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Volumn 7, Issue 3, 2012, Pages

Expression and characterization of Drosophila Signal Peptide Peptidase-like (sppL), a gene that encodes an intramembrane protease

Author keywords

[No Author keywords available]

Indexed keywords

PROTEINASE; SIGNAL PEPTIDE PEPTIDASE LIKE PROTEIN; UNCLASSIFIED DRUG; ASPARTIC PROTEINASE; COMPLEMENTARY DNA; DROSOPHILA PROTEIN; SIGNAL PEPTIDE PEPTIDASE; SPPL PROTEIN, DROSOPHILA;

EID: 84863340153     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0033827     Document Type: Article
Times cited : (5)

References (50)
  • 1
    • 67649827390 scopus 로고    scopus 로고
    • Intramembrane-cleaving Proteases
    • Wolfe MS, (2009) Intramembrane-cleaving Proteases. J Biol Chem 284: 13969-13973.
    • (2009) J Biol Chem , vol.284 , pp. 13969-13973
    • Wolfe, M.S.1
  • 2
    • 0033535504 scopus 로고    scopus 로고
    • A presenilin-1-dependent gamma-secretase-like protease mediates release of Notch intracellular domain
    • De Strooper B, Annaert W, Cupers P, Saftig P, Craessaerts K, et al. (1999) A presenilin-1-dependent gamma-secretase-like protease mediates release of Notch intracellular domain. Nature 398: 518-522.
    • (1999) Nature , vol.398 , pp. 518-522
    • de Strooper, B.1    Annaert, W.2    Cupers, P.3    Saftig, P.4    Craessaerts, K.5
  • 3
    • 0033535508 scopus 로고    scopus 로고
    • Presenilin is required for activity and nuclear access of Notch in Drosophila
    • Struhl G, Greenwald I, (1999) Presenilin is required for activity and nuclear access of Notch in Drosophila. Nature 398: 522-525.
    • (1999) Nature , vol.398 , pp. 522-525
    • Struhl, G.1    Greenwald, I.2
  • 4
    • 0033535555 scopus 로고    scopus 로고
    • Neurogenic phenotypes and altered Notch processing in Drosophila Presenilin mutants
    • Ye Y, Lukinova N, Fortini ME, (1999) Neurogenic phenotypes and altered Notch processing in Drosophila Presenilin mutants. Nature 398: 525-529.
    • (1999) Nature , vol.398 , pp. 525-529
    • Ye, Y.1    Lukinova, N.2    Fortini, M.E.3
  • 5
    • 0037102238 scopus 로고    scopus 로고
    • A family of Rhomboid intramembrane proteases activates all Drosophila membrane-tethered EGF ligands
    • Urban S, Lee JR, Freeman M, (2002) A family of Rhomboid intramembrane proteases activates all Drosophila membrane-tethered EGF ligands. EMBO J 21: 4277-4286.
    • (2002) EMBO J , vol.21 , pp. 4277-4286
    • Urban, S.1    Lee, J.R.2    Freeman, M.3
  • 6
    • 61549138703 scopus 로고    scopus 로고
    • Alternative processing of sterol regulatory element binding protein during larval development in Drosophila melanogaster
    • Matthews KA, Kunte AS, Tambe-Ebot E, Rawson RB, (2009) Alternative processing of sterol regulatory element binding protein during larval development in Drosophila melanogaster. Genetics 181: 119-128.
    • (2009) Genetics , vol.181 , pp. 119-128
    • Matthews, K.A.1    Kunte, A.S.2    Tambe-Ebot, E.3    Rawson, R.B.4
  • 7
    • 0034613193 scopus 로고    scopus 로고
    • Release of signal peptide fragments into the cytosol requires cleavage in the transmembrane region by a protease activity that is specifically blocked by a novel cysteine protease inhibitor
    • Weihofen A, Lemberg MK, Ploegh HL, Bogyo M, Martoglio B, (2000) Release of signal peptide fragments into the cytosol requires cleavage in the transmembrane region by a protease activity that is specifically blocked by a novel cysteine protease inhibitor. J Biol Chem 275: 30951-30956.
    • (2000) J Biol Chem , vol.275 , pp. 30951-30956
    • Weihofen, A.1    Lemberg, M.K.2    Ploegh, H.L.3    Bogyo, M.4    Martoglio, B.5
  • 8
    • 0037150672 scopus 로고    scopus 로고
    • Identification of signal peptide peptidase, a presenilin-type aspartic protease
    • Weihofen A, Binns K, Lemberg MK, Ashman K, Martoglio B, (2002) Identification of signal peptide peptidase, a presenilin-type aspartic protease. Science 296: 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
  • 9
    • 0035576260 scopus 로고    scopus 로고
    • Intramembrane proteolysis of signal peptides: an essential step in the generation of HLA-E epitopes
    • Lemberg MK, Bland FA, Weihofen A, Braud VM, Martoglio B, (2001) Intramembrane proteolysis of signal peptides: an essential step in the generation of HLA-E epitopes. J Immunol 167: 6441-6446.
