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Volumn 32, Issue , 2016, Pages 51-64

Intramembrane proteolysis within lysosomes

Author keywords

Alzheimer Disease; CD74; Intramembrane proteolysis; Lysosome; Signal peptide peptidase like 2a protease; Secretase

Indexed keywords

AMYLOID BETA PROTEIN; CD74 ANTIGEN; FAS LIGAND; GAMMA SECRETASE; INTRAMEMBRANE PROTEOLYSIS OF BRI2; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 2; MEMBRANE PROTEIN; MUTANT PROTEIN; PRESENILIN; SIGNAL PEPTIDE; SIGNAL PEPTIDE PEPTIDASE LIKE PROTEASE 2A; TRANSMEMBRANE PROTEIN 106B; TUMOR NECROSIS FACTOR; UNCLASSIFIED DRUG; ASPARTIC PROTEINASE; B LYMPHOCYTE ANTIGEN; HLA ANTIGEN CLASS 2; INVARIANT CHAIN; SECRETASE; SIGNAL PEPTIDE PEPTIDASE;

EID: 84965140076     PISSN: 15681637     EISSN: 18729649     Source Type: Journal    
DOI: 10.1016/j.arr.2016.04.012     Document Type: Review
Times cited : (16)

References (205)
  • 1
    • 84942087481 scopus 로고    scopus 로고
    • Clipping or extracting: two ways to membrane protein degradation
    • Avci, D., Lemberg, M.K., Clipping or extracting: two ways to membrane protein degradation. Trends Cell Biol. 25 (2015), 611–622.
    • (2015) Trends Cell Biol. , vol.25 , pp. 611-622
    • Avci, D.1    Lemberg, M.K.2
  • 2
    • 84919466648 scopus 로고    scopus 로고
    • The yeast ER-intramembrane protease Ypf1 refines nutrient sensing by regulating transporter abundance
    • Avci, D., Fuchs, S., Schrul, B., Fukumori, A., Breker, M., Frumkin, I., Chen, C.Y., Biniossek, M.L., et al. The yeast ER-intramembrane protease Ypf1 refines nutrient sensing by regulating transporter abundance. Mol. Cell 56 (2014), 630–640.
    • (2014) Mol. Cell , vol.56 , pp. 630-640
    • Avci, D.1    Fuchs, S.2    Schrul, B.3    Fukumori, A.4    Breker, M.5    Frumkin, I.6    Chen, C.Y.7    Biniossek, M.L.8
  • 3
    • 84883450693 scopus 로고    scopus 로고
    • The balance of protein expression and degradation: an ESCRTs point of view
    • Babst, M., Odorizzi, G., The balance of protein expression and degradation: an ESCRTs point of view. Curr. Opin. Cell Biol. 25 (2013), 489–494.
    • (2013) Curr. Opin. Cell Biol. , vol.25 , pp. 489-494
    • Babst, M.1    Odorizzi, G.2
  • 4
    • 79960743373 scopus 로고    scopus 로고
    • MVB vesicle formation ESCRT-dependent, ESCRT-independent and everything in between
    • Babst, M., MVB vesicle formation ESCRT-dependent, ESCRT-independent and everything in between. Curr. Opin. Cell Biol. 23 (2011), 452–457.
    • (2011) Curr. Opin. Cell Biol. , vol.23 , pp. 452-457
    • Babst, M.1
  • 5
    • 51349158272 scopus 로고    scopus 로고
    • Role of MIF in inflammation and tumorigenesis
    • Bach, J.P., Rinn, B., Meyer, B., Dodel, R., Bacher, M., Role of MIF in inflammation and tumorigenesis. Oncology 75 (2008), 127–133.
    • (2008) Oncology , vol.75 , pp. 127-133
    • Bach, J.P.1    Rinn, B.2    Meyer, B.3    Dodel, R.4    Bacher, M.5
  • 7
    • 23344454950 scopus 로고    scopus 로고
    • Lysosomal membrane proteomics and biogenesis of lysosomes
    • Bagshaw, R.D., Mahuran, D.J., Callahan, J.W., Lysosomal membrane proteomics and biogenesis of lysosomes. Mol. Neurobiol. 32 (2005), 27–41.
    • (2005) Mol. Neurobiol. , vol.32 , pp. 27-41
    • Bagshaw, R.D.1    Mahuran, D.J.2    Callahan, J.W.3
  • 8
    • 27644575670 scopus 로고    scopus 로고
    • CD74 is a member of the regulated intramembrane proteolysis-processed protein family
    • Becker-Herman, S., Arie, G., Medvedovsky, H., Kerem, A., Shachar, I., CD74 is a member of the regulated intramembrane proteolysis-processed protein family. Mol. Biol. Cell 16 (2005), 5061–5069.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 5061-5069
    • Becker-Herman, S.1    Arie, G.2    Medvedovsky, H.3    Kerem, A.4    Shachar, I.5
  • 9
    • 80053248954 scopus 로고    scopus 로고
    • Signal-peptide-peptidase-like 2a (SPPL2a) is targeted to lysosomes/late endosomes by a tyrosine motif in its C-terminal tail
    • Behnke, J., Schneppenheim, J., Koch-Nolte, F., Haag, F., Saftig, P., Schröder, B., Signal-peptide-peptidase-like 2a (SPPL2a) is targeted to lysosomes/late endosomes by a tyrosine motif in its C-terminal tail. FEBS Lett. 585 (2011), 2951–2957.
    • (2011) FEBS Lett. , vol.585 , pp. 2951-2957
    • Behnke, J.1    Schneppenheim, J.2    Koch-Nolte, F.3    Haag, F.4    Saftig, P.5    Schröder, B.6
  • 10
    • 84874516142 scopus 로고    scopus 로고
    • The intramembrane protease Sppl2a is required for B cell and DC development and survival via cleavage of the invariant chain
    • Beisner, D.R., Langerak, P., Parker, A.E., Dahlberg, C., Otero, F.J., Sutton, S.E., Poirot, L., Barnes, W., et al. The intramembrane protease Sppl2a is required for B cell and DC development and survival via cleavage of the invariant chain. J. Exp. Med. 210 (2013), 23–30.
    • (2013) J. Exp. Med. , vol.210 , pp. 23-30
    • Beisner, D.R.1    Langerak, P.2    Parker, A.E.3    Dahlberg, C.4    Otero, F.J.5    Sutton, S.E.6    Poirot, L.7    Barnes, W.8
  • 11
    • 84874520391 scopus 로고    scopus 로고
    • B cell survival, surface BCR and BAFFR expression, CD74 metabolism, and CD8- dendritic cells require the intramembrane endopeptidase SPPL2A
    • Bergmann, H., Yabas, M., Short, A., Miosge, L., Barthel, N., Teh, C.E., Roots, C.M., Bull, K.R., et al. B cell survival, surface BCR and BAFFR expression, CD74 metabolism, and CD8- dendritic cells require the intramembrane endopeptidase SPPL2A. J. Exp. Med. 210 (2013), 31–40.
    • (2013) J. Exp. Med. , vol.210 , pp. 31-40
    • Bergmann, H.1    Yabas, M.2    Short, A.3    Miosge, L.4    Barthel, N.5    Teh, C.E.6    Roots, C.M.7    Bull, K.R.8
  • 13
    • 84904215127 scopus 로고    scopus 로고
    • Regulated intramembrane proteolysis of the frontotemporal lobar degeneration risk factor, TMEM106B, by signal peptide peptidase-like 2a (SPPL2a)
    • Brady, O.A., Zhou, X., Hu, F., Regulated intramembrane proteolysis of the frontotemporal lobar degeneration risk factor, TMEM106B, by signal peptide peptidase-like 2a (SPPL2a). J. Biol. Chem. 289 (2014), 19670–19680.
    • (2014) J. Biol. Chem. , vol.289 , pp. 19670-19680
    • Brady, O.A.1    Zhou, X.2    Hu, F.3
  • 15
    • 0030941803 scopus 로고    scopus 로고
    • The SREBP pathway: regulation of cholesterol metabolism by proteolysis of a membrane-bound transcription factor
    • Brown, M.S., Goldstein, J.L., The SREBP pathway: regulation of cholesterol metabolism by proteolysis of a membrane-bound transcription factor. Cell 89 (1997), 331–340.
    • (1997) Cell , vol.89 , pp. 331-340
    • Brown, M.S.1    Goldstein, J.L.2
  • 19
    • 0034711207 scopus 로고    scopus 로고
    • Carboxyl-terminal fragments of Alzheimer beta-amyloid precursor protein accumulate in restricted and unpredicted intracellular compartments in presenilin 1-deficient cells
    • Chen, F., Yang, D.S., Petanceska, S., Yang, A., Tandon, A., Yu, G., Rozmahel, R., Ghiso, J., et al. Carboxyl-terminal fragments of Alzheimer beta-amyloid precursor protein accumulate in restricted and unpredicted intracellular compartments in presenilin 1-deficient cells. J. Biol. Chem. 275 (2000), 36794–36802.
    • (2000) J. Biol. Chem. , vol.275 , pp. 36794-36802
    • Chen, F.1    Yang, D.S.2    Petanceska, S.3    Yang, A.4    Tandon, A.5    Yu, G.6    Rozmahel, R.7    Ghiso, J.8
  • 20
    • 84922219279 scopus 로고    scopus 로고
    • Signal peptide peptidase functions in ERAD to cleave the unfolded protein response regulator XBP1u
    • Chen, C.Y., Malchus, N.S., Hehn, B., Stelzer, W., Avci, D., Langosch, D., Lemberg, M.K., Signal peptide peptidase functions in ERAD to cleave the unfolded protein response regulator XBP1u. EMBO J. 33 (2014), 2492–2506.
    • (2014) EMBO J. , vol.33 , pp. 2492-2506
    • Chen, C.Y.1    Malchus, N.S.2    Hehn, B.3    Stelzer, W.4    Avci, D.5    Langosch, D.6    Lemberg, M.K.7
  • 21
    • 84979996194 scopus 로고    scopus 로고
    • Physical and functional interaction between the alpha- and gamma-secretases: a new model of regulated intramembrane proteolysis
    • Chen, A.C., Kim, S., Shepardson, N., Patel, S., Hong, S., Selkoe, D.J., Physical and functional interaction between the alpha- and gamma-secretases: a new model of regulated intramembrane proteolysis. J. Cell Biol. 211 (2015), 1157–1176.
    • (2015) J. Cell Biol. , vol.211 , pp. 1157-1176
    • Chen, A.C.1    Kim, S.2    Shepardson, N.3    Patel, S.4    Hong, S.5    Selkoe, D.J.6
  • 22
    • 1442265701 scopus 로고    scopus 로고
    • Axonal transport of British and Danish amyloid peptides via secretory vesicles
    • Choi, S.I., Vidal, R., Frangione, B., Levy, E., Axonal transport of British and Danish amyloid peptides via secretory vesicles. FASEB J. 18 (2004), 373–375.
    • (2004) FASEB J. , vol.18 , pp. 373-375
    • Choi, S.I.1    Vidal, R.2    Frangione, B.3    Levy, E.4
  • 23
    • 84865086929 scopus 로고    scopus 로고
    • Lysosomal calcium homeostasis defects, not proton pump defects, cause endo-lysosomal dysfunction in PSEN-deficient cells
    • Coen, K., Flannagan, R.S., Baron, S., Carraro-Lacroix, L.R., Wang, D., Vermeire, W., Michiels, C., Munck, S., et al. Lysosomal calcium homeostasis defects, not proton pump defects, cause endo-lysosomal dysfunction in PSEN-deficient cells. J. Cell Biol. 198 (2012), 23–35.
