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Artigo de periodico-carta/editorial
Restoring endoplasmic reticulum proteostasis to treat neurological disorders [Editorial] (2023)
Medinas, Danilo Bilches ; Arshad, Najla; Parakh, Sonam ; Miyamoto, Sayuri ; Zambelli, Vanessa Olzon
Source: Frontiers in Pharmacology. Unidade: IQ
Subjects: SISTEMA NERVOSO, RETÍCULO ENDOPLASMÁTICO
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ABNT
MEDINAS, Danilo Bilches et al. Restoring endoplasmic reticulum proteostasis to treat neurological disorders [Editorial]. Frontiers in Pharmacology. Lausanne: Instituto de Química, Universidade de São Paulo. Disponível em: https://doi.org/10.3389/fphar.2023.1176805. Acesso em: 07 nov. 2024. , 2023
APA
Medinas, D. B., Arshad, N., Parakh, S., Miyamoto, S., & Zambelli, V. O. (2023). Restoring endoplasmic reticulum proteostasis to treat neurological disorders [Editorial]. Frontiers in Pharmacology. Lausanne: Instituto de Química, Universidade de São Paulo. doi:10.3389/fphar.2023.1176805
NLM
Medinas DB, Arshad N, Parakh S, Miyamoto S, Zambelli VO. Restoring endoplasmic reticulum proteostasis to treat neurological disorders [Editorial] [Internet]. Frontiers in Pharmacology. 2023 ; 14 1-3 art. 1176805.[citado 2024 nov. 07 ] Available from: https://doi.org/10.3389/fphar.2023.1176805
Vancouver
Medinas DB, Arshad N, Parakh S, Miyamoto S, Zambelli VO. Restoring endoplasmic reticulum proteostasis to treat neurological disorders [Editorial] [Internet]. Frontiers in Pharmacology. 2023 ; 14 1-3 art. 1176805.[citado 2024 nov. 07 ] Available from: https://doi.org/10.3389/fphar.2023.1176805
Artigo de periodico
HSPB1 is essential for inducing resistance to proteotoxic stress in beta-cells (2021)
Gomes, Vinícius Maron; Mansano, Rosangela Aparecida Wailemann ; Arini, Gabriel Santos ; Oliveira, Talita Cristina de; Almeida, Daria Raquel Queiroz de ; Santos, Ancély Ferreira dos ; Terra, Letícia Ferreira; Lortz, Stephan ; Labriola, Leticia
Source: Cells. Unidades: IQ, FMRP
Subjects: APOPTOSE, PROTEÍNAS DO CHOQUE TÉRMICO, DIABETES MELLITUS, RETÍCULO ENDOPLASMÁTICO
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ABNT
GOMES, Vinícius Maron et al. HSPB1 is essential for inducing resistance to proteotoxic stress in beta-cells. Cells, v. 10, n. 9, p. 1-16, 2021Tradução . . Disponível em: https://doi.org/10.3390/cells10092178. Acesso em: 07 nov. 2024.
APA
Gomes, V. M., Mansano, R. A. W., Arini, G. S., Oliveira, T. C. de, Almeida, D. R. Q. de, Santos, A. F. dos, et al. (2021). HSPB1 is essential for inducing resistance to proteotoxic stress in beta-cells. Cells, 10( 9), 1-16. doi:10.3390/cells10092178
NLM
Gomes VM, Mansano RAW, Arini GS, Oliveira TC de, Almeida DRQ de, Santos AF dos, Terra LF, Lortz S, Labriola L. HSPB1 is essential for inducing resistance to proteotoxic stress in beta-cells [Internet]. Cells. 2021 ; 10( 9): 1-16.[citado 2024 nov. 07 ] Available from: https://doi.org/10.3390/cells10092178
Vancouver
Gomes VM, Mansano RAW, Arini GS, Oliveira TC de, Almeida DRQ de, Santos AF dos, Terra LF, Lortz S, Labriola L. HSPB1 is essential for inducing resistance to proteotoxic stress in beta-cells [Internet]. Cells. 2021 ; 10( 9): 1-16.[citado 2024 nov. 07 ] Available from: https://doi.org/10.3390/cells10092178
Trabalho de evento-resumo periodico
HSPB1 is essential for inducing resistance to proteotoxic stress in beta cells (2020)
Labriola, Leticia ; Gomes, Vinicius M; Wailemann, Rosângela A. M; Almeida, Daria Raquel Queiroz de ; Arini, Gabriel Santos ; Santos, Ancély Ferreira dos ; Terra, Letícia Ferreira; Lortz, S
Source: Diabetologia. Conference titles: Virtual Meeting of the European Association for the Study of Diabetes (EASD). Unidade: IQ
Subjects: APOPTOSE, DIABETES MELLITUS, RETÍCULO ENDOPLASMÁTICO, PROTEÍNAS DO CHOQUE TÉRMICO
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ABNT
LABRIOLA, Leticia et al. HSPB1 is essential for inducing resistance to proteotoxic stress in beta cells. Diabetologia. New York: Instituto de Química, Universidade de São Paulo. . Acesso em: 07 nov. 2024. , 2020
APA
Labriola, L., Gomes, V. M., Wailemann, R. A. M., Almeida, D. R. Q. de, Arini, G. S., Santos, A. F. dos, et al. (2020). HSPB1 is essential for inducing resistance to proteotoxic stress in beta cells. Diabetologia. New York: Instituto de Química, Universidade de São Paulo.
