Registro:

Referencias:

• Chock, P.B., Stadtman, E.R., Covalently interconvertible enzyme cascade systems, Methods (1980) Enzymol., 64, pp. 325-397
• Helmreich, E., (2001) The Biochemistry of Cell Signalling, , Oxford University Press, Oxford, U.K
• Nollen, E.A., Morimoto, R.I., Chaperoning signaling pathways: Molecular chaperones as stress-sensing 'heat shock' proteins (2002) J. Cell. Sci., 115, pp. 2809-2816
• Kang, C.B., Hong, Y., Dhe-Paganon, S., Yoon, H.S., FKBP family proteins: Immunophilins with versatile biological functions (2008) Neurosignals, 16, pp. 318-325
• Rahfeld, J.U., Rucknagel, K.P., Schelbert, B., Ludwig, B., Hacker, J., Mann, K., Fischer, G., Confirmation of the existence of a third family among peptidyl-prolyl cis/trans isomerases. Amino acid sequence and recombinant production of parvulin (1994) FEBS Lett., 352, pp. 180-184
• Li, H., Rao, A., Hogan, P.G., Interaction of calcineurin with substrates and targeting proteins (2011) Trends. Cell.Biol., 21, pp. 91-103
• Callebaut, I., Renoir, J.M., Lebeau, M.C., Massol, N., Burny, A., Baulieu, E.E., Mornon, J.P., An immunophilin that binds M(R) 90,000 heat shock protein: Main structural features of a mammalian p59 protein (1992) Proc. Natl. Acad. Sci.U S A., 89, pp. 6270-6274
• Smith, D.F., Tetratricopeptide repeat cochaperones in steroid receptor complexes, Cell. Stress (2004) Chaperones., 9, pp. 109-121
• Aviezer-Hagai, K., Skovorodnikova, J., Galigniana, M., Farchi-Pisanty, O., Maayan, E., Bocovza, S., Efrat, Y., Breiman, A., Arabidopsis immunophilins ROF1 (AtFKBP62) and ROF2 (AtFKBP65) exhibit tissue specificity, are heat-stress induced, and bind HSP90 (2007) Plant. Mol. Biol., 63, pp. 237-255
• Ma, Q., Whitlock, J.P., A novel cytoplasmic protein that interacts with the Ah receptor, contains tetratricopeptide repeat motifs, and augments the transcriptional response to 2,3,7,8-tetrachlorodibenzo-p-dioxin (1997) J.Biol. Chem., 272, pp. 8878-8884
• Carver, L.A., Bradfield, C.A., Ligand-dependent interaction of the aryl hydrocarbon receptor with a novel immunophilin homolog in vivo (1997) J. Biol.Chem., 272, pp. 11452-11456
• Sumanasekera, W.K., Tien, E.S., Turpey, R., Vanden Heuvel, J.P., Perdew, G.H., Evidence that peroxisome proliferator-activated receptor alpha is complexed with the 90-kDa heat shock protein and the hepatitis virus B X-associated protein 2 (2003) J. Biol.Chem, 278, pp. 4467-4473
• Hiukka, A., Maranghi, M., Matikainen, N., Taskinen, M.R., PPARalpha: An emerging therapeutic target in diabetic microvascular damage (2010) Nat. Rev. Endocrinol., 6, pp. 454-463
• Edlich, F., Lucke, C., From cell death to viral replication: The diverse functions of the membrane-associated FKBP38 (2011) Curr. Opin. Pharmacol., 11, pp. 348-353
• Shirane, M., Nakayama, K.I., Inherent calcineurin inhibitor FKBP38 targets Bcl-2 to mitochondria and inhibits apoptosis (2003) Nat. Cell. Biol., 5, pp. 28-37
• Hoi, B.H.C., Yoon, H.S., FKBP38-Bcl-2 interaction: A novel link to chemoresistance (2011) Curr. Opin. Pharmacol., pp. 11354-11359
• Crackower, M.A., Kolas, N.K., Noguchi, J., Sarao, R., Kikuchi, K., Kaneko, H., Kobayashi, E., Penninger, J.M., Essential role of Fkbp6 in male fertility and homologous chromosome pairing in meiosis (2003) Science, 300, pp. 1291-1295