    • (2012) J. Cell Biol. , vol.198 , pp. 23-35
    • Coen, K.1    Flannagan, R.S.2    Baron, S.3    Carraro-Lacroix, L.R.4    Wang, D.5    Vermeire, W.6    Michiels, C.7    Munck, S.8
  • 24
    • 84896730305 scopus 로고    scopus 로고
    • Lysosomal alkalization and dysfunction in human fibroblasts with the Alzheimer's disease-linked presenilin 1 A246E mutation can be reversed with cAMP
    • Coffey, E.E., Beckel, J.M., Laties, A.M., Mitchell, C.H., Lysosomal alkalization and dysfunction in human fibroblasts with the Alzheimer's disease-linked presenilin 1 A246E mutation can be reversed with cAMP. Neuroscience 263 (2014), 111–124.
    • (2014) Neuroscience , vol.263 , pp. 111-124
    • Coffey, E.E.1    Beckel, J.M.2    Laties, A.M.3    Mitchell, C.H.4
  • 25
    • 70449336081 scopus 로고    scopus 로고
    • Diverse regulatory roles for lysosomal proteases in the immune response
    • Colbert, J.D., Matthews, S.P., Miller, G., Watts, C., Diverse regulatory roles for lysosomal proteases in the immune response. Eur. J. Immunol. 39 (2009), 2955–2965.
    • (2009) Eur. J. Immunol. , vol.39 , pp. 2955-2965
    • Colbert, J.D.1    Matthews, S.P.2    Miller, G.3    Watts, C.4
  • 26
    • 84868516038 scopus 로고    scopus 로고
    • Safety and tolerability of the gamma-secretase inhibitor avagacestat in a phase 2 study of mild to moderate Alzheimer disease
    • Coric, V., van Dyck, C.H., Salloway, S., Andreasen, N., Brody, M., Richter, R.W., Soininen, H., Thein, S., et al. Safety and tolerability of the gamma-secretase inhibitor avagacestat in a phase 2 study of mild to moderate Alzheimer disease. Arch. Neurol. 69 (2012), 1430–1440.
    • (2012) Arch. Neurol. , vol.69 , pp. 1430-1440
    • Coric, V.1    van Dyck, C.H.2    Salloway, S.3    Andreasen, N.4    Brody, M.5    Richter, R.W.6    Soininen, H.7    Thein, S.8
  • 27
    • 84872389663 scopus 로고    scopus 로고
    • Roles of proteolysis in regulation of GPCR function
    • Cottrell, G.S., Roles of proteolysis in regulation of GPCR function. Br. J. Pharmacol. 168 (2013), 576–590.
    • (2013) Br. J. Pharmacol. , vol.168 , pp. 576-590
    • Cottrell, G.S.1
  • 28
    • 84877762179 scopus 로고    scopus 로고
    • Development and mechanism of gamma-secretase modulators for Alzheimer's disease
    • Crump, C.J., Johnson, D.S., Li, Y.M., Development and mechanism of gamma-secretase modulators for Alzheimer's disease. Biochemistry 52 (2013), 3197–3216.
    • (2013) Biochemistry , vol.52 , pp. 3197-3216
    • Crump, C.J.1    Johnson, D.S.2    Li, Y.M.3
  • 29
    • 0037413688 scopus 로고    scopus 로고
    • Cathepsin A regulates chaperone-mediated autophagy through cleavage of the lysosomal receptor
    • Cuervo, A.M., Mann, L., Bonten, E.J., d'Azzo, A., Dice, J.F., Cathepsin A regulates chaperone-mediated autophagy through cleavage of the lysosomal receptor. EMBO J. 22 (2003), 47–59.
    • (2003) EMBO J. , vol.22 , pp. 47-59
    • Cuervo, A.M.1    Mann, L.2    Bonten, E.J.3    d'Azzo, A.4    Dice, J.F.5
  • 30
    • 84920771964 scopus 로고    scopus 로고
    • Learning by failing: ideas and concepts to tackle gamma-secretases in Alzheimer's disease and beyond
    • De Strooper, B., Chavez Gutierrez, L., Learning by failing: ideas and concepts to tackle gamma-secretases in Alzheimer's disease and beyond. Annu. Rev. Pharmacol. Toxicol. 55 (2015), 419–437.
    • (2015) Annu. Rev. Pharmacol. Toxicol. , vol.55 , pp. 419-437
    • De Strooper, B.1    Chavez Gutierrez, L.2
  • 33
    • 84863939887 scopus 로고    scopus 로고
    • Presenilins and gamma-secretase: structure, function, and role in Alzheimer Disease
    • De Strooper, B., Iwatsubo, T., Wolfe, M.S., Presenilins and gamma-secretase: structure, function, and role in Alzheimer Disease. Cold Spring Harb. Perspect. Med., 2, 2012, a006304.
    • (2012) Cold Spring Harb. Perspect. Med. , vol.2 , pp. a006304
    • De Strooper, B.1    Iwatsubo, T.2    Wolfe, M.S.3
  • 34
    • 84909971843 scopus 로고    scopus 로고
    • Lessons from a failed gamma-secretase Alzheimer trial
    • De Strooper, B., Lessons from a failed gamma-secretase Alzheimer trial. Cell 159 (2014), 721–726.
    • (2014) Cell , vol.159 , pp. 721-726
    • De Strooper, B.1
  • 37
    • 77049229661 scopus 로고
    • Tissue fractionation studies. 6. Intracellular distribution patterns of enzymes in rat-liver tissue
    • de Duve, C., Pressman, B.C., Gianetto, R., Wattiaux, R., Appelmans, F., Tissue fractionation studies. 6. Intracellular distribution patterns of enzymes in rat-liver tissue. Biochem. J. 60 (1955), 604–617.
    • (1955) Biochem. J. , vol.60 , pp. 604-617
    • de Duve, C.1    Pressman, B.C.2    Gianetto, R.3    Wattiaux, R.4    Appelmans, F.5
  • 38
    • 26944475263 scopus 로고    scopus 로고
    • The lysosome turns fifty
    • de Duve, C., The lysosome turns fifty. Nat. Cell Biol. 7 (2005), 847–849.
    • (2005) Nat. Cell Biol. , vol.7 , pp. 847-849
    • de Duve, C.1
  • 39
    • 0034808209 scopus 로고    scopus 로고
    • Receptor-like properties of the 26 kDa transmembrane form of TNF
    • Domonkos, A., Udvardy, A., Laszlo, L., Nagy, T., Duda, E., Receptor-like properties of the 26 kDa transmembrane form of TNF. Eur. Cytokine Netw. 12 (2001), 411–419.
    • (2001) Eur. Cytokine Netw. , vol.12 , pp. 411-419
    • Domonkos, A.1    Udvardy, A.2    Laszlo, L.3    Nagy, T.4    Duda, E.5
  • 41
    • 77956362155 scopus 로고    scopus 로고
    • Protein homeostasis and aging in neurodegeneration
    • Douglas, P.M., Dillin, A., Protein homeostasis and aging in neurodegeneration. J. Cell Biol. 190 (2010), 719–729.
    • (2010) J. Cell Biol. , vol.190 , pp. 719-729
    • Douglas, P.M.1    Dillin, A.2
  • 43
    • 84924025819 scopus 로고    scopus 로고
    • Subcellular localization and activation of ADAM proteases in the context of FasL shedding in T lymphocytes
    • Ebsen, H., Lettau, M., Kabelitz, D., Janssen, O., Subcellular localization and activation of ADAM proteases in the context of FasL shedding in T lymphocytes. Mol. Immunol. 65 (2015), 416–428.
    • (2015) Mol. Immunol. , vol.65 , pp. 416-428
    • Ebsen, H.1    Lettau, M.2    Kabelitz, D.3    Janssen, O.4
  • 45
    • 0034660144 scopus 로고    scopus 로고
    • Reverse signaling through transmembrane TNF confers resistance to lipopolysaccharide in human monocytes and macrophages
    • Eissner, G., Kirchner, S., Lindner, H., Kolch, W., Janosch, P., Grell, M., Scheurich, P., Andreesen, R., Holler, E., Reverse signaling through transmembrane TNF confers resistance to lipopolysaccharide in human monocytes and macrophages. J. Immunol. 164 (2000), 6193–6198.
    • (2000) J. Immunol. , vol.164 , pp. 6193-6198
    • Eissner, G.1    Kirchner, S.2    Lindner, H.3    Kolch, W.4    Janosch, P.5    Grell, M.6    Scheurich, P.7    Andreesen, R.8    Holler, E.9
  • 47
    • 84961141394 scopus 로고    scopus 로고
    • A new perspective of lysosomal cation channel-dependent homeostasis in Alzheimer's disease
    • Ezeani, M., Omabe, M., A new perspective of lysosomal cation channel-dependent homeostasis in Alzheimer's disease. Mol. Neurobiol. 53 (2016), 1672–1678.
    • (2016) Mol. Neurobiol. , vol.53 , pp. 1672-1678
    • Ezeani, M.1    Omabe, M.2
  • 48
    • 58149247727 scopus 로고    scopus 로고
    • Regulation of dendritic cell migration by CD74, the MHC class II-associated invariant chain
    • Faure-Andre, G., Vargas, P., Yuseff, M.I., Heuze, M., Diaz, J., Lankar, D., Steri, V., Manry, J., et al. Regulation of dendritic cell migration by CD74, the MHC class II-associated invariant chain. Science 322 (2008), 1705–1710.
    • (2008) Science , vol.322 , pp. 1705-1710
    • Faure-Andre, G.1    Vargas, P.2    Yuseff, M.I.3    Heuze, M.4    Diaz, J.5    Lankar, D.6    Steri, V.7    Manry, J.8
  • 50
    • 49449101906 scopus 로고    scopus 로고
    • Phase 2 safety trial targeting amyloid beta production with a gamma-secretase inhibitor in Alzheimer disease
    • Fleisher, A.S., Raman, R., Siemers, E.R., Becerra, L., Clark, C.M., Dean, R.A., Farlow, M.R., Galvin, J.E., et al. Phase 2 safety trial targeting amyloid beta production with a gamma-secretase inhibitor in Alzheimer disease. Arch. Neurol. 65 (2008), 1031–1038.
    • (2008) Arch. Neurol. , vol.65 , pp. 1031-1038
    • Fleisher, A.S.1    Raman, R.2    Siemers, E.R.3    Becerra, L.4    Clark, C.M.5    Dean, R.A.6    Farlow, M.R.7    Galvin, J.E.8
  • 53
    • 18444417998 scopus 로고    scopus 로고
    • aph-1 and pen-2 are required for Notch pathway signaling gamma-secretase cleavage of betaAPP, and presenilin protein accumulation
    • Francis, R., McGrath, G., Zhang, J., Ruddy, D.A., Sym, M., Apfeld, J., Nicoll, M., Maxwell, M., et al. aph-1 and pen-2 are required for Notch pathway signaling gamma-secretase cleavage of betaAPP, and presenilin protein accumulation. Dev. Cell 3 (2002), 85–97.
    • (2002) Dev. Cell , vol.3 , pp. 85-97
    • Francis, R.1    McGrath, G.2    Zhang, J.3    Ruddy, D.A.4    Sym, M.5    Apfeld, J.6    Nicoll, M.7    Maxwell, M.8
  • 54
    • 10944270703 scopus 로고    scopus 로고
    • Consensus analysis of signal peptide peptidase and homologous human aspartic proteases reveals opposite topology of catalytic domains compared with presenilins
    • Friedmann, E., Lemberg, M.K., Weihofen, A., Dev, K.K., Dengler, U., Rovelli, G., Martoglio, B., Consensus analysis of signal peptide peptidase and homologous human aspartic proteases reveals opposite topology of catalytic domains compared with presenilins. J. Biol. Chem. 279 (2004), 50790–50798.
    • (2004) J. Biol. Chem. , vol.279 , pp. 50790-50798
    • Friedmann, E.1    Lemberg, M.K.2    Weihofen, A.3    Dev, K.K.4    Dengler, U.5    Rovelli, G.6    Martoglio, B.7
  • 56
    • 84933179778 scopus 로고    scopus 로고
    • Age-related dysfunctions of the autophagy lysosomal pathway in hippocampal pyramidal neurons under proteasome stress
    • Gavilan, E., Pintado, C., Gavilan, M.P., Daza, P., Sanchez-Aguayo, I., Castano, A., Ruano, D., Age-related dysfunctions of the autophagy lysosomal pathway in hippocampal pyramidal neurons under proteasome stress. Neurobiol. Aging 36 (2015), 1953–1963.
    • (2015) Neurobiol. Aging , vol.36 , pp. 1953-1963
    • Gavilan, E.1    Pintado, C.2    Gavilan, M.P.3    Daza, P.4    Sanchez-Aguayo, I.5    Castano, A.6    Ruano, D.7
  • 57
    • 0028962656 scopus 로고
    • Lysosomal storage diseases
    • Gieselmann, V., Lysosomal storage diseases. Biochim. Biophys. Acta 1270 (1995), 103–136.
    • (1995) Biochim. Biophys. Acta , vol.1270 , pp. 103-136
    • Gieselmann, V.1
  • 58
    • 0026539090 scopus 로고
    • Processing of the amyloid protein precursor to potentially amyloidogenic derivatives
    • Golde, T.E., Estus, S., Younkin, L.H., Selkoe, D.J., Younkin, S.G., Processing of the amyloid protein precursor to potentially amyloidogenic derivatives. Science 255 (1992), 728–730.
    • (1992) Science , vol.255 , pp. 728-730
    • Golde, T.E.1    Estus, S.2    Younkin, L.H.3    Selkoe, D.J.4    Younkin, S.G.5
  • 60
    • 0034080403 scopus 로고    scopus 로고
    • aph-2 encodes a novel extracellular protein required for GLP-1-mediated signaling
    • Goutte, C., Hepler, W., Mickey, K.M., Priess, J.R., aph-2 encodes a novel extracellular protein required for GLP-1-mediated signaling. Development 127 (2000), 2481–2492.
    • (2000) Development , vol.127 , pp. 2481-2492
    • Goutte, C.1    Hepler, W.2    Mickey, K.M.3    Priess, J.R.4
  • 61
    • 0037154158 scopus 로고    scopus 로고
    • APH-1 is a multipass membrane protein essential for the Notch signaling pathway in Caenorhabditis elegans embryos
    • Goutte, C., Tsunozaki, M., Hale, V.A., Priess, J.R., APH-1 is a multipass membrane protein essential for the Notch signaling pathway in Caenorhabditis elegans embryos. Proc. Natl. Acad. Sci. U. S. A. 99 (2002), 775–779.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 775-779
    • Goutte, C.1    Tsunozaki, M.2    Hale, V.A.3    Priess, J.R.4
  • 62
    • 72549105935 scopus 로고    scopus 로고
    • Effect of tarenflurbil on cognitive decline and activities of daily living in patients with mild Alzheimer disease: a randomized controlled trial
    • Green, R.C., Schneider, L.S., Amato, D.A., Beelen, A.P., Wilcock, G., Swabb, E.A., Zavitz, K.H., Effect of tarenflurbil on cognitive decline and activities of daily living in patients with mild Alzheimer disease: a randomized controlled trial. JAMA 302 (2009), 2557–2564.
    • (2009) JAMA , vol.302 , pp. 2557-2564
    • Green, R.C.1    Schneider, L.S.2    Amato, D.A.3    Beelen, A.P.4    Wilcock, G.5    Swabb, E.A.6    Zavitz, K.H.7
  • 64
    • 79959636033 scopus 로고    scopus 로고
    • The many substrates of presenilin/gamma-secretase
    • Haapasalo, A., Kovacs, D.M., The many substrates of presenilin/gamma-secretase. J. Alzheimers Dis. 25 (2011), 3–28.
    • (2011) J. Alzheimers Dis. , vol.25 , pp. 3-28
    • Haapasalo, A.1    Kovacs, D.M.2
  • 65
    • 0026735070 scopus 로고
    • Targeting of cell-surface beta-amyloid precursor protein to lysosomes: alternative processing into amyloid-bearing fragments
    • Haass, C., Koo, E.H., Mellon, A., Hung, A.Y., Selkoe, D.J., Targeting of cell-surface beta-amyloid precursor protein to lysosomes: alternative processing into amyloid-bearing fragments. Nature 357 (1992), 500–503.
    • (1992) Nature , vol.357 , pp. 500-503
    • Haass, C.1    Koo, E.H.2    Mellon, A.3    Hung, A.Y.4    Selkoe, D.J.5
  • 66
    • 0027535111 scopus 로고
    • beta-Amyloid peptide and a 3-kDa fragment are derived by distinct cellular mechanisms
    • Haass, C., Hung, A.Y., Schlossmacher, M.G., Teplow, D.B., Selkoe, D.J., beta-Amyloid peptide and a 3-kDa fragment are derived by distinct cellular mechanisms. J. Biol. Chem. 268 (1993), 3021–3024.
    • (1993) J. Biol. Chem. , vol.268 , pp. 3021-3024
    • Haass, C.1    Hung, A.Y.2    Schlossmacher, M.G.3    Teplow, D.B.4    Selkoe, D.J.5
  • 67
    • 41149090339 scopus 로고    scopus 로고
    • Regulation of GPCRs by endocytic membrane trafficking and its potential implications
    • Hanyaloglu, A.C., von Zastrow, M., Regulation of GPCRs by endocytic membrane trafficking and its potential implications. Annu. Rev. Pharmacol. Toxicol. 48 (2008), 537–568.
    • (2008) Annu. Rev. Pharmacol. Toxicol. , vol.48 , pp. 537-568
    • Hanyaloglu, A.C.1    von Zastrow, M.2
  • 69
    • 77954444618 scopus 로고    scopus 로고
    • Macrophage migration inhibitory factor-knockout mice are long lived and respond to caloric restriction
    • Harper, J.M., Wilkinson, J.E., Miller, R.A., Macrophage migration inhibitory factor-knockout mice are long lived and respond to caloric restriction. FASEB J. 24 (2010), 2436–2442.
    • (2010) FASEB J. , vol.24 , pp. 2436-2442
    • Harper, J.M.1    Wilkinson, J.E.2    Miller, R.A.3
  • 70
    • 79960566232 scopus 로고    scopus 로고
    • Dynamics of Abeta42 reduction in plasma, CSF and brain of rats treated with the gamma-secretase modulator, GSM-10 h
    • Hawkins, J., Harrison, D.C., Ahmed, S., Davis, R.P., Chapman, T., Marshall, I., Smith, B., Mead, T.L., et al. Dynamics of Abeta42 reduction in plasma, CSF and brain of rats treated with the gamma-secretase modulator, GSM-10 h. Neurodegener. Dis. 8 (2011), 455–464.
    • (2011) Neurodegener. Dis. , vol.8 , pp. 455-464
    • Hawkins, J.1    Harrison, D.C.2    Ahmed, S.3    Davis, R.P.4    Chapman, T.5    Marshall, I.6    Smith, B.7    Mead, T.L.8
  • 71
    • 84960153868 scopus 로고    scopus 로고
    • Homeostatic regulation of trace mineral transport by ubiquitination of membrane transporters
    • Hennigar, S.R., McClung, J.P., Homeostatic regulation of trace mineral transport by ubiquitination of membrane transporters. Nutr. Rev. 74 (2016), 59–67.
    • (2016) Nutr. Rev. , vol.74 , pp. 59-67
    • Hennigar, S.R.1    McClung, J.P.2
  • 72
    • 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
    • Herreman, A., Hartmann, D., Annaert, W., Saftig, P., Craessaerts, K., Serneels, L., Umans, L., Schrijvers, V., et al. 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 (1999), 11872–11877.
    • (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    Serneels, L.6    Umans, L.7    Schrijvers, V.8
  • 73
    • 0028987849 scopus 로고
    • Inhibition of beta-amyloid formation identifies proteolytic precursors and subcellular site of catabolism
    • Higaki, J., Quon, D., Zhong, Z., Cordell, B., Inhibition of beta-amyloid formation identifies proteolytic precursors and subcellular site of catabolism. Neuron 14 (1995), 651–659.
    • (1995) Neuron , vol.14 , pp. 651-659
    • Higaki, J.1    Quon, D.2    Zhong, Z.3    Cordell, B.4
  • 74
    • 0031081260 scopus 로고    scopus 로고
    • Membrane tumor necrosis factor-alpha (TNF-alpha) expressed on HTLV-I-infected T cells mediates a costimulatory signal for B cell activation–characterization of membrane TNF-alpha
    • Higuchi, M., Nagasawa, K., Horiuchi, T., Oike, M., Ito, Y., Yasukawa, M., Niho, Y., Membrane tumor necrosis factor-alpha (TNF-alpha) expressed on HTLV-I-infected T cells mediates a costimulatory signal for B cell activation–characterization of membrane TNF-alpha. Clin. Immunol. Immunopathol. 82 (1997), 133–140.
    • (1997) Clin. Immunol. Immunopathol. , vol.82 , pp. 133-140
    • Higuchi, M.1    Nagasawa, K.2    Horiuchi, T.3    Oike, M.4    Ito, Y.5    Yasukawa, M.6    Niho, Y.7
  • 75
    • 77954232611 scopus 로고    scopus 로고
    • Transmembrane TNF-alpha: structure, function and interaction with anti-TNF agents
    • Horiuchi, T., Mitoma, H., Harashima, S., Tsukamoto, H., Shimoda, T., Transmembrane TNF-alpha: structure, function and interaction with anti-TNF agents. Rheumatology (Oxford) 49 (2010), 1215–1228.
    • (2010) Rheumatology (Oxford) , vol.49 , pp. 1215-1228
    • Horiuchi, T.1    Mitoma, H.2    Harashima, S.3    Tsukamoto, H.4    Shimoda, T.5
  • 76
  • 77
    • 84885088410 scopus 로고    scopus 로고
    • A fast growing spectrum of biological functions of gamma-secretase in development and disease
    • Jurisch-Yaksi, N., Sannerud, R., Annaert, W., A fast growing spectrum of biological functions of gamma-secretase in development and disease. Biochim. Biophys. Acta 1828 (2013), 2815–2827.
