ReP USP - Resultado da busca

Artigo de periodico
Characterization of heparin-induced glyceraldehyde 3-phosphate dehydrogenase early amyloid-like oligomers and their implication in `alfa´-synuclein aggregation (2012)
Torres-Bugeau, Clarisa M; Ávila, César L; Raisman-Vozzari, R; Papy-Garcia, Dulce; Itri, Rosangela ; Barbosa, Leandro Ramos Souza ; Cortez, Leonardo M; Chehín, Rosana N
Source: Journal of Biological Chemistry. Unidade: IF
Assunto: BIOQUÍMICA
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ABNT
TORRES-BUGEAU, Clarisa M et al. Characterization of heparin-induced glyceraldehyde 3-phosphate dehydrogenase early amyloid-like oligomers and their implication in `alfa´-synuclein aggregation. Journal of Biological Chemistry, v. 287, n. 4, p. 2398–2409, 2012Tradução . . Disponível em: https://doi.org/10.1074/jbc.M111.303503. Acesso em: 17 out. 2024.
APA
Torres-Bugeau, C. M., Ávila, C. L., Raisman-Vozzari, R., Papy-Garcia, D., Itri, R., Barbosa, L. R. S., et al. (2012). Characterization of heparin-induced glyceraldehyde 3-phosphate dehydrogenase early amyloid-like oligomers and their implication in `alfa´-synuclein aggregation. Journal of Biological Chemistry, 287( 4), 2398–2409. doi:10.1074/jbc.M111.303503
NLM
Torres-Bugeau CM, Ávila CL, Raisman-Vozzari R, Papy-Garcia D, Itri R, Barbosa LRS, Cortez LM, Chehín RN. Characterization of heparin-induced glyceraldehyde 3-phosphate dehydrogenase early amyloid-like oligomers and their implication in `alfa´-synuclein aggregation [Internet]. Journal of Biological Chemistry. 2012 ; 287( 4): 2398–2409.[citado 2024 out. 17 ] Available from: https://doi.org/10.1074/jbc.M111.303503
Vancouver
Torres-Bugeau CM, Ávila CL, Raisman-Vozzari R, Papy-Garcia D, Itri R, Barbosa LRS, Cortez LM, Chehín RN. Characterization of heparin-induced glyceraldehyde 3-phosphate dehydrogenase early amyloid-like oligomers and their implication in `alfa´-synuclein aggregation [Internet]. Journal of Biological Chemistry. 2012 ; 287( 4): 2398–2409.[citado 2024 out. 17 ] Available from: https://doi.org/10.1074/jbc.M111.303503
Artigo de periodico
Structural insights into the "beta"-xylosidase from trichoderma reesei obtained by synchrotron small-angle X-ray scattering and circular dichroism spectroscopy (2005)
Rojas, Adriana L; Fischer, H; Eneiskaya, E V; Kulminskaya, A A; Shabalin, K A; Neustroev, K N; Golubev, A M; Craievich, A F; Polikarpov, Igor
Source: Biochemistry. Unidade: IF
Subjects: BIOQUÍMICA, BIOLOGIA MOLECULAR
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ABNT
ROJAS, Adriana L et al. Structural insights into the "beta"-xylosidase from trichoderma reesei obtained by synchrotron small-angle X-ray scattering and circular dichroism spectroscopy. Biochemistry, v. 44, n. 47, p. 15578-15584, 2005Tradução . . Disponível em: http://pubs.acs.org/cgi-bin/article.cgi/bichaw/2005/44/i47/html/bi050826j.html. Acesso em: 17 out. 2024.
