메뉴 건너뛰기




Volumn 8, Issue 8, 2013, Pages

The Coxsackievirus and Adenovirus Receptor (CAR) Undergoes Ectodomain Shedding and Regulated Intramembrane Proteolysis (RIP)

Author keywords

[No Author keywords available]

Indexed keywords

ADAM10 ENDOPEPTIDASE; AMYLOID PRECURSOR PROTEIN; CALCIUM IONOPHORE; COXSACKIE VIRUS AND ADENOVIRUS RECEPTOR; GAMMA SECRETASE; IONOMYCIN; NOTCH RECEPTOR; PHORBOL 13 ACETATE 12 MYRISTATE; PRESENILIN;

EID: 84883392478     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0073296     Document Type: Article
Times cited : (27)

References (77)
  • 1
    • 0034902286 scopus 로고    scopus 로고
    • Receptor for the group B coxsackieviruses and adenoviruses: CAR
    • doi:10.1002/rmv.318
    • Carson SD, (2001) Receptor for the group B coxsackieviruses and adenoviruses: CAR. Rev Med Virol 11: 219-226. doi:10.1002/rmv.318. PubMed: 11479928.
    • (2001) Rev Med Virol , vol.11 , pp. 219-226
    • Carson, S.D.1
  • 2
    • 16844382964 scopus 로고    scopus 로고
    • CAR: a virus receptor within the tight junction
    • doi:10.1016/j.addr.2005.01.007
    • Coyne CB, Bergelson JM, (2005) CAR: a virus receptor within the tight junction. Adv Drug Deliv Rev 57: 869-882. doi:10.1016/j.addr.2005.01.007. PubMed: 15820557.
    • (2005) Adv Drug Deliv Rev , vol.57 , pp. 869-882
    • Coyne, C.B.1    Bergelson, J.M.2
  • 3
    • 0031052263 scopus 로고    scopus 로고
    • Isolation of a common receptor for Coxsackie B viruses and adenoviruses 2 and 5
    • doi:10.1126/science.275.5304.1320
    • Bergelson JM, Cunningham JA, Droguett G, Kurt-Jones EA, Krithivas A, et al. (1997) Isolation of a common receptor for Coxsackie B viruses and adenoviruses 2 and 5. Science 275: 1320-1323. doi:10.1126/science.275.5304.1320. PubMed: 9036860.
    • (1997) Science , vol.275 , pp. 1320-1323
    • Bergelson, J.M.1    Cunningham, J.A.2    Droguett, G.3    Kurt-Jones, E.A.4    Krithivas, A.5
  • 4
    • 0030915715 scopus 로고    scopus 로고
    • HCAR and MCAR: the human and mouse cellular receptors for subgroup C adenoviruses and group B coxsackieviruses
    • doi:10.1073/pnas.94.7.3352
    • Tomko RP, Xu R, Philipson L, (1997) HCAR and MCAR: the human and mouse cellular receptors for subgroup C adenoviruses and group B coxsackieviruses. Proc Natl Acad Sci U S A 94: 3352-3356. doi:10.1073/pnas.94.7.3352. PubMed: 9096397.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 3352-3356
    • Tomko, R.P.1    Xu, R.2    Philipson, L.3
  • 5
    • 0031575920 scopus 로고    scopus 로고
    • Purification of the putative coxsackievirus B receptor from HeLa cells
    • doi:10.1006/bbrc.1997.6449
    • Carson SD, Chapman NN, Tracy SM, (1997) Purification of the putative coxsackievirus B receptor from HeLa cells. Biochem Biophys Res Commun 233: 325-328. doi:10.1006/bbrc.1997.6449. PubMed: 9144533.
    • (1997) Biochem Biophys Res Commun , vol.233 , pp. 325-328
    • Carson, S.D.1    Chapman, N.N.2    Tracy, S.M.3
  • 6
    • 0034646786 scopus 로고    scopus 로고
    • The coxsackievirus-adenovirus receptor protein as a cell adhesion molecule in the developing mouse brain
    • doi:10.1016/S0169-328X(00)00036-X
    • Honda T, Saitoh H, Masuko M, Katagiri-Abe T, Tominaga K, et al. (2000) The coxsackievirus-adenovirus receptor protein as a cell adhesion molecule in the developing mouse brain. Brain Res Mol Brain Res 77: 19-28. doi:10.1016/S0169-328X(00)00036-X. PubMed: 10814828.
    • (2000) Brain Res Mol Brain Res , vol.77 , pp. 19-28
    • Honda, T.1    Saitoh, H.2    Masuko, M.3    Katagiri-Abe, T.4    Tominaga, K.5
  • 7
    • 34249666768 scopus 로고    scopus 로고
    • Interaction of the Coxsackie and adenovirus receptor (CAR) with the cytoskeleton: binding to actin
    • doi:10.1016/j.febslet.2007.05.019
    • Huang KC, Yasruel Z, Guérin C, Holland PC, Nalbantoglu J, (2007) Interaction of the Coxsackie and adenovirus receptor (CAR) with the cytoskeleton: binding to actin. FEBS Lett 581: 2702-2708. doi:10.1016/j.febslet.2007.05.019. PubMed: 17531226.
    • (2007) FEBS Lett , vol.581 , pp. 2702-2708
    • Huang, K.C.1    Yasruel, Z.2    Guérin, C.3    Holland, P.C.4    Nalbantoglu, J.5
  • 8
    • 77649108637 scopus 로고    scopus 로고
    • The coxsackievirus-adenovirus receptor reveals complex homophilic and heterophilic interactions on neural cells
    • doi:10.1523/JNEUROSCI.5725-09.2010
    • Patzke C, Max KE, Behlke J, Schreiber J, Schmidt H, et al. (2010) The coxsackievirus-adenovirus receptor reveals complex homophilic and heterophilic interactions on neural cells. J Neurosci 30: 2897-2910. doi:10.1523/JNEUROSCI.5725-09.2010. PubMed: 20181587.
    • (2010) J Neurosci , vol.30 , pp. 2897-2910
    • Patzke, C.1    Max, K.E.2    Behlke, J.3    Schreiber, J.4    Schmidt, H.5
  • 9
    • 0035910098 scopus 로고    scopus 로고
    • The coxsackievirus and adenovirus receptor is a transmembrane component of the tight junction
    • doi:10.1073/pnas.261452898
    • Cohen CJ, Shieh JT, Pickles RJ, Okegawa T, Hsieh JT, et al. (2001) The coxsackievirus and adenovirus receptor is a transmembrane component of the tight junction. Proc Natl Acad Sci U S A 98: 15191-15196. doi:10.1073/pnas.261452898. PubMed: 11734628.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 15191-15196
    • Cohen, C.J.1    Shieh, J.T.2    Pickles, R.J.3    Okegawa, T.4    Hsieh, J.T.5
  • 10
    • 9144243706 scopus 로고    scopus 로고
    • The coxsackievirus and adenovirus receptor interacts with the multi-PDZ domain protein-1 (MUPP-1) within the tight junction
    • doi:10.1074/jbc.M409061200
    • Coyne CB, Voelker T, Pichla SL, Bergelson JM, (2004) The coxsackievirus and adenovirus receptor interacts with the multi-PDZ domain protein-1 (MUPP-1) within the tight junction. J Biol Chem 279: 48079-48084. doi:10.1074/jbc.M409061200. PubMed: 15364909.