    • (2001) J Immunol , vol.167 , pp. 6441-6446
    • Lemberg, M.K.1    Bland, F.A.2    Weihofen, A.3    Braud, V.M.4    Martoglio, B.5
  • 10
    • 0036683052 scopus 로고    scopus 로고
    • Intramembrane proteolysis promotes trafficking of hepatitis C virus core protein to lipid droplets
    • McLauchlan J, Lemberg MK, Hope G, Martoglio B, (2002) Intramembrane proteolysis promotes trafficking of hepatitis C virus core protein to lipid droplets. EMBO J 21: 3980-3988.
    • (2002) EMBO J , vol.21 , pp. 3980-3988
    • McLauchlan, J.1    Lemberg, M.K.2    Hope, G.3    Martoglio, B.4
  • 11
    • 0030732847 scopus 로고    scopus 로고
    • Signal peptide fragments of preprolactin and HIV-1 p-gp160 interact with calmodulin
    • Martoglio B, Graf R, Dobberstein B, (1997) Signal peptide fragments of preprolactin and HIV-1 p-gp160 interact with calmodulin. EMBO J 16: 6636-6645.
    • (1997) EMBO J , vol.16 , pp. 6636-6645
    • Martoglio, B.1    Graf, R.2    Dobberstein, B.3
  • 12
    • 33745207334 scopus 로고    scopus 로고
    • Signal peptide peptidase is required for dislocation from the endoplasmic reticulum
    • Loureiro J, Lilley BN, Spooner E, Noriega V, Tortorella D, et al. (2006) Signal peptide peptidase is required for dislocation from the endoplasmic reticulum. Nature 441: 894-897.
    • (2006) Nature , vol.441 , pp. 894-897
    • Loureiro, J.1    Lilley, B.N.2    Spooner, E.3    Noriega, V.4    Tortorella, D.5
  • 13
    • 77951938375 scopus 로고    scopus 로고
    • The Drosophila Crumbs signal peptide is unusually long and is a substrate for signal peptide peptidase
    • Kilic A, Klose S, Dobberstein B, Knust E, Kapp K, (2010) The Drosophila Crumbs signal peptide is unusually long and is a substrate for signal peptide peptidase. Eur J Cell Biol 89: 449-461.
    • (2010) Eur J Cell Biol , vol.89 , pp. 449-461
    • Kilic, A.1    Klose, S.2    Dobberstein, B.3    Knust, E.4    Kapp, K.5
  • 14
  • 15
    • 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 MK, Weihofen A, Dev KK, Dengler U, et al. (2004) Consensus analysis of signal peptide peptidase and homologous human aspartic proteases reveals opposite topology of catalytic domains compared with presenilins. J Biol Chem 279: 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
  • 16
    • 33746608185 scopus 로고    scopus 로고
    • A gamma-secretase-like intramembrane cleavage of TNFalpha by the GxGD aspartyl protease SPPL2b
    • Fluhrer R, Grammer G, Israel L, Condron MM, Haffner C, et al. (2006) A gamma-secretase-like intramembrane cleavage of TNFalpha by the GxGD aspartyl protease SPPL2b. Nat Cell Biol 8: 894-896.
    • (2006) Nat Cell Biol , vol.8 , pp. 894-896
    • Fluhrer, R.1    Grammer, G.2    Israel, L.3    Condron, M.M.4    Haffner, C.5
  • 17
    • 34548040200 scopus 로고    scopus 로고
    • The Fas ligand intracellular domain is released by ADAM10 and SPPL2a cleavage in T-cells
    • Kirkin V, Cahuzac N, Guardiola-Serrano F, Huault S, Luckerath K, et al. (2007) The Fas ligand intracellular domain is released by ADAM10 and SPPL2a cleavage in T-cells. Cell Death Differ 14: 1678-1687.
