메뉴 건너뛰기




Volumn 3, Issue 4-5, 2006, Pages 275-283

Assembly, trafficking and function of γ-secretase

Author keywords

Secretase; Alzheimer's disease; Amyloid peptide; Presenilin

Indexed keywords

AMYLOID PRECURSOR PROTEIN; ANTERIOR PHARYNX DEFECTIVE 1 PROTEIN; ASPARTIC PROTEINASE; GAMMA SECRETASE; GREEN FLUORESCENT PROTEIN; MEMBRANE PROTEIN; NICASTRIN; PRESENILIN 1; PRESENILIN 2; PROTEIN APH 1B; PROTEIN PEN 2; PROTEINASE; UNCLASSIFIED DRUG;

EID: 33750151419     PISSN: 16602854     EISSN: 16602862     Source Type: Journal    
DOI: 10.1159/000095267     Document Type: Conference Paper
Times cited : (128)

References (77)
  • 1
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • Hardy J, Selkoe DJ: The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science 2002;297:353-356.
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 2
    • 1442264828 scopus 로고    scopus 로고
    • Take five-BACE and the gamma-secretase quartet conduct Alzheimer's amyloid beta-peptide generation
    • Haass C: Take five-BACE and the gamma-secretase quartet conduct Alzheimer's amyloid beta-peptide generation. EMBO J 2004;23:483-488.
    • (2004) EMBO J , vol.23 , pp. 483-488
    • Haass, C.1
  • 3
    • 24144441879 scopus 로고    scopus 로고
    • Uncovering gamma-secretase
    • Steiner H: Uncovering gamma-secretase. Curr Alzheimer Res 2004;1:175-181.
    • (2004) Curr Alzheimer Res , vol.1 , pp. 175-181
    • Steiner, H.1
  • 5
    • 0029101491 scopus 로고
    • Familial Alzheimer's disease in kindreds with missense mutations in a gene on chromosome 1 related to the Alzheimer's disease type 3 gene
    • Rogaev EI, Sherrington R, Rogaeva EA, Levesque G, Ikeda M, Liang Y, Chi H, Lin C, Holman K, Tsuda T, et al: Familial Alzheimer's disease in kindreds with missense mutations in a gene on chromosome 1 related to the Alzheimer's disease type 3 gene. Nature 1995;376:775-778.
    • (1995) Nature , vol.376 , pp. 775-778
    • Rogaev, E.I.1    Sherrington, R.2    Rogaeva, E.A.3    Levesque, G.4    Ikeda, M.5    Liang, Y.6    Chi, H.7    Lin, C.8    Holman, K.9    Tsuda, T.10
  • 9
    • 23944511109 scopus 로고    scopus 로고
    • Evidence that the COOH terminus of human presenilin 1 is located in extracytoplasmic space
    • Oh YS, Turner RJ: Evidence that the COOH terminus of human presenilin 1 is located in extracytoplasmic space. Am J Physiol Cell Physiol 2005;289:C576-581.
    • (2005) Am J Physiol Cell Physiol , vol.289
    • Oh, Y.S.1    Turner, R.J.2
  • 10
    • 20444481683 scopus 로고    scopus 로고
    • A novel transmembrane topology of presenilin based on reconciling experimental and computational evidence
    • Henricson A, Kall L, Sonnhammer EL: A novel transmembrane topology of presenilin based on reconciling experimental and computational evidence. FEBS J 2005;272:2727-2733.
    • (2005) FEBS J , vol.272 , pp. 2727-2733
    • Henricson, A.1    Kall, L.2    Sonnhammer, E.L.3
  • 12
    • 0029116848 scopus 로고
    • Facilitation of lin12-mediated signalling by sel-12, a Caenorhabditis elegans S182 Alzheimer's disease gene
    • Levitan D, Greenwald I: Facilitation of lin12-mediated signalling by sel-12, a Caenorhabditis elegans S182 Alzheimer's disease gene. Nature 1995;377:351-354.
    • (1995) Nature , vol.377 , pp. 351-354
    • Levitan, D.1    Greenwald, I.2
  • 15
    • 0033535553 scopus 로고    scopus 로고
    • Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and gamma-secretase activity
    • Wolfe MS, Xia W, Ostaszewski BL, Diehl TS, Kimberly WT, Selkoe DJ: Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and gamma-secretase activity. Nature 1999;398:513-517.
