메뉴 건너뛰기




Volumn 108, Issue 10, 2017, Pages 1907-1912

Novel molecular mechanism of cellular transformation by a mutant molecular chaperone in myeloproliferative neoplasms

Author keywords

Autocrine; calreticulin; JAK2; myeloproliferative neoplasm; thrombopoietin receptor

Indexed keywords

CALRETICULIN; THROMBOPOIETIN RECEPTOR; CALRETICULIN, HUMAN; MPL PROTEIN, HUMAN; PROTEIN BINDING;

EID: 85030155677     PISSN: 13479032     EISSN: 13497006     Source Type: Journal    
DOI: 10.1111/cas.13327     Document Type: Review
Times cited : (17)

References (54)
  • 1
    • 79952284127 scopus 로고    scopus 로고
    • Hallmarks of cancer: the next generation
    • Hanahan D, Weinberg RA. Hallmarks of cancer: the next generation. Cell 2011; 144: 646–74.
    • (2011) Cell , vol.144 , pp. 646-674
    • Hanahan, D.1    Weinberg, R.A.2
  • 2
    • 17644424955 scopus 로고    scopus 로고
    • A gain-of-function mutation of JAK2 in myeloproliferative disorders
    • Kralovics R, Passamonti F, Buser AS et al. A gain-of-function mutation of JAK2 in myeloproliferative disorders. N Engl J Med 2005; 352: 1779–90.
    • (2005) N Engl J Med , vol.352 , pp. 1779-1790
    • Kralovics, R.1    Passamonti, F.2    Buser, A.S.3
  • 3
    • 20244369569 scopus 로고    scopus 로고
    • Activating mutation in the tyrosine kinase JAK2 in polycythemia vera, essential thrombocythemia, and myeloid metaplasia with myelofibrosis
    • Levine RL, Wadleigh M, Cools J et al. Activating mutation in the tyrosine kinase JAK2 in polycythemia vera, essential thrombocythemia, and myeloid metaplasia with myelofibrosis. Cancer Cell 2005; 7: 387–97.
    • (2005) Cancer Cell , vol.7 , pp. 387-397
    • Levine, R.L.1    Wadleigh, M.2    Cools, J.3
  • 4
    • 17844383458 scopus 로고    scopus 로고
    • A unique clonal JAK2 mutation leading to constitutive signalling causes polycythaemia vera
    • James C, Ugo V, Le Couedic JP et al. A unique clonal JAK2 mutation leading to constitutive signalling causes polycythaemia vera. Nature 2005; 434: 1144–8.
    • (2005) Nature , vol.434 , pp. 1144-1148
    • James, C.1    Ugo, V.2    Le Couedic, J.P.3
  • 5
    • 20144363192 scopus 로고    scopus 로고
    • Acquired mutation of the tyrosine kinase JAK2 in human myeloproliferative disorders
    • Baxter EJ, Scott LM, Campbell PJ et al. Acquired mutation of the tyrosine kinase JAK2 in human myeloproliferative disorders. Lancet 2005; 365: 1054–61.
    • (2005) Lancet , vol.365 , pp. 1054-1061
    • Baxter, E.J.1    Scott, L.M.2    Campbell, P.J.3
  • 6
    • 33746437130 scopus 로고    scopus 로고
    • MPLW515L is a novel somatic activating mutation in myelofibrosis with myeloid metaplasia
    • Pikman Y, Lee BH, Mercher T et al. MPLW515L is a novel somatic activating mutation in myelofibrosis with myeloid metaplasia. PLoS Med 2006; 3: e270.
    • (2006) PLoS Med , vol.3
    • Pikman, Y.1    Lee, B.H.2    Mercher, T.3
  • 7
    • 43249084493 scopus 로고    scopus 로고
    • Ratio of mutant JAK2-V617F to wild-type Jak2 determines the MPD phenotypes in transgenic mice
    • Tiedt R, Hao-Shen H, Sobas MA et al. Ratio of mutant JAK2-V617F to wild-type Jak2 determines the MPD phenotypes in transgenic mice. Blood 2008; 111: 3931–40.