    • (2007) Cell Death Differ , vol.14 , pp. 1678-1687
    • Kirkin, V.1    Cahuzac, N.2    Guardiola-Serrano, F.3    Huault, S.4    Luckerath, K.5
  • 18
    • 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, et al. (2008) Regulated intramembrane proteolysis of Bri2 (Itm2b) by ADAM10 and SPPL2a/SPPL2b. J Biol Chem 283: 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
  • 19
    • 33746618450 scopus 로고    scopus 로고
    • SPPL2a and SPPL2b promote intramembrane proteolysis of TNFalpha in activated dendritic cells to trigger IL-12 production
    • Friedmann E, Hauben E, Maylandt K, Schleeger S, Vreugde S, et al. (2006) SPPL2a and SPPL2b promote intramembrane proteolysis of TNFalpha in activated dendritic cells to trigger IL-12 production. Nat Cell Biol 8: 843-848.
    • (2006) Nat Cell Biol , vol.8 , pp. 843-848
    • Friedmann, E.1    Hauben, E.2    Maylandt, K.3    Schleeger, S.4    Vreugde, S.5
  • 20
    • 6944250394 scopus 로고    scopus 로고
    • The Caenorhabditis elegans IMPAS gene, imp-2, is essential for development and is functionally distinct from related presenilins
    • Grigorenko AP, Moliaka YK, Soto MC, Mello CC, Rogaev EI, (2004) The Caenorhabditis elegans IMPAS gene, imp-2, is essential for development and is functionally distinct from related presenilins. Proc Natl Acad Sci U S A 101: 14955-14960.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 14955-14960
    • Grigorenko, A.P.1    Moliaka, Y.K.2    Soto, M.C.3    Mello, C.C.4    Rogaev, E.I.5
  • 21
    • 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, et al. (2005) Differential localization and identification of a critical aspartate suggest non-redundant proteolytic functions of the presenilin homologues SPPL2b and SPPL3. J Biol Chem 280: 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
  • 22
    • 63549137592 scopus 로고    scopus 로고
    • The signal peptide peptidase is required for pollen function in Arabidopsis
    • Han S, Green L, Schnell DJ, (2009) The signal peptide peptidase is required for pollen function in Arabidopsis. Plant Physiol 149: 1289-1301.
    • (2009) Plant Physiol , vol.149 , pp. 1289-1301
    • Han, S.1    Green, L.2    Schnell, D.J.3
  • 23
    • 20444429794 scopus 로고    scopus 로고
    • Drosophila signal peptide peptidase is an essential protease for larval development
    • Casso DJ, Tanda S, Biehs B, Martoglio B, Kornberg TB, (2005) Drosophila signal peptide peptidase is an essential protease for larval development. Genetics 170: 139-148.
    • (2005) Genetics , vol.170 , pp. 139-148
    • Casso, D.J.1    Tanda, S.2    Biehs, B.3    Martoglio, B.4    Kornberg, T.B.5
  • 24
    • 0021924743 scopus 로고
    • The engrailed locus of Drosophila: structural analysis of an embryonic transcript
    • Poole SJ, Kauvar LM, Drees B, Kornberg T, (1985) The engrailed locus of Drosophila: structural analysis of an embryonic transcript. Cell 40: 37-43.
    • (1985) Cell , vol.40 , pp. 37-43
    • Poole, S.J.1    Kauvar, L.M.2    Drees, B.3    Kornberg, T.4
  • 25
    • 0027160708 scopus 로고
    • Targeted gene expression as a means of altering cell fates and generating dominant phenotypes
    • Brand AH, Perrimon N, (1993) Targeted gene expression as a means of altering cell fates and generating dominant phenotypes. Development 118: 401-415.
    • (1993) Development , vol.118 , pp. 401-415
    • Brand, A.H.1    Perrimon, N.2
  • 26
    • 0033062009 scopus 로고    scopus 로고
    • DCRY is a Drosophila photoreceptor protein implicated in light entrainment of circadian rhythm
    • Ishikawa T, Matsumoto A, Kato T Jr, Togashi S, Ryo H, et al. (1999) DCRY is a Drosophila photoreceptor protein implicated in light entrainment of circadian rhythm. Genes Cells 4: 57-65.
    • (1999) Genes Cells , vol.4 , pp. 57-65
    • Ishikawa, T.1    Matsumoto, A.2    Kato Jr., T.3    Togashi, S.4    Ryo, H.5
  • 27
    • 0031766716 scopus 로고    scopus 로고
    • Boundaries in the Drosophila wing imaginal disc organize vein-specific genetic programs
    • Biehs B, Sturtevant MA, Bier E, (1998) Boundaries in the Drosophila wing imaginal disc organize vein-specific genetic programs. Development 125: 4245-4257.
    • (1998) Development , vol.125 , pp. 4245-4257
    • Biehs, B.1    Sturtevant, M.A.2    Bier, E.3
  • 28
    • 0037274701 scopus 로고    scopus 로고
    • A P-element insertion screen identified mutations in 455 novel essential genes in Drosophila
    • Oh SW, Kingsley T, Shin HH, Zheng Z, Chen HW, et al. (2003) A P-element insertion screen identified mutations in 455 novel essential genes in Drosophila. Genetics 163: 195-201.