    • (2004) J Biol Chem , vol.279 , pp. 48079-48084
    • Coyne, C.B.1    Voelker, T.2    Pichla, S.L.3    Bergelson, J.M.4
  • 11
    • 0033541587 scopus 로고    scopus 로고
    • Expression of the primary coxsackie and adenovirus receptor is downregulated during skeletal muscle maturation and limits the efficacy of adenovirus-mediated gene delivery to muscle cells
    • doi:10.1089/10430349950018409
    • Nalbantoglu J, Pari G, Karpati G, Holland PC, (1999) Expression of the primary coxsackie and adenovirus receptor is downregulated during skeletal muscle maturation and limits the efficacy of adenovirus-mediated gene delivery to muscle cells. Hum Gene Ther 10: 1009-1019. doi:10.1089/10430349950018409. PubMed: 10223734.
    • (1999) Hum Gene Ther , vol.10 , pp. 1009-1019
    • Nalbantoglu, J.1    Pari, G.2    Karpati, G.3    Holland, P.C.4
  • 12
    • 10144246575 scopus 로고    scopus 로고
    • Isoform-specific expression of the Coxsackie and adenovirus receptor (CAR) in neuromuscular junction and cardiac intercalated discs
    • doi:10.1186/1471-2121-5-42
    • Shaw CA, Holland PC, Sinnreich M, Allen C, Sollerbrant K, et al. (2004) Isoform-specific expression of the Coxsackie and adenovirus receptor (CAR) in neuromuscular junction and cardiac intercalated discs. BMC Cell Biol 5: 42. doi:10.1186/1471-2121-5-42. PubMed: 15533241.
    • (2004) BMC Cell Biol , vol.5 , pp. 42
    • Shaw, C.A.1    Holland, P.C.2    Sinnreich, M.3    Allen, C.4    Sollerbrant, K.5
  • 13
    • 22244489661 scopus 로고    scopus 로고
    • Coxsackievirus and adenovirus receptor is essential for cardiomyocyte development
    • doi:10.1002/gene.20127
    • Asher DR, Cerny AM, Weiler SR, Horner JW, Keeler ML, et al. (2005) Coxsackievirus and adenovirus receptor is essential for cardiomyocyte development. Genesis 42: 77-85. doi:10.1002/gene.20127. PubMed: 15864812.
    • (2005) Genesis , vol.42 , pp. 77-85
    • Asher, D.R.1    Cerny, A.M.2    Weiler, S.R.3    Horner, J.W.4    Keeler, M.L.5
  • 14
    • 24344465923 scopus 로고    scopus 로고
    • Coxsackievirus-adenovirus receptor (CAR) is essential for early embryonic cardiac development
    • doi:10.1242/jcs.02476
    • Dorner AA, Wegmann F, Butz S, Wolburg-Buchholz K, Wolburg H, et al. (2005) Coxsackievirus-adenovirus receptor (CAR) is essential for early embryonic cardiac development. J Cell Sci 118: 3509-3521. doi:10.1242/jcs.02476. PubMed: 16079292.
    • (2005) J Cell Sci , vol.118 , pp. 3509-3521
    • Dorner, A.A.1    Wegmann, F.2    Butz, S.3    Wolburg-Buchholz, K.4    Wolburg, H.5
  • 15
    • 33646123538 scopus 로고    scopus 로고
    • Cardiomyocyte-specific deletion of the coxsackievirus and adenovirus receptor results in hyperplasia of the embryonic left ventricle and abnormalities of sinuatrial valves
    • doi:10.1161/01.RES.0000218041.41932.e3
    • Chen JW, Zhou B, Yu QC, Shin SJ, Jiao K, et al. (2006) Cardiomyocyte-specific deletion of the coxsackievirus and adenovirus receptor results in hyperplasia of the embryonic left ventricle and abnormalities of sinuatrial valves. Circ Res 98: 923-930. doi:10.1161/01.RES.0000218041.41932.e3. PubMed: 16543498.
    • (2006) Circ Res , vol.98 , pp. 923-930
    • Chen, J.W.1    Zhou, B.2    Yu, Q.C.3    Shin, S.J.4    Jiao, K.5
  • 16
    • 48749127844 scopus 로고    scopus 로고
    • Coxsackievirus and adenovirus receptor (CAR) mediates atrioventricular-node function and connexin 45 localization in the murine heart
    • doi:10.1172/JCI34777
    • Lim BK, Xiong D, Dorner A, Youn TJ, Yung A, et al. (2008) Coxsackievirus and adenovirus receptor (CAR) mediates atrioventricular-node function and connexin 45 localization in the murine heart. J Clin Invest 118: 2758-2770. doi:10.1172/JCI34777. PubMed: 18636119.
    • (2008) J Clin Invest , vol.118 , pp. 2758-2770
    • Lim, B.K.1    Xiong, D.2    Dorner, A.3    Youn, T.J.4    Yung, A.5
  • 17
    • 53349097084 scopus 로고    scopus 로고
    • The tight junction protein CAR regulates cardiac conduction and cell-cell communication
    • doi:10.1084/jem.20080897
    • Lisewski U, Shi Y, Wrackmeyer U, Fischer R, Chen C, et al. (2008) The tight junction protein CAR regulates cardiac conduction and cell-cell communication. J Exp Med 205: 2369-2379. doi:10.1084/jem.20080897. PubMed: 18794341.
    • (2008) J Exp Med , vol.205 , pp. 2369-2379
    • Lisewski, U.1    Shi, Y.2    Wrackmeyer, U.3    Fischer, R.4    Chen, C.5
  • 18
    • 79958063088 scopus 로고    scopus 로고
    • Multiple phenotypes in adult mice following inactivation of the Coxsackievirus and Adenovirus Receptor (Car) gene
    • doi:10.1371/journal.pone.0020203
    • Pazirandeh A, Sultana T, Mirza M, Rozell B, Hultenby K, et al. (2011) Multiple phenotypes in adult mice following inactivation of the Coxsackievirus and Adenovirus Receptor (Car) gene. PLOS ONE 6: e20203. doi:10.1371/journal.pone.0020203. PubMed: 21674029.