    • (2008) Blood , vol.111 , pp. 3931-3940
    • Tiedt, R.1    Hao-Shen, H.2    Sobas, M.A.3
  • 8
    • 38349035684 scopus 로고    scopus 로고
    • Development of ET, primary myelofibrosis and PV in mice expressing JAK2 V617F
    • Shide K, Shimoda HK, Kumano T et al. Development of ET, primary myelofibrosis and PV in mice expressing JAK2 V617F. Leukemia 2008; 22: 87–95.
    • (2008) Leukemia , vol.22 , pp. 87-95
    • Shide, K.1    Shimoda, H.K.2    Kumano, T.3
  • 9
    • 46749137278 scopus 로고    scopus 로고
    • Transgenic expression of JAK2V617F causes myeloproliferative disorders in mice
    • Xing S, Wanting TH, Zhao W et al. Transgenic expression of JAK2V617F causes myeloproliferative disorders in mice. Blood 2008; 111: 5109–17.
    • (2008) Blood , vol.111 , pp. 5109-5117
    • Xing, S.1    Wanting, T.H.2    Zhao, W.3
  • 10
    • 77951759127 scopus 로고    scopus 로고
    • Conditional expression of heterozygous or homozygous Jak2V617F from its endogenous promoter induces a polycythemia vera-like disease
    • Akada H, Yan D, Zou H, Fiering S, Hutchison RE, Mohi MG. Conditional expression of heterozygous or homozygous Jak2V617F from its endogenous promoter induces a polycythemia vera-like disease. Blood 2010; 115: 3589–97.
    • (2010) Blood , vol.115 , pp. 3589-3597
    • Akada, H.1    Yan, D.2    Zou, H.3    Fiering, S.4    Hutchison, R.E.5    Mohi, M.G.6
  • 11
    • 77956280929 scopus 로고    scopus 로고
    • Myeloproliferative neoplasm induced by constitutive expression of JAK2V617F in knock-in mice
    • Marty C, Lacout C, Martin A et al. Myeloproliferative neoplasm induced by constitutive expression of JAK2V617F in knock-in mice. Blood 2010; 116: 783–7.
    • (2010) Blood , vol.116 , pp. 783-787
    • Marty, C.1    Lacout, C.2    Martin, A.3
  • 12
    • 77956578342 scopus 로고    scopus 로고
    • JAK2 V617F impairs hematopoietic stem cell function in a conditional knock-in mouse model of JAK2 V617F-positive essential thrombocythemia
    • Li J, Spensberger D, Ahn JS et al. JAK2 V617F impairs hematopoietic stem cell function in a conditional knock-in mouse model of JAK2 V617F-positive essential thrombocythemia. Blood 2010; 116: 1528–38.
    • (2010) Blood , vol.116 , pp. 1528-1538
    • Li, J.1    Spensberger, D.2    Ahn, J.S.3
  • 13
    • 84886850069 scopus 로고    scopus 로고
    • JAK2V617F expression in mice amplifies early hematopoietic cells and gives them a competitive advantage that is hampered by IFNalpha
    • Hasan S, Lacout C, Marty C et al. JAK2V617F expression in mice amplifies early hematopoietic cells and gives them a competitive advantage that is hampered by IFNalpha. Blood 2013; 122: 1464–77.
    • (2013) Blood , vol.122 , pp. 1464-1477
    • Hasan, S.1    Lacout, C.2    Marty, C.3
  • 14
    • 84890372480 scopus 로고    scopus 로고
    • Somatic mutations of calreticulin in myeloproliferative neoplasms
    • Klampfl T, Gisslinger H, Harutyunyan AS et al. Somatic mutations of calreticulin in myeloproliferative neoplasms. N Engl J Med 2013; 369: 2379–90.
    • (2013) N Engl J Med , vol.369 , pp. 2379-2390
    • Klampfl, T.1    Gisslinger, H.2    Harutyunyan, A.S.3
  • 15
    • 84890328032 scopus 로고    scopus 로고
    • Somatic CALR mutations in myeloproliferative neoplasms with nonmutated JAK2
    • Nangalia J, Massie CE, Baxter EJ et al. Somatic CALR mutations in myeloproliferative neoplasms with nonmutated JAK2. N Engl J Med 2013; 369: 2391–405.
    • (2013) N Engl J Med , vol.369 , pp. 2391-2405
    • Nangalia, J.1    Massie, C.E.2    Baxter, E.J.3
  • 16
    • 0015955240 scopus 로고
    • Isolation of a high affinity calcium-binding protein from sarcoplasmic reticulum
    • Ostwald TJ, MacLennan DH. Isolation of a high affinity calcium-binding protein from sarcoplasmic reticulum. J Biol Chem 1974; 249: 974–9.
    • (1974) J Biol Chem , vol.249 , pp. 974-979
    • Ostwald, T.J.1    MacLennan, D.H.2
  • 17
    • 0024819297 scopus 로고
    • Molecular cloning of the high affinity calcium-binding protein (calreticulin) of skeletal muscle sarcoplasmic reticulum
    • Fliegel L, Burns K, MacLennan DH, Reithmeier RA, Michalak M. Molecular cloning of the high affinity calcium-binding protein (calreticulin) of skeletal muscle sarcoplasmic reticulum. J Biol Chem 1989; 264: 21522–8.
    • (1989) J Biol Chem , vol.264 , pp. 21522-21528
    • Fliegel, L.1    Burns, K.2    MacLennan, D.H.3    Reithmeier, R.A.4    Michalak, M.5
  • 18
    • 0024829021 scopus 로고
    • Multiple zones in the sequence of calreticulin (CRP55, calregulin, HACBP), a major calcium binding ER/SR protein
    • Smith MJ, Koch GL. Multiple zones in the sequence of calreticulin (CRP55, calregulin, HACBP), a major calcium binding ER/SR protein. EMBO J 1989; 8: 3581–6.
    • (1989) EMBO J , vol.8 , pp. 3581-3586
    • Smith, M.J.1    Koch, G.L.2
  • 19
    • 0025937289 scopus 로고
    • SSR alpha and associated calnexin are major calcium binding proteins of the endoplasmic reticulum membrane
    • Wada I, Rindress D, Cameron PH et al. SSR alpha and associated calnexin are major calcium binding proteins of the endoplasmic reticulum membrane. J Biol Chem 1991; 266: 19599–610.
    • (1991) J Biol Chem , vol.266 , pp. 19599-19610
    • Wada, I.1    Rindress, D.2    Cameron, P.H.3
  • 20
    • 0027156495 scopus 로고
    • Interaction with newly synthesized and retained proteins in the endoplasmic reticulum suggests a chaperone function for human integral membrane protein IP90 (calnexin)
    • David V, Hochstenbach F, Rajagopalan S, Brenner MB. Interaction with newly synthesized and retained proteins in the endoplasmic reticulum suggests a chaperone function for human integral membrane protein IP90 (calnexin). J Biol Chem 1993; 268: 9585–92.
    • (1993) J Biol Chem , vol.268 , pp. 9585-9592
    • David, V.1    Hochstenbach, F.2    Rajagopalan, S.3    Brenner, M.B.4
  • 21
    • 0035802110 scopus 로고    scopus 로고
    • Functional specialization of calreticulin domains
    • Nakamura K, Zuppini A, Arnaudeau S et al. Functional specialization of calreticulin domains. J Cell Biol 2001; 154: 961–72.
