[1]
Venkateswaran, K.; Verma, A.; Bhatt, A.N.; Shrivastava, A.; Manda, K.; Raj, H.G.; Prasad, A.; Len, C.; Parmar, V.S.; Dwarakanath, B.S. Emerging roles of calreticulin in cancer: Implications for therapy. Curr. Protein Pept. Sci., 2018, 19, 344-357.
[2]
Wang, W.A.; Groenendyk, J.; Michalak, M. Calreticulin signaling in health and disease. Int. J. Biochem. Cell Biol., 2012, 44, 842-846.
[3]
Chouquet, A.; Païdassi, H.; Ling, W.L.; Frachet, P.; Houen, G.; Arlaud, G.J.; Gaboriaud, C. X-ray structure of the human calreticulin globular domain reveals a peptide-binding area and suggests a multi-molecular mechanism. PLoS One, 2011, 6, e17886.
[4]
Kozlov, G.; Pocanschi, C.L.; Rosenauer, A.; Bastos-Aristizabal, S.; Gorelik, A.; Williams, D.B.; Gehring, K. Structural basis of carbohydrate recognition by calreticulin. J. Biol. Chem., 2010, 285, 38612-38620.
[5]
Pocanschi, C.L.; Kozlov, G.; Brockmeier, U.; Brockmeier, A.; Williams, D.B.; Gehring, K. Structural and functional relationships between the lectin and arm domains of calreticulin. J. Biol. Chem., 2011, 286, 27266-27277.
[6]
Boelt, S.G.; Norn, C.; Rasmussen, M.I.; André, I.; Čiplys, E.; Slibinskas, R.; Houen, G.; Højrup, P. Mapping the Ca(2+) induced structural change in calreticulin. J. Proteomics, 2016, 142, 138-148.
[7]
Giorgi, C.; Danese, A.; Missiroli, S.; Patergnani, S.; Pinton, P. calcium dynamics as a machine for decoding signals. Trends Cell Biol., 2018, 28, 258-273.
[8]
Marchi, S.; Pinton, P. Alterations of calcium homeostasis in cancer cells. Curr. Opin. Pharmacol., 2016, 29, 1-6.
[9]
Villagomez, M.; Szabo, E.; Podcheko, A.; Feng, T.; Papp, S.; Opas, M. Calreticulin and focal-contact-dependent adhesion. Biochem. Cell Biol., 2009, 87, 545-556.
[10]
Gold, L.I.; Eggleton, P.; Sweetwyne, M.T.; Van Duyn, L.B.; Greives, M.R.; Naylor, S.M.; Michalak, M.; Murphy-Ullrich, J.E. Calreticulin: Non-endoplasmic reticulum functions in physiology and disease. FASEB J., 2010, 24, 665-683.
[11]
Pike, S.E.; Yao, L.; Jones, K.D.; Cherney, B.; Appella, E.; Sakaguchi, K.; Nakhasi, H.; Teruya-Feldstein, J.; Wirth, P.; Gupta, G.; Tosato, G. Vasostatin, a calreticulin fragment, inhibits angiogenesis and suppresses tumor growth. J. Exp. Med., 1998, 188, 2349-2356.
[12]
Friis, T.; Engel, A.M.; Bendiksen, C.D.; Larsen, L.S.; Houen, G. Influence of levamisole and other angiogenesis inhibitors on angiogenesis and endothelial cell morphology in vitro. Cancers (Basel), 2013, 5, 762-785.
[13]
Blees, A.; Januliene, D.; Hofmann, T.; Koller, N.; Schmidt, C.; Trowitzsch, S.; Moeller, A.; Tampé, R. Structure of the human MHC-I peptide-loading complex. Nature, 2017, 551, 525-528.
[14]
Raghavan, M.; Wijeyesakere, S.J.; Peters, L.R.; Del Cid, N. Calreticulin in the immune system: Ins and outs. Trends Immunol., 2013, 34, 13-21.
[15]
Obeid, M.; Tesniere, A.; Panaretakis, T.; Tufi, R.; Joza, N.; van Endert, P.; Ghiringhelli, F.; Apetoh, L.; Chaput, N.; Flament, C.; Ullrich, E.; de Botton, S.; Zitvogel, L.; Kroemer, G. Ecto-calreticulin in immunogenic chemotherapy. Immunol. Rev., 2007, 220, 22-34.
[16]
Kumari, R.; Bansal, S.; Gupta, G.; Arora, S.; Kumar, A.; Goel, S.; Singh, P.; Ponnan, P.; Priya, N.; Tyagi, T.K.; Baghel, A.S.; Manral, S.; Tandon, R.; Joshi, R.; Rohil, V.; Gaspari, M.; Kohli, E.; Tyagi, Y.K.; Dwarakanath, B.S.; Saluja, D.; Chatterji, S.; Sharma, S.K.; Prasad, A.K.; Rastogi, R.C.; Raj, H.G.; Parmar, V.S. Calreticulin transacylase: Genesis, mechanism of action and biological applications. Biochimie, 2010, 92, 1173-1179.
[17]
Farria, A.; Li, W.; Dent, S.Y. KATs in cancer: Functions and therapies. Oncogene, 2015, 34, 4901-4913.
[18]
Kaypee, S.; Sudarshan, D.; Shanmugam, M.K.; Mukherjee, D.; Sethi, G.; Kundu, T.K. Berrant lysine acetylation in tumorigenesis: Implications in the development of therapeutics. Pharmacol. Ther., 2016, 162, 98-119.
[19]
Imai, M.; Araki, M.; Komatsu, N. Somatic mutations of calreticulin in myeloproliferative neoplasms. Int. J. Hematol., 2017, 105, 743-747.
[20]
Cahu, X.; Constantinescu, S.N. Oncogenic drivers in myeloproliferative neoplasms: From JAK2 to calreticulin mutations. Curr. Hematol. Malig. Rep., 2015, 10, 335-343.
[21]
Sun, C.; Zhang, S.; Li, J. Calreticulin gene mutations in myeloproliferative neoplasms without Janus kinase 2 mutations. Leuk. Lymphoma, 2015, 56, 1593-1598.
[22]
Varghese, L.N.; Defour, J.P.; Pecquet, C.; Constantinescu, S.N. The thrombopoietin receptor: Structural basis of traffic and activation by ligand, mutations, agonists, and mutated calreticulin. Front. Endocrinol., 2017, 8, 59.
[23]
Fucikova, J.; Kasikova, L.; Truxova, I.; Laco, J.; Skapa, P.; Ryska, A.; Spisek, R. Relevance of the chaperone-like protein calreticulin for the biological behavior and clinical outcome of cancer. Immunol. Lett., 2018, 193, 25-34.
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