• Jarczowski, F., Jahreis, G., Erdmann, F., Schierhorn, A., Fischer, G., Edlich, F., FKBP36 is an inherent multifunctional glyceraldehyde-3-phosphate dehydrogenase inhibitor (2009) J. Biol. Chem., 284, pp. 766-773
• Rahfeld, J.U., Schierhorn, A., Mann, K., Fischer, G., A novel peptidyl-prolyl cis/trans isomerase from Escherichia coli (1994) FEBS Lett., 343, pp. 65-69
• Gothel, S.F., Marahiel, M.A., Peptidyl-prolyl cis-trans isomerases, a superfamily of ubiquitous folding catalysts (1999) Cell. Mol. Life. Sci., 55, pp. 423-436
• Lu, K.P., Zhou, X.Z., The prolyl isomerase PIN1: A pivotal new twist in phosphorylation signalling and disease (2007) Nat. Rev. Mol.Cell Biol., 8, pp. 904-916
• Lin, C.H., Li, H.Y., Lee, Y.C., Calkins, M.J., Lee, K.H., Yang, C.N., Lu, P.J., Landscape of Pin1 in the cell cycle (2015) Exp. Biol. Med, 240 (3), pp. 403-408
• Theuerkorn, M., Fischer, G., Schiene-Fischer, C., Prolyl cis/trans isomerase signalling pathways in cancer (2011) Curr. Opin. Pharmacol., 11, pp. 281-287
• Lee, T.H., Pastorino, M.L., Lu, K.P., Peptidyl-prolyl cis-trans isomerase Pin1 in ageing, cancer and Alzheimer disease (2011) Expert Rev.Mol. Med., p. 13
• Dong, L., Marakovits, J., Hou, X., Guo, C., Greasley, S., Dagostino, E., Ferre, R., Murray, B.W., Structure-based design of novel human Pin1 inhibitors (II) (2010) Bioorg. Med. Chem.Lett., 20, pp. 2210-2214
• Liu, C., Jin, J., Chen, L., Zhou, J., Chen, X., Fu, D., Song, H., Xu, B., Synthesis and biological evaluation of novel human Pin1 inhibitors with benzophenone skeleton. (2012) Bioorg. Med. Chem., 20, pp. 2992-2999
• Napetschnig, J., Wu, H., Molecular basis of NF-kappaB signaling (2013) Annu. Rev. Biophys., 42, pp. 443-468
• Sen, R., Baltimore, D., Multiple nuclear factors interact with the immunoglobulin enhancer sequences (1986) Cell, 46, pp. 705-716
• Hoesel, B., Schmid, J., A The complexity of NF-kappaB signaling in inflammation and cancer (2013) Mol. Cancer., 12, p. 86
• Diamant, G., Dikstein, R., Transcriptional control by NF-kappaB: Elongation in focus (2013) Biochim. Biophys. Acta., 1829, pp. 937-945
• Tornatore, L., Thotakura, A.K., Bennett, J., Moretti, M., Franzoso, G., The nuclear factor kappa B signaling pathway: Integrating metabolism with inflammation (2012) Trends. Cell. Biol., 22, pp. 557-566
• Oeckinghaus, A., Ghosh, S., The NF-kappaB family of transcription factors and its regulation (2009) Cold Spring Harb Perspect Biol, p. 1
• Tam, W.F., Sen, R., IkappaB family members function by different mechanisms (2001) J. Biol. Chem., 276, pp. 7701-7704
• Zabel, U., Baeuerle, P.A., Purified human I kappa B can rapidly dissociate the complex of the NF-kappa B transcription factor with its cognate DNA (1990) Cell, 61, pp. 255-265
• Scott, M.L., Fujita, T., Liou, H.C., Nolan, G.P., Baltimore, D., The p65 subunit of NF-kappa B regulates I kappa B by two distinct mechanisms (1993) Genes. Dev, 7, pp. 1266-1276
• Hayden, M.S., Ghosh, S., Shared principles in NF-kappaB signaling (2008) Cell, 132, pp. 344-362
• Perkins, N.D., Integrating cell-signalling pathways with NFkappaB and IKK function (2007) Nat. Rev. Mol. Cell.Biol, 8, pp. 49-62
• Xiao, G., Harhaj, E.W., Sun, S.C., NF-kappaB-inducing kinase regulates the processing of NF-kappaB2 p100 (2001) Mol.Cell., 7, pp. 401-409