    • (2001) J Cell Biol , vol.154 , pp. 961-972
    • Nakamura, K.1    Zuppini, A.2    Arnaudeau, S.3
  • 22
    • 0034680794 scopus 로고    scopus 로고
    • Thrombospondin mediates focal adhesion disassembly through interactions with cell surface calreticulin
    • Goicoechea S, Orr AW, Pallero MA, Eggleton P, Murphy-Ullrich JE. Thrombospondin mediates focal adhesion disassembly through interactions with cell surface calreticulin. J Biol Chem 2000; 275: 36358–68.
    • (2000) J Biol Chem , vol.275 , pp. 36358-36368
    • Goicoechea, S.1    Orr, A.W.2    Pallero, M.A.3    Eggleton, P.4    Murphy-Ullrich, J.E.5
  • 23
    • 0036169941 scopus 로고    scopus 로고
    • Assembly and antigen-presenting function of MHC class I molecules in cells lacking the ER chaperone calreticulin
    • Gao B, Adhikari R, Howarth M et al. Assembly and antigen-presenting function of MHC class I molecules in cells lacking the ER chaperone calreticulin. Immunity 2002; 16: 99–109.
    • (2002) Immunity , vol.16 , pp. 99-109
    • Gao, B.1    Adhikari, R.2    Howarth, M.3
  • 24
    • 0035903289 scopus 로고    scopus 로고
    • C1q and mannose binding lectin engagement of cell surface calreticulin and CD91 initiates macropinocytosis and uptake of apoptotic cells
    • Ogden CA, de Cathelineau A, Hoffmann PR et al. C1q and mannose binding lectin engagement of cell surface calreticulin and CD91 initiates macropinocytosis and uptake of apoptotic cells. J Exp Med 2001; 194: 781–95.
    • (2001) J Exp Med , vol.194 , pp. 781-795
    • Ogden, C.A.1    de Cathelineau, A.2    Hoffmann, P.R.3
  • 25
    • 26844468253 scopus 로고    scopus 로고
    • Cell-surface calreticulin initiates clearance of viable or apoptotic cells through trans-activation of LRP on the phagocyte
    • Gardai SJ, McPhillips KA, Frasch SC et al. Cell-surface calreticulin initiates clearance of viable or apoptotic cells through trans-activation of LRP on the phagocyte. Cell 2005; 123: 321–34.
    • (2005) Cell , vol.123 , pp. 321-334
    • Gardai, S.J.1    McPhillips, K.A.2    Frasch, S.C.3
  • 27
    • 0030910249 scopus 로고    scopus 로고
    • Calreticulin biosynthesis and processing in human myeloid cells: demonstration of signal peptide cleavage and N-glycosylation
    • Denning GM, Leidal KG, Holst VA et al. Calreticulin biosynthesis and processing in human myeloid cells: demonstration of signal peptide cleavage and N-glycosylation. Blood 1997; 90: 372–81.
    • (1997) Blood , vol.90 , pp. 372-381
    • Denning, G.M.1    Leidal, K.G.2    Holst, V.A.3
  • 28
    • 0037458633 scopus 로고    scopus 로고
    • Interactions of substrate with calreticulin, an endoplasmic reticulum chaperone
    • Kapoor M, Srinivas H, Kandiah E et al. Interactions of substrate with calreticulin, an endoplasmic reticulum chaperone. J Biol Chem 2003; 278: 6194–200.
    • (2003) J Biol Chem , vol.278 , pp. 6194-6200
    • Kapoor, M.1    Srinivas, H.2    Kandiah, E.3
  • 29
    • 0346727443 scopus 로고    scopus 로고
    • Mutational analysis provides molecular insight into the carbohydrate-binding region of calreticulin: pivotal roles of tyrosine-109 and aspartate-135 in carbohydrate recognition
    • Kapoor M, Ellgaard L, Gopalakrishnapai J et al. Mutational analysis provides molecular insight into the carbohydrate-binding region of calreticulin: pivotal roles of tyrosine-109 and aspartate-135 in carbohydrate recognition. Biochemistry 2004; 43: 97–106.