APA
Rojas, A. L., Fischer, H., Eneiskaya, E. V., Kulminskaya, A. A., Shabalin, K. A., Neustroev, K. N., et al. (2005). Structural insights into the "beta"-xylosidase from trichoderma reesei obtained by synchrotron small-angle X-ray scattering and circular dichroism spectroscopy. Biochemistry, 44( 47), 15578-15584. Recuperado de http://pubs.acs.org/cgi-bin/article.cgi/bichaw/2005/44/i47/html/bi050826j.html
NLM
Rojas AL, Fischer H, Eneiskaya EV, Kulminskaya AA, Shabalin KA, Neustroev KN, Golubev AM, Craievich AF, Polikarpov I. Structural insights into the "beta"-xylosidase from trichoderma reesei obtained by synchrotron small-angle X-ray scattering and circular dichroism spectroscopy [Internet]. Biochemistry. 2005 ; 44( 47): 15578-15584.[citado 2024 out. 17 ] Available from: http://pubs.acs.org/cgi-bin/article.cgi/bichaw/2005/44/i47/html/bi050826j.html
Vancouver
Rojas AL, Fischer H, Eneiskaya EV, Kulminskaya AA, Shabalin KA, Neustroev KN, Golubev AM, Craievich AF, Polikarpov I. Structural insights into the "beta"-xylosidase from trichoderma reesei obtained by synchrotron small-angle X-ray scattering and circular dichroism spectroscopy [Internet]. Biochemistry. 2005 ; 44( 47): 15578-15584.[citado 2024 out. 17 ] Available from: http://pubs.acs.org/cgi-bin/article.cgi/bichaw/2005/44/i47/html/bi050826j.html
Artigo de periodico
Low resolution structural study of two human HSP40 chaperonesin solution (2005)
Borges, Julio Cesar ; Fischer, Hannes; Craievich, Aldo Felix; Ramos, Carlos H I
Source: Journal of Biological Chemistry. Unidade: IF
Subjects: BIOQUÍMICA, DIFRAÇÃO POR RAIOS X, CRISTALOGRAFIA FÍSICA
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ABNT
BORGES, Julio Cesar et al. Low resolution structural study of two human HSP40 chaperonesin solution. Journal of Biological Chemistry, v. 280, p. 13671-13681, 2005Tradução . . Disponível em: http://intl.jbc.org/pips/pips.0.shtml. Acesso em: 17 out. 2024.
APA
Borges, J. C., Fischer, H., Craievich, A. F., & Ramos, C. H. I. (2005). Low resolution structural study of two human HSP40 chaperonesin solution. Journal of Biological Chemistry, 280, 13671-13681. Recuperado de http://intl.jbc.org/pips/pips.0.shtml
NLM
Borges JC, Fischer H, Craievich AF, Ramos CHI. Low resolution structural study of two human HSP40 chaperonesin solution [Internet]. Journal of Biological Chemistry. 2005 ; 280 13671-13681.[citado 2024 out. 17 ] Available from: http://intl.jbc.org/pips/pips.0.shtml
Vancouver
Borges JC, Fischer H, Craievich AF, Ramos CHI. Low resolution structural study of two human HSP40 chaperonesin solution [Internet]. Journal of Biological Chemistry. 2005 ; 280 13671-13681.[citado 2024 out. 17 ] Available from: http://intl.jbc.org/pips/pips.0.shtml
Artigo de periodico
Bovine serum albumin (BSA) plays a role in the size of SDS micelle-like aggregates at the saturarion binding: the ionic strenght effect (2004)
Shweitzer, Bianca; Zanette, Dino; Itri, Rosangela
Source: Journal of Colloid and Interface Science. Unidade: IF
Subjects: DIFRAÇÃO POR RAIOS X, POLÍMEROS (MATERIAIS), BIOQUÍMICA
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ABNT
SHWEITZER, Bianca e ZANETTE, Dino e ITRI, Rosangela. Bovine serum albumin (BSA) plays a role in the size of SDS micelle-like aggregates at the saturarion binding: the ionic strenght effect. Journal of Colloid and Interface Science, v. 277, n. 2, p. 285-291, 2004Tradução . . Disponível em: https://doi.org/10.1016/j.jcis.2004.04.059. Acesso em: 17 out. 2024.