    • (2011) PLOS ONE , vol.6
    • Pazirandeh, A.1    Sultana, T.2    Mirza, M.3    Rozell, B.4    Hultenby, K.5
  • 19
    • 19644367752 scopus 로고    scopus 로고
    • Neutrophil migration across tight junctions is mediated by adhesive interactions between epithelial coxsackie and adenovirus receptor and a junctional adhesion molecule-like protein on neutrophils
    • doi:10.1091/mbc.E05-01-0036
    • Zen K, Liu Y, McCall IC, Wu T, Lee W, et al. (2005) Neutrophil migration across tight junctions is mediated by adhesive interactions between epithelial coxsackie and adenovirus receptor and a junctional adhesion molecule-like protein on neutrophils. Mol Biol Cell 16: 2694-2703. doi:10.1091/mbc.E05-01-0036. PubMed: 15800062.
    • (2005) Mol Biol Cell , vol.16 , pp. 2694-2703
    • Zen, K.1    Liu, Y.2    McCall, I.C.3    Wu, T.4    Lee, W.5
  • 20
    • 58849114504 scopus 로고    scopus 로고
    • Role of junctional adhesion molecule-like protein in mediating monocyte transendothelial migration
    • doi:10.1161/ATVBAHA.108.177717
    • Guo YL, Bai R, Chen CX, Liu DQ, Liu Y, et al. (2009) Role of junctional adhesion molecule-like protein in mediating monocyte transendothelial migration. Arterioscler Thromb Vasc Biol 29: 75-83. doi:10.1161/ATVBAHA.108.177717. PubMed: 18948633.
    • (2009) Arterioscler Thromb Vasc Biol , vol.29 , pp. 75-83
    • Guo, Y.L.1    Bai, R.2    Chen, C.X.3    Liu, D.Q.4    Liu, Y.5
  • 21
    • 77956273963 scopus 로고    scopus 로고
    • The junctional adhesion molecule JAML is a costimulatory receptor for epithelial gammadelta T cell activation
    • doi:10.1126/science.1192698
    • Witherden DA, Verdino P, Rieder SE, Garijo O, Mills RE, et al. (2010) The junctional adhesion molecule JAML is a costimulatory receptor for epithelial gammadelta T cell activation. Science 329: 1205-1210. doi:10.1126/science.1192698. PubMed: 20813954.
    • (2010) Science , vol.329 , pp. 1205-1210
    • Witherden, D.A.1    Verdino, P.2    Rieder, S.E.3    Garijo, O.4    Mills, R.E.5
  • 22
    • 0035420192 scopus 로고    scopus 로고
    • The mechanism of the growth-inhibitory effect of coxsackie and adenovirus receptor (CAR) on human bladder cancer: a functional analysis of car protein structure
    • Okegawa T, Pong RC, Li Y, Bergelson JM, Sagalowsky AI, et al. (2001) The mechanism of the growth-inhibitory effect of coxsackie and adenovirus receptor (CAR) on human bladder cancer: a functional analysis of car protein structure. Cancer Res 61: 6592-6600. PubMed: 11522659.
    • (2001) Cancer Res , vol.61 , pp. 6592-6600
    • Okegawa, T.1    Pong, R.C.2    Li, Y.3    Bergelson, J.M.4    Sagalowsky, A.I.5
  • 23
    • 0038146845 scopus 로고    scopus 로고
    • The coxsackievirus and adenovirus receptor acts as a tumour suppressor in malignant glioma cells
    • doi:10.1038/sj.bjc.6600932
    • Kim M, Sumerel LA, Belousova N, Lyons GR, Carey DE, et al. (2003) The coxsackievirus and adenovirus receptor acts as a tumour suppressor in malignant glioma cells. Br J Cancer 88: 1411-1416. doi:10.1038/sj.bjc.6600932. PubMed: 12778071.
    • (2003) Br J Cancer , vol.88 , pp. 1411-1416
    • Kim, M.1    Sumerel, L.A.2    Belousova, N.3    Lyons, G.R.4    Carey, D.E.5
  • 24
    • 11944269529 scopus 로고    scopus 로고
    • Impact of the coxsackie and adenovirus receptor (CAR) on glioma cell growth and invasion: requirement for the C-terminal domain
    • doi:10.1002/ijc.20623
    • Huang KC, Altinoz M, Wosik K, Larochelle N, Koty Z, et al. (2005) Impact of the coxsackie and adenovirus receptor (CAR) on glioma cell growth and invasion: requirement for the C-terminal domain. Int J Cancer 113: 738-745. doi:10.1002/ijc.20623. PubMed: 15499626.
    • (2005) Int J Cancer , vol.113 , pp. 738-745
    • Huang, K.C.1    Altinoz, M.2    Wosik, K.3    Larochelle, N.4    Koty, Z.5
  • 25
    • 52949099119 scopus 로고    scopus 로고
    • The ADAM metalloproteinases
    • doi:10.1016/j.mam.2008.08.001
    • Edwards DR, Handsley MM, Pennington CJ, (2008) The ADAM metalloproteinases. Mol Aspects Med 29: 258-289. doi:10.1016/j.mam.2008.08.001. PubMed: 18762209.
    • (2008) Mol Aspects Med , vol.29 , pp. 258-289
    • Edwards, D.R.1    Handsley, M.M.2    Pennington, C.J.3
  • 26
    • 26444448409 scopus 로고    scopus 로고
    • L1 is sequentially processed by two differently activated metalloproteases and presenilin/gamma-secretase and regulates neural cell adhesion, cell migration, and neurite outgrowth
    • doi:10.1128/MCB.25.20.9040-9053.2005
    • Maretzky T, Schulte M, Ludwig A, Rose-John S, Blobel C, et al. (2005) L1 is sequentially processed by two differently activated metalloproteases and presenilin/gamma-secretase and regulates neural cell adhesion, cell migration, and neurite outgrowth. Mol Cell Biol 25: 9040-9053. doi:10.1128/MCB.25.20.9040-9053.2005. PubMed: 16199880.
    • (2005) Mol Cell Biol , vol.25 , pp. 9040-9053
    • Maretzky, T.1    Schulte, M.2    Ludwig, A.3    Rose-John, S.4    Blobel, C.5
  • 27
    • 1942533555 scopus 로고    scopus 로고
    • Ectodomain shedding of the neural recognition molecule CHL1 by the metalloprotease-disintegrin ADAM8 promotes neurite outgrowth and suppresses neuronal cell death
    • doi:10.1074/jbc.M400560200
    • Naus S, Richter M, Wildeboer D, Moss M, Schachner M, et al. (2004) Ectodomain shedding of the neural recognition molecule CHL1 by the metalloprotease-disintegrin ADAM8 promotes neurite outgrowth and suppresses neuronal cell death. J Biol Chem 279: 16083-16090. doi:10.1074/jbc.M400560200. PubMed: 14761956.