    • (2004) Biochemistry , vol.43 , pp. 97-106
    • Kapoor, M.1    Ellgaard, L.2    Gopalakrishnapai, J.3
  • 30
    • 0028973422 scopus 로고
    • Identification of the Zn2 + binding region in calreticulin
    • Baksh S, Spamer C, Heilmann C, Michalak M. Identification of the Zn2 + binding region in calreticulin. FEBS Lett 1995; 376: 53–7.
    • (1995) FEBS Lett , vol.376 , pp. 53-57
    • Baksh, S.1    Spamer, C.2    Heilmann, C.3    Michalak, M.4
  • 31
    • 0346118859 scopus 로고    scopus 로고
    • Identification of an N-domain histidine essential for chaperone function in calreticulin
    • Guo L, Groenendyk J, Papp S et al. Identification of an N-domain histidine essential for chaperone function in calreticulin. J Biol Chem 2003; 278: 50645–53.
    • (2003) J Biol Chem , vol.278 , pp. 50645-50653
    • Guo, L.1    Groenendyk, J.2    Papp, S.3
  • 33
    • 33644860723 scopus 로고    scopus 로고
    • Identification by mutational analysis of amino acid residues essential in the chaperone function of calreticulin
    • Martin V, Groenendyk J, Steiner SS et al. Identification by mutational analysis of amino acid residues essential in the chaperone function of calreticulin. J Biol Chem 2006; 281: 2338–46.
    • (2006) J Biol Chem , vol.281 , pp. 2338-2346
    • Martin, V.1    Groenendyk, J.2    Steiner, S.S.3
  • 34
    • 0025788270 scopus 로고
    • Expression of calreticulin in Escherichia coli and identification of its Ca2 + binding domains
    • Baksh S, Michalak M. Expression of calreticulin in Escherichia coli and identification of its Ca2 + binding domains. J Biol Chem 1991; 266: 21458–65.
    • (1991) J Biol Chem , vol.266 , pp. 21458-21465
    • Baksh, S.1    Michalak, M.2
  • 35
    • 0034799402 scopus 로고    scopus 로고
    • The Structure of calnexin, an ER chaperone involved in quality control of protein folding
    • Schrag JD, Bergeron JJ, Li Y et al. The Structure of calnexin, an ER chaperone involved in quality control of protein folding. Mol Cell 2001; 8: 633–44.
    • (2001) Mol Cell , vol.8 , pp. 633-644
    • Schrag, J.D.1    Bergeron, J.J.2    Li, Y.3
  • 37
    • 78649641361 scopus 로고    scopus 로고
    • Structural basis of carbohydrate recognition by calreticulin
    • Kozlov G, Pocanschi CL, Rosenauer A et al. Structural basis of carbohydrate recognition by calreticulin. J Biol Chem 2010; 285: 38612–20.
    • (2010) J Biol Chem , vol.285 , pp. 38612-38620
    • Kozlov, G.1    Pocanschi, C.L.2    Rosenauer, A.3
  • 38
    • 79952663496 scopus 로고    scopus 로고
    • X-ray structure of the human calreticulin globular domain reveals a peptide-binding area and suggests a multi-molecular mechanism
    • Chouquet A, Paidassi H, Ling WL et al. 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.
    • (2011) PLoS ONE , vol.6
    • Chouquet, A.1    Paidassi, H.2    Ling, W.L.3
  • 39
    • 84929159925 scopus 로고    scopus 로고
    • Endogenous megakaryocytic colonies underline association between megakaryocytes and calreticulin mutations in essential thrombocythemia
    • Mondet J, Park JH, Menard A et al. Endogenous megakaryocytic colonies underline association between megakaryocytes and calreticulin mutations in essential thrombocythemia. Haematologica 2015; 100: e176–8.