    • (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
  • 16
    • 0033551099 scopus 로고    scopus 로고
    • Peptidomimetic probes and molecular modeling suggest that Alzheimer's gamma-secretase is an intramembrane-cleaving aspartyl protease
    • Wolfe MS, Xia W, Moore CL, Leatherwood DD, Ostaszewski B, Rahmati T, Donkor IO, Selkoe DJ: Peptidomimetic probes and molecular modeling suggest that Alzheimer's gamma-secretase is an intramembrane-cleaving aspartyl protease. Biochemistry 1999;38:4720-4727.
    • (1999) Biochemistry , vol.38 , pp. 4720-4727
    • Wolfe, M.S.1    Xia, W.2    Moore, C.L.3    Leatherwood, D.D.4    Ostaszewski, B.5    Rahmati, T.6    Donkor, I.O.7    Selkoe, D.J.8
  • 18
    • 0033550061 scopus 로고    scopus 로고
    • Zebrafish (Danio rerio) presenilin promotes aberrant amyloid beta- peptide production and requires a critical aspartate residue for its function in amyloidogenesis
    • Leimer U, Lun K, Romig H, Walter J, Grunberg J, Brand M, Haass C: Zebrafish (Danio rerio) presenilin promotes aberrant amyloid beta- peptide production and requires a critical aspartate residue for its function in amyloidogenesis. Biochemistry 1999;38:13602-13609.
    • (1999) Biochemistry , vol.38 , pp. 13602-13609
    • Leimer, U.1    Lun, K.2    Romig, H.3    Walter, J.4    Grunberg, J.5    Brand, M.6    Haass, C.7
  • 22
    • 0033978638 scopus 로고    scopus 로고
    • The type 4 prepilin peptidases comprise a novel family of aspartic acid proteases
    • LaPointe CF, Taylor RK: The type 4 prepilin peptidases comprise a novel family of aspartic acid proteases. J Biol Chem 2000;275:1502-1510.
    • (2000) J Biol Chem , vol.275 , pp. 1502-1510
    • Lapointe, C.F.1    Taylor, R.K.2
  • 23
    • 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: Identification of signal peptide peptidase, a presenilin-type aspartic protease. Science 2002;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
  • 24
    • 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 2005;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    Haass, C.6
  • 25
    • 0036898485 scopus 로고    scopus 로고
    • Alzheimer disease gamma-secretase: A complex story of GxGD-type presenilin proteases
    • Haass C, Steiner H: Alzheimer disease gamma-secretase: a complex story of GxGD-type presenilin proteases. Trends Cell Biol 2002;12:556-562.
    • (2002) Trends Cell Biol , vol.12 , pp. 556-562
    • Haass, C.1    Steiner, H.2
  • 27
    • 0032488995 scopus 로고    scopus 로고
    • The proteolytic fragments of the Alzheimer's disease-associated presenilin-1 form heterodimers and occur as a 100-150-kDa molecular mass complex
    • Capell A, Grunberg J, Pesold B, Diehlmann A, Citron M, Nixon R, Beyreuther K, Selkoe DJ, Haass C: The proteolytic fragments of the Alzheimer's disease-associated presenilin-1 form heterodimers and occur as a 100-150-kDa molecular mass complex. J Biol Chem 1998;273:3205-3211.
    • (1998) J Biol Chem , vol.273 , pp. 3205-3211
    • Capell, A.1    Grunberg, J.2    Pesold, B.3    Diehlmann, A.4    Citron, M.5    Nixon, R.6    Beyreuther, K.7    Selkoe, D.J.8    Haass, C.9
  • 31
    • 0033610863 scopus 로고    scopus 로고
    • Expression of Alzheimer's disease-associated presenilin-1 is controlled by proteolytic degradation and complex formation
    • Steiner H, Capell A, Pesold B, Citron M, Kloetzel PM, Selkoe DJ, Romig H, Mendla K, Haass C: Expression of Alzheimer's disease-associated presenilin-1 is controlled by proteolytic degradation and complex formation. J Biol Chem 1998;273:32322-32331.