    • (2004) J Biol Chem , vol.279 , pp. 16083-16090
    • Naus, S.1    Richter, M.2    Wildeboer, D.3    Moss, M.4    Schachner, M.5
  • 28
    • 15444371289 scopus 로고    scopus 로고
    • ADAM10 cleavage of N-cadherin and regulation of cell-cell adhesion and beta-catenin nuclear signalling
    • doi:10.1038/sj.emboj.7600548
    • Reiss K, Maretzky T, Ludwig A, Tousseyn T, de Strooper B, et al. (2005) ADAM10 cleavage of N-cadherin and regulation of cell-cell adhesion and beta-catenin nuclear signalling. EMBO J 24: 742-752. doi:10.1038/sj.emboj.7600548. PubMed: 15692570.
    • (2005) EMBO J , vol.24 , pp. 742-752
    • Reiss, K.1    Maretzky, T.2    Ludwig, A.3    Tousseyn, T.4    de Strooper, B.5
  • 29
    • 79955663580 scopus 로고    scopus 로고
    • Regulated intramembrane proteolysis--lessons from amyloid precursor protein processing
    • doi:10.1111/j.1471-4159.2011.07248.x
    • Lichtenthaler SF, Haass C, Steiner H, (2011) Regulated intramembrane proteolysis--lessons from amyloid precursor protein processing. J Neurochem 117: 779-796. doi:10.1111/j.1471-4159.2011.07248.x. PubMed: 21413990.
    • (2011) J Neurochem , vol.117 , pp. 779-796
    • Lichtenthaler, S.F.1    Haass, C.2    Steiner, H.3
  • 30
    • 53749105377 scopus 로고    scopus 로고
    • Presenilins: members of the gamma-secretase quartets, but part-time soloists too
    • doi:10.1152/physiol.00009.2008
    • Wakabayashi T, De Strooper B, (2008) Presenilins: members of the gamma-secretase quartets, but part-time soloists too. Physiol (Bethesda) 23: 194-204. doi:10.1152/physiol.00009.2008. PubMed: 18697993.
    • (2008) Physiol (Bethesda) , vol.23 , pp. 194-204
    • Wakabayashi, T.1    De Strooper, B.2
  • 31
    • 0035816661 scopus 로고    scopus 로고
    • A transcriptionally [correction of transcriptively] active complex of APP with Fe65 and histone acetyltransferase Tip60
    • doi:10.1126/science.1058783
    • Cao X, Südhof TC, (2001) A transcriptionally [correction of transcriptively] active complex of APP with Fe65 and histone acetyltransferase Tip60. Science 293: 115-120. doi:10.1126/science.1058783. PubMed: 11441186.
    • (2001) Science , vol.293 , pp. 115-120
    • Cao, X.1    Südhof, T.C.2
  • 32
    • 0033920919 scopus 로고    scopus 로고
    • Notch signal transduction: a real rip and more
    • doi:10.1016/S0959-437X(00)00097-6
    • Weinmaster G, (2000) Notch signal transduction: a real rip and more. Curr Opin Genet Dev 10: 363-369. doi:10.1016/S0959-437X(00)00097-6. PubMed: 10889061.
    • (2000) Curr Opin Genet Dev , vol.10 , pp. 363-369
    • Weinmaster, G.1
  • 33
    • 0037470179 scopus 로고    scopus 로고
    • The Coxsackievirus and adenovirus receptor (CAR) forms a complex with the PDZ domain-containing protein ligand-of-numb protein-X (LNX)
    • doi:10.1074/jbc.M205927200
    • Sollerbrant K, Raschperger E, Mirza M, Engstrom U, Philipson L, et al. (2003) The Coxsackievirus and adenovirus receptor (CAR) forms a complex with the PDZ domain-containing protein ligand-of-numb protein-X (LNX). J Biol Chem 278: 7439-7444. doi:10.1074/jbc.M205927200. PubMed: 12468544.
    • (2003) J Biol Chem , vol.278 , pp. 7439-7444
    • Sollerbrant, K.1    Raschperger, E.2    Mirza, M.3    Engstrom, U.4    Philipson, L.5
  • 34
    • 13044278313 scopus 로고    scopus 로고
    • Presenilin 2 deficiency causes a mild pulmonary phenotype and no changes in amyloid precursor protein processing but enhances the embryonic lethal phenotype of presenilin 1 deficiency
    • doi:10.1073/pnas.96.21.11872
    • Herreman A, Hartmann D, Annaert W, Saftig P, Craessaerts K, et al. (1999) Presenilin 2 deficiency causes a mild pulmonary phenotype and no changes in amyloid precursor protein processing but enhances the embryonic lethal phenotype of presenilin 1 deficiency. Proc Natl Acad Sci U S A 96: 11872-11877. doi:10.1073/pnas.96.21.11872. PubMed: 10518543.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 11872-11877
    • Herreman, A.1    Hartmann, D.2    Annaert, W.3    Saftig, P.4    Craessaerts, K.5
  • 35
    • 0037444574 scopus 로고    scopus 로고
    • gamma-Secretase activity requires the presenilin-dependent trafficking of nicastrin through the Golgi apparatus but not its complex glycosylation
    • doi:10.1242/jcs.00292
    • Herreman A, Van Gassen G, Bentahir M, Nyabi O, Craessaerts K, et al. (2003) gamma-Secretase activity requires the presenilin-dependent trafficking of nicastrin through the Golgi apparatus but not its complex glycosylation. J Cell Sci 116: 1127-1136. doi:10.1242/jcs.00292. PubMed: 12584255.
    • (2003) J Cell Sci , vol.116 , pp. 1127-1136
    • Herreman, A.1    Van Gassen, G.2    Bentahir, M.3    Nyabi, O.4    Craessaerts, K.5
  • 36
    • 0027157536 scopus 로고
    • Mechanism of kit ligand, phorbol ester, and calcium-induced down-regulation of c-kit receptors in mast cells
    • Yee NS, Langen H, Besmer P, (1993) Mechanism of kit ligand, phorbol ester, and calcium-induced down-regulation of c-kit receptors in mast cells. J Biol Chem 268: 14189-14201. PubMed: 7686152.