APA
Shweitzer, B., Zanette, D., & Itri, R. (2004). Bovine serum albumin (BSA) plays a role in the size of SDS micelle-like aggregates at the saturarion binding: the ionic strenght effect. Journal of Colloid and Interface Science, 277( 2), 285-291. doi:10.1016/j.jcis.2004.04.059
NLM
Shweitzer B, Zanette D, Itri R. Bovine serum albumin (BSA) plays a role in the size of SDS micelle-like aggregates at the saturarion binding: the ionic strenght effect [Internet]. Journal of Colloid and Interface Science. 2004 ; 277( 2): 285-291.[citado 2024 out. 17 ] Available from: https://doi.org/10.1016/j.jcis.2004.04.059
Vancouver
Shweitzer B, Zanette D, Itri R. Bovine serum albumin (BSA) plays a role in the size of SDS micelle-like aggregates at the saturarion binding: the ionic strenght effect [Internet]. Journal of Colloid and Interface Science. 2004 ; 277( 2): 285-291.[citado 2024 out. 17 ] Available from: https://doi.org/10.1016/j.jcis.2004.04.059
Artigo de periodico
Average protein density is a molecular-weight-dependent function (2004)
Fischer, Hannes; Polikarpov, Igor ; Craievich, Aldo Felix
Source: Protein Science. Unidades: IF, IFSC
Subjects: CRISTALOGRAFIA FÍSICA, BIOQUÍMICA, BIOLOGIA MOLECULAR
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ABNT
FISCHER, Hannes e POLIKARPOV, Igor e CRAIEVICH, Aldo Felix. Average protein density is a molecular-weight-dependent function. Protein Science, 2004Tradução . . Disponível em: https://doi.org/10.1110/ps.04688204. Acesso em: 17 out. 2024.
APA
Fischer, H., Polikarpov, I., & Craievich, A. F. (2004). Average protein density is a molecular-weight-dependent function. Protein Science. doi:10.1110/ps.04688204
NLM
Fischer H, Polikarpov I, Craievich AF. Average protein density is a molecular-weight-dependent function [Internet]. Protein Science. 2004 ;[citado 2024 out. 17 ] Available from: https://doi.org/10.1110/ps.04688204
Vancouver
Fischer H, Polikarpov I, Craievich AF. Average protein density is a molecular-weight-dependent function [Internet]. Protein Science. 2004 ;[citado 2024 out. 17 ] Available from: https://doi.org/10.1110/ps.04688204
Artigo de periodico
Small angle X-ray Scattering (SAXS) study of the extracellular hemoglobin of Glossoscolex paulistus: effect of pH, iron oxidation state, and interaction with anionic SDS surfactant (2004)
Gelamo, Emerson Luiz; Itri, Rosangela; Tabak, Marcel
Source: The Journal of Biological Chemistry. Unidades: IQSC, IF
Subjects: BIOQUÍMICA, BIOLOGIA MOLECULAR
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ABNT
GELAMO, Emerson Luiz e ITRI, Rosangela e TABAK, Marcel. Small angle X-ray Scattering (SAXS) study of the extracellular hemoglobin of Glossoscolex paulistus: effect of pH, iron oxidation state, and interaction with anionic SDS surfactant. The Journal of Biological Chemistry, v. 279, n. 32, p. 33298-33305, 2004Tradução . . Acesso em: 17 out. 2024.
APA
Gelamo, E. L., Itri, R., & Tabak, M. (2004). Small angle X-ray Scattering (SAXS) study of the extracellular hemoglobin of Glossoscolex paulistus: effect of pH, iron oxidation state, and interaction with anionic SDS surfactant. The Journal of Biological Chemistry, 279( 32), 33298-33305.
NLM
Gelamo EL, Itri R, Tabak M. Small angle X-ray Scattering (SAXS) study of the extracellular hemoglobin of Glossoscolex paulistus: effect of pH, iron oxidation state, and interaction with anionic SDS surfactant. The Journal of Biological Chemistry. 2004 ; 279( 32): 33298-33305.[citado 2024 out. 17 ]
Vancouver
Gelamo EL, Itri R, Tabak M. Small angle X-ray Scattering (SAXS) study of the extracellular hemoglobin of Glossoscolex paulistus: effect of pH, iron oxidation state, and interaction with anionic SDS surfactant. The Journal of Biological Chemistry. 2004 ; 279( 32): 33298-33305.[citado 2024 out. 17 ]
Artigo de periodico
Small-angle X-ray scattering and electron paramagnetic resonance study of the interaction of bovine serum albumin with ionic surfactants (2004)
Gelamo, Emerson Luiz; Itri, Rosangela; Alonso, Antonio; Silva, Junaine Vasques da; Tabak, Marcel
Source: Journal of Colloid and Interface Science. Unidades: IF, IQSC
Assunto: BIOQUÍMICA
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ABNT
GELAMO, Emerson Luiz et al. Small-angle X-ray scattering and electron paramagnetic resonance study of the interaction of bovine serum albumin with ionic surfactants. Journal of Colloid and Interface Science, v. 277, n. 2, p. 471-482, 2004Tradução . . Disponível em: https://doi.org/10.1016/j.jcis.2004.04.065. Acesso em: 17 out. 2024.