    • (2013) Biochim. Biophys. Acta , vol.1828 , pp. 2815-2827
    • Jurisch-Yaksi, N.1    Sannerud, R.2    Annaert, W.3
  • 79
    • 33750151419 scopus 로고    scopus 로고
    • Assembly, trafficking and function of gamma-secretase
    • Kaether, C., Haass, C., Steiner, H., Assembly, trafficking and function of gamma-secretase. Neurodegener. Dis. 3 (2006), 275–283.
    • (2006) Neurodegener. Dis. , vol.3 , pp. 275-283
    • Kaether, C.1    Haass, C.2    Steiner, H.3
  • 80
    • 0011596655 scopus 로고
    • Phosphohexosyl components of a lysosomal enzyme are recognized by pinocytosis receptors on human fibroblasts
    • Kaplan, A., Achord, D.T., Sly, W.S., Phosphohexosyl components of a lysosomal enzyme are recognized by pinocytosis receptors on human fibroblasts. Proc. Natl. Acad. Sci. U. S. A. 74 (1977), 2026–2030.
    • (1977) Proc. Natl. Acad. Sci. U. S. A. , vol.74 , pp. 2026-2030
    • Kaplan, A.1    Achord, D.T.2    Sly, W.S.3
  • 81
    • 84949559900 scopus 로고    scopus 로고
    • Proteostasis and aging
    • Kaushik, S., Cuervo, A.M., Proteostasis and aging. Nat. Med. 21 (2015), 1406–1415.
    • (2015) Nat. Med. , vol.21 , pp. 1406-1415
    • Kaushik, S.1    Cuervo, A.M.2
  • 84
    • 84937605093 scopus 로고    scopus 로고
    • Evidence that the rab5 effector APPL1 mediates APP-betaCTF-induced dysfunction of endosomes in Down syndrome and Alzheimer's disease
    • Kim, S., Sato, Y., Mohan, P.S., Peterhoff, C., Pensalfini, A., Rigoglioso, A., Jiang, Y., Nixon, R.A., Evidence that the rab5 effector APPL1 mediates APP-betaCTF-induced dysfunction of endosomes in Down syndrome and Alzheimer's disease. Mol. Psychiatry 21 (2015), 707–716.
    • (2015) Mol. Psychiatry , vol.21 , pp. 707-716
    • Kim, S.1    Sato, Y.2    Mohan, P.S.3    Peterhoff, C.4    Pensalfini, A.5    Rigoglioso, A.6    Jiang, Y.7    Nixon, R.A.8
  • 86
    • 34447649563 scopus 로고    scopus 로고
    • Abeta oligomer-mediated long-term potentiation impairment involves protein phosphatase 1-dependent mechanisms
    • Knobloch, M., Farinelli, M., Konietzko, U., Nitsch, R.M., Mansuy, I.M., Abeta oligomer-mediated long-term potentiation impairment involves protein phosphatase 1-dependent mechanisms. J. Neurosci. 27 (2007), 7648–7653.
    • (2007) J. Neurosci. , vol.27 , pp. 7648-7653
    • Knobloch, M.1    Farinelli, M.2    Konietzko, U.3    Nitsch, R.M.4    Mansuy, I.M.5
  • 87
    • 0028817351 scopus 로고
    • Cell-type and amyloid precursor protein-type specific inhibition of A beta release by bafilomycin A1, a selective inhibitor of vacuolar ATPases
    • Knops, J., Suomensaari, S., Lee, M., McConlogue, L., Seubert, P., Sinha, S., Cell-type and amyloid precursor protein-type specific inhibition of A beta release by bafilomycin A1, a selective inhibitor of vacuolar ATPases. J. Biol. Chem. 270 (1995), 2419–2422.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2419-2422
    • Knops, J.1    Suomensaari, S.2    Lee, M.3    McConlogue, L.4    Seubert, P.5    Sinha, S.6
  • 88
    • 0028276801 scopus 로고
    • Evidence that production and release of amyloid beta-protein involves the endocytic pathway
    • Koo, E.H., Squazzo, S.L., Evidence that production and release of amyloid beta-protein involves the endocytic pathway. J. Biol. Chem. 269 (1994), 17386–17389.
    • (1994) J. Biol. Chem. , vol.269 , pp. 17386-17389
    • Koo, E.H.1    Squazzo, S.L.2
  • 89
    • 2942557122 scopus 로고    scopus 로고
    • Gamma-secretase: proteasome of the membrane?
    • Kopan, R., Ilagan, M.X., Gamma-secretase: proteasome of the membrane?. Nat. Rev. Mol. Cell Biol. 5 (2004), 499–504.
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 499-504
    • Kopan, R.1    Ilagan, M.X.2
  • 90
    • 77956311201 scopus 로고    scopus 로고
    • Modulation of gamma-secretase reduces beta-amyloid deposition in a transgenic mouse model of Alzheimer's disease
    • Kounnas, M.Z., Danks, A.M., Cheng, S., Tyree, C., Ackerman, E., Zhang, X., Ahn, K., Nguyen, P., et al. Modulation of gamma-secretase reduces beta-amyloid deposition in a transgenic mouse model of Alzheimer's disease. Neuron 67 (2010), 769–780.
    • (2010) Neuron , vol.67 , pp. 769-780
    • Kounnas, M.Z.1    Danks, A.M.2    Cheng, S.3    Tyree, C.4    Ackerman, E.5    Zhang, X.6    Ahn, K.7    Nguyen, P.8
  • 91
    • 13344282063 scopus 로고    scopus 로고
    • Alzheimer-associated presenilins 1 and 2: neuronal expression in brain and localization to intracellular membranes in mammalian cells
    • Kovacs, D.M., Fausett, H.J., Page, K.J., Kim, T.W., Moir, R.D., Merriam, D.E., Hollister, R.D., Hallmark, O.G., et al. Alzheimer-associated presenilins 1 and 2: neuronal expression in brain and localization to intracellular membranes in mammalian cells. Nat. Med. 2 (1996), 224–229.
    • (1996) Nat. Med. , vol.2 , pp. 224-229
    • Kovacs, D.M.1    Fausett, H.J.2    Page, K.J.3    Kim, T.W.4    Moir, R.D.5    Merriam, D.E.6    Hollister, R.D.7    Hallmark, O.G.8
  • 92
    • 28244456207 scopus 로고    scopus 로고
    • Differential localization and identification of a critical aspartate suggest non-redundant proteolytic functions of the presenilin homologues SPPL2b and SPPL3
    • Krawitz, P., Haffner, C., Fluhrer, R., Steiner, H., Schmid, B., Haass, C., Differential localization and identification of a critical aspartate suggest non-redundant proteolytic functions of the presenilin homologues SPPL2b and SPPL3. J. Biol. Chem. 280 (2005), 39515–39523.
    • (2005) J. Biol. Chem. , vol.280 , pp. 39515-39523
    • Krawitz, P.1    Haffner, C.2    Fluhrer, R.3    Steiner, H.4    Schmid, B.5    Haass, C.6
  • 95
    • 84894254592 scopus 로고    scopus 로고
    • Proteostasis and longevity: when does aging really begin?
    • Labbadia, J., Morimoto, R.I., Proteostasis and longevity: when does aging really begin?. F1000Prime Rep., 6, 2014, 7.
    • (2014) F1000Prime Rep. , vol.6 , pp. 7
    • Labbadia, J.1    Morimoto, R.I.2
  • 96
    • 84930746830 scopus 로고    scopus 로고
    • The biology of proteostasis in aging and disease
    • Labbadia, J., Morimoto, R.I., The biology of proteostasis in aging and disease. Annu. Rev. Biochem. 84 (2015), 435–464.
    • (2015) Annu. Rev. Biochem. , vol.84 , pp. 435-464
    • Labbadia, J.1    Morimoto, R.I.2
  • 97
    • 69149103002 scopus 로고    scopus 로고
    • MHC II and the endocytic pathway: regulation by invariant chain
    • Landsverk, O.J., Bakke, O., Gregers, T.F., MHC II and the endocytic pathway: regulation by invariant chain. Scand. J. Immunol. 70 (2009), 184–193.
    • (2009) Scand. J. Immunol. , vol.70 , pp. 184-193
    • Landsverk, O.J.1    Bakke, O.2    Gregers, T.F.3
  • 98
    • 84861722031 scopus 로고    scopus 로고
    • Membrane orientation and subcellular localization of transmembrane protein 106B (TMEM106B), a major risk factor for frontotemporal lobar degeneration
    • Lang, C.M., Fellerer, K., Schwenk, B.M., Kuhn, P.H., Kremmer, E., Edbauer, D., Capell, A., Haass, C., Membrane orientation and subcellular localization of transmembrane protein 106B (TMEM106B), a major risk factor for frontotemporal lobar degeneration. J. Biol. Chem. 287 (2012), 19355–19365.
    • (2012) J. Biol. Chem. , vol.287 , pp. 19355-19365
    • Lang, C.M.1    Fellerer, K.2    Schwenk, B.M.3    Kuhn, P.H.4    Kremmer, E.5    Edbauer, D.6    Capell, A.7    Haass, C.8
  • 99
    • 84869014029 scopus 로고    scopus 로고
    • The beta-secretase-derived C-terminal fragment of betaAPP, C99, but not Abeta, is a key contributor to early intraneuronal lesions in triple-transgenic mouse hippocampus
    • 16243–11655
    • Lauritzen, I., Pardossi-Piquard, R., Bauer, C., Brigham, E., Abraham, J.D., Ranaldi, S., Fraser, P., St-George-Hyslop, P., et al. The beta-secretase-derived C-terminal fragment of betaAPP, C99, but not Abeta, is a key contributor to early intraneuronal lesions in triple-transgenic mouse hippocampus. J. Neurosci., 32, 2012 16243–11655.
    • (2012) J. Neurosci. , vol.32
    • Lauritzen, I.1    Pardossi-Piquard, R.2    Bauer, C.3    Brigham, E.4    Abraham, J.D.5    Ranaldi, S.6    Fraser, P.7    St-George-Hyslop, P.8
  • 100
    • 77953913051 scopus 로고    scopus 로고
    • Lysosomal proteolysis and autophagy require presenilin 1 and are disrupted by Alzheimer-related PS1 mutations
    • Lee, J.H., Yu, W.H., Kumar, A., Lee, S., Mohan, P.S., Peterhoff, C.M., Wolfe, D.M., Martinez-Vicente, M., et al. Lysosomal proteolysis and autophagy require presenilin 1 and are disrupted by Alzheimer-related PS1 mutations. Cell 141 (2010), 1146–1158.
    • (2010) Cell , vol.141 , pp. 1146-1158
    • Lee, J.H.1    Yu, W.H.2    Kumar, A.3    Lee, S.4    Mohan, P.S.5    Peterhoff, C.M.6    Wolfe, D.M.7    Martinez-Vicente, M.8
  • 101
    • 84940796652 scopus 로고    scopus 로고
    • Presenilin 1 maintains lysosomal Ca(2 + ) homeostasis via TRPML1 by regulating vATPase-mediated lysosome acidification
    • Lee, J.H., McBrayer, M.K., Wolfe, D.M., Haslett, L.J., Kumar, A., Sato, Y., Lie, P.P., Mohan, P., et al. Presenilin 1 maintains lysosomal Ca(2 + ) homeostasis via TRPML1 by regulating vATPase-mediated lysosome acidification. Cell Rep. 12 (2015), 1430–1444.