    • (1993) J Biol Chem , vol.268 , pp. 14189-14201
    • Yee, N.S.1    Langen, H.2    Besmer, P.3
  • 37
    • 33846056925 scopus 로고    scopus 로고
    • Substrate selectivity of epidermal growth factor-receptor ligand sheddases and their regulation by phorbol esters and calcium influx
    • Horiuchi K, Le Gall S, Schulte M, Yamaguchi T, Reiss K, et al. (2007) Substrate selectivity of epidermal growth factor-receptor ligand sheddases and their regulation by phorbol esters and calcium influx. Mol Biol Cell 18: 176-188. PubMed: 17079736.
    • (2007) Mol Biol Cell , vol.18 , pp. 176-188
    • Horiuchi, K.1    Le Gall, S.2    Schulte, M.3    Yamaguchi, T.4    Reiss, K.5
  • 38
    • 65249090883 scopus 로고    scopus 로고
    • ADAMs 10 and 17 represent differentially regulated components of a general shedding machinery for membrane proteins such as transforming growth factor alpha, L-selectin, and tumor necrosis factor alpha
    • doi:10.1091/mbc.E08-11-1135
    • Le Gall, Bobé P, Reiss K, Horiuchi K, Niu XD, et al. (2009) ADAMs 10 and 17 represent differentially regulated components of a general shedding machinery for membrane proteins such as transforming growth factor alpha, L-selectin, and tumor necrosis factor alpha. Mol Biol Cell 20: 1785-1794. doi:10.1091/mbc.E08-11-1135. PubMed: 19158376.
    • (2009) Mol Biol Cell , vol.20 , pp. 1785-1794
    • Le, G.1    Bobé, P.2    Reiss, K.3    Horiuchi, K.4    Niu, X.D.5
  • 39
    • 0020326790 scopus 로고
    • Direct activation of calcium-activated, phospholipid-dependent protein kinase by tumor-promoting phorbol esters
    • Castagna M, Takai Y, Kaibuchi K, Sano K, Kikkawa U, et al. (1982) Direct activation of calcium-activated, phospholipid-dependent protein kinase by tumor-promoting phorbol esters. J Biol Chem 257: 7847-7851. PubMed: 7085651.
    • (1982) J Biol Chem , vol.257 , pp. 7847-7851
    • Castagna, M.1    Takai, Y.2    Kaibuchi, K.3    Sano, K.4    Kikkawa, U.5
  • 40
    • 0036882397 scopus 로고    scopus 로고
    • Protein ectodomain shedding
    • doi:10.1021/cr010202t
    • Arribas J, Borroto A, (2002) Protein ectodomain shedding. Chem Rev 102: 4627-4638. doi:10.1021/cr010202t. PubMed: 12475204.
    • (2002) Chem Rev , vol.102 , pp. 4627-4638
    • Arribas, J.1    Borroto, A.2
  • 41
    • 1442358746 scopus 로고    scopus 로고
    • Distinct roles for ADAM10 and ADAM17 in ectodomain shedding of six EGFR ligands
    • doi:10.1083/jcb.200307137
    • Sahin U, Weskamp G, Kelly K, Zhou HM, Higashiyama S, et al. (2004) Distinct roles for ADAM10 and ADAM17 in ectodomain shedding of six EGFR ligands. J Cell Biol 164: 769-779. doi:10.1083/jcb.200307137. PubMed: 14993236.
    • (2004) J Cell Biol , vol.164 , pp. 769-779
    • Sahin, U.1    Weskamp, G.2    Kelly, K.3    Zhou, H.M.4    Higashiyama, S.5
  • 42
    • 81255188391 scopus 로고    scopus 로고
    • Tissue inhibitors of metalloproteinases
    • doi:10.1186/gb-2011-12-11-233
    • Murphy G, (2011) Tissue inhibitors of metalloproteinases. Genome Biol 12: 233. doi:10.1186/gb-2011-12-11-233. PubMed: 22078297.
    • (2011) Genome Biol , vol.12 , pp. 233
    • Murphy, G.1
  • 43
    • 37249079599 scopus 로고    scopus 로고
    • The ADAM10 prodomain is a specific inhibitor of ADAM10 proteolytic activity and inhibits cellular shedding events
    • doi:10.1074/jbc.M703231200
    • Moss ML, Bomar M, Liu Q, Sage H, Dempsey P, et al. (2007) The ADAM10 prodomain is a specific inhibitor of ADAM10 proteolytic activity and inhibits cellular shedding events. J Biol Chem 282: 35712-35721. doi:10.1074/jbc.M703231200. PubMed: 17895248.
    • (2007) J Biol Chem , vol.282 , pp. 35712-35721
    • Moss, M.L.1    Bomar, M.2    Liu, Q.3    Sage, H.4    Dempsey, P.5
  • 44
    • 33847268830 scopus 로고    scopus 로고
    • Solution structure of the coxsackievirus and adenovirus receptor domain 2
    • doi:10.1110/ps.062643507
    • Jiang S, Caffrey M, (2007) Solution structure of the coxsackievirus and adenovirus receptor domain 2. Protein Sci 16: 539-542. doi:10.1110/ps.062643507. PubMed: 17322536.
    • (2007) Protein Sci , vol.16 , pp. 539-542
    • Jiang, S.1    Caffrey, M.2
  • 45
    • 77956315469 scopus 로고    scopus 로고
    • Gamma-secretase and the intramembrane proteolysis of Notch
    • doi:10.1016/S0070-2153(10)92006-1
    • Jorissen E, De Strooper B, (2010) Gamma-secretase and the intramembrane proteolysis of Notch. Curr Top Dev Biol 92: 201-230. doi:10.1016/S0070-2153(10)92006-1. PubMed: 20816396.
    • (2010) Curr Top Dev Biol , vol.92 , pp. 201-230
    • Jorissen, E.1    De Strooper, B.2
  • 46
    • 2342661720 scopus 로고    scopus 로고
    • Regulators of neurite outgrowth: role of cell adhesion molecules
    • doi:10.1196/annals.1294.015
    • Kiryushko D, Berezin V, Bock E, (2004) Regulators of neurite outgrowth: role of cell adhesion molecules. Ann N Y Acad Sci 1014: 140-154. doi:10.1196/annals.1294.015. PubMed: 15153429.
    • (2004) Ann N Y Acad Sci , vol.1014 , pp. 140-154
    • Kiryushko, D.1    Berezin, V.2    Bock, E.3
  • 47
    • 16244411349 scopus 로고    scopus 로고
    • Calcium signalling in growth cone migration
    • doi:10.1016/j.ceca.2005.01.007
    • Bolsover SR, (2005) Calcium signalling in growth cone migration. Cell Calcium 37: 395-402. doi:10.1016/j.ceca.2005.01.007. PubMed: 15820386.