NLM
Labriola L, Gomes VM, Wailemann RAM, Almeida DRQ de, Arini GS, Santos AF dos, Terra LF, Lortz S. HSPB1 is essential for inducing resistance to proteotoxic stress in beta cells. Diabetologia. 2020 ; 63 S184-S185 res. 372.[citado 2024 nov. 07 ]
Vancouver
Labriola L, Gomes VM, Wailemann RAM, Almeida DRQ de, Arini GS, Santos AF dos, Terra LF, Lortz S. HSPB1 is essential for inducing resistance to proteotoxic stress in beta cells. Diabetologia. 2020 ; 63 S184-S185 res. 372.[citado 2024 nov. 07 ]
Artigo de periodico
Mice born to females with oocytespecific deletion of mitofusin 2 have increased weight gain and impaired glucose homeostasis (2020)
Garcia, Bruna M. ; Machado, Thiago Simões; Carvalho, Karen F.; Nolasco, Patrícia ; Nociti, Ricardo Perecin ; Del Collado, Maite Barrondo ; Bianco, Maria J. D. Capo ; Grejo, Mateus P.; Augustro Neto, José Djaci Augusto ; Sugiyama, Fabrícia H. C. ; Tostes, Katiane ; Pandey, Anand K. ; Gonçalves, Luciana M.; Perecin, Felipe ; Meirelles, Flávio Vieira ; Ferraz, José Bento Sterman ; Vanzela, Emerielle C.; Boschero, Antônio C. ; Guimarães, Francisco Eduardo Gontijo ; Abdulkader, Fernando Rodrigues de Moraes ; Laurindo, Francisco R. M; Kowaltowski, Alicia Juliana ; Chiaratti, Marcos Roberto
Source: Molecular Human Reproduction. Unidades: FZEA, IFSC, ICB, IQ, IB
Subjects: MITOCÔNDRIAS, OBESIDADE, DIABETES MELLITUS, FISIOLOGIA, INSULINA, OÓCITOS, DOENÇAS METABÓLICAS, RETÍCULO ENDOPLASMÁTICO, CAMUNDONGOS, GLICOSE, HOMEOSTASE
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ABNT
GARCIA, Bruna M. et al. Mice born to females with oocytespecific deletion of mitofusin 2 have increased weight gain and impaired glucose homeostasis. Molecular Human Reproduction, v. 26, n. 12, p. 938-952 + supplementary data, 2020Tradução . . Disponível em: https://doi.org/10.1093/molehr/gaaa071. Acesso em: 07 nov. 2024.
