\nPubMed ID: 22134157\n\nLanguage of Original Document: English\n\nCorrespondence Address: Delgado, J.J.; Departamento Ciencia de Materiales e Ingenieria Metalurgica y Quimica Inorganica, Universidad de Ć{a}diz, Campus Río San Pedro, 11510 Ć{a}diz, Spain; email: juanjose.delgado@uca.es\n\nChemicals/CAS: ferritin, 9007-73-2; iron, 14093-02-8, 53858-86-9, 7439-89-6; Ferritins, 9007-73-2; Iron, 7439-89-6; Protein Subunits\n\nReferences: Corbett, J.V., (1995) Am. 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Biol., 221, pp. 1443-1452; \nHarrison, P.M., (1959) J. Mol. Biol., 1, pp. 69-80; \nMassover, W.H., (1993) Micron, 24, pp. 389-437; \nPan, Y.-H., Sader, K., Powell, J.J., Bleloch, A., Gass, M., Trinick, J., Warley, A., Brown, A., (2009) J. Struct. Biol., 166, pp. 22-31; \nTrikha, J., Theil, E.C., Allewell, N.M., (1995) J. Mol. Biol., 248, pp. 949-967; \nGranier, T., D'Estaintot, B.L., Gallois, B., Chevalier, J.M., Precigoux, G., Santambrogio, P., Arosio, P., (2003) J. Biol. Inorg. Chem., 8, pp. 105-111; \nToussaint, L., Bertrand, L., Hue, L., Crichton, R.R., Declercq, J.P., (2007) J. Mol. Biol., 365, pp. 440-452; \nKim, J.-W., Choi, S.H., Lillehei, P.T., Chu, S.-H., King, G.C., Watt, G.D., (2005) Chem. Commun., pp. 4101-4103; \nLuscieti, S., Santambrogio, P., Langlois, B., Granier, T., Cozzi, A., Poli, M., Gallois, B., Arosio, P., (2010) J. Mol. Biol. Chem., 285, p. 11948; \nLopez-Castro, J.D., Maraloiu, A.V., Delgado, J.J., Calvino, J.J., Blanchin, M.-G., Galvez, N., Domíinguez-Vera, J.M., (2011) Nanoscale, 3, p. 4597; \nSantambrogio, P., Cozzi, A., Levi, S., Rovida, E., Magni, F., Albertini, A., Arosio, P., (2000) Protein Expression Purif., 19, pp. 212-218},\n author = {Ĺ{o}pez-Castro, J D and Delgado, J J and Perez-Omil, J A and Ǵ{a}lvez, N and Cuesta, R and Watt, R K and Domínguez-Vera, J M},\n issn = {14779226 (ISSN) },\n journal = {Dalton Transactions},\n keywords = {Chemistry,Ferritin iron,Ferritins,Heteropolymers,Human heart,Humans,Image simulations,Inorganic compounds,Iron,Iron cores,Microscopy, Electron,Models, Molecular,Protein Multimerization,Protein Structure, Quaternary,Protein Subunits,article,chemical structure,chemistry,electron microscopy,ferritin,human,iron,protein multimerization,protein quaternary structure,protein subunit},\n number = {4},\n pages = {1320--1324},\n title = {{A new approach to the ferritin iron core growth: Influence of the H/L ratio on the core shape}},\n url = {https://www.scopus.com/inward/record.url?eid=2-s2.0-84855827234\\&partnerID=40\\&md5=d8a09445fa5eb03a7566adb65db754a4},\n volume = {41},\n year = {2012}\n}","bibtype":"article","id":"Lopez-Castro2012","issn":"14779226 (ISSN)","journal":"Dalton Transactions","key":"Lopez-Castro2012","keywords":"Chemistry,Ferritin iron,Ferritins,Heteropolymers,Human heart,Humans,Image simulations,Inorganic compounds,Iron,Iron cores,Microscopy, Electron,Models, Molecular,Protein Multimerization,Protein Structure, Quaternary,Protein Subunits,article,chemical structure,chemistry,electron microscopy,ferritin,human,iron,protein multimerization,protein quaternary structure,protein subunit","number":"4","pages":"1320--1324","title":"A new approach to the ferritin iron core growth: Influence of the H/L ratio on the core shape","type":"article","url":"https://www.scopus.com/inward/record.url?eid=2-s2.0-84855827234\\&partnerID=40\\&md5=d8a09445fa5eb03a7566adb65db754a4","volume":"41","year":"2012","role":"author","urls":{"Paper":"https://www.scopus.com/inward/record.url?eid=2-s2.0-84855827234\\&partnerID=40\\&md5=d8a09445fa5eb03a7566adb65db754a4"},"bibbaseid":"-d--j--a-galvez-cuesta--k--m-anewapproachtotheferritinironcoregrowthinfluenceofthehlratioonthecoreshape-2012"},"bibtype":"article","biburl":"http://www2.uca.es/dept/cmat_qinor/nanomat/People/PerezOmil.bib","downloads":1,"search_terms":["new","approach","ferritin","iron","core","growth","influence","ratio","core","shape","ĺopez-castro","d","delgado","j","perez-omil","a","ǵalvez","cuesta","watt","k","domínguez-vera","m"],"title":"A new approach to the ferritin iron core growth: Influence of the H/L ratio on the core shape","title_words":["new","approach","ferritin","iron","core","growth","influence","ratio","shape"],"year":2012,"dataSources":["PWTDKAHZu4X8o2kXp"]}