APA
Gelamo, E. L., Itri, R., Alonso, A., Silva, J. V. da, & Tabak, M. (2004). Small-angle X-ray scattering and electron paramagnetic resonance study of the interaction of bovine serum albumin with ionic surfactants. Journal of Colloid and Interface Science, 277( 2), 471-482. doi:10.1016/j.jcis.2004.04.065
NLM
Gelamo EL, Itri R, Alonso A, Silva JV da, Tabak M. Small-angle X-ray scattering and electron paramagnetic resonance study of the interaction of bovine serum albumin with ionic surfactants [Internet]. Journal of Colloid and Interface Science. 2004 ; 277( 2): 471-482.[citado 2024 out. 17 ] Available from: https://doi.org/10.1016/j.jcis.2004.04.065
Vancouver
Gelamo EL, Itri R, Alonso A, Silva JV da, Tabak M. Small-angle X-ray scattering and electron paramagnetic resonance study of the interaction of bovine serum albumin with ionic surfactants [Internet]. Journal of Colloid and Interface Science. 2004 ; 277( 2): 471-482.[citado 2024 out. 17 ] Available from: https://doi.org/10.1016/j.jcis.2004.04.065
Artigo de periodico
Free human mitochondrial GrpE is a symmetric dimer in solution (2003)
Borges, Julio Cesar ; Fischer, Hannes; Craievich, Aldo Felix; Hansen, Lee D.; Ramos, Carlos H. I.
Source: The Journal of Biological Chemistry. Unidade: IF
Subjects: BIOLOGIA MOLECULAR, BIOLOGIA CELULAR, BIOQUÍMICA
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ABNT
BORGES, Julio Cesar et al. Free human mitochondrial GrpE is a symmetric dimer in solution. The Journal of Biological Chemistry, v. 278, n. 37, p. 35337-35344, 2003Tradução . . Disponível em: http://intl.jbc.org/cgi/reprint/278/37/35337.pdf. Acesso em: 17 out. 2024.
APA
Borges, J. C., Fischer, H., Craievich, A. F., Hansen, L. D., & Ramos, C. H. I. (2003). Free human mitochondrial GrpE is a symmetric dimer in solution. The Journal of Biological Chemistry, 278( 37), 35337-35344. Recuperado de http://intl.jbc.org/cgi/reprint/278/37/35337.pdf
NLM
Borges JC, Fischer H, Craievich AF, Hansen LD, Ramos CHI. Free human mitochondrial GrpE is a symmetric dimer in solution [Internet]. The Journal of Biological Chemistry. 2003 ; 278( 37): 35337-35344.[citado 2024 out. 17 ] Available from: http://intl.jbc.org/cgi/reprint/278/37/35337.pdf
Vancouver
Borges JC, Fischer H, Craievich AF, Hansen LD, Ramos CHI. Free human mitochondrial GrpE is a symmetric dimer in solution [Internet]. The Journal of Biological Chemistry. 2003 ; 278( 37): 35337-35344.[citado 2024 out. 17 ] Available from: http://intl.jbc.org/cgi/reprint/278/37/35337.pdf
Artigo de periodico
Trifluoperazine effects on anionic and zwitterionic micelles: a study by small angle X-ray scattering (2003)
Caetano, Wilker; Barbosa, Leandro R. S.; Itri, Rosangela; Tabak, Marcel
Source: Journal of Colloid and Interface Science. Unidades: IF, IQSC
Subjects: BIOQUÍMICA, DIFRAÇÃO POR RAIOS X, FÍSICO-QUÍMICA
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ABNT
CAETANO, Wilker et al. Trifluoperazine effects on anionic and zwitterionic micelles: a study by small angle X-ray scattering. Journal of Colloid and Interface Science, v. 260, n. 2, p. 414-422, 2003Tradução . . Disponível em: https://doi.org/10.1016/s0021-9797(02)00248-5. Acesso em: 17 out. 2024.