    • (2005) Cell Calcium , vol.37 , pp. 395-402
    • Bolsover, S.R.1
  • 48
    • 27844539756 scopus 로고    scopus 로고
    • Protein kinase C and the regulation of the actin cytoskeleton
    • doi:10.1016/j.cellsig.2005.07.010
    • Larsson C, (2006) Protein kinase C and the regulation of the actin cytoskeleton. Cell Signal 18: 276-284. doi:10.1016/j.cellsig.2005.07.010. PubMed: 16109477.
    • (2006) Cell Signal , vol.18 , pp. 276-284
    • Larsson, C.1
  • 50
    • 3042554386 scopus 로고    scopus 로고
    • Cell-matrix interaction via CD44 is independently regulated by different metalloproteinases activated in response to extracellular Ca(2+) influx and PKC activation
    • doi:10.1083/jcb.200310024
    • Nagano O, Murakami D, Hartmann D, De Strooper B, Saftig P, et al. (2004) Cell-matrix interaction via CD44 is independently regulated by different metalloproteinases activated in response to extracellular Ca(2+) influx and PKC activation. J Cell Biol 165: 893-902. doi:10.1083/jcb.200310024. PubMed: 15197174.
    • (2004) J Cell Biol , vol.165 , pp. 893-902
    • Nagano, O.1    Murakami, D.2    Hartmann, D.3    De Strooper, B.4    Saftig, P.5
  • 51
    • 83555165986 scopus 로고    scopus 로고
    • MMP-9 induces CD44 cleavage and CD44 mediated cell migration in glioblastoma xenograft cells
    • doi:10.1016/j.cellsig.2011.10.008
    • Chetty C, Vanamala SK, Gondi CS, Dinh DH, Gujrati M, et al. (2012) MMP-9 induces CD44 cleavage and CD44 mediated cell migration in glioblastoma xenograft cells. Cell Signal 24: 549-559. doi:10.1016/j.cellsig.2011.10.008. PubMed: 22024282.
    • (2012) Cell Signal , vol.24 , pp. 549-559
    • Chetty, C.1    Vanamala, S.K.2    Gondi, C.S.3    Dinh, D.H.4    Gujrati, M.5
  • 52
    • 0035947766 scopus 로고    scopus 로고
    • Membrane-type 1 matrix metalloproteinase cleaves CD44 and promotes cell migration
    • doi:10.1083/jcb.153.5.893
    • Kajita M, Itoh Y, Chiba T, Mori H, Okada A, et al. (2001) Membrane-type 1 matrix metalloproteinase cleaves CD44 and promotes cell migration. J Cell Biol 153: 893-904. doi:10.1083/jcb.153.5.893. PubMed: 11381077.
    • (2001) J Cell Biol , vol.153 , pp. 893-904
    • Kajita, M.1    Itoh, Y.2    Chiba, T.3    Mori, H.4    Okada, A.5
  • 53
    • 77955060812 scopus 로고    scopus 로고
    • Fell-Muir Lecture: Metalloproteinases: from demolition squad to master regulators
    • doi:10.1111/j.1365-2613.2010.00736.x
    • Murphy G, (2010) Fell-Muir Lecture: Metalloproteinases: from demolition squad to master regulators. Int J Exp Pathol 91: 303-313. doi:10.1111/j.1365-2613.2010.00736.x. PubMed: 20666850.
    • (2010) Int J Exp Pathol , vol.91 , pp. 303-313
    • Murphy, G.1
  • 54
    • 33646565312 scopus 로고    scopus 로고
    • (Make) stick and cut loose--disintegrin metalloproteases in development and disease
    • doi:10.1002/bdrc.20066
    • Tousseyn T, Jorissen E, Reiss K, Hartmann D, (2006) (Make) stick and cut loose--disintegrin metalloproteases in development and disease. Birth Defects Res C Embryo TODAY 78: 24-46. doi:10.1002/bdrc.20066. PubMed: 16622847.
    • (2006) Birth Defects Res C Embryo TODAY , vol.78 , pp. 24-46
    • Tousseyn, T.1    Jorissen, E.2    Reiss, K.3    Hartmann, D.4
  • 55
    • 84864106172 scopus 로고    scopus 로고
    • The cytosolic domain of protein-tyrosine kinase 7 (PTK7), generated from sequential cleavage by a disintegrin and metalloprotease 17 (ADAM17) and gamma-secretase, enhances cell proliferation and migration in colon cancer cells
    • doi:10.1074/jbc.M112.348904
    • Na HW, Shin WS, Ludwig A, Lee ST, (2012) The cytosolic domain of protein-tyrosine kinase 7 (PTK7), generated from sequential cleavage by a disintegrin and metalloprotease 17 (ADAM17) and gamma-secretase, enhances cell proliferation and migration in colon cancer cells. J Biol Chem 287: 25001-25009. doi:10.1074/jbc.M112.348904. PubMed: 22665490.
    • (2012) J Biol Chem , vol.287 , pp. 25001-25009
    • Na, H.W.1    Shin, W.S.2    Ludwig, A.3    Lee, S.T.4
  • 56
    • 77954380513 scopus 로고    scopus 로고
    • Sequential and gamma-secretase-dependent processing of the betacellulin precursor generates a palmitoylated intracellular-domain fragment that inhibits cell growth
    • doi:10.1242/jcs.060830
    • Stoeck A, Shang L, Dempsey PJ, (2010) Sequential and gamma-secretase-dependent processing of the betacellulin precursor generates a palmitoylated intracellular-domain fragment that inhibits cell growth. J Cell Sci 123: 2319-2331. doi:10.1242/jcs.060830. PubMed: 20530572.
    • (2010) J Cell Sci , vol.123 , pp. 2319-2331
    • Stoeck, A.1    Shang, L.2    Dempsey, P.J.3
  • 57
    • 54949110552 scopus 로고    scopus 로고
    • Proteomic profiling of gamma-secretase substrates and mapping of substrate requirements
    • doi:10.1371/journal.pbio.0060257
    • Hemming ML, Elias JE, Gygi SP, Selkoe DJ, (2008) Proteomic profiling of gamma-secretase substrates and mapping of substrate requirements. PLOS Biol 6: e257. doi:10.1371/journal.pbio.0060257. PubMed: 18942891.
    • (2008) PLOS Biol , vol.6
    • Hemming, M.L.1    Elias, J.E.2    Gygi, S.P.3    Selkoe, D.J.4
  • 58
    • 23744491374 scopus 로고    scopus 로고
    • Nicastrin functions as a gamma-secretase-substrate receptor
    • doi:10.1016/j.cell.2005.05.022
    • Shah S, Lee SF, Tabuchi K, Hao YH, Yu C, et al. (2005) Nicastrin functions as a gamma-secretase-substrate receptor. Cell 122: 435-447. doi:10.1016/j.cell.2005.05.022. PubMed: 16096062.
