Presenilin-1 influences processing of the acetylcholinesterase membrane anchor PRiMA

Presenilin-1 (PS1) is the catalytic component of the γ-secretase complex. In this study, we explore if PS1 participates in the processing of the cholinergic acetylcholinesterase (AChE). The major AChE variant expressed in the brain is a tetramer (G4) bound to a proline-rich membrane anchor (PRiMA)....

Full description

Saved in:
Bibliographic Details
Published inNeurobiology of aging Vol. 35; no. 7; pp. 1526 - 1536
Main Authors García-Ayllón, María-Salud, Campanari, María-Letizia, Montenegro, María-Fernanda, Cuchillo-Ibáñez, Inmaculada, Belbin, Olivia, Lleó, Alberto, Tsim, Karl, Vidal, Cecilio J., Sáez-Valero, Javier
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 01.07.2014
Subjects
Acetylcholinesterase
Acetylcholinesterase - metabolism
Acetylcholinesterase - physiology
Acetylcholinesterase - therapeutic use
Alzheimer Disease - drug therapy
Alzheimer Disease - etiology
Alzheimer's disease
Amyloid Precursor Protein Secretases - physiology
Amyloid Precursor Protein Secretases - therapeutic use
Animals
Brