References analysis of the Wikipedia article "MTOR" in the Portuguese version

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Sabers CJ, Martin MM, Brunn GJ, Williams JM, Dumont FJ, Wiederrecht G, Abraham RT (Jan 1995). «Isolation of a Protein Target of the FKBP12-Rapamycin Complex in Mammalian Cells». J. Biol. Chem. 270 (2): 815–22. PMID 7822316. doi:10.1074/jbc.270.2.815

Brown EJ, Albers MW, Shin TB, Ichikawa K, Keith CT, Lane WS, Schreiber SL (Junho de 1994). «A mammalian protein targeted by G1-arresting rapamycin-receptor complex». Nature. 369 (6483): 756–8. Bibcode:1994Natur.369..756B. PMID 8008069. doi:10.1038/369756a0

Sabatini DM, Erdjument-Bromage H, Lui M, Tempst P, Snyder SH (Julho de 1994). «RAFT1: a mammalian protein that binds to FKBP12 in a rapamycin-dependent fashion and is homologous to yeast TORs». Cell. 78 (1): 35–43. PMID 7518356. doi:10.1016/0092-8674(94)90570-3

Sabers CJ, Martin MM, Brunn GJ, Williams JM, Dumont FJ, Wiederrecht G, Abraham RT (Janeiro de 1995). «Isolation of a protein target of the FKBP12-rapamycin complex in mammalian cells». The Journal of Biological Chemistry. 270 (2): 815–22. PMID 7822316. doi:10.1074/jbc.270.2.815

Mitra A, Luna JI, Marusina AI, Merleev A, Kundu-Raychaudhuri S, Fiorentino D, Raychaudhuri SP, Maverakis E (Novembro de 2015). «Dual mTOR Inhibition Is Required to Prevent TGF-β-Mediated Fibrosis: Implications for Scleroderma». The Journal of Investigative Dermatology. 135 (11): 2873–6. PMC 4640976

. PMID 26134944. doi:10.1038/jid.2015.252

Lipton JO, Sahin M (Outubro de 2014). «The neurology of mTOR». Neuron. 84 (2): 275–291. PMC 4223653

. PMID 25374355. doi:10.1016/j.neuron.2014.09.034. A via de sinalização mTOR atua como um integrador de sistemas moleculares para apoiar as interações celulares e do organismo com o ambiente. A via da mTOR regula a homeostase influenciando diretamente a síntese de proteínas, a transcrição, a autofagia, o metabolismo e a biogênese e manutenção de organelas. Não é de surpreender, portanto, que a sinalização mTOR esteja envolvida em toda a hierarquia da função cerebral, incluindo a proliferação de células-tronco neurais, a montagem e a manutenção de circuitos, a plasticidade dependente da experiência e a regulação de comportamentos complexos como alimentação, sono e ritmos circadianos...
A função da mTOR é mediada por dois grandes complexos bioquímicos definidos por sua respectiva composição proteica e foram amplamente revisados em outros lugares (Dibble e Manning, 2013; Laplante e Sabatini, 2012 - Figura 1B). Em resumo, são comuns ao complexo mTOR 1 (mTORC1) e ao complexo mTOR 2 (mTORC2): o próprio mTOR, a proteína 8 letal de mamíferos com sec13 (mLST8; também conhecida como GβL) e a proteína de interação com mTOR contendo domínio DEP inibitório (DEPTOR). Específica para mTORC1 é a proteína associada ao regulador do alvo de rapamicina em mamíferos (Raptor) e substrato de Akt rico em prolina de 40 kDa (PRAS40) (Kim et al., 2002; Laplante e Sabatini, 2012). O Raptor é essencial para a atividade do mTORC1. O complexo mTORC2 inclui o companheiro insensível à rapamicina do mTOR (Rictor), a proteína 1 (mSIN1) que interage com a MAP quinase ativada por estresse em mamíferos e as proteínas observadas com o rictor 1 e 2 (PROTOR 1 e 2) (Jacinto et al., 2006; Jacinto et al., 2004; Pearce et al., 2007; Sarbassov et al., 2004 - Figura 1B). Rictor e mSIN1 são essenciais para a função de mTORC2. Figure 1: Domain structure of the mTOR kinase and components of mTORC1 and mTORC2 Figure 2: The mTOR Signaling Pathway