• Huang, T.T., Wuerzberger-Davis, S.M., Wu, Z.H., Miyamoto, S., Sequential modification of NEMO/IKKgamma by SUMO-1 and ubiquitin mediates NF-kappaB activation by genotoxic stress (2003) Cell, 115, pp. 565-576
• Huang, T.T., Kudo, N., Yoshida, M., Miyamoto, S., A nuclear export signal in the N-terminal regulatory domain of IkappaBalpha controls cytoplasmic localization of inactive NFkappaB/ IkappaBalpha complexes (2000) Proc. Natl. Acad. Sci. U S A., 97, pp. 1014-1019
• Fusco, F., Pescatore, A., Bal, E., Ghoul, A., Paciolla, M., Lioi, M.B., D'urso, M., Ursini, M.V., Alterations of the IKBKG locus and diseases: An update and a report of 13 novel mutations. Hum (2008) Mutat., 29, pp. 595-604
• Muller, C.W., Rey, F.A., Sodeoka, M., Verdine, G.L., Harrison, S.C., Structure of the NF-kappa B p50 homodimer bound to DNA (1995) Nature, 373, pp. 311-317
• Muller, C.W., Harrison, S.C., The structure of the NF-kappa B p50:DNA-complex: A starting point for analyzing the Rel family (1995) FEBS Lett., 369, pp. 113-117
• Hoffmann, A., Natoli, G.G., Ghosh, Transcriptional regulation via the NF-kappaB signaling module (2006) Oncogene, 25, pp. 6706-6716
• Gilmore, T.D., The Rel/NF-kappaB signal transduction pathway: Introduction (1999) Oncogene, 18, pp. 6842-6844
• Birbach, A., Gold, P., Binder, B.R., Hofer, E., De Martin, R., Schmid, R., J.A.; Signaling molecules of the NF-kappa B pathway shuttle constitutively between cytoplasm and nucleus (2002) J. Biol.Chem., 277, pp. 10842-10851
• Mikenberg, I., Widera, D., Kaus, A., Kaltschmidt, B., Kaltschmidt, C., Transcription factor NF-kappaB is transported to the nucleus via cytoplasmic dynein/dynactin motor complex in hippocampal neurons (2007) Plos.One., p. 2. , e589
• Elbi, C., Walker, D.A., Romero, G., Sullivan, W.P., Toft, D.O., Hager, G.L., Defranco, D.B., Molecular chaperones function as steroid receptor nuclear mobility factors (2004) Proc. Natl. Acad. Sci.U S A., 101, pp. 2876-2881
• Madan, A.P., Defranco, D.B., Bidirectional transport of glucocorticoid receptors across the nuclear envelope (1993) Proc. Natl Acad. Sci. U S A., 90, pp. 3588-3592
• Galigniana, M.D., Echeverria, P.C., Erlejman, A.G., Piwien-Pilipuk, G., Role of molecular chaperones and TPR-domain proteins in the cytoplasmic transport of steroid receptors and their passage through the nuclear pore (2010) Nucleus, 1, pp. 299-308
• Galigniana, M.D., Radanyi, C., Renoir, J.M., Housley, P.R., Pratt, W.B., Evidence that the peptidylprolyl isomerase domain of the hsp90-binding immunophilin FKBP52 is involved in both dynein interaction and glucocorticoid receptor movement to the nucleus (2001) J Biol. Chem., 276, pp. 14884-14889
• Davies, T.H., Ning, Y.M., Sanchez, E.R., A new first step in activation of steroid receptors: Hormone-induced switching of FKBP51 and FKBP52 immunophilins (2002) J. Biol. Chem., 277, pp. 4597-4600
• Galigniana, M.D., Erlejman, A.G., Monte, M., Gomez-Sanchez, C., Piwien-Pilipuk, G., The hsp90-FKBP52 complex links the mineralocorticoid receptor to motor proteins and persists bound to the receptor in early nuclear events (2010) Mol. Cell. Biol., 30, pp. 1285-1298
• Gallo, L.I., Ghini, A.A., Piwien Pilipuk, G., Galigniana, M.D., Differential recruitment of tetratricorpeptide repeat domain immunophilins to the mineralocorticoid receptor influences both heat-shock protein 90-dependent retrotransport and hormonedependent transcriptional activity (2007) Biochemistry, 46, pp. 14044-14057