    • (2005) Cell , vol.122 , pp. 435-447
    • Shah, S.1    Lee, S.F.2    Tabuchi, K.3    Hao, Y.H.4    Yu, C.5
  • 59
    • 0027991383 scopus 로고
    • The intracellular domain of mouse Notch: a constitutively activated repressor of myogenesis directed at the basic helix-loop-helix region of MyoD
    • Kopan R, Nye JS, Weintraub H, (1994) The intracellular domain of mouse Notch: a constitutively activated repressor of myogenesis directed at the basic helix-loop-helix region of MyoD. Development 120: 2385-2396. PubMed: 7956819.
    • (1994) Development , vol.120 , pp. 2385-2396
    • Kopan, R.1    Nye, J.S.2    Weintraub, H.3
  • 60
    • 66449103810 scopus 로고    scopus 로고
    • ADAM10, the rate-limiting protease of regulated intramembrane proteolysis of Notch and other proteins, is processed by ADAMS-9, ADAMS-15, and the gamma-secretase
    • Tousseyn T, Thathiah A, Jorissen E, Raemaekers T, Konietzko U, et al. (2009) ADAM10, the rate-limiting protease of regulated intramembrane proteolysis of Notch and other proteins, is processed by ADAMS-9, ADAMS-15, and the gamma-secretase. J Biol Chem 284: 11738-11747. PubMed: 19213735.
    • (2009) J Biol Chem , vol.284 , pp. 11738-11747
    • Tousseyn, T.1    Thathiah, A.2    Jorissen, E.3    Raemaekers, T.4    Konietzko, U.5
  • 61
    • 0038322593 scopus 로고    scopus 로고
    • gamma-Secretase cleavage and binding to FE65 regulate the nuclear translocation of the intracellular C-terminal domain (ICD) of the APP family of proteins
    • doi:10.1021/bi027375c
    • Walsh DM, Fadeeva JV, LaVoie MJ, Paliga K, Eggert S, et al. (2003) gamma-Secretase cleavage and binding to FE65 regulate the nuclear translocation of the intracellular C-terminal domain (ICD) of the APP family of proteins. Biochemistry 42: 6664-6673. doi:10.1021/bi027375c. PubMed: 12779321.
    • (2003) Biochemistry , vol.42 , pp. 6664-6673
    • Walsh, D.M.1    Fadeeva, J.V.2    LaVoie, M.J.3    Paliga, K.4    Eggert, S.5
  • 62
    • 37549016046 scopus 로고    scopus 로고
    • Regulation of Notch signaling by dynamic changes in the precision of S3 cleavage of Notch-1
    • doi:10.1128/MCB.00863-07
    • Tagami S, Okochi M, Yanagida K, Ikuta A, Fukumori A, et al. (2008) Regulation of Notch signaling by dynamic changes in the precision of S3 cleavage of Notch-1. Mol Cell Biol 28: 165-176. doi:10.1128/MCB.00863-07. PubMed: 17967888.
    • (2008) Mol Cell Biol , vol.28 , pp. 165-176
    • Tagami, S.1    Okochi, M.2    Yanagida, K.3    Ikuta, A.4    Fukumori, A.5
  • 63
    • 8844229536 scopus 로고    scopus 로고
    • Mastermind recruits CycC:CDK8 to phosphorylate the Notch ICD and coordinate activation with turnover
    • doi:10.1016/j.molcel.2004.10.014
    • Fryer CJ, White JB, Jones KA, (2004) Mastermind recruits CycC:CDK8 to phosphorylate the Notch ICD and coordinate activation with turnover. Mol Cell 16: 509-520. doi:10.1016/j.molcel.2004.10.014. PubMed: 15546612.
    • (2004) Mol Cell , vol.16 , pp. 509-520
    • Fryer, C.J.1    White, J.B.2    Jones, K.A.3
  • 64
    • 2942557122 scopus 로고    scopus 로고
    • Gamma-secretase: proteasome of the membrane?
    • doi:10.1038/nrg1380
    • Kopan R, Ilagan MX, (2004) Gamma-secretase: proteasome of the membrane? Nat Rev Mol Cell Biol 5: 499-504. doi:10.1038/nrg1380. PubMed: 15173829.
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 499-504
    • Kopan, R.1    Ilagan, M.X.2
  • 65
    • 0032574993 scopus 로고    scopus 로고
    • Notch-1 signalling requires ligand-induced proteolytic release of intracellular domain
    • doi:10.1038/30756
    • Schroeter EH, Kisslinger JA, Kopan R, (1998) Notch-1 signalling requires ligand-induced proteolytic release of intracellular domain. Nature 393: 382-386. doi:10.1038/30756. PubMed: 9620803.
    • (1998) Nature , vol.393 , pp. 382-386
    • Schroeter, E.H.1    Kisslinger, J.A.2    Kopan, R.3
  • 66
    • 0036102154 scopus 로고    scopus 로고
    • Fatty acid modification of the coxsackievirus and adenovirus receptor
    • doi:10.1128/JVI.76.12.6382-6386.2002
    • van't Hof W, Crystal RG, (2002) Fatty acid modification of the coxsackievirus and adenovirus receptor. J Virol 76: 6382-6386. doi:10.1128/JVI.76.12.6382-6386.2002. PubMed: 12021372.
    • (2002) J Virol , vol.76 , pp. 6382-6386
    • van't Hof, W.1    Crystal, R.G.2
  • 67
    • 78650718836 scopus 로고    scopus 로고
    • The intracellular dynamic of protein palmitoylation
    • doi:10.1083/jcb.201008160
    • Salaun C, Greaves J, Chamberlain LH, (2010) The intracellular dynamic of protein palmitoylation. J Cell Biol 191: 1229-1238. doi:10.1083/jcb.201008160. PubMed: 21187327.
    • (2010) J Cell Biol , vol.191 , pp. 1229-1238
    • Salaun, C.1    Greaves, J.2    Chamberlain, L.H.3
  • 68
    • 67349131266 scopus 로고    scopus 로고
    • Dynamic protein palmitoylation in cellular signaling
    • doi:10.1016/j.plipres.2009.02.001
    • Iwanaga T, Tsutsumi R, Noritake J, Fukata Y, Fukata M, (2009) Dynamic protein palmitoylation in cellular signaling. Prog Lipid Res 48: 117-127. doi:10.1016/j.plipres.2009.02.001. PubMed: 19233228.