Hay N, Sonenberg N (Agosto de 2004). «Upstream and downstream of mTOR». Genes & Development. 18 (16): 1926–45. PMID 15314020. doi:10.1101/gad.1212704

Yin Y, Hua H, Li M, Liu S, Kong Q, Shao T, Wang J, Luo Y, Wang Q, Luo T, Jiang Y (Janeiro de 2016). «mTORC2 promotes type I insulin-like growth factor receptor and insulin receptor activation through the tyrosine kinase activity of mTOR». Cell Research. 26 (1): 46–65. PMC 4816127

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Jacinto E, Loewith R, Schmidt A, Lin S, Rüegg MA, Hall A, Hall MN (Novembro de 2004). «Mammalian TOR complex 2 controls the actin cytoskeleton and is rapamycin insensitive». Nature Cell Biology. 6 (11): 1122–8. PMID 15467718. doi:10.1038/ncb1183

Sehgal, S. N.; Baker, H.; VéZina, Claude (1975). «Rapamycin (AY-22,989), a new antifungal antibiotic. II. Fermentation, isolation and characterization.». The Journal of Antibiotics (em inglês). 28 (10): 727–732. ISSN 0021-8820. doi:10.7164/antibiotics.28.727

Powers, Ted (1 de novembro de 2022). Kellogg, Doug, ed. «The origin story of rapamycin: systemic bias in biomedical research and cold war politics». Molecular Biology of the Cell (em inglês). 33 (13). ISSN 1059-1524. PMID 36228182. doi:10.1091/mbc.E22-08-0377

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Cafferkey R, Young PR, McLaughlin MM, Bergsma DJ, Koltin Y, Sathe GM, Faucette L, Eng WK, Johnson RK, Livi GP (Outubro de 1993). «Dominant missense mutations in a novel yeast protein related to mammalian phosphatidylinositol 3-kinase and VPS34 abrogate rapamycin cytotoxicity». Mol Cell Biol. 13 (10): 6012–23. PMC 364661

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Abraham RT, Wiederrecht GJ (1996). «Immunopharmacology of rapamycin». Annual Review of Immunology. 14: 483–510. PMID 8717522. doi:10.1146/annurev.immunol.14.1.483

Bierer BE, Mattila PS, Standaert RF, Herzenberg LA, Burakoff SJ, Crabtree G, Schreiber SL (Dezembro de 1990). «Two distinct signal transmission pathways in T lymphocytes are inhibited by complexes formed between an immunophilin and either FK506 or rapamycin». Proceedings of the National Academy of Sciences of the United States of America. 87 (23): 9231–5. Bibcode:1990PNAS...87.9231B. PMC 55138

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Dumont FJ, Melino MR, Staruch MJ, Koprak SL, Fischer PA, Sigal NH (Fevereiro de 1990). «The immunosuppressive macrolides FK-506 and rapamycin act as reciprocal antagonists in murine T cells». J Immunol. 144 (4): 1418–24. PMID 1689353. doi:10.4049/jimmunol.144.4.1418

Dumont FJ, Staruch MJ, Koprak SL, Melino MR, Sigal NH (Janeiro de 1990). «Distinct mechanisms of suppression of murine T cell activation by the related macrolides FK-506 and rapamycin». J Immunol. 144 (1): 251–8. PMID 1688572. doi:10.4049/jimmunol.144.1.251