• Wochnik, G.M., Ruegg, J., Abel, G.A., Schmidt, U., Holsboer, F., Rein, T., FK506-binding proteins 51 and 52 differentially regulate dynein interaction and nuclear translocation of the glucocorticoid receptor in mammalian cells (2005) J. Biol. Chem., 280, pp. 4609-4616
• Riggs, D.L., Roberts, P.J., Chirillo, S.C., Cheung-Flynn, J., Prapapanich, V., Ratajczak, T., Gaber, R., Smith, D.F., The Hsp90-binding peptidylprolyl isomerase FKBP52 potentiates glucocorticoid signaling in vivo (2003) Embo. J., 22, pp. 1158-1167
• Tranguch, S., Cheung-Flynn, J., Daikoku, T., Prapapanich, V., Cox, M.B., Xie, H., Wang, H., Dey, S.K., Cochaperone immunophilin FKBP52 is critical to uterine receptivity for embryo implantation (2005) Proc. Natl. Acad. Sci. USA, 102, pp. 14326-14331
• Yang, Z., Wolf, I.M., Chen, H., Periyasamy, S., Chen, Z., Yong, W., Shi, S., Shou, W., FK506-binding protein 52 is essential to uterine reproductive physiology controlled by the progesterone receptor A isoform (2006) Mol. Endocrinol., 20, pp. 2682-2694
• Cheung-Flynn, J., Prapapanich, V., Cox, M.B., Riggs, D.L., Suarez-Quian, C., Smith, D.F., Physiological role for the cochaperone FKBP52 in androgen receptor signaling (2005) Mol. Endocrinol, 19, pp. 1654-1666
• Periyasamy, S., Hinds, T., Jr., Shemshedini, L., Shou, W., Sanchez, E.R., FKBP51 and Cyp40 are positive regulators of androgendependent prostate cancer cell growth and the targets of FK506 and cyclosporin A (2010) Oncogene, 29, pp. 1691-1701
• Schulke, J.P., Wochnik, G.M., Lang-Rollin, I., Gassen, N.C., Knapp, R.T., Berning, B., Yassouridis, A., Rein, T., Differential impact of tetratricopeptide repeat proteins on the steroid hormone receptors (2010) Plos. One, p. 5. , e11717
• Cioffi, D.L., Hubler, T.R., Scammell, J.G., Organization and function of the FKBP52 and FKBP51 genes (2011) Curr. Opin. Pharmacol., 11, pp. 308-313
• Sivils, J.C., Storer, C.L., Galigniana, M.D., Cox, M.B., Regulation of steroid hormone receptor function by the 52-kDa FK506-binding protein (FKBP52) (2011) Curr. Opin. Pharmacol., 11, pp. 314-319
• Storer, C.L., Dickey, C.A., Galigniana, M.D., Rein, T., Cox, M.B. FKBP51 and FKBP52 in signaling and disease, Trends (2011) Endocrinol. Metab., 22, pp. 481-490
• Galigniana, M.D., Steroid receptor coupling becomes nuclear (2012) Chem. Biol., 19, pp. 662-663
• Erlejman, A.G., De Leo, S.A., Mazaira, G.I., Molinari, A.M., Camisay, M.F., Fontana, V., Cox, M.B., Galigniana, M.D., NF-kappa, B. Transcriptional activity is modulated by fk506-binding proteins FKBP51 and FKBP52: A role for peptidyl-prolyl isomerase activity (2014) J.Biol. Chem., 289, pp. 26263-26276
• Cluning, C., Ward, B.K., Rea, S.L., Arulpragasam, A., Fuller, P.J., Ratajczak, T., The helix 1-3 loop in the glucocorticoid receptor LBD is a regulatory element for FKBP cochaperones (2013) Mol. Endocrinol., 27, pp. 1020-1035
• Riggs, D.L., Cox, M.B., Cheung-Flynn, J., Prapapanich, V., Carrigan, P.E., Smith, D.F., Functional specificity of co-chaperone interactions with Hsp90 client proteins (2004) Crit. Rev. Biochem. Mol. Biol., 39, pp. 279-295
• Klenke, C., Widera, D., Engelen, T., Muller, J., Noll, T., Niehaus, K., Schmitz, M.L., Kaltschmidt, C., Hsc70 is a novel interactor of NF-kappaB p65 in living hippocampal neurons (2013) Plos One., p. 8