APA
Garcia, B. M., Machado, T. S., Carvalho, K. F., Nolasco, P., Nociti, R. P., Del Collado, M. B., et al. (2020). Mice born to females with oocytespecific deletion of mitofusin 2 have increased weight gain and impaired glucose homeostasis. Molecular Human Reproduction, 26( 12), 938-952 + supplementary data. doi:10.1093/molehr/gaaa071
NLM
Garcia BM, Machado TS, Carvalho KF, Nolasco P, Nociti RP, Del Collado MB, Bianco MJDC, Grejo MP, Augustro Neto JDA, Sugiyama FHC, Tostes K, Pandey AK, Gonçalves LM, Perecin F, Meirelles FV, Ferraz JBS, Vanzela EC, Boschero AC, Guimarães FEG, Abdulkader FR de M, Laurindo FRM, Kowaltowski AJ, Chiaratti MR. Mice born to females with oocytespecific deletion of mitofusin 2 have increased weight gain and impaired glucose homeostasis [Internet]. Molecular Human Reproduction. 2020 ; 26( 12): 938-952 + supplementary data.[citado 2024 nov. 07 ] Available from: https://doi.org/10.1093/molehr/gaaa071
Vancouver
Garcia BM, Machado TS, Carvalho KF, Nolasco P, Nociti RP, Del Collado MB, Bianco MJDC, Grejo MP, Augustro Neto JDA, Sugiyama FHC, Tostes K, Pandey AK, Gonçalves LM, Perecin F, Meirelles FV, Ferraz JBS, Vanzela EC, Boschero AC, Guimarães FEG, Abdulkader FR de M, Laurindo FRM, Kowaltowski AJ, Chiaratti MR. Mice born to females with oocytespecific deletion of mitofusin 2 have increased weight gain and impaired glucose homeostasis [Internet]. Molecular Human Reproduction. 2020 ; 26( 12): 938-952 + supplementary data.[citado 2024 nov. 07 ] Available from: https://doi.org/10.1093/molehr/gaaa071
Artigo de periodico
Calcium signalling: a common target in neurological disorders and neurogenesis (2019)
Glaser, Talita ; Sampaio, Vanessa Fernandes Arnaud ; Lameu, Claudiana ; Ulrich, Henning
Source: Seminars in Cell and Developmental Biology. Unidade: IQ
Subjects: DOENÇA DE ALZHEIMER, DOENÇA DE PARKINSON, CÉLULAS-TRONCO, RETÍCULO ENDOPLASMÁTICO
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ABNT
GLASER, Talita et al. Calcium signalling: a common target in neurological disorders and neurogenesis. Seminars in Cell and Developmental Biology, v. 95, p. 25-33, 2019Tradução . . Disponível em: https://doi.org/10.1016/j.semcdb.2018.12.002. Acesso em: 07 nov. 2024.
APA
Glaser, T., Sampaio, V. F. A., Lameu, C., & Ulrich, H. (2019). Calcium signalling: a common target in neurological disorders and neurogenesis. Seminars in Cell and Developmental Biology, 95, 25-33. doi:10.1016/j.semcdb.2018.12.002
NLM
Glaser T, Sampaio VFA, Lameu C, Ulrich H. Calcium signalling: a common target in neurological disorders and neurogenesis [Internet]. Seminars in Cell and Developmental Biology. 2019 ; 95 25-33.[citado 2024 nov. 07 ] Available from: https://doi.org/10.1016/j.semcdb.2018.12.002
Vancouver
Glaser T, Sampaio VFA, Lameu C, Ulrich H. Calcium signalling: a common target in neurological disorders and neurogenesis [Internet]. Seminars in Cell and Developmental Biology. 2019 ; 95 25-33.[citado 2024 nov. 07 ] Available from: https://doi.org/10.1016/j.semcdb.2018.12.002
Trabalho de evento-resumo
HSPB1 protects beta-cells against endoplasmic reticulum (ER) stress-induced apoptosis and modulates the unfolded protein response (2017)
Gomes, Vinícius de Maron; Mansano, Rosangela Aparecida Wailemann; Terra, Letícia Ferreira; Oliveira, Talita Cristina de; Santos, Ancély Ferreira dos; Labriola, Leticia
Source: Abstracts. Conference titles: Annual Meeting of the Brazilian Society for Biochemistry and Molecular Biology. Unidade: IQ
Subjects: APOPTOSE, RETÍCULO ENDOPLASMÁTICO
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ABNT
GOMES, Vinícius de Maron et al. HSPB1 protects beta-cells against endoplasmic reticulum (ER) stress-induced apoptosis and modulates the unfolded protein response. 2017, Anais.. São Paulo: Sociedade Brasileira de Bioquímica e Biologia Molecular/SBBq, 2017. . Acesso em: 07 nov. 2024.
APA
Gomes, V. de M., Mansano, R. A. W., Terra, L. F., Oliveira, T. C. de, Santos, A. F. dos, & Labriola, L. (2017). HSPB1 protects beta-cells against endoplasmic reticulum (ER) stress-induced apoptosis and modulates the unfolded protein response. In Abstracts. São Paulo: Sociedade Brasileira de Bioquímica e Biologia Molecular/SBBq.