    • (2015) Cell Rep. , vol.12 , pp. 1430-1444
    • Lee, J.H.1    McBrayer, M.K.2    Wolfe, D.M.3    Haslett, L.J.4    Kumar, A.5    Sato, Y.6    Lie, P.P.7    Mohan, P.8
  • 103
    • 84890859528 scopus 로고    scopus 로고
    • Differential protein–protein interactions of full length human FasL and FasL fragments generated by proteolysis
    • Lettau, M., Voss, M., Ebsen, H., Kabelitz, D., Janssen, O., Differential protein–protein interactions of full length human FasL and FasL fragments generated by proteolysis. Exp. Cell Res. 320 (2014), 290–301.
    • (2014) Exp. Cell Res. , vol.320 , pp. 290-301
    • Lettau, M.1    Voss, M.2    Ebsen, H.3    Kabelitz, D.4    Janssen, O.5
  • 104
    • 0035894534 scopus 로고    scopus 로고
    • APH-2/nicastrin functions in LIN-12/Notch signaling in the Caenorhabditis elegans somatic gonad
    • Levitan, D., Yu, G., St George, H.P., Goutte, C., APH-2/nicastrin functions in LIN-12/Notch signaling in the Caenorhabditis elegans somatic gonad. Dev. Biol. 240 (2001), 654–661.
    • (2001) Dev. Biol. , vol.240 , pp. 654-661
    • Levitan, D.1    Yu, G.2    St George, H.P.3    Goutte, C.4
  • 106
    • 84960158035 scopus 로고    scopus 로고
    • A molecular mechanism to regulate lysosome motility for lysosome positioning and tubulation
    • Li, X., Rydzewski, N., Hider, A., Zhang, X., Yang, J., Wang, W., Gao, Q., Cheng, X., Xu, H., A molecular mechanism to regulate lysosome motility for lysosome positioning and tubulation. Nat. Cell Biol. 18 (2016), 404–417.
    • (2016) Nat. Cell Biol. , vol.18 , pp. 404-417
    • Li, X.1    Rydzewski, N.2    Hider, A.3    Zhang, X.4    Yang, J.5    Wang, W.6    Gao, Q.7    Cheng, X.8    Xu, H.9
  • 107
    • 0742269846 scopus 로고    scopus 로고
    • Function and regulation of the CD95 (APO-1/Fas) ligand in the immune system
    • Li-Weber, M., Krammer, P.H., Function and regulation of the CD95 (APO-1/Fas) ligand in the immune system. Semin. Immunol. 15 (2003), 145–157.
    • (2003) Semin. Immunol. , vol.15 , pp. 145-157
    • Li-Weber, M.1    Krammer, P.H.2
  • 109
    • 78751472228 scopus 로고    scopus 로고
    • Immune modulation by Fas ligand reverse signaling: lymphocyte proliferation is attenuated by the intracellular Fas ligand domain
    • Luckerath, K., Kirkin, V., Melzer, I.M., Thalheimer, F.B., Siele, D., Milani, W., Adler, T., Aguilar-Pimentel, A., et al. Immune modulation by Fas ligand reverse signaling: lymphocyte proliferation is attenuated by the intracellular Fas ligand domain. Blood 117 (2011), 519–529.
    • (2011) Blood , vol.117 , pp. 519-529
    • Luckerath, K.1    Kirkin, V.2    Melzer, I.M.3    Thalheimer, F.B.4    Siele, D.5    Milani, W.6    Adler, T.7    Aguilar-Pimentel, A.8
  • 110
    • 84861867814 scopus 로고    scopus 로고
    • Ubiquitin and membrane protein turnover: from cradle to grave
    • MacGurn, J.A., Hsu, P.C., Emr, S.D., Ubiquitin and membrane protein turnover: from cradle to grave. Annu. Rev. Biochem. 81 (2012), 231–259.
    • (2012) Annu. Rev. Biochem. , vol.81 , pp. 231-259
    • MacGurn, J.A.1    Hsu, P.C.2    Emr, S.D.3
  • 112
    • 38349144907 scopus 로고    scopus 로고
    • Regulated intramembrane proteolysis of Bri2 (Itm2b) by ADAM10 and SPPL2a/SPPL2b
    • Martin, L., Fluhrer, R., Reiss, K., Kremmer, E., Saftig, P., Haass, C., Regulated intramembrane proteolysis of Bri2 (Itm2b) by ADAM10 and SPPL2a/SPPL2b. J. Biol. Chem. 283 (2008), 1644–1652.
    • (2008) J. Biol. Chem. , vol.283 , pp. 1644-1652
    • Martin, L.1    Fluhrer, R.2    Reiss, K.3    Kremmer, E.4    Saftig, P.5    Haass, C.6
  • 113
    • 23844491144 scopus 로고    scopus 로고
    • The familial dementia BRI2 gene binds the Alzheimer gene amyloid-beta precursor protein and inhibits amyloid-beta production
    • Matsuda, S., Giliberto, L., Matsuda, Y., Davies, P., McGowan, E., Pickford, F., Ghiso, J., Frangione, B., D'Adamio, L., The familial dementia BRI2 gene binds the Alzheimer gene amyloid-beta precursor protein and inhibits amyloid-beta production. J. Biol. Chem. 280 (2005), 28912–28916.
    • (2005) J. Biol. Chem. , vol.280 , pp. 28912-28916
    • Matsuda, S.1    Giliberto, L.2    Matsuda, Y.3    Davies, P.4    McGowan, E.5    Pickford, F.6    Ghiso, J.7    Frangione, B.8    D'Adamio, L.9
  • 114
    • 52049089901 scopus 로고    scopus 로고
    • BRI2 inhibits amyloid beta-peptide precursor protein processing by interfering with the docking of secretases to the substrate
    • Matsuda, S., Giliberto, L., Matsuda, Y., McGowan, E.M., D'Adamio, L., BRI2 inhibits amyloid beta-peptide precursor protein processing by interfering with the docking of secretases to the substrate. J. Neurosci. 28 (2008), 8668–8676.
    • (2008) J. Neurosci. , vol.28 , pp. 8668-8676
    • Matsuda, S.1    Giliberto, L.2    Matsuda, Y.3    McGowan, E.M.4    D'Adamio, L.5
  • 115
    • 0035920144 scopus 로고    scopus 로고
    • Invariant chain induces B cell maturation by activating a TAF(II)105-NF-kappaB-dependent transcription program
    • Matza, D., Wolstein, O., Dikstein, R., Shachar, I., Invariant chain induces B cell maturation by activating a TAF(II)105-NF-kappaB-dependent transcription program. J. Biol. Chem. 276 (2001), 27203–27206.
    • (2001) J. Biol. Chem. , vol.276 , pp. 27203-27206
    • Matza, D.1    Wolstein, O.2    Dikstein, R.3    Shachar, I.4
  • 116
    • 0036849769 scopus 로고    scopus 로고
    • Invariant chain-induced B cell differentiation requires intramembrane proteolytic release of the cytosolic domain
    • Matza, D., Kerem, A., Medvedovsky, H., Lantner, F., Shachar, I., Invariant chain-induced B cell differentiation requires intramembrane proteolytic release of the cytosolic domain. Immunity 17 (2002), 549–560.
    • (2002) Immunity , vol.17 , pp. 549-560
    • Matza, D.1    Kerem, A.2    Medvedovsky, H.3    Lantner, F.4    Shachar, I.5
  • 117
  • 118
    • 0038401145 scopus 로고    scopus 로고
    • Invariant chain, a chain of command
    • Matza, D., Kerem, A., Shachar, I., Invariant chain, a chain of command. Trends Immunol. 24 (2003), 264–268.
    • (2003) Trends Immunol. , vol.24 , pp. 264-268
    • Matza, D.1    Kerem, A.2    Shachar, I.3
  • 121
    • 84937191033 scopus 로고    scopus 로고
    • A cell-based assay reveals nuclear translocation of intracellular domains released by SPPL proteases
    • Mentrup, T., Hasler, R., Fluhrer, R., Saftig, P., Schröder, B., A cell-based assay reveals nuclear translocation of intracellular domains released by SPPL proteases. Traffic 16 (2015), 871–892.
    • (2015) Traffic , vol.16 , pp. 871-892
    • Mentrup, T.1    Hasler, R.2    Fluhrer, R.3    Saftig, P.4    Schröder, B.5
  • 122
    • 84855952173 scopus 로고    scopus 로고
    • The gamma-secretase cleavage product of polycystin-1 regulates TCF and CHOP-mediated transcriptional activation through a p300-dependent mechanism
    • Merrick, D., Chapin, H., Baggs, J.E., Yu, Z., Somlo, S., Sun, Z., Hogenesch, J.B., Caplan, M.J., The gamma-secretase cleavage product of polycystin-1 regulates TCF and CHOP-mediated transcriptional activation through a p300-dependent mechanism. Dev. Cell 22 (2012), 197–210.
    • (2012) Dev. Cell , vol.22 , pp. 197-210
    • Merrick, D.1    Chapin, H.2    Baggs, J.E.3    Yu, Z.4    Somlo, S.5    Sun, Z.6    Hogenesch, J.B.7    Caplan, M.J.8
  • 123
    • 0037592332 scopus 로고    scopus 로고
    • Glutamate receptor subunit 3 is modified by site-specific limited proteolysis including cleavage by gamma-secretase
    • Meyer, E.L., Strutz, N., Gahring, L.C., Rogers, S.W., Glutamate receptor subunit 3 is modified by site-specific limited proteolysis including cleavage by gamma-secretase. J. Biol. Chem. 278 (2003), 23786–23796.
    • (2003) J. Biol. Chem. , vol.278 , pp. 23786-23796
    • Meyer, E.L.1    Strutz, N.2    Gahring, L.C.3    Rogers, S.W.4
  • 124
    • 84857020179 scopus 로고    scopus 로고
    • Differential effects between gamma-secretase inhibitors and modulators on cognitive function in amyloid precursor protein-transgenic and nontransgenic mice
    • Mitani, Y., Yarimizu, J., Saita, K., Uchino, H., Akashiba, H., Shitaka, Y., Ni, K., Matsuoka, N., Differential effects between gamma-secretase inhibitors and modulators on cognitive function in amyloid precursor protein-transgenic and nontransgenic mice. J. Neurosci. 32 (2012), 2037–2050.
    • (2012) J. Neurosci. , vol.32 , pp. 2037-2050
    • Mitani, Y.1    Yarimizu, J.2    Saita, K.3    Uchino, H.4    Akashiba, H.5    Shitaka, Y.6    Ni, K.7    Matsuoka, N.8
  • 125
    • 8044250278 scopus 로고    scopus 로고
    • Cloning of a disintegrin metalloproteinase that processes precursor tumour-necrosis factor-alpha
    • Moss, M.L., Jin, S.L., Milla, M.E., Bickett, D.M., Burkhart, W., Carter, H.L., Chen, W.J., Clay, W.C., et al. Cloning of a disintegrin metalloproteinase that processes precursor tumour-necrosis factor-alpha. Nature 385 (1997), 733–736.
    • (1997) Nature , vol.385 , pp. 733-736
    • Moss, M.L.1    Jin, S.L.2    Milla, M.E.3    Bickett, D.M.4    Burkhart, W.5    Carter, H.L.6    Chen, W.J.7    Clay, W.C.8
  • 126
    • 84929938315 scopus 로고    scopus 로고
    • Three dimensions of the amyloid hypothesis: time, space and ‘wingmen'
    • Musiek, E.S., Holtzman, D.M., Three dimensions of the amyloid hypothesis: time, space and ‘wingmen'. Nat. Neurosci. 18 (2015), 800–806.