Harding MW, Galat A, Uehling DE, Schreiber SL (Outubro de 1989). «A receptor for the immunosuppressant FK506 is a cis-trans peptidyl-prolyl isomerase». Nature. 341 (6244): 758–60. Bibcode:1989Natur.341..758H. PMID 2477715. doi:10.1038/341758a0

Fretz H, Albers MW, Galat A, Standaert RF, Lane WS, Burakoff SJ, Bierer BE, Schreiber SL (Fevereiro de 1991). «Rapamycin and FK506 binding proteins (immunophilins)». Journal of the American Chemical Society. 113 (4): 1409–1411. doi:10.1021/ja00004a051

Liu J, Farmer JD, Lane WS, Friedman J, Weissman I, Schreiber SL (Agosto de 1991). «Calcineurin is a common target of cyclophilin-cyclosporin A and FKBP-FK506 complexes». Cell. 66 (4): 807–15. PMID 1715244. doi:10.1016/0092-8674(91)90124-H

Heitman J (Novembro de 2015). «On the discovery of TOR as the target of rapamycin». PLOS Pathogens. 11 (11): e1005245. PMC 4634758

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Kennedy BK, Lamming DW (2016). «The Mechanistic Target of Rapamycin: The Grand ConducTOR of Metabolism and Aging». Cell Metabolism. 23 (6): 990–1003. PMC 4910876

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Tokunaga C, Yoshino K, Yonezawa K (Janeiro de 2004). «mTOR integrates amino acid- and energy-sensing pathways». Biochemical and Biophysical Research Communications. 313 (2): 443–6. PMID 14684182. doi:10.1016/j.bbrc.2003.07.019

Wipperman MF, Montrose DC, Gotto AM, Hajjar DP (2019). «Mammalian Target of Rapamycin: A Metabolic Rheostat for Regulating Adipose Tissue Function and Cardiovascular Health». The American Journal of Pathology. 189 (3): 492–501. PMC 6412382

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Beevers CS, Li F, Liu L, Huang S (Agosto de 2006). «Curcumin inhibits the mammalian target of rapamycin-mediated signaling pathways in cancer cells». International Journal of Cancer. 119 (4): 757–64. PMID 16550606. doi:10.1002/ijc.21932

Kennedy BK, Lamming DW (Junho de 2016). «The Mechanistic Target of Rapamycin: The Grand ConducTOR of Metabolism and Aging». Cell Metabolism. 23 (6): 990–1003. PMC 4910876

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Ingargiola C, Turqueto Duarte G, Robaglia C, Leprince AS, Meyer C (Outubro de 2020). «The Plant Target of Rapamycin: A Conduc TOR of Nutrition and Metabolism in Photosynthetic Organisms». Genes. 11 (11). 1285 páginas. PMC 7694126

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Shi L, Wu Y, Sheen J (Julho de 2018). «TOR signaling in plants: conservation and innovation». Development. 145 (13). PMC 6053665

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Betz C, Hall MN (Novembro de 2013). «Where is mTOR and what is it doing there?». The Journal of Cell Biology. 203 (4): 563–74. PMC 3840941

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Groenewoud MJ, Zwartkruis FJ (Agosto de 2013). «Rheb and Rags come together at the lysosome to activate mTORC1». Biochemical Society Transactions. 41 (4): 951–5. PMID 23863162. doi:10.1042/bst20130037

Efeyan A, Zoncu R, Sabatini DM (Setembro de 2012). «Amino acids and mTORC1: from lysosomes to disease». Trends in Molecular Medicine. 18 (9): 524–33. PMC 3432651

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Kim DH, Sarbassov DD, Ali SM, King JE, Latek RR, Erdjument-Bromage H, Tempst P, Sabatini DM (Julho de 2002). «mTOR interacts with raptor to form a nutrient-sensitive complex that signals to the cell growth machinery». Cell. 110 (2): 163–75. PMID 12150925. doi:10.1016/S0092-8674(02)00808-5

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dx.doi.org

doi.org

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