    • (2003) Genetics , vol.163 , pp. 195-201
    • Oh, S.W.1    Kingsley, T.2    Shin, H.H.3    Zheng, Z.4    Chen, H.W.5
  • 29
    • 0003455528 scopus 로고
    • Cold Spring Harbor, Cold Spring Harbor Laboratory Press
    • Ashburner M, (1989) Drosophila: A laboratory manual Cold Spring Harbor Cold Spring Harbor Laboratory Press pp. 44-49.
    • (1989) Drosophila: A Laboratory Manual , pp. 44-49
    • Ashburner, M.1
  • 30
    • 10744231523 scopus 로고    scopus 로고
    • A complementary transposon tool kit for Drosophila melanogaster using P and piggyBac
    • Thibault ST, Singer MA, Miyazaki WY, Milash B, Dompe NA, et al. (2004) A complementary transposon tool kit for Drosophila melanogaster using P and piggyBac. Nat Genet 36: 283-287.
    • (2004) Nat Genet , vol.36 , pp. 283-287
    • Thibault, S.T.1    Singer, M.A.2    Miyazaki, W.Y.3    Milash, B.4    Dompe, N.A.5
  • 31
    • 10744233572 scopus 로고    scopus 로고
    • Systematic generation of high-resolution deletion coverage of the Drosophila melanogaster genome
    • Parks AL, Cook KR, Belvin M, Dompe NA, Fawcett R, et al. (2004) Systematic generation of high-resolution deletion coverage of the Drosophila melanogaster genome. Nat Genet 36: 288-292.
    • (2004) Nat Genet , vol.36 , pp. 288-292
    • Parks, A.L.1    Cook, K.R.2    Belvin, M.3    Dompe, N.A.4    Fawcett, R.5
  • 33
    • 0027968068 scopus 로고
    • CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DG, Gibson TJ, (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 22: 4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 34
  • 35
    • 77952540430 scopus 로고    scopus 로고
    • TreeVector: scalable, interactive, phylogenetic trees for the web
    • Pethica R, Barker G, Kovacs T, Gough J, (2010) TreeVector: scalable, interactive, phylogenetic trees for the web. PLoS One 5: e8934.
    • (2010) PLoS One , vol.5
    • Pethica, R.1    Barker, G.2    Kovacs, T.3    Gough, J.4
  • 36
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes
    • Krogh A, Larsson B, von Heijne G, Sonnhammer EL, (2001) Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes. J Mol Biol 305: 567-580.
    • (2001) J Mol Biol , vol.305 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    von Heijne, G.3    Sonnhammer, E.L.4
  • 37
    • 0034786532 scopus 로고    scopus 로고
    • The HMMTOP transmembrane topology prediction server
    • Tusnady GE, Simon I, (2001) The HMMTOP transmembrane topology prediction server. Bioinformatics 17: 849-850.
    • (2001) Bioinformatics , vol.17 , pp. 849-850
    • Tusnady, G.E.1    Simon, I.2
  • 38
    • 78650331647 scopus 로고    scopus 로고
    • Identification of functional elements and regulatory circuits by Drosophila modENCODE
    • Roy S, Ernst J, Kharchenko PV, Kheradpour P, Negre N, et al. (2010) Identification of functional elements and regulatory circuits by Drosophila modENCODE. Science 330: 1787-1797.
    • (2010) Science , vol.330 , pp. 1787-1797
    • Roy, S.1    Ernst, J.2    Kharchenko, P.V.3    Kheradpour, P.4    Negre, N.5
  • 39
    • 19044365796 scopus 로고    scopus 로고
    • The Drosophila gene collection: identification of putative full-length cDNAs for 70% of D. melanogaster genes
    • Stapleton M, Liao G, Brokstein P, Hong L, Carninci P, et al. (2002) The Drosophila gene collection: identification of putative full-length cDNAs for 70% of D. melanogaster genes. Genome Res 12: 1294-1300.
    • (2002) Genome Res , vol.12 , pp. 1294-1300
    • Stapleton, M.1    Liao, G.2    Brokstein, P.3    Hong, L.4    Carninci, P.5
  • 40
    • 77950406092 scopus 로고    scopus 로고
    • Regulation of lifespan, metabolism, and stress responses by the Drosophila SH2B protein, Lnk
    • Slack C, Werz C, Wieser D, Alic N, Foley A, et al. (2010) Regulation of lifespan, metabolism, and stress responses by the Drosophila SH2B protein, Lnk. PLoS Genet 6: e1000881.