    • (2015) Nat. Neurosci. , vol.18 , pp. 800-806
    • Musiek, E.S.1    Holtzman, D.M.2
  • 127
    • 82255164138 scopus 로고    scopus 로고
    • Towards a systems understanding of MHC class I and MHC class II antigen presentation
    • Neefjes, J., Jongsma, M.L., Paul, P., Bakke, O., Towards a systems understanding of MHC class I and MHC class II antigen presentation. Nat. Rev. Immunol. 11 (2011), 823–836.
    • (2011) Nat. Rev. Immunol. , vol.11 , pp. 823-836
    • Neefjes, J.1    Jongsma, M.L.2    Paul, P.3    Bakke, O.4
  • 128
    • 84869488059 scopus 로고    scopus 로고
    • Presenilin-null cells have altered two-pore calcium channel expression and lysosomal calcium: implications for lysosomal function
    • Neely Kayala, K.M., Dickinson, G.D., Minassian, A., Walls, K.C., Green, K.N., LaFerla, F.M., Presenilin-null cells have altered two-pore calcium channel expression and lysosomal calcium: implications for lysosomal function. Brain Res. 1489 (2012), 8–16.
    • (2012) Brain Res. , vol.1489 , pp. 8-16
    • Neely Kayala, K.M.1    Dickinson, G.D.2    Minassian, A.3    Walls, K.C.4    Green, K.N.5    LaFerla, F.M.6
  • 129
    • 79951985639 scopus 로고    scopus 로고
    • Presenilin is necessary for efficient proteolysis through the autophagy-lysosome system in a gamma-secretase-independent manner
    • Neely, K.M., Green, K.N., LaFerla, F.M., Presenilin is necessary for efficient proteolysis through the autophagy-lysosome system in a gamma-secretase-independent manner. J. Neurosci. 31 (2011), 2781–2791.
    • (2011) J. Neurosci. , vol.31 , pp. 2781-2791
    • Neely, K.M.1    Green, K.N.2    LaFerla, F.M.3
  • 133
    • 27144519492 scopus 로고
    • Electron microscopy of lysosomerich fractions from rat liver
    • Novikoff, A.B., Beaufay, H., de Duve, C., Electron microscopy of lysosomerich fractions from rat liver. J. Biophys. Biochem. Cytol. 2 (1956), 179–184.
    • (1956) J. Biophys. Biochem. Cytol. , vol.2 , pp. 179-184
    • Novikoff, A.B.1    Beaufay, H.2    de Duve, C.3
  • 134
    • 0344845132 scopus 로고    scopus 로고
    • Amyloid deposition precedes tangle formation in a triple transgenic model of Alzheimer's disease
    • Oddo, S., Caccamo, A., Kitazawa, M., Tseng, B.P., LaFerla, F.M., Amyloid deposition precedes tangle formation in a triple transgenic model of Alzheimer's disease. Neurobiol. Aging 24 (2003), 1063–1070.
    • (2003) Neurobiol. Aging , vol.24 , pp. 1063-1070
    • Oddo, S.1    Caccamo, A.2    Kitazawa, M.3    Tseng, B.P.4    LaFerla, F.M.5
  • 135
    • 79851473226 scopus 로고    scopus 로고
    • Gamma-secretase modulators as potential disease modifying anti-Alzheimer's drugs
    • Oehlrich, D., Berthelot, D.J., Gijsen, H.J., Gamma-secretase modulators as potential disease modifying anti-Alzheimer's drugs. J. Med. Chem. 54 (2011), 669–698.
    • (2011) J. Med. Chem. , vol.54 , pp. 669-698
    • Oehlrich, D.1    Berthelot, D.J.2    Gijsen, H.J.3
  • 137
    • 38149013121 scopus 로고    scopus 로고
    • Generation of Abeta38 and Abeta42 is independently and differentially affected by familial Alzheimer disease-associated presenilin mutations and gamma-secretase modulation
    • Page, R.M., Baumann, K., Tomioka, M., Perez-Revuelta, B.I., Fukumori, A., Jacobsen, H., Flohr, A., Luebbers, T., Ozmen, L., Steiner, H., Haass, C., Generation of Abeta38 and Abeta42 is independently and differentially affected by familial Alzheimer disease-associated presenilin mutations and gamma-secretase modulation. J. Biol. Chem. 283 (2008), 677–683.
    • (2008) J. Biol. Chem. , vol.283 , pp. 677-683
    • Page, R.M.1    Baumann, K.2    Tomioka, M.3    Perez-Revuelta, B.I.4    Fukumori, A.5    Jacobsen, H.6    Flohr, A.7    Luebbers, T.8    Ozmen, L.9    Steiner, H.10    Haass, C.11
  • 138
    • 84921324921 scopus 로고    scopus 로고
    • Lysosomal storage diseases: from pathophysiology to therapy
    • Parenti, G., Andria, G., Ballabio, A., Lysosomal storage diseases: from pathophysiology to therapy. Annu. Rev. Med. 66 (2015), 471–486.
    • (2015) Annu. Rev. Med. , vol.66 , pp. 471-486
    • Parenti, G.1    Andria, G.2    Ballabio, A.3
  • 139
    • 84883451249 scopus 로고    scopus 로고
    • Selective autophagy: talking with the UPS
    • Park, C., Cuervo, A.M., Selective autophagy: talking with the UPS. Cell Biochem. Biophys. 67 (2013), 3–13.
    • (2013) Cell Biochem. Biophys. , vol.67 , pp. 3-13
    • Park, C.1    Cuervo, A.M.2
  • 140
    • 0037698096 scopus 로고    scopus 로고
    • Presenilin-1, nicastrin, amyloid precursor protein, and gamma-secretase activity are co-localized in the lysosomal membrane
    • Pasternak, S.H., Bagshaw, R.D., Guiral, M., Zhang, S., Ackerley, C.A., Pak, B.J., Callahan, J.W., Mahuran, D.J., Presenilin-1, nicastrin, amyloid precursor protein, and gamma-secretase activity are co-localized in the lysosomal membrane. J. Biol. Chem. 278 (2003), 26687–26694.
    • (2003) J. Biol. Chem. , vol.278 , pp. 26687-26694
    • Pasternak, S.H.1    Bagshaw, R.D.2    Guiral, M.3    Zhang, S.4    Ackerley, C.A.5    Pak, B.J.6    Callahan, J.W.7    Mahuran, D.J.8
  • 141
    • 1842532328 scopus 로고    scopus 로고
    • The role of the endosomal/lysosomal system in amyloid-beta production and the pathophysiology of Alzheimer's disease: reexamining the spatial paradox from a lysosomal perspective
    • Pasternak, S.H., Callahan, J.W., Mahuran, D.J., The role of the endosomal/lysosomal system in amyloid-beta production and the pathophysiology of Alzheimer's disease: reexamining the spatial paradox from a lysosomal perspective. J. Alzheimers Dis. 6 (2004), 53–65.
    • (2004) J. Alzheimers Dis. , vol.6 , pp. 53-65
    • Pasternak, S.H.1    Callahan, J.W.2    Mahuran, D.J.3
  • 143
    • 84884559939 scopus 로고    scopus 로고
    • Novel gamma-secretase modulators for the treatment of Alzheimer's disease: a review focusing on patents from 2010 to 2012
    • Pettersson, M., Stepan, A.F., Kauffman, G.W., Johnson, D.S., Novel gamma-secretase modulators for the treatment of Alzheimer's disease: a review focusing on patents from 2010 to 2012. Expert. Opin. Ther. Patents 23 (2013), 1349–1366.
    • (2013) Expert. Opin. Ther. Patents , vol.23 , pp. 1349-1366
    • Pettersson, M.1    Stepan, A.F.2    Kauffman, G.W.3    Johnson, D.S.4
  • 144
    • 37749018903 scopus 로고    scopus 로고
    • Biogenesis and function of multivesicular bodies
    • Piper, R.C., Katzmann, D.J., Biogenesis and function of multivesicular bodies. Annu. Rev. Cell Dev. Biol. 23 (2007), 519–547.
    • (2007) Annu. Rev. Cell Dev. Biol. , vol.23 , pp. 519-547
    • Piper, R.C.1    Katzmann, D.J.2
  • 145
    • 84862889144 scopus 로고    scopus 로고
    • Physiological functions of the amyloid precursor protein secretases ADAM10, BACE1, and presenilin
    • Prox, J., Rittger, A., Saftig, P., Physiological functions of the amyloid precursor protein secretases ADAM10, BACE1, and presenilin. Exp. Brain Res. 217 (2012), 331–341.
    • (2012) Exp. Brain Res. , vol.217 , pp. 331-341
    • Prox, J.1    Rittger, A.2    Saftig, P.3
  • 146
    • 84860919373 scopus 로고    scopus 로고
    • Membrane trafficking pathways in Alzheimer's disease
    • Rajendran, L., Annaert, W., Membrane trafficking pathways in Alzheimer's disease. Traffic 13 (2012), 759–770.
    • (2012) Traffic , vol.13 , pp. 759-770
    • Rajendran, L.1    Annaert, W.2
  • 148
    • 77957096840 scopus 로고    scopus 로고
    • Amyloid beta 42 peptide (Abeta42)-lowering compounds directly bind to Abeta and interfere with amyloid precursor protein (APP) transmembrane dimerization
    • Richter, L., Munter, L.M., Ness, J., Hildebrand, P.W., Dasari, M., Unterreitmeier, S., Bulic, B., Beyermann, M., et al. Amyloid beta 42 peptide (Abeta42)-lowering compounds directly bind to Abeta and interfere with amyloid precursor protein (APP) transmembrane dimerization. Proc. Natl. Acad. Sci. U. S. A. 107 (2010), 14597–14602.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 14597-14602
    • Richter, L.1    Munter, L.M.2    Ness, J.3    Hildebrand, P.W.4    Dasari, M.5    Unterreitmeier, S.6    Bulic, B.7    Beyermann, M.8
  • 149
    • 84871151505 scopus 로고    scopus 로고
    • Modulation of gamma-secretase by EVP-0015962 reduces amyloid deposition and behavioral deficits in Tg2576 mice
    • Rogers, K., Felsenstein, K.M., Hrdlicka, L., Tu, Z., Albayya, F., Lee, W., Hopp, S., Miller, M.J., et al. Modulation of gamma-secretase by EVP-0015962 reduces amyloid deposition and behavioral deficits in Tg2576 mice. Mol. Neurodegener., 7, 2012, 61.
    • (2012) Mol. Neurodegener. , vol.7 , pp. 61
    • Rogers, K.1    Felsenstein, K.M.2    Hrdlicka, L.3    Tu, Z.4    Albayya, F.5    Lee, W.6    Hopp, S.7    Miller, M.J.8
  • 150
    • 69249227502 scopus 로고    scopus 로고
    • Lysosome biogenesis and lysosomal membrane proteins: trafficking meets function
    • Saftig, P., Klumperman, J., Lysosome biogenesis and lysosomal membrane proteins: trafficking meets function. Nat. Rev. Mol. Cell Biol. 10 (2009), 623–635.