NLM
Gomes V de M, Mansano RAW, Terra LF, Oliveira TC de, Santos AF dos, Labriola L. HSPB1 protects beta-cells against endoplasmic reticulum (ER) stress-induced apoptosis and modulates the unfolded protein response. Abstracts. 2017 ;[citado 2024 nov. 07 ]
Vancouver
Gomes V de M, Mansano RAW, Terra LF, Oliveira TC de, Santos AF dos, Labriola L. HSPB1 protects beta-cells against endoplasmic reticulum (ER) stress-induced apoptosis and modulates the unfolded protein response. Abstracts. 2017 ;[citado 2024 nov. 07 ]
Trabalho de evento-resumo
The endoplasmic reticulum chaperone protein disulfide isomerase (PDII) is required for PDGF-induced RhoGTPase activation and Nox1 NADPH oxidase-dependent vascular smooth muscle cell migration (2012)
Pescatore, L. A; Bonatto, Diego; Forti, Fabio Luis ; Sadok, Amin; Kovacic, Herve; Laurindo, Francisco Rafael Martins
Source: Abstracts. Conference titles: International Congress on Cell Biology. Unidade: IQ
Subjects: RETÍCULO ENDOPLASMÁTICO, PROTEÍNAS
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ABNT
PESCATORE, L. A et al. The endoplasmic reticulum chaperone protein disulfide isomerase (PDII) is required for PDGF-induced RhoGTPase activation and Nox1 NADPH oxidase-dependent vascular smooth muscle cell migration. 2012, Anais.. São Paulo: Sociedade Brasileira de Biologia Celular (SBBC), 2012. . Acesso em: 07 nov. 2024.
APA
Pescatore, L. A., Bonatto, D., Forti, F. L., Sadok, A., Kovacic, H., & Laurindo, F. R. M. (2012). The endoplasmic reticulum chaperone protein disulfide isomerase (PDII) is required for PDGF-induced RhoGTPase activation and Nox1 NADPH oxidase-dependent vascular smooth muscle cell migration. In Abstracts. São Paulo: Sociedade Brasileira de Biologia Celular (SBBC).
NLM
Pescatore LA, Bonatto D, Forti FL, Sadok A, Kovacic H, Laurindo FRM. The endoplasmic reticulum chaperone protein disulfide isomerase (PDII) is required for PDGF-induced RhoGTPase activation and Nox1 NADPH oxidase-dependent vascular smooth muscle cell migration. Abstracts. 2012 ;[citado 2024 nov. 07 ]
Vancouver
Pescatore LA, Bonatto D, Forti FL, Sadok A, Kovacic H, Laurindo FRM. The endoplasmic reticulum chaperone protein disulfide isomerase (PDII) is required for PDGF-induced RhoGTPase activation and Nox1 NADPH oxidase-dependent vascular smooth muscle cell migration. Abstracts. 2012 ;[citado 2024 nov. 07 ]
Artigo de periodico
The promoter of filamentation (POF1) protein from Saccharomyces cerevisiae is an ATPase involved in the protein quality control process (2011)
Costa, Iris Munhoz; Nasser, Tallybia H. T; Demasi, Marilene; Nascimento, Rafaella Maria Pessutti; Netto, Luis Eduardo Soares ; Miyamoto, Sayuri ; Prado, Fernanda Manso ; Monteiro, Gisele
Source: BMC Microbiology. Unidades: IB, IQ
Subjects: RETÍCULO ENDOPLASMÁTICO, SACCHAROMYCES
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ABNT
COSTA, Iris Munhoz et al. The promoter of filamentation (POF1) protein from Saccharomyces cerevisiae is an ATPase involved in the protein quality control process. BMC Microbiology, v. 11, p. 1-11, 2011Tradução . . Disponível em: https://doi.org/10.1186/1471-2180-11-268. Acesso em: 07 nov. 2024.