    • (2010) PLoS Genet , vol.6
    • Slack, C.1    Werz, C.2    Wieser, D.3    Alic, N.4    Foley, A.5
  • 41
    • 77954937345 scopus 로고    scopus 로고
    • SH2B regulation of growth, metabolism, and longevity in both insects and mammals
    • Song W, Ren D, Li W, Jiang L, Cho KW, et al. (2010) SH2B regulation of growth, metabolism, and longevity in both insects and mammals. Cell Metab 11: 427-437.
    • (2010) Cell Metab , vol.11 , pp. 427-437
    • Song, W.1    Ren, D.2    Li, W.3    Jiang, L.4    Cho, K.W.5
  • 42
    • 70149101855 scopus 로고    scopus 로고
    • The Drosophila SH2B family adaptor Lnk acts in parallel to chico in the insulin signaling pathway
    • Werz C, Kohler K, Hafen E, Stocker H, (2009) The Drosophila SH2B family adaptor Lnk acts in parallel to chico in the insulin signaling pathway. PLoS Genet 5: e1000596.
    • (2009) PLoS Genet , vol.5
    • Werz, C.1    Kohler, K.2    Hafen, E.3    Stocker, H.4
  • 43
    • 69249113100 scopus 로고    scopus 로고
    • Dissecting the genetics of longevity in Drosophila melanogaster
    • Paaby AB, Schmidt PS, (2009) Dissecting the genetics of longevity in Drosophila melanogaster. Fly (Austin) 3: 29-38.
    • (2009) Fly (Austin) , vol.3 , pp. 29-38
    • Paaby, A.B.1    Schmidt, P.S.2
  • 44
    • 0042422245 scopus 로고    scopus 로고
    • Testing an 'aging gene' in long-lived drosophila strains: increased longevity depends on sex and genetic background
    • Spencer CC, Howell CE, Wright AR, Promislow DE, (2003) Testing an 'aging gene' in long-lived drosophila strains: increased longevity depends on sex and genetic background. Aging Cell 2: 123-130.
    • (2003) Aging Cell , vol.2 , pp. 123-130
    • Spencer, C.C.1    Howell, C.E.2    Wright, A.R.3    Promislow, D.E.4
  • 45
    • 34250899722 scopus 로고    scopus 로고
    • Signal integration in the endoplasmic reticulum unfolded protein response
    • Ron D, Walter P, (2007) Signal integration in the endoplasmic reticulum unfolded protein response. Nat Rev Mol Cell Biol 8: 519-529.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 519-529
    • Ron, D.1    Walter, P.2
  • 47
    • 34547094392 scopus 로고    scopus 로고
    • A C-terminal region of signal peptide peptidase defines a functional domain for intramembrane aspartic protease catalysis
    • Narayanan S, Sato T, Wolfe MS, (2007) A C-terminal region of signal peptide peptidase defines a functional domain for intramembrane aspartic protease catalysis. J Biol Chem 282: 20172-20179.
    • (2007) J Biol Chem , vol.282 , pp. 20172-20179
    • Narayanan, S.1    Sato, T.2    Wolfe, M.S.3
  • 48
    • 0033152441 scopus 로고    scopus 로고
    • Presenilins, processing of beta-amyloid precursor protein, and notch signaling
    • Chan YM, Jan YN, (1999) Presenilins, processing of beta-amyloid precursor protein, and notch signaling. Neuron 23: 201-204.
    • (1999) Neuron , vol.23 , pp. 201-204
    • Chan, Y.M.1    Jan, Y.N.2
  • 49
    • 84863349956 scopus 로고    scopus 로고
    • Activation of SREBP by the caspase drice in Drosophila larvae
    • Amarneh B, Matthews KA, Rawson RB, (2009) Activation of SREBP by the caspase drice in Drosophila larvae. J Biol Chem.
    • (2009) J Biol Chem
    • Amarneh, B.1    Matthews, K.A.2    Rawson, R.B.3
  • 50
    • 77955500335 scopus 로고    scopus 로고
    • Matrix metalloproteinases are modifiers of huntingtin proteolysis and toxicity in Huntington's disease
    • Miller JP, Holcomb J, Al-Ramahi I, de Haro M, Gafni J, et al. (2010) Matrix metalloproteinases are modifiers of huntingtin proteolysis and toxicity in Huntington's disease. Neuron 67: 199-212.
    • (2010) Neuron , vol.67 , pp. 199-212
    • Miller, J.P.1    Holcomb, J.2    Al-Ramahi, I.3    de Haro, M.4    Gafni, J.5


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