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 623-635
    • Saftig, P.1    Klumperman, J.2
  • 151
    • 44949083106 scopus 로고    scopus 로고
    • Lysosomes
    • Springer Landes Bioscience
    • Lysosomes. Saftig, P., (eds.), 2005, Springer Landes Bioscience.
    • (2005)
    • Saftig, P.1
  • 152
    • 0019590652 scopus 로고
    • Characterization of a membrane-associated receptor from bovine liver that binds phosphomannosyl residues of bovine testicular beta-galactosidase
    • Sahagian, G.G., Distler, J., Jourdian, G.W., Characterization of a membrane-associated receptor from bovine liver that binds phosphomannosyl residues of bovine testicular beta-galactosidase. Proc. Natl. Acad. Sci. U. S. A. 78 (1981), 4289–4293.
    • (1981) Proc. Natl. Acad. Sci. U. S. A. , vol.78 , pp. 4289-4293
    • Sahagian, G.G.1    Distler, J.2    Jourdian, G.W.3
  • 153
    • 33745512851 scopus 로고    scopus 로고
    • Increased App expression in a mouse model of Down's syndrome disrupts NGF transport and causes cholinergic neuron degeneration
    • Salehi, A., Delcroix, J.D., Belichenko, P.V., Zhan, K., Wu, C., Valletta, J.S., Takimoto-Kimura, R., Kleschevnikov, A.M., et al. Increased App expression in a mouse model of Down's syndrome disrupts NGF transport and causes cholinergic neuron degeneration. Neuron 51 (2006), 29–42.
    • (2006) Neuron , vol.51 , pp. 29-42
    • Salehi, A.1    Delcroix, J.D.2    Belichenko, P.V.3    Zhan, K.4    Wu, C.5    Valletta, J.S.6    Takimoto-Kimura, R.7    Kleschevnikov, A.M.8
  • 154
    • 0017752809 scopus 로고
    • Recognition and receptor-mediated uptake of a lysosomal enzyme, alpha-l-iduronidase, by cultured human fibroblasts
    • Sando, G.N., Neufeld, E.F., Recognition and receptor-mediated uptake of a lysosomal enzyme, alpha-l-iduronidase, by cultured human fibroblasts. Cell 12 (1977), 619–627.
    • (1977) Cell , vol.12 , pp. 619-627
    • Sando, G.N.1    Neufeld, E.F.2
  • 155
    • 63649164073 scopus 로고    scopus 로고
    • Trafficking, a key player in regulated intramembrane proteolysis
    • Sannerud, R., Annaert, W., Trafficking, a key player in regulated intramembrane proteolysis. Semin. Cell Dev. Biol. 20 (2009), 183–190.
    • (2009) Semin. Cell Dev. Biol. , vol.20 , pp. 183-190
    • Sannerud, R.1    Annaert, W.2
  • 164
    • 0029972129 scopus 로고    scopus 로고
    • Effect of alkalizing agents on the processing of the beta-amyloid precursor protein
    • Schrader-Fischer, G., Paganetti, P.A., Effect of alkalizing agents on the processing of the beta-amyloid precursor protein. Brain Res. 716 (1996), 91–100.
    • (1996) Brain Res. , vol.716 , pp. 91-100
    • Schrader-Fischer, G.1    Paganetti, P.A.2
  • 166
    • 84878998458 scopus 로고    scopus 로고
    • Lysosomal membrane proteins and their central role in physiology
    • Schwake, M., Schröder, B., Saftig, P., Lysosomal membrane proteins and their central role in physiology. Traffic 14 (2013), 739–748.
    • (2013) Traffic , vol.14 , pp. 739-748
    • Schwake, M.1    Schröder, B.2    Saftig, P.3
  • 169
    • 43249087541 scopus 로고    scopus 로고
    • Inhibition of gamma-secretase causes increased secretion of amyloid precursor protein C-terminal fragments in association with exosomes
    • Sharples, R.A., Vella, L.J., Nisbet, R.M., Naylor, R., Perez, K., Barnham, K.J., Masters, C.L., Hill, A.F., Inhibition of gamma-secretase causes increased secretion of amyloid precursor protein C-terminal fragments in association with exosomes. FASEB J. 22 (2008), 1469–1478.
    • (2008) FASEB J. , vol.22 , pp. 1469-1478
    • Sharples, R.A.1    Vella, L.J.2    Nisbet, R.M.3    Naylor, R.4    Perez, K.5    Barnham, K.J.6    Masters, C.L.7    Hill, A.F.8
  • 170
    • 33846282302 scopus 로고    scopus 로고
    • The presenilin hypothesis of Alzheimer's disease: evidence for a loss-of-function pathogenic mechanism
    • Shen, J., Kelleher, R.J.3, The presenilin hypothesis of Alzheimer's disease: evidence for a loss-of-function pathogenic mechanism. Proc. Natl. Acad. Sci. U. S. A. 104 (2007), 403–409.
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 403-409
    • Shen, J.1    Kelleher, R.J.2
  • 171
    • 0029004341 scopus 로고
    • Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease
    • Sherrington, R., Rogaev, E.I., Liang, Y., Rogaeva, E.A., Levesque, G., Ikeda, M., Chi, H., Lin, C., et al. Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease. Nature 375 (1995), 754–760.
    • (1995) Nature , vol.375 , pp. 754-760
    • Sherrington, R.1    Rogaev, E.I.2    Liang, Y.3    Rogaeva, E.A.4    Levesque, G.5    Ikeda, M.6    Chi, H.7    Lin, C.8
  • 172
    • 33749508911 scopus 로고    scopus 로고
    • CD44 is the signaling component of the macrophage migration inhibitory factor-CD74 receptor complex
    • Shi, X., Leng, L., Wang, T., Wang, W., Du, X., Li, J., McDonald, C., Chen, Z., et al. CD44 is the signaling component of the macrophage migration inhibitory factor-CD74 receptor complex. Immunity 25 (2006), 595–606.
    • (2006) Immunity , vol.25 , pp. 595-606
    • Shi, X.1    Leng, L.2    Wang, T.3    Wang, W.4    Du, X.5    Li, J.6    McDonald, C.7    Chen, Z.8
  • 173
    • 0027250352 scopus 로고
    • Processing of the beta-amyloid precursor. Multiple proteases generate and degrade potentially amyloidogenic fragments
    • Siman, R., Mistretta, S., Durkin, J.T., Savage, M.J., Loh, T., Trusko, S., Scott, R.W., Processing of the beta-amyloid precursor. Multiple proteases generate and degrade potentially amyloidogenic fragments. J. Biol. Chem. 268 (1993), 16602–16609.
    • (1993) J. Biol. Chem. , vol.268 , pp. 16602-16609
    • Siman, R.1    Mistretta, S.2    Durkin, J.T.3    Savage, M.J.4    Loh, T.5    Trusko, S.6    Scott, R.W.7
  • 174
    • 0029935765 scopus 로고    scopus 로고
    • Amyloidogenic processing of the human amyloid precursor protein in primary cultures of rat hippocampal neurons
    • Simons, M., De Strooper, B., Multhaup, G., Tienari, P.J., Dotti, C.G., Beyreuther, K., Amyloidogenic processing of the human amyloid precursor protein in primary cultures of rat hippocampal neurons. J. Neurosci. 16 (1996), 899–908.
    • (1996) J. Neurosci. , vol.16 , pp. 899-908
    • Simons, M.1    De Strooper, B.2    Multhaup, G.3    Tienari, P.J.4    Dotti, C.G.5    Beyreuther, K.6
  • 175
    • 84905373368 scopus 로고    scopus 로고
    • Lysosome size, motility and stress response regulated by fronto-temporal dementia modifier TMEM106B
    • Stagi, M., Klein, Z.A., Gould, T.J., Bewersdorf, J., Strittmatter, S.M., Lysosome size, motility and stress response regulated by fronto-temporal dementia modifier TMEM106B. Mol. Cell Neurosci. 61 (2014), 226–240.
    • (2014) Mol. Cell Neurosci. , vol.61 , pp. 226-240
    • Stagi, M.1    Klein, Z.A.2    Gould, T.J.3    Bewersdorf, J.4    Strittmatter, S.M.5
  • 176
    • 84864340485 scopus 로고    scopus 로고
    • Proteolytic cleavage of the disease-related lysosomal membrane glycoprotein CLN7
    • Steenhuis, P., Froemming, J., Reinheckel, T., Storch, S., Proteolytic cleavage of the disease-related lysosomal membrane glycoprotein CLN7. Biochim. Biophys. Acta 1822 (2012), 1617–1628.
    • (2012) Biochim. Biophys. Acta , vol.1822 , pp. 1617-1628
    • Steenhuis, P.1    Froemming, J.2    Reinheckel, T.3    Storch, S.4
  • 177
    • 0033778262 scopus 로고    scopus 로고
    • Glycine 384 is required for presenilin-1 function and is conserved in bacterial polytopic aspartyl proteases
    • Steiner, H., Kostka, M., Romig, H., Basset, G., Pesold, B., Hardy, J., Capell, A., Meyn, L., et al. Glycine 384 is required for presenilin-1 function and is conserved in bacterial polytopic aspartyl proteases. Nat. Cell Biol. 2 (2000), 848–851.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 848-851
    • Steiner, H.1    Kostka, M.2    Romig, H.3    Basset, G.4    Pesold, B.5    Hardy, J.6    Capell, A.7    Meyn, L.8
  • 178
    • 57649174625 scopus 로고    scopus 로고
    • Intramembrane proteolysis by gamma-secretase
    • Steiner, H., Fluhrer, R., Haass, C., Intramembrane proteolysis by gamma-secretase. J. Biol. Chem. 283 (2008), 29627–29631.
    • (2008) J. Biol. Chem. , vol.283 , pp. 29627-29631
    • Steiner, H.1    Fluhrer, R.2    Haass, C.3
  • 179
    • 42949162823 scopus 로고    scopus 로고
    • A new class of reverse signaling costimulators belongs to the TNF family
    • Sun, M., Fink, P.J., A new class of reverse signaling costimulators belongs to the TNF family. J. Immunol. 179 (2007), 4307–4312.
    • (2007) J. Immunol. , vol.179 , pp. 4307-4312
    • Sun, M.1    Fink, P.J.2
  • 180
    • 84920881831 scopus 로고    scopus 로고
    • The Amyloid Precursor Protein is rapidly transported from the Golgi apparatus to the lysosome and where it is processed into beta-amyloid
    • Tam, J.H., Seah, C., Pasternak, S.H., The Amyloid Precursor Protein is rapidly transported from the Golgi apparatus to the lysosome and where it is processed into beta-amyloid. Mol. Brain, 7, 2014, 54.
    • (2014) Mol. Brain , vol.7 , pp. 54
    • Tam, J.H.1    Seah, C.2    Pasternak, S.H.3
  • 181
    • 84937216724 scopus 로고    scopus 로고
    • Arf6 controls beta-amyloid production by regulating macropinocytosis of the Amyloid Precursor Protein to lysosomes
    • Tang, W., Tam, J.H., Seah, C., Chiu, J., Tyrer, A., Cregan, S.P., Meakin, S.O., Pasternak, S.H., Arf6 controls beta-amyloid production by regulating macropinocytosis of the Amyloid Precursor Protein to lysosomes. Mol. Brain, 8, 2015, 41.