    • (1998) J Biol Chem , vol.273 , pp. 32322-32331
    • Steiner, H.1    Capell, A.2    Pesold, B.3    Citron, M.4    Kloetzel, P.M.5    Selkoe, D.J.6    Romig, H.7    Mendla, K.8    Haass, C.9
  • 34
    • 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 VA, Priess JR: APH-1 is a multipass membrane protein essential for the Notch signaling pathway in Caenorhabditis elegans embryos. Proc Natl Acad Sci USA 2002;99:775-779.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 775-779
    • Goutte, C.1    Tsunozaki, M.2    Hale, V.A.3    Priess, J.R.4
  • 35
    • 0037131218 scopus 로고    scopus 로고
    • PEN-2 is an integral component of the gamma-secretase complex required for coordinated expression of presenilin and nicastrin
    • Steiner H, Winkler E, Edbauer D, Prokop S, Basset G, Yamasaki A, Kostka M, Haass C: PEN-2 is an integral component of the gamma-secretase complex required for coordinated expression of presenilin and nicastrin. J Biol Chem 2002;277:39062-39065.
    • (2002) J Biol Chem , vol.277 , pp. 39062-39065
    • Steiner, H.1    Winkler, E.2    Edbauer, D.3    Prokop, S.4    Basset, G.5    Yamasaki, A.6    Kostka, M.7    Haass, C.8
  • 36
    • 0037160063 scopus 로고    scopus 로고
    • Mammalian APH-1 interacts with presenilin and nicastrin and is required for intra-membrane proteolysis of amyloid-beta precursor protein and Notch
    • Lee SF, Shah S, Li H, Yu C, Han W, Yu G: Mammalian APH-1 interacts with presenilin and nicastrin and is required for intra-membrane proteolysis of amyloid-beta precursor protein and Notch. J Biol Chem 2002;277:45013-45019.
    • (2002) J Biol Chem , vol.277 , pp. 45013-45019
    • Lee, S.F.1    Shah, S.2    Li, H.3    Yu, C.4    Han, W.5    Yu, G.6
  • 38
    • 0141483380 scopus 로고    scopus 로고
    • Regulated hyperaccumulation of presenilin-1 and the 'gamma-secretase' complex. Evidence for differential intramembranous processing of transmembrane subatrates
    • Kim SH, Ikeuchi T, Yu C, Sisodia SS: Regulated hyperaccumulation of presenilin-1 and the 'gamma-secretase' complex. Evidence for differential intramembranous processing of transmembrane subatrates. J Biol Chem 2003;278:33992-34002.
    • (2003) J Biol Chem , vol.278 , pp. 33992-34002
    • Kim, S.H.1    Ikeuchi, T.2    Yu, C.3    Sisodia, S.S.4
  • 41
    • 3042520872 scopus 로고    scopus 로고
    • Immature nicastrin stabilizes APH-1 independent of PEN-2 and presenilin: Identification of nicastrin mutants that selectively interact with APH-1
    • Shirotani K, Edbauer D, Kostka M, Steiner H, Haass C: Immature nicastrin stabilizes APH-1 independent of PEN-2 and presenilin: identification of nicastrin mutants that selectively interact with APH-1. J Neurochem 2004;89:1520-1527.
    • (2004) J Neurochem , vol.89 , pp. 1520-1527
    • Shirotani, K.1    Edbauer, D.2    Kostka, M.3    Steiner, H.4    Haass, C.5
  • 44
    • 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 SH, Callahan JW, Mahuran DJ: 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 2004;6:53-65.
    • (2004) J Alzheimers Dis , vol.6 , pp. 53-65
    • Pasternak, S.H.1    Callahan, J.W.2    Mahuran, D.J.3
  • 45
    • 0033214675 scopus 로고    scopus 로고
    • Presenilins: Molecular switches between proteolysis and signal transduction
    • Annaert W, De Strooper B: Presenilins: molecular switches between proteolysis and signal transduction. Trends Neurosci 1999;22:439-443.
    • (1999) Trends Neurosci , vol.22 , pp. 439-443
    • Annaert, W.1    De Strooper, B.2
  • 46
    • 0036327098 scopus 로고    scopus 로고
    • Presenilin-1 affects trafficking and processing of beta APP and is targeted in a complex with nicastrin to the plasma membrane
    • Kaether C, Lammich S, Edbauer D, Ertl M, Rietdorf J, Capell A, Steiner H, Haass C: Presenilin-1 affects trafficking and processing of beta APP and is targeted in a complex with nicastrin to the plasma membrane. J Cell Biol 2002;158:551-561.