• Dokladny, K., Lobb, R., Wharton, W., Ma, T.Y., Moseley, P.L., LPS-induced cytokine levels are repressed by elevated expression of HSP70 in rats: Possible role of NF-kappaB. Cell. Stress (2010) Chaperones., 15, pp. 153-163
• Feinstein, D.L., Galea, E., Aquino, D.A., Li, G.C., Xu, H., Reis, D.J., Heat shock protein 70 suppresses astroglial-inducible nitricoxide synthase expression by decreasing NFkappaB activation (1996) J. Biol. Chem., 271, pp. 17724-17732
• Guzhova, I.V., Darieva, Z.A., Melo, A.R., Margulis, B.A., Major stress protein Hsp70 interacts with NF-kB regulatory complex in human T-lymphoma cells (1997) Cell Stress Chaperones, 2, pp. 132-139
• Sharp, F.R., Zhan, X., Liu, D.Z., Heat shock proteins in the brain: Role of Hsp70, Hsp 27, and HO-1 (Hsp32) and their therapeutic potential (2013) Transl. Stroke. Res., 4, pp. 685-692
• Ran, R., Lu, A., Zhang, L., Tang, Y., Zhu, H., Xu, H., Feng, Y., Rigby, A.C., Sharp, F.R.Hsp70 promotes TNFmediated apoptosis by binding IKK gamma and impairing NFkappa B survival signaling (2004) Genes. Dev., 18, pp. 1466-1481
• Giffard, R.G., Han, R.Q., Emery, J.F., Duan, M., Pittet, J.F., Regulation of apoptotic and inflammatory cell signaling in cerebral ischemia: The complex roles of heat shock protein 70 (2008) Anesthesiology, 109, pp. 339-348
• Kim, J.Y., Yenari, M.A., The immune modulating properties of the heat shock proteins after brain injury (2013) Anat. Cell. Biol., 46, pp. 1-7
• Sil, A.K., Maeda, S., Sano, Y., Roop, D.R., Karin, M., IkappaB kinase-alpha acts in the epidermis to control skeletal and craniofacial morphogenesis (2004) Nature, 428, pp. 660-664
• Lawrence, T., Bebien, M., Liu, G.Y., Nizet, V., Karin, M., IKKalpha limits macrophage NF-kappaB activation and contributes to the resolution of inflammation (2005) Nature, 434, pp. 1138-1143
• Bouwmeester, T., Bauch, A., Ruffner, H., Angrand, P.O., Bergamini, G., Croughton, K., Cruciat, C., Superti-Furga, G., A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway (2004) Nat. Cell Biol., 6, pp. 97-105
• Hinz, M., Broemer, M., Arslan, S.C., Otto, A., Mueller, E.C., Dettmer, R., Scheidereit, C., Signal responsiveness of IkappaB kinases is determined by Cdc37-assisted transient interaction with Hsp90 (2007) J. Biol.Chem., 282, pp. 32311-32319
• Silverstein, A.M., Grammatikakis, N., Cochran, B.H., Chinkers, M., Pratt, W.B., P50(Cdc37) binds directly to the catalytic domain of Raf as well as to a site on hsp90 that is topologically adjacent to the tetratricopeptide repeat binding site (1998) J. Biol. Chem., 273, pp. 20090-20095
• Pratt, W.B., Galigniana, M.D., Morishima, Y., Murphy, P.J., Role of molecular chaperones in steroid receptor action (2004) Essays Biochem., 40, pp. 41-58
• Park, K.J., Krishnan, V., O'malley, B.W., Yamamoto, Y., Gaynor, R.B., Formation of an IKKalpha-dependent transcription complex is required for estrogen receptor-mediated gene activation (2005) Mol Cell., 18, pp. 71-82
• Park, G.Y., Wang, X., Hu, N., Pedchenko, T.V., Blackwell, T.S., Christman, J.W., NIK is involved in nucleosomal regulation by enhancing histone H3 phosphorylation by IKKalpha (2006) J. Biol.Chem, 281, pp. 18684-18690