APA
Caetano, W., Barbosa, L. R. S., Itri, R., & Tabak, M. (2003). Trifluoperazine effects on anionic and zwitterionic micelles: a study by small angle X-ray scattering. Journal of Colloid and Interface Science, 260( 2), 414-422. doi:10.1016/s0021-9797(02)00248-5
NLM
Caetano W, Barbosa LRS, Itri R, Tabak M. Trifluoperazine effects on anionic and zwitterionic micelles: a study by small angle X-ray scattering [Internet]. Journal of Colloid and Interface Science. 2003 ; 260( 2): 414-422.[citado 2024 out. 17 ] Available from: https://doi.org/10.1016/s0021-9797(02)00248-5
Vancouver
Caetano W, Barbosa LRS, Itri R, Tabak M. Trifluoperazine effects on anionic and zwitterionic micelles: a study by small angle X-ray scattering [Internet]. Journal of Colloid and Interface Science. 2003 ; 260( 2): 414-422.[citado 2024 out. 17 ] Available from: https://doi.org/10.1016/s0021-9797(02)00248-5
Artigo de periodico
Free Human Mitochondrial GrpE is a symmetric dimer in solution (2003)
Borges, Julio Cesar ; Fischer, Hannes; Craievich, Aldo Felix; Hansen, Lee D; Ramos, Carlos H I
Source: Journal of Biological Chemistry. Unidade: IF
Subjects: MITOCÔNDRIAS, BIOLOGIA, BIOQUÍMICA
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ABNT
BORGES, Julio Cesar et al. Free Human Mitochondrial GrpE is a symmetric dimer in solution. Journal of Biological Chemistry, 2003Tradução . . Disponível em: http://www.jbc.org/cgi/reprint/278/37/35337.pdf. Acesso em: 17 out. 2024.
APA
Borges, J. C., Fischer, H., Craievich, A. F., Hansen, L. D., & Ramos, C. H. I. (2003). Free Human Mitochondrial GrpE is a symmetric dimer in solution. Journal of Biological Chemistry. Recuperado de http://www.jbc.org/cgi/reprint/278/37/35337.pdf
NLM
Borges JC, Fischer H, Craievich AF, Hansen LD, Ramos CHI. Free Human Mitochondrial GrpE is a symmetric dimer in solution [Internet]. Journal of Biological Chemistry. 2003 ;[citado 2024 out. 17 ] Available from: http://www.jbc.org/cgi/reprint/278/37/35337.pdf
Vancouver
Borges JC, Fischer H, Craievich AF, Hansen LD, Ramos CHI. Free Human Mitochondrial GrpE is a symmetric dimer in solution [Internet]. Journal of Biological Chemistry. 2003 ;[citado 2024 out. 17 ] Available from: http://www.jbc.org/cgi/reprint/278/37/35337.pdf
Artigo de periodico
Domain motions and quartenary packing of phosphofructokinase-2 from Escherichia coli studied by small angle x-ray scattering and homology modeling (2003)
Cabrera, Ricardo; Fischer, Hannes; Trapani, Stefano; Craievich, Aldo Felix; Garratt, Richard Charles ; Guixé, Victoria; Babul, Jorge
Source: Journal of Biological Chemistry. Unidades: IF, IFSC
Subjects: BIOQUÍMICA, DIFRAÇÃO POR RAIOS X, ENZIMAS, PROTEÍNAS, ESCHERICHIA COLI
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ABNT
CABRERA, Ricardo et al. Domain motions and quartenary packing of phosphofructokinase-2 from Escherichia coli studied by small angle x-ray scattering and homology modeling. Journal of Biological Chemistry, v. 278, n. 15, p. 12913-12919, 2003Tradução . . Disponível em: http://www.jbc.org/cgi/reprint/278/15/12913.pdf. Acesso em: 17 out. 2024.