    • (2015) Haematologica , vol.100 , pp. e176-e178
    • Mondet, J.1    Park, J.H.2    Menard, A.3
  • 40
    • 84960906311 scopus 로고    scopus 로고
    • Activation of the thrombopoietin receptor by mutant calreticulin in CALR-mutant myeloproliferative neoplasms
    • Araki M, Yang Y, Masubuchi N et al. Activation of the thrombopoietin receptor by mutant calreticulin in CALR-mutant myeloproliferative neoplasms. Blood 2016; 127: 1307–16.
    • (2016) Blood , vol.127 , pp. 1307-1316
    • Araki, M.1    Yang, Y.2    Masubuchi, N.3
  • 41
    • 84960864909 scopus 로고    scopus 로고
    • Calreticulin mutants in mice induce an MPL-dependent thrombocytosis with frequent progression to myelofibrosis
    • Marty C, Pecquet C, Nivarthi H et al. Calreticulin mutants in mice induce an MPL-dependent thrombocytosis with frequent progression to myelofibrosis. Blood 2016; 127: 1317–24.
    • (2016) Blood , vol.127 , pp. 1317-1324
    • Marty, C.1    Pecquet, C.2    Nivarthi, H.3
  • 42
    • 84962360217 scopus 로고    scopus 로고
    • Mutant calreticulin requires both its mutant c-terminus and the thrombopoietin receptor for oncogenic transformation
    • Elf S, Abdelfattah NS, Chen E et al. Mutant calreticulin requires both its mutant c-terminus and the thrombopoietin receptor for oncogenic transformation. Cancer Discov 2016; 6: 368–81.
    • (2016) Cancer Discov , vol.6 , pp. 368-381
    • Elf, S.1    Abdelfattah, N.S.2    Chen, E.3
  • 43
    • 84960851640 scopus 로고    scopus 로고
    • Thrombopoietin receptor activation by myeloproliferative neoplasm associated calreticulin mutants
    • Chachoua I, Pecquet C, El-Khoury M et al. Thrombopoietin receptor activation by myeloproliferative neoplasm associated calreticulin mutants. Blood 2016; 127: 1325–35.
    • (2016) Blood , vol.127 , pp. 1325-1335
    • Chachoua, I.1    Pecquet, C.2    El-Khoury, M.3
  • 44
    • 84997787492 scopus 로고    scopus 로고
    • Calreticulin mutant mice develop essential thrombocythemia that is ameliorated by the JAK inhibitor ruxolitinib
    • Shide K, Kameda T, Yamaji T et al. Calreticulin mutant mice develop essential thrombocythemia that is ameliorated by the JAK inhibitor ruxolitinib. Leukemia 2017; 31: 1136–44.
    • (2017) Leukemia , vol.31 , pp. 1136-1144
    • Shide, K.1    Kameda, T.2    Yamaji, T.3
  • 45
    • 84904401956 scopus 로고    scopus 로고
    • Type 1 versus Type 2 calreticulin mutations in essential thrombocythemia: a collaborative study of 1027 patients
    • Tefferi A, Wassie EA, Guglielmelli P et al. Type 1 versus Type 2 calreticulin mutations in essential thrombocythemia: a collaborative study of 1027 patients. Am J Hematol 2014; 89: E121–4.
    • (2014) Am J Hematol , vol.89 , pp. E121-E124
    • Tefferi, A.1    Wassie, E.A.2    Guglielmelli, P.3
  • 46
    • 84959370553 scopus 로고    scopus 로고
    • Differential clinical effects of different mutation subtypes in CALR-mutant myeloproliferative neoplasms
    • Pietra D, Rumi E, Ferretti VV et al. Differential clinical effects of different mutation subtypes in CALR-mutant myeloproliferative neoplasms. Leukemia 2016; 30: 431–8.
    • (2016) Leukemia , vol.30 , pp. 431-438
    • Pietra, D.1    Rumi, E.2    Ferretti, V.V.3
  • 47
    • 84900432315 scopus 로고    scopus 로고
    • Mechanism of activation of protein kinase JAK2 by the growth hormone receptor
    • Brooks AJ, Dai W, O'Mara ML et al. Mechanism of activation of protein kinase JAK2 by the growth hormone receptor. Science 2014; 344: 1249783.