APA
Costa, I. M., Nasser, T. H. T., Demasi, M., Nascimento, R. M. P., Netto, L. E. S., Miyamoto, S., et al. (2011). The promoter of filamentation (POF1) protein from Saccharomyces cerevisiae is an ATPase involved in the protein quality control process. BMC Microbiology, 11, 1-11. doi:10.1186/1471-2180-11-268
NLM
Costa IM, Nasser THT, Demasi M, Nascimento RMP, Netto LES, Miyamoto S, Prado FM, Monteiro G. The promoter of filamentation (POF1) protein from Saccharomyces cerevisiae is an ATPase involved in the protein quality control process [Internet]. BMC Microbiology. 2011 ; 11 1-11.[citado 2024 nov. 07 ] Available from: https://doi.org/10.1186/1471-2180-11-268
Vancouver
Costa IM, Nasser THT, Demasi M, Nascimento RMP, Netto LES, Miyamoto S, Prado FM, Monteiro G. The promoter of filamentation (POF1) protein from Saccharomyces cerevisiae is an ATPase involved in the protein quality control process [Internet]. BMC Microbiology. 2011 ; 11 1-11.[citado 2024 nov. 07 ] Available from: https://doi.org/10.1186/1471-2180-11-268
Artigo de periodico
Expression of genes encoding cytosolic and endoplasmic reticulum HSP90 proteins in the aquatic fungus Blastocladiella emersonii (2008)
Pugliese, Luciana; Georg, Raphaela de Castro; Fietto, Luciano Gomes; Gomes, Suely Lopes
Source: Gene. Unidade: IQ
Subjects: EXPRESSÃO GÊNICA, RETÍCULO ENDOPLASMÁTICO
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ABNT
PUGLIESE, Luciana et al. Expression of genes encoding cytosolic and endoplasmic reticulum HSP90 proteins in the aquatic fungus Blastocladiella emersonii. Gene, v. 411, n. 1-2, p. 59-68, 2008Tradução . . Disponível em: https://doi.org/10.1016/j.gene.2008.01.005. Acesso em: 07 nov. 2024.
APA
Pugliese, L., Georg, R. de C., Fietto, L. G., & Gomes, S. L. (2008). Expression of genes encoding cytosolic and endoplasmic reticulum HSP90 proteins in the aquatic fungus Blastocladiella emersonii. Gene, 411( 1-2), 59-68. doi:10.1016/j.gene.2008.01.005
NLM
Pugliese L, Georg R de C, Fietto LG, Gomes SL. Expression of genes encoding cytosolic and endoplasmic reticulum HSP90 proteins in the aquatic fungus Blastocladiella emersonii [Internet]. Gene. 2008 ;411( 1-2): 59-68.[citado 2024 nov. 07 ] Available from: https://doi.org/10.1016/j.gene.2008.01.005
Vancouver
Pugliese L, Georg R de C, Fietto LG, Gomes SL. Expression of genes encoding cytosolic and endoplasmic reticulum HSP90 proteins in the aquatic fungus Blastocladiella emersonii [Internet]. Gene. 2008 ;411( 1-2): 59-68.[citado 2024 nov. 07 ] Available from: https://doi.org/10.1016/j.gene.2008.01.005
Artigo de periodico
Searching for the ligands of odorant receptors (2007)
Malnic, Bettina
Source: Molecular Neurobiology. Unidade: IQ
Subjects: RETÍCULO ENDOPLASMÁTICO, LIGANTES
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ABNT
MALNIC, Bettina. Searching for the ligands of odorant receptors. Molecular Neurobiology, v. 35, n. 2, p. 175-181, 2007Tradução . . Acesso em: 07 nov. 2024.
APA
Malnic, B. (2007). Searching for the ligands of odorant receptors. Molecular Neurobiology, 35( 2), 175-181.
NLM
Malnic B. Searching for the ligands of odorant receptors. Molecular Neurobiology. 2007 ;35( 2): 175-181.[citado 2024 nov. 07 ]
Vancouver
Malnic B. Searching for the ligands of odorant receptors. Molecular Neurobiology. 2007 ;35( 2): 175-181.[citado 2024 nov. 07 ]
Trabalho de evento-resumo
Functional consequences of alteractions to W854 and W855 located in the M7-M8 loop of the 'CA POT. 2+'-ATPase of sarcoplasmic reticulum (2007)
Carreira, Ana Claudia Oliveira; Verjovski-Almeida, Sergio
Source: Abstracts. Conference titles: Reunião Anual da Sociedade Brasileira de Bioquímica e Biologia Molecular. Unidade: IQ
Subjects: RETÍCULO ENDOPLASMÁTICO, BIOQUÍMICA
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ABNT
CARREIRA, Ana Claudia Oliveira e VERJOVSKI-ALMEIDA, Sergio. Functional consequences of alteractions to W854 and W855 located in the M7-M8 loop of the 'CA POT. 2+'-ATPase of sarcoplasmic reticulum. 2007, Anais.. São Paulo: SBBq, 2007. . Acesso em: 07 nov. 2024.
APA
Carreira, A. C. O., & Verjovski-Almeida, S. (2007). Functional consequences of alteractions to W854 and W855 located in the M7-M8 loop of the 'CA POT. 2+'-ATPase of sarcoplasmic reticulum. In Abstracts. São Paulo: SBBq.