• Raghuram, N., Strickfaden, H., McDonald, D., Williams, K., Fang, H., Mizzen, C., Hayes, J.J., Hendzel, M.J., Pin1 promotes histone H1 dephosphorylation and stabilizes its binding to chromatin (2013) <ref-sourcetitle type="journal"></ref-sourcetitle>, 203, pp. 57-71
• Ryo, A., Suizu, F., Yoshida, Y., Perrem, K., Liou, Y.C., Wulf, G., Rottapel, R., Lu, K.P., Regulation of NF-kappaB signaling by Pin1-dependent prolyl isomerization and ubiquitinmediated proteolysis of p65/RelA (2003) Mol. Cell., 12, pp. 1413-1426
• Pang, R.W., Lee, T.K., Man, K., Poon, R.T., Fan, S.T., Kwong, Y.L., Tse, E., PIN1 expression contributes to hepatic carcinogenesis (2006) J. Pathol., 210, pp. 19-25
• Lu, K.P., Liou, Y.C., Zhou, X.Z., Pinning down proline-directed phosphorylation signaling (2002) Trends. Cell. Biol., 12, pp. 164-172
• Wulf, G.M., Ryo, A., Wulf, G.G., Lee, S.W., Niu, T., Petkova, V., Lu, K.P., Pin1 is overexpressed in breast cancer and cooperates with Ras signaling in increasing the transcriptional activity of c-Jun towards cyclin D1 (2001) EMBO. J., 20, pp. 3459-3472
• Oshimo, Y., Kuraoka, K., Nakayama, H., Kitadai, Y., Yoshida, K., Chayama, K., Yasui, W., Epigenetic inactivation of SOCS-1 by CpG island hypermethylation in human gastric carcinoma (2004) Int. J. Cancer, 112, pp. 1003-1009
• Oh, J., Kim, S.H., Ahn, S., Lee, C.E., Suppressors of cytokine signaling promote Fas-induced apoptosis through downregulation of NF-kappaB and mitochondrial Bfl-1 in leukemic T cells (2012) J. Immunol., 189, pp. 5561-5571
• Zhao, X.D., Zhang, W., Liang, H.J., Ji, W.Y., Overexpression of miR-155 promotes proliferation and invasion of human laryngeal squamous cell carcinoma via targeting SOCS1 and STAT3 (2013) Plos One, p. 8. , e56395
• Schif, B., Lennerz, J.K., Kohler, C.W., Bentink, S., Kreuz, M., Melzner, I., Ritz, O., Moller, P., SOCS1 mutation subtypes predict divergent outcomes in diffuse large B-Cell lymphoma (DLBCL) patients (2013) Oncotarget, 4, pp. 35-47
• Fuchs, O., Transcription factor NF-kappaB inhibitors as single therapeutic agents or in combination with classical chemotherapeutic agents for the treatment of hematologic malignancies (2010) Curr. Mol. Pharmacol., 3, pp. 98-122
• Fabre, C., Mimura, N., Bobb, K., Kong, S.Y., Gorgun, G., Cirstea, D., Hu, Y., Anderson, K.C., Dual inhibition of canonical and noncanonical NFkappaB pathways demonstrates significant antitumor activities in multiple myeloma (2012) Clin. Cancer Res., 18, pp. 4669-4681
• Salem, K., Brown, C.O., Schibler, J., Goel, A., Combination chemotherapy increases cytotoxicity of multiple myeloma cells by modification of nuclear factor (NF)-kappa B activity (2013) Exp. Hematol., 41, pp. 209-218
• Gaali, S., Gopalakrishnan, R., Wang, Y., Kozany, C., Hausch, F., The chemical biology of immunophilin ligands (2011) Curr. Med. Chem., 18, pp. 5355-5379
• Gaali, S., Kirschner, A., Cuboni, S., Hartmann, J., Kozany, C., Balsevich, G., Namendorf, C., Hausch, F., Selective inhibitors of the FK506-binding protein 51 by induced fit. Nat (2015) Chem. Biol., 11, pp. 33-37
• Quintá, H.R., Maschi, D., Gomez-Sanchez, C., Piwien-Pilipuk, G., Galigniana, M.D., Subcellular rearrangement of hsp90-binding immunophilins accompanies neuronal differentiation and neurite outgrowth (2010) J. Neurochem., 115, pp. 716-734

Citas:

---------- APA ----------

---------- CHICAGO ----------

---------- MLA ----------

---------- VANCOUVER ----------