APA
Cabrera, R., Fischer, H., Trapani, S., Craievich, A. F., Garratt, R. C., Guixé, V., & Babul, J. (2003). Domain motions and quartenary packing of phosphofructokinase-2 from Escherichia coli studied by small angle x-ray scattering and homology modeling. Journal of Biological Chemistry, 278( 15), 12913-12919. Recuperado de http://www.jbc.org/cgi/reprint/278/15/12913.pdf
NLM
Cabrera R, Fischer H, Trapani S, Craievich AF, Garratt RC, Guixé V, Babul J. Domain motions and quartenary packing of phosphofructokinase-2 from Escherichia coli studied by small angle x-ray scattering and homology modeling [Internet]. Journal of Biological Chemistry. 2003 ; 278( 15): 12913-12919.[citado 2024 out. 17 ] Available from: http://www.jbc.org/cgi/reprint/278/15/12913.pdf
Vancouver
Cabrera R, Fischer H, Trapani S, Craievich AF, Garratt RC, Guixé V, Babul J. Domain motions and quartenary packing of phosphofructokinase-2 from Escherichia coli studied by small angle x-ray scattering and homology modeling [Internet]. Journal of Biological Chemistry. 2003 ; 278( 15): 12913-12919.[citado 2024 out. 17 ] Available from: http://www.jbc.org/cgi/reprint/278/15/12913.pdf
Artigo de periodico
Low resolution structures of the retinoid X receptor DNA-binding and ligand-binding domains revealed by synchrotron X-ray solution scattering (2003)
Fischer, Hannes; Dias, Sandra M. G.; Santos, Maria A. M.; Alves, Adriana C.; Zanchin, Nilson; Craievich, Aldo Felix; Apriletti, James W.; Baxter, John; Webb, Paul; Neves, Francisco A. R.; Ribeiro, Ralff C. J.; Polikarpov, Igor
Source: Journal of Biological Chemistry. Unidades: IF, IFSC
Subjects: BIOLOGIA MOLECULAR, CRISTALOGRAFIA FÍSICA, DNA, BIOQUÍMICA, PROTEÍNAS
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ABNT
FISCHER, Hannes et al. Low resolution structures of the retinoid X receptor DNA-binding and ligand-binding domains revealed by synchrotron X-ray solution scattering. Journal of Biological Chemistry, v. 278, n. 18, p. 16030-16038, 2003Tradução . . Acesso em: 17 out. 2024.
APA
Fischer, H., Dias, S. M. G., Santos, M. A. M., Alves, A. C., Zanchin, N., Craievich, A. F., et al. (2003). Low resolution structures of the retinoid X receptor DNA-binding and ligand-binding domains revealed by synchrotron X-ray solution scattering. Journal of Biological Chemistry, 278( 18), 16030-16038.
NLM
Fischer H, Dias SMG, Santos MAM, Alves AC, Zanchin N, Craievich AF, Apriletti JW, Baxter J, Webb P, Neves FAR, Ribeiro RCJ, Polikarpov I. Low resolution structures of the retinoid X receptor DNA-binding and ligand-binding domains revealed by synchrotron X-ray solution scattering. Journal of Biological Chemistry. 2003 ; 278( 18): 16030-16038.[citado 2024 out. 17 ]
Vancouver
Fischer H, Dias SMG, Santos MAM, Alves AC, Zanchin N, Craievich AF, Apriletti JW, Baxter J, Webb P, Neves FAR, Ribeiro RCJ, Polikarpov I. Low resolution structures of the retinoid X receptor DNA-binding and ligand-binding domains revealed by synchrotron X-ray solution scattering. Journal of Biological Chemistry. 2003 ; 278( 18): 16030-16038.[citado 2024 out. 17 ]
Artigo de periodico
Structural insights into the 'beta'-mannosidase from T. reesei obtained by synchrotron small-angle X-ray solution scattering enhanced by X-ray crystallography (2002)
Aparicio, Ricardo; Fischer, Hannes; Scott, David J; Verschueren, Koen H G; Kulminskaya, Anna A; Eneiskaya, Elena V; Neustroev, Kirill N; Craievich, Aldo Felix; Golubev, Alexander M; Polikarpov, Igor
Source: Biochemistry. Unidade: IF
Subjects: CRISTALOGRAFIA FÍSICA, DIFRAÇÃO POR RAIOS X, BIOQUÍMICA
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ABNT
APARICIO, Ricardo et al. Structural insights into the 'beta'-mannosidase from T. reesei obtained by synchrotron small-angle X-ray solution scattering enhanced by X-ray crystallography. Biochemistry, v. 41, n. 30, p. 9370-9375, 2002Tradução . . Disponível em: http://pubs.acs.org/journals/bichaw/article.cgi/bichaw/2002/41/i30/pdf/bi025811p.pdf. Acesso em: 17 out. 2024.