NLM
Carreira ACO, Verjovski-Almeida S. Functional consequences of alteractions to W854 and W855 located in the M7-M8 loop of the 'CA POT. 2+'-ATPase of sarcoplasmic reticulum. Abstracts. 2007 ;[citado 2024 nov. 07 ]
Vancouver
Carreira ACO, Verjovski-Almeida S. Functional consequences of alteractions to W854 and W855 located in the M7-M8 loop of the 'CA POT. 2+'-ATPase of sarcoplasmic reticulum. Abstracts. 2007 ;[citado 2024 nov. 07 ]
Artigo de periodico
N-terminal chimeric constructs improve the expression of sarcoplasmic reticulum `Ca POT. 2+´-ATPase in yeast (1999)
Reis, Eduardo Moraes ; Kurtenbach, Eleonora; Ferreira, Alessandra R.; Biselli, Paolo J. C.; Slayman, Carolyn W.; Verjovski-Almeida, Sergio
Source: Biochimica et Biophysica Acta. Unidade: IQ
Subjects: BIOQUÍMICA, RETÍCULO ENDOPLASMÁTICO
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ABNT
REIS, Eduardo Moraes et al. N-terminal chimeric constructs improve the expression of sarcoplasmic reticulum `Ca POT. 2+´-ATPase in yeast. Biochimica et Biophysica Acta, v. 1461, n. 1, p. 83-95, 1999Tradução . . Disponível em: https://doi.org/10.1016/s0005-2736(99)00151-0. Acesso em: 07 nov. 2024.
APA
Reis, E. M., Kurtenbach, E., Ferreira, A. R., Biselli, P. J. C., Slayman, C. W., & Verjovski-Almeida, S. (1999). N-terminal chimeric constructs improve the expression of sarcoplasmic reticulum `Ca POT. 2+´-ATPase in yeast. Biochimica et Biophysica Acta, 1461( 1), 83-95. doi:10.1016/s0005-2736(99)00151-0
NLM
Reis EM, Kurtenbach E, Ferreira AR, Biselli PJC, Slayman CW, Verjovski-Almeida S. N-terminal chimeric constructs improve the expression of sarcoplasmic reticulum `Ca POT. 2+´-ATPase in yeast [Internet]. Biochimica et Biophysica Acta. 1999 ; 1461( 1): 83-95.[citado 2024 nov. 07 ] Available from: https://doi.org/10.1016/s0005-2736(99)00151-0
Vancouver
Reis EM, Kurtenbach E, Ferreira AR, Biselli PJC, Slayman CW, Verjovski-Almeida S. N-terminal chimeric constructs improve the expression of sarcoplasmic reticulum `Ca POT. 2+´-ATPase in yeast [Internet]. Biochimica et Biophysica Acta. 1999 ; 1461( 1): 83-95.[citado 2024 nov. 07 ] Available from: https://doi.org/10.1016/s0005-2736(99)00151-0
Artigo de periodico
Effect of insulin on the synthesis of rat liver ribosomal and endoplasmic reticulum proteins (1985)
Raw, I; Juliani, M H; Rocha, M C; Maia, J C C
Source: Brazilian Journal of Medical and Biological Research. Unidade: IQ
Subjects: INSULINA, RETÍCULO ENDOPLASMÁTICO
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ABNT
RAW, I et al. Effect of insulin on the synthesis of rat liver ribosomal and endoplasmic reticulum proteins. Brazilian Journal of Medical and Biological Research, v. 18, n. 4 , p. 421-6, 1985Tradução . . Acesso em: 07 nov. 2024.
APA
Raw, I., Juliani, M. H., Rocha, M. C., & Maia, J. C. C. (1985). Effect of insulin on the synthesis of rat liver ribosomal and endoplasmic reticulum proteins. Brazilian Journal of Medical and Biological Research, 18( 4 ), 421-6.
NLM
Raw I, Juliani MH, Rocha MC, Maia JCC. Effect of insulin on the synthesis of rat liver ribosomal and endoplasmic reticulum proteins. Brazilian Journal of Medical and Biological Research. 1985 ;18( 4 ): 421-6.[citado 2024 nov. 07 ]
Vancouver
Raw I, Juliani MH, Rocha MC, Maia JCC. Effect of insulin on the synthesis of rat liver ribosomal and endoplasmic reticulum proteins. Brazilian Journal of Medical and Biological Research. 1985 ;18( 4 ): 421-6.[citado 2024 nov. 07 ]

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