    • (2009) Prog Lipid Res , vol.48 , pp. 117-127
    • Iwanaga, T.1    Tsutsumi, R.2    Noritake, J.3    Fukata, Y.4    Fukata, M.5
  • 69
    • 84867722362 scopus 로고    scopus 로고
    • Activity-dependent proteolytic cleavage of neuroligin-1
    • doi:10.1016/j.neuron.2012.10.003
    • Suzuki K, Hayashi Y, Nakahara S, Kumazaki H, Prox J, et al. (2012) Activity-dependent proteolytic cleavage of neuroligin-1. Neuron 76: 410-422. doi:10.1016/j.neuron.2012.10.003. PubMed: 23083742.
    • (2012) Neuron , vol.76 , pp. 410-422
    • Suzuki, K.1    Hayashi, Y.2    Nakahara, S.3    Kumazaki, H.4    Prox, J.5
  • 70
    • 33745086859 scopus 로고    scopus 로고
    • Proteolytic cleavage of the neural cell adhesion molecule by ADAM17/TACE is involved in neurite outgrowth
    • doi:10.1111/j.1471-4159.2006.03847.x
    • Kalus I, Bormann U, Mzoughi M, Schachner M, Kleene R, (2006) Proteolytic cleavage of the neural cell adhesion molecule by ADAM17/TACE is involved in neurite outgrowth. J Neurochem 98: 78-88. doi:10.1111/j.1471-4159.2006.03847.x. PubMed: 16805798.
    • (2006) J Neurochem , vol.98 , pp. 78-88
    • Kalus, I.1    Bormann, U.2    Mzoughi, M.3    Schachner, M.4    Kleene, R.5
  • 71
    • 21844474852 scopus 로고    scopus 로고
    • Neural cell adhesion molecule function is regulated by metalloproteinase-mediated ectodomain release
    • doi:10.1002/jnr.20530
    • Hübschmann MV, Skladchikova G, Bock E, Berezin V, (2005) Neural cell adhesion molecule function is regulated by metalloproteinase-mediated ectodomain release. J Neurosci Res 80: 826-837. doi:10.1002/jnr.20530. PubMed: 15884014.
    • (2005) J Neurosci Res , vol.80 , pp. 826-837
    • Hübschmann, M.V.1    Skladchikova, G.2    Bock, E.3    Berezin, V.4
  • 72
    • 41149135274 scopus 로고    scopus 로고
    • Developmental regulation of GABAergic interneuron branching and synaptic development in the prefrontal cortex by soluble neural cell adhesion molecule
    • doi:10.1016/j.mcn.2008.01.006
    • Brennaman LH, Maness PF, (2008) Developmental regulation of GABAergic interneuron branching and synaptic development in the prefrontal cortex by soluble neural cell adhesion molecule. Mol Cell Neurosci 37: 781-793. doi:10.1016/j.mcn.2008.01.006. PubMed: 18289872.
    • (2008) Mol Cell Neurosci , vol.37 , pp. 781-793
    • Brennaman, L.H.1    Maness, P.F.2
  • 73
    • 33750807736 scopus 로고    scopus 로고
    • Metalloprotease-induced ectodomain shedding of neural cell adhesion molecule (NCAM)
    • doi:10.1002/neu.20257
    • Hinkle CL, Diestel S, Lieberman J, Maness PF, (2006) Metalloprotease-induced ectodomain shedding of neural cell adhesion molecule (NCAM). J Neurobiol 66: 1378-1395. doi:10.1002/neu.20257. PubMed: 16967505.
    • (2006) J Neurobiol , vol.66 , pp. 1378-1395
    • Hinkle, C.L.1    Diestel, S.2    Lieberman, J.3    Maness, P.F.4
  • 74
    • 33845567392 scopus 로고    scopus 로고
    • TACE-induced cleavage of NgR and p75NTR in dorsal root ganglion cultures disinhibits outgrowth and promotes branching of neurites in the presence of inhibitory CNS myelin
    • doi:10.1096/fj.05-5339fje
    • Ahmed Z, Mazibrada G, Seabright RJ, Dent RG, Berry M, et al. (2006) TACE-induced cleavage of NgR and p75NTR in dorsal root ganglion cultures disinhibits outgrowth and promotes branching of neurites in the presence of inhibitory CNS myelin. FASEB J 20: 1939-1941. doi:10.1096/fj.05-5339fje. PubMed: 16849393.
    • (2006) FASEB J , vol.20 , pp. 1939-1941
    • Ahmed, Z.1    Mazibrada, G.2    Seabright, R.J.3    Dent, R.G.4    Berry, M.5
  • 75
    • 84876553840 scopus 로고    scopus 로고
    • An intracellular domain fragment of the p75 neurotrophin receptor (p75(NTR)) enhances tropomyosin receptor kinase A (TrkA) receptor function
    • doi:10.1074/jbc.M112.436469
    • Matusica D, Skeldal S, Sykes AM, Palstra N, Sharma A, et al. (2013) An intracellular domain fragment of the p75 neurotrophin receptor (p75(NTR)) enhances tropomyosin receptor kinase A (TrkA) receptor function. J Biol Chem 288: 11144-11154. doi:10.1074/jbc.M112.436469. PubMed: 23471969.
    • (2013) J Biol Chem , vol.288 , pp. 11144-11154
    • Matusica, D.1    Skeldal, S.2    Sykes, A.M.3    Palstra, N.4    Sharma, A.5
  • 76
    • 33646153988 scopus 로고    scopus 로고
    • The coxsackie- and adenovirus receptor (CAR) is an in vivo marker for epithelial tight junctions, with a potential role in regulating permeability and tissue homeostasis
    • doi:10.1016/j.yexcr.2006.01.025
    • Raschperger E, Thyberg J, Pettersson S, Philipson L, Fuxe J, et al. (2006) The coxsackie- and adenovirus receptor (CAR) is an in vivo marker for epithelial tight junctions, with a potential role in regulating permeability and tissue homeostasis. Exp Cell Res 312: 1566-1580. doi:10.1016/j.yexcr.2006.01.025. PubMed: 16542650.
    • (2006) Exp Cell Res , vol.312 , pp. 1566-1580
    • Raschperger, E.1    Thyberg, J.2    Pettersson, S.3    Philipson, L.4    Fuxe, J.5
  • 77
    • 33747736649 scopus 로고    scopus 로고
    • A basolateral sorting signal directs ADAM10 to adherens junctions and is required for its function in cell migration
    • doi:10.1074/jbc.M601542200
    • Wild-Bode C, Fellerer K, Kugler J, Haass C, Capell A, (2006) A basolateral sorting signal directs ADAM10 to adherens junctions and is required for its function in cell migration. J Biol Chem 281: 23824-23829. doi:10.1074/jbc.M601542200. PubMed: 16777847.
    • (2006) J Biol Chem , vol.281 , pp. 23824-23829
    • Wild-Bode, C.1    Fellerer, K.2    Kugler, J.3    Haass, C.4    Capell, A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.