    • (2002) J Cell Biol , vol.158 , pp. 551-561
    • Kaether, C.1    Lammich, S.2    Edbauer, D.3    Ertl, M.4    Rietdorf, J.5    Capell, A.6    Steiner, H.7    Haass, C.8
  • 47
    • 14244268498 scopus 로고    scopus 로고
    • Gamma-secretase exists on the plasma membrane as an intact complex that accepts substrates and effects intramembrane cleavage
    • Chyung JH, Raper DM, Selkoe DJ: Gamma-secretase exists on the plasma membrane as an intact complex that accepts substrates and effects intramembrane cleavage. J Biol Chem 2005;280:4383-4392.
    • (2005) J Biol Chem , vol.280 , pp. 4383-4392
    • Chyung, J.H.1    Raper, D.M.2    Selkoe, D.J.3
  • 48
  • 49
    • 33644862462 scopus 로고    scopus 로고
    • APP and Notch intracellular domains are generated after transport of their precursors to the cell surface
    • in press
    • Kaether C, Schmitt S, Willem M, Haass C: APP and Notch intracellular domains are generated after transport of their precursors to the cell surface. Traffic 2006, in press.
    • (2006) Traffic
    • Kaether, C.1    Schmitt, S.2    Willem, M.3    Haass, C.4
  • 50
    • 0037173115 scopus 로고    scopus 로고
    • Presenilin and nicastrin regulate each other and determine amyloid beta -peptide production via complex formation
    • Edbauer D, Winkler E, Haass C, Steiner H: Presenilin and nicastrin regulate each other and determine amyloid beta -peptide production via complex formation. Proc Natl Acad Sci USA 2002;99:8666-8671.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 8666-8671
    • Edbauer, D.1    Winkler, E.2    Haass, C.3    Steiner, H.4
  • 51
    • 2542454942 scopus 로고    scopus 로고
    • Requirement of PEN-2 for stabilization of the presenilin NTF/CTF heterodimer within the gamma-secretase complex
    • Prokop S, Shirotani K, Edbauer D, Haass C, Steiner H: Requirement of PEN-2 for stabilization of the presenilin NTF/CTF heterodimer within the gamma-secretase complex. J Biol Chem 2004;279:23255-23261.
    • (2004) J Biol Chem , vol.279 , pp. 23255-23261
    • Prokop, S.1    Shirotani, K.2    Edbauer, D.3    Haass, C.4    Steiner, H.5
  • 52
    • 0038607071 scopus 로고    scopus 로고
    • Gamma-secretase activity is associated with a conformational change of nicastrin
    • Shirotani K, Edbauer D, Capell A, Schmitz J, Steiner H, Haass C: Gamma-secretase activity is associated with a conformational change of nicastrin. J Biol Chem 2003;278:16474-16477.
    • (2003) J Biol Chem , vol.278 , pp. 16474-16477
    • Shirotani, K.1    Edbauer, D.2    Capell, A.3    Schmitz, J.4    Steiner, H.5    Haass, C.6
  • 55
    • 4444221162 scopus 로고    scopus 로고
    • Co-expression of nicastrin and presenilin rescues a loss of function mutant of APH-1
    • Edbauer D, Kaether C, Steiner H, Haass C: Co-expression of nicastrin and presenilin rescues a loss of function mutant of APH-1. J Biol Chem 2004;279:37311-37315.
    • (2004) J Biol Chem , vol.279 , pp. 37311-37315
    • Edbauer, D.1    Kaether, C.2    Steiner, H.3    Haass, C.4
  • 57
    • 21344463310 scopus 로고    scopus 로고
    • Length and overall sequence of the PEN-2 C-terminal domain determines its function in the stabilization of presenilin fragments
    • Prokop S, Haass C, Steiner H: Length and overall sequence of the PEN-2 C-terminal domain determines its function in the stabilization of presenilin fragments. J Neurochem 2005;94:57-62.
    • (2005) J Neurochem , vol.94 , pp. 57-62
    • Prokop, S.1    Haass, C.2    Steiner, H.3
  • 59
    • 10344243551 scopus 로고    scopus 로고
    • Evidence that assembly of an active gamma-secretase complex occurs in the early compartments of the secretory pathway
    • Kim SH, Yin YI, Li YM, Sisodia SS: Evidence that assembly of an active gamma-secretase complex occurs in the early compartments of the secretory pathway. J Biol Chem 2004;279:48615-48619.