    • (2015) Mol. Brain , vol.8 , pp. 41
    • Tang, W.1    Tam, J.H.2    Seah, C.3    Chiu, J.4    Tyrer, A.5    Cregan, S.P.6    Meakin, S.O.7    Pasternak, S.H.8
  • 182
    • 77955895130 scopus 로고    scopus 로고
    • B-cell targeted therapies in human autoimmune diseases: an updated perspective
    • Townsend, M.J., Monroe, J.G., Chan, A.C., B-cell targeted therapies in human autoimmune diseases: an updated perspective. Immunol. Rev. 237 (2010), 264–283.
    • (2010) Immunol. Rev. , vol.237 , pp. 264-283
    • Townsend, M.J.1    Monroe, J.G.2    Chan, A.C.3
  • 183
    • 84921601654 scopus 로고    scopus 로고
    • The amazing ubiquitin-proteasome system: structural components and implication in aging
    • Tsakiri, E.N., Trougakos, I.P., The amazing ubiquitin-proteasome system: structural components and implication in aging. Int. Rev. Cell Mol. Biol. 314 (2015), 171–237.
    • (2015) Int. Rev. Cell Mol. Biol. , vol.314 , pp. 171-237
    • Tsakiri, E.N.1    Trougakos, I.P.2
  • 186
    • 0033600228 scopus 로고    scopus 로고
    • A stop-codon mutation in the BRI gene associated with familial British dementia
    • Vidal, R., Frangione, B., Rostagno, A., Mead, S., Revesz, T., Plant, G., Ghiso, J., A stop-codon mutation in the BRI gene associated with familial British dementia. Nature 399 (1999), 776–781.
    • (1999) Nature , vol.399 , pp. 776-781
    • Vidal, R.1    Frangione, B.2    Rostagno, A.3    Mead, S.4    Revesz, T.5    Plant, G.6    Ghiso, J.7
  • 188
    • 84922606978 scopus 로고    scopus 로고
    • The role of protein clearance mechanisms in organismal ageing and age-related diseases
    • Vilchez, D., Saez, I., Dillin, A., The role of protein clearance mechanisms in organismal ageing and age-related diseases. Nat. Commun., 5, 2014, 5659.
    • (2014) Nat. Commun. , vol.5 , pp. 5659
    • Vilchez, D.1    Saez, I.2    Dillin, A.3
  • 189
    • 70449510239 scopus 로고    scopus 로고
    • Identification of SH3 domain interaction partners of human FasL (CD178) by phage display screening
    • Voss, M., Lettau, M., Janssen, O., Identification of SH3 domain interaction partners of human FasL (CD178) by phage display screening. BMC. Immunol., 10, 2009, 53.
    • (2009) BMC. Immunol. , vol.10 , pp. 53
    • Voss, M.1    Lettau, M.2    Janssen, O.3
  • 190
    • 84885092137 scopus 로고    scopus 로고
    • Mechanism, specificity, and physiology of signal peptide peptidase (SPP) and SPP-like proteases
    • Voss, M., Schröder, B., Fluhrer, R., Mechanism, specificity, and physiology of signal peptide peptidase (SPP) and SPP-like proteases. Biochim. Biophys. Acta 1828 (2013), 2828–2839.
    • (2013) Biochim. Biophys. Acta , vol.1828 , pp. 2828-2839
    • Voss, M.1    Schröder, B.2    Fluhrer, R.3
  • 192
    • 84959229698 scopus 로고    scopus 로고
    • The cybernetics of TNF: Old views and newer ones
    • Wallach, D., The cybernetics of TNF: Old views and newer ones. Semin. Cell Dev. Biol. 50 (2015), 105–114.
    • (2015) Semin. Cell Dev. Biol. , vol.50 , pp. 105-114
    • Wallach, D.1
  • 194
  • 195
    • 0037150672 scopus 로고    scopus 로고
    • Identification of signal peptide peptidase, a presenilin-type aspartic protease
    • Weihofen, A., Binns, K., Lemberg, M.K., Ashman, K., Martoglio, B., Identification of signal peptide peptidase, a presenilin-type aspartic protease. Science 296 (2002), 2215–2218.
    • (2002) Science , vol.296 , pp. 2215-2218
    • Weihofen, A.1    Binns, K.2    Lemberg, M.K.3    Ashman, K.4    Martoglio, B.5
  • 196
    • 0036019155 scopus 로고    scopus 로고
    • Intraneuronal APP/A beta trafficking and plaque formation in beta-amyloid precursor protein and presenilin-1 transgenic mice
    • Wirths, O., Multhaup, G., Czech, C., Feldmann, N., Blanchard, V., Tremp, G., Beyreuther, K., Pradier, L., Bayer, T.A., Intraneuronal APP/A beta trafficking and plaque formation in beta-amyloid precursor protein and presenilin-1 transgenic mice. Brain Pathol. 12 (2002), 275–286.
    • (2002) Brain Pathol. , vol.12 , pp. 275-286
    • Wirths, O.1    Multhaup, G.2    Czech, C.3    Feldmann, N.4    Blanchard, V.5    Tremp, G.6    Beyreuther, K.7    Pradier, L.8    Bayer, T.A.9
  • 197
    • 0033535553 scopus 로고    scopus 로고
    • Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and gamma-secretase activity
    • Wolfe, M.S., Xia, W., Ostaszewski, B.L., Diehl, T.S., Kimberly, W.T., Selkoe, D.J., Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and gamma-secretase activity. Nature 398 (1999), 513–517.
    • (1999) Nature , vol.398 , pp. 513-517
    • Wolfe, M.S.1    Xia, W.2    Ostaszewski, B.L.3    Diehl, T.S.4    Kimberly, W.T.5    Selkoe, D.J.6
  • 198
    • 11144355129 scopus 로고    scopus 로고
    • Chronic treatment with the gamma-secretase inhibitor LY-411,575 inhibits beta-amyloid peptide production and alters lymphopoiesis and intestinal cell differentiation
    • Wong, G.T., Manfra, D., Poulet, F.M., Zhang, Q., Josien, H., Bara, T., Engstrom, L., Pinzon-Ortiz, M., et al. Chronic treatment with the gamma-secretase inhibitor LY-411,575 inhibits beta-amyloid peptide production and alters lymphopoiesis and intestinal cell differentiation. J. Biol. Chem. 279 (2004), 12876–12882.
    • (2004) J. Biol. Chem. , vol.279 , pp. 12876-12882
    • Wong, G.T.1    Manfra, D.2    Poulet, F.M.3    Zhang, Q.4    Josien, H.5    Bara, T.6    Engstrom, L.7    Pinzon-Ortiz, M.8
  • 199
    • 39049179933 scopus 로고    scopus 로고
    • Dual regulation of soluble tumor necrosis factor-alpha induced activation of human monocytic cells via modulating transmembrane TNF-alpha-mediated ‘reverse signaling'
    • Xin, L., Wang, J., Zhang, H., Shi, W., Yu, M., Li, Q., Jiang, X., Gong, F., Gardner, K., Li, Q.Q., Li, Z., Dual regulation of soluble tumor necrosis factor-alpha induced activation of human monocytic cells via modulating transmembrane TNF-alpha-mediated ‘reverse signaling'. Int. J. Mol. Med. 18 (2006), 885–892.
    • (2006) Int. J. Mol. Med. , vol.18 , pp. 885-892
    • Xin, L.1    Wang, J.2    Zhang, H.3    Shi, W.4    Yu, M.5    Li, Q.6    Jiang, X.7    Gong, F.8    Gardner, K.9    Li, Q.Q.10    Li, Z.11
  • 200
    • 0034618715 scopus 로고    scopus 로고
    • Nicastrin modulates presenilin-mediated notch/glp-1 signal transduction and betaAPP processing
    • Yu, G., Nishimura, M., Arawaka, S., Levitan, D., Zhang, L., Tandon, A., Song, Y.Q., Rogaeva, E., et al. Nicastrin modulates presenilin-mediated notch/glp-1 signal transduction and betaAPP processing. Nature 407 (2000), 48–54.
    • (2000) Nature , vol.407 , pp. 48-54
    • Yu, G.1    Nishimura, M.2    Arawaka, S.3    Levitan, D.4    Zhang, L.5    Tandon, A.6    Song, Y.Q.7    Rogaeva, E.8
  • 201
    • 4344689871 scopus 로고    scopus 로고
    • Autophagic vacuoles are enriched in amyloid precursor protein-secretase activities: implications for beta-amyloid peptide over-production and localization in Alzheimer's disease
    • Yu, W.H., Kumar, A., Peterhoff, C., Shapiro, K.L., Uchiyama, Y., Lamb, B.T., Cuervo, A.M., Nixon, R.A., Autophagic vacuoles are enriched in amyloid precursor protein-secretase activities: implications for beta-amyloid peptide over-production and localization in Alzheimer's disease. Int. J. Biochem. Cell Biol. 36 (2004), 2531–2540.
    • (2004) Int. J. Biochem. Cell Biol. , vol.36 , pp. 2531-2540
    • Yu, W.H.1    Kumar, A.2    Peterhoff, C.3    Shapiro, K.L.4    Uchiyama, Y.5    Lamb, B.T.6    Cuervo, A.M.7    Nixon, R.A.8
  • 203
    • 58349103882 scopus 로고    scopus 로고
    • Influence of reverse signaling via membrane TNF-alpha on cytotoxicity of NK92 cells
    • Yu, M., Shi, W., Zhang, J., Niu, L., Chen, Q., Yan, D., Liu, T., Jing, W., et al. Influence of reverse signaling via membrane TNF-alpha on cytotoxicity of NK92 cells. Eur. J. Cell Biol. 88 (2009), 181–191.
    • (2009) Eur. J. Cell Biol. , vol.88 , pp. 181-191
    • Yu, M.1    Shi, W.2    Zhang, J.3    Niu, L.4    Chen, Q.5    Yan, D.6    Liu, T.7    Jing, W.8
  • 204
    • 84946781429 scopus 로고    scopus 로고
    • Delta-secretase cleaves amyloid precursor protein and regulates the pathogenesis in Alzheimer's disease
    • Zhang, Z., Song, M., Liu, X., Su, K.S., Duong, D.M., Seyfried, N.T., Cao, X., Cheng, L., et al. Delta-secretase cleaves amyloid precursor protein and regulates the pathogenesis in Alzheimer's disease. Nat. Commun., 6, 2015, 8762.
    • (2015) Nat. Commun. , vol.6 , pp. 8762
    • Zhang, Z.1    Song, M.2    Liu, X.3    Su, K.S.4    Duong, D.M.5    Seyfried, N.T.6    Cao, X.7    Cheng, L.8
  • 205
    • 84903464290 scopus 로고    scopus 로고
    • An iron-regulated and glycosylation-dependent proteasomal degradation pathway for the plasma membrane metal transporter ZIP14
    • Zhao, N., Zhang, A.S., Worthen, C., Knutson, M.D., Enns, C.A., An iron-regulated and glycosylation-dependent proteasomal degradation pathway for the plasma membrane metal transporter ZIP14. Proc. Natl. Acad. Sci. U. S. A. 111 (2014), 9175–9180.
    • (2014) Proc. Natl. Acad. Sci. U. S. A. , vol.111 , pp. 9175-9180
    • Zhao, N.1    Zhang, A.S.2    Worthen, C.3    Knutson, M.D.4    Enns, C.A.5


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