    • (2014) Science , vol.344 , pp. 1249783
    • Brooks, A.J.1    Dai, W.2    O'Mara, M.L.3
  • 48
    • 79960190017 scopus 로고    scopus 로고
    • Thrombopoietin receptor activation: transmembrane helix dimerization, rotation, and allosteric modulation
    • Matthews EE, Thevenin D, Rogers JM et al. Thrombopoietin receptor activation: transmembrane helix dimerization, rotation, and allosteric modulation. FASEB J 2011; 25: 2234–44.
    • (2011) FASEB J , vol.25 , pp. 2234-2244
    • Matthews, E.E.1    Thevenin, D.2    Rogers, J.M.3
  • 49
    • 80455174620 scopus 로고    scopus 로고
    • Orientation-specific signalling by thrombopoietin receptor dimers
    • Staerk J, Defour JP, Pecquet C et al. Orientation-specific signalling by thrombopoietin receptor dimers. EMBO J 2011; 30: 4398–413.
    • (2011) EMBO J , vol.30 , pp. 4398-4413
    • Staerk, J.1    Defour, J.P.2    Pecquet, C.3
  • 50
    • 0027507325 scopus 로고
    • The calcium-binding protein calreticulin is a major constituent of lytic granules in cytolytic T lymphocytes
    • Dupuis M, Schaerer E, Krause KH, Tschopp J. The calcium-binding protein calreticulin is a major constituent of lytic granules in cytolytic T lymphocytes. J Exp Med 1993; 177: 1–7.
    • (1993) J Exp Med , vol.177 , pp. 1-7
    • Dupuis, M.1    Schaerer, E.2    Krause, K.H.3    Tschopp, J.4
  • 51
    • 0027956447 scopus 로고
    • Calreticulin is released from activated neutrophils and binds to C1q and mannan-binding protein
    • Eggleton P, Lieu TS, Zappi EG et al. Calreticulin is released from activated neutrophils and binds to C1q and mannan-binding protein. Clin Immunol Immunopathol 1994; 72: 405–9.
    • (1994) Clin Immunol Immunopathol , vol.72 , pp. 405-409
    • Eggleton, P.1    Lieu, T.S.2    Zappi, E.G.3
  • 52
    • 84971254922 scopus 로고    scopus 로고
    • Calreticulin-mutant proteins induce megakaryocytic signaling to transform hematopoietic cells and undergo accelerated degradation and Golgi-mediated secretion
    • Han L, Schubert C, Kohler J et al. Calreticulin-mutant proteins induce megakaryocytic signaling to transform hematopoietic cells and undergo accelerated degradation and Golgi-mediated secretion. J Hematol Oncol 2016; 9: 45.
    • (2016) J Hematol Oncol , vol.9 , pp. 45
    • Han, L.1    Schubert, C.2    Kohler, J.3
  • 53
    • 84923322628 scopus 로고    scopus 로고
    • Oncogenic Kit signals on endolysosomes and endoplasmic reticulum are essential for neoplastic mast cell proliferation
    • Obata Y, Toyoshima S, Wakamatsu E et al. Oncogenic Kit signals on endolysosomes and endoplasmic reticulum are essential for neoplastic mast cell proliferation. Nat Commun 2014; 5: 5715.
    • (2014) Nat Commun , vol.5 , pp. 5715
    • Obata, Y.1    Toyoshima, S.2    Wakamatsu, E.3
  • 54
    • 70350013557 scopus 로고    scopus 로고
    • Mislocalized activation of oncogenic RTKs switches downstream signaling outcomes
    • Choudhary C, Olsen JV, Brandts C et al. Mislocalized activation of oncogenic RTKs switches downstream signaling outcomes. Mol Cell 2009; 36: 326–39.
    • (2009) Mol Cell , vol.36 , pp. 326-339
    • Choudhary, C.1    Olsen, J.V.2    Brandts, C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.