    • (2004) J Biol Chem , vol.279 , pp. 48615-48619
    • Kim, S.H.1    Yin, Y.I.2    Li, Y.M.3    Sisodia, S.S.4
  • 60
    • 0346732290 scopus 로고    scopus 로고
    • Nicastrin interacts with gamma-secretase complex components via the N-terminal part of its transmembrane domain
    • Capell A, Kaether C, Edbauer D, Shirotani K, Merkl S, Steiner H, Haass C: Nicastrin interacts with gamma-secretase complex components via the N-terminal part of its transmembrane domain. J Biol Chem 2003;278:52519-52523.
    • (2003) J Biol Chem , vol.278 , pp. 52519-52523
    • Capell, A.1    Kaether, C.2    Edbauer, D.3    Shirotani, K.4    Merkl, S.5    Steiner, H.6    Haass, C.7
  • 61
    • 0242321985 scopus 로고    scopus 로고
    • The transmembrane domain region of nicastrin mediates direct interactions with APH-1 and the gamma-secretase complex
    • Morais VA, Crystal AS, Pijak DS, Carlin D, Costa J, Lee VM, Doms RW: The transmembrane domain region of nicastrin mediates direct interactions with APH-1 and the gamma-secretase complex. J Biol Chem 2003;278:43284-43291.
    • (2003) J Biol Chem , vol.278 , pp. 43284-43291
    • Morais, V.A.1    Crystal, A.S.2    Pijak, D.S.3    Carlin, D.4    Costa, J.5    Lee, V.M.6    Doms, R.W.7
  • 62
    • 11244272819 scopus 로고    scopus 로고
    • The presenilin C-terminus is required for ER-retention, nicastrin-binding and gamma-secretase activity
    • Kaether C, Capell A, Edbauer D, Winkler E, Novak B, Steiner H, Haass C: The presenilin C-terminus is required for ER-retention, nicastrin-binding and gamma-secretase activity. EMBO J 2004;23:4738-4748.
    • (2004) EMBO J , vol.23 , pp. 4738-4748
    • Kaether, C.1    Capell, A.2    Edbauer, D.3    Winkler, E.4    Novak, B.5    Steiner, H.6    Haass, C.7
  • 63
    • 8544219758 scopus 로고    scopus 로고
    • The extreme C terminus of presenilin 1 is essential for gamma-secretase complex assembly and activity
    • Bergman A, Laudon H, Winblad B, Lundkvist J, Naslund J: The extreme C terminus of presenilin 1 is essential for gamma-secretase complex assembly and activity. J Biol Chem 2004;279:45564-45572.
    • (2004) J Biol Chem , vol.279 , pp. 45564-45572
    • Bergman, A.1    Laudon, H.2    Winblad, B.3    Lundkvist, J.4    Naslund, J.5
  • 64
    • 29644435433 scopus 로고    scopus 로고
    • Evidence that the 'NF' motif in transmembrane domain 4 of presenilin 1 is critical for binding with PEN-2
    • Kim SH, Sisodia SS: Evidence that the 'NF' motif in transmembrane domain 4 of presenilin 1 is critical for binding with PEN-2. J Biol Chem 2005;280:41953-41966.
    • (2005) J Biol Chem , vol.280 , pp. 41953-41966
    • Kim, S.H.1    Sisodia, S.S.2
  • 65
    • 29644432040 scopus 로고    scopus 로고
    • Pen-2 is incorporated into the gamma-secretase complex through binding to transmembrane domain 4 of presenilin 1
    • Watanabe N, Tomita T, Sato C, Kitamura T, Morohashi Y, Iwatsubo T: Pen-2 is incorporated into the gamma-secretase complex through binding to transmembrane domain 4 of presenilin 1. J Biol Chem 2005;280:41967-41975.
    • (2005) J Biol Chem , vol.280 , pp. 41967-41975
    • Watanabe, N.1    Tomita, T.2    Sato, C.3    Kitamura, T.4    Morohashi, Y.5    Iwatsubo, T.6
  • 67
    • 0141856357 scopus 로고    scopus 로고
    • Rer1p, a retrieval receptor for ER membrane proteins, recognizes transmembrane domains in multiple modes
    • Sato K, Sato M, Nakano A: Rer1p, a retrieval receptor for ER membrane proteins, recognizes transmembrane domains in multiple modes. Mol Biol Cell 2003;14:3605-3616.