APA
Aparicio, R., Fischer, H., Scott, D. J., Verschueren, K. H. G., Kulminskaya, A. A., Eneiskaya, E. V., et al. (2002). Structural insights into the 'beta'-mannosidase from T. reesei obtained by synchrotron small-angle X-ray solution scattering enhanced by X-ray crystallography. Biochemistry, 41( 30), 9370-9375. Recuperado de http://pubs.acs.org/journals/bichaw/article.cgi/bichaw/2002/41/i30/pdf/bi025811p.pdf
NLM
Aparicio R, Fischer H, Scott DJ, Verschueren KHG, Kulminskaya AA, Eneiskaya EV, Neustroev KN, Craievich AF, Golubev AM, Polikarpov I. Structural insights into the 'beta'-mannosidase from T. reesei obtained by synchrotron small-angle X-ray solution scattering enhanced by X-ray crystallography [Internet]. Biochemistry. 2002 ; 41( 30): 9370-9375.[citado 2024 out. 17 ] Available from: http://pubs.acs.org/journals/bichaw/article.cgi/bichaw/2002/41/i30/pdf/bi025811p.pdf
Vancouver
Aparicio R, Fischer H, Scott DJ, Verschueren KHG, Kulminskaya AA, Eneiskaya EV, Neustroev KN, Craievich AF, Golubev AM, Polikarpov I. Structural insights into the 'beta'-mannosidase from T. reesei obtained by synchrotron small-angle X-ray solution scattering enhanced by X-ray crystallography [Internet]. Biochemistry. 2002 ; 41( 30): 9370-9375.[citado 2024 out. 17 ] Available from: http://pubs.acs.org/journals/bichaw/article.cgi/bichaw/2002/41/i30/pdf/bi025811p.pdf
Artigo de periodico
Structure determination of aot / n- hexane / water / urea reversed micelles by light and small angle x-ray scattering (1996)
Amaral, C L C; Itri, R; Politi, Mário José
Source: Langmuir. Unidades: IF, IQ
Assunto: BIOQUÍMICA
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ABNT
AMARAL, C L C e ITRI, R e POLITI, Mário José. Structure determination of aot / n- hexane / water / urea reversed micelles by light and small angle x-ray scattering. Langmuir, v. 12, n. 20, p. 4638-43, 1996Tradução . . Acesso em: 17 out. 2024.
APA
Amaral, C. L. C., Itri, R., & Politi, M. J. (1996). Structure determination of aot / n- hexane / water / urea reversed micelles by light and small angle x-ray scattering. Langmuir, 12( 20), 4638-43.
NLM
Amaral CLC, Itri R, Politi MJ. Structure determination of aot / n- hexane / water / urea reversed micelles by light and small angle x-ray scattering. Langmuir. 1996 ;12( 20): 4638-43.[citado 2024 out. 17 ]
Vancouver
Amaral CLC, Itri R, Politi MJ. Structure determination of aot / n- hexane / water / urea reversed micelles by light and small angle x-ray scattering. Langmuir. 1996 ;12( 20): 4638-43.[citado 2024 out. 17 ]

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