    • (2003) Mol Biol Cell , vol.14 , pp. 3605-3616
    • Sato, K.1    Sato, M.2    Nakano, A.3
  • 68
    • 1842410168 scopus 로고    scopus 로고
    • Human Rer1 is localized to the Golgi apparatus and complements the deletion of the homologous Rer1 protein of Saccharomyces cerevisiae
    • Füllekrug J, Boehm J, Rottger S, Nilsson T, Mieskes G, Schmitt HD: Human Rer1 is localized to the Golgi apparatus and complements the deletion of the homologous Rer1 protein of Saccharomyces cerevisiae. Eur J Cell Biol 1997;74:31-40.
    • (1997) Eur J Cell Biol , vol.74 , pp. 31-40
    • Füllekrug, J.1    Boehm, J.2    Rottger, S.3    Nilsson, T.4    Mieskes, G.5    Schmitt, H.D.6
  • 69
    • 18844378852 scopus 로고    scopus 로고
    • Presenilin function and gamma-secretase activity
    • Brunkan AL, Goate AM: Presenilin function and gamma-secretase activity. J Neurochem 2005;93:769-792.
    • (2005) J Neurochem , vol.93 , pp. 769-792
    • Brunkan, A.L.1    Goate, A.M.2
  • 70
    • 0031108103 scopus 로고    scopus 로고
    • Human presenilin-1, but not familial Alzheimer's disease (FAD) mutants, facilitate Caenorhabditis elegans Notch signalling independently of proteolytic processing
    • Baumeister R, Leimer U, Zweckbronner I, Jakubek C, Grunberg J, Haass C: Human presenilin-1, but not familial Alzheimer's disease (FAD) mutants, facilitate Caenorhabditis elegans Notch signalling independently of proteolytic processing. Genes Funct 1997;1:149-159.
    • (1997) Genes Funct , vol.1 , pp. 149-159
    • Baumeister, R.1    Leimer, U.2    Zweckbronner, I.3    Jakubek, C.4    Grunberg, J.5    Haass, C.6
  • 71
    • 0033583047 scopus 로고    scopus 로고
    • The biological and pathological function of the presenilin-1delta exon 9 mutation is independent of its defect to undergo proteolytic processing
    • Steiner H, Romig H, Grim MG, Philipp U, Pesold B, Citron M, Baumeister R, Haass C: The biological and pathological function of the presenilin-1delta exon 9 mutation is independent of its defect to undergo proteolytic processing. J Biol Chem 1999;274:7615-7618.
    • (1999) J Biol Chem , vol.274 , pp. 7615-7618
    • Steiner, H.1    Romig, H.2    Grim, M.G.3    Philipp, U.4    Pesold, B.5    Citron, M.6    Baumeister, R.7    Haass, C.8
  • 74
    • 0347785491 scopus 로고    scopus 로고
    • Presenilin-dependent intramembrane proteolysis of CD44 leads to the liberation of its intracellular domain and the secretion of an Abeta - Like peptide
    • Lammich S, Okochi M, Takeda M, Kaether C, Capell A, Zimmer AK, Edbauer D, Walter J, Steiner H, Haass C: Presenilin-dependent intramembrane proteolysis of CD44 leads to the liberation of its intracellular domain and the secretion of an Abeta - like peptide. J Biol Chem 2002;277:44754-44759.
    • (2002) J Biol Chem , vol.277 , pp. 44754-44759
    • Lammich, S.1    Okochi, M.2    Takeda, M.3    Kaether, C.4    Capell, A.5    Zimmer, A.K.6    Edbauer, D.7    Walter, J.8    Steiner, H.9    Haass, C.10
  • 76
    • 0033639117 scopus 로고    scopus 로고
    • Requirements for presenilin-dependent cleavage of Notch and other transmembrane proteins
    • Struhl G, Adachi A: Requirements for presenilin-dependent cleavage of Notch and other transmembrane proteins. Mol Cell 2000;6:625-636.
    • (2000) Mol Cell , vol.6 , pp. 625-636
    • Struhl, G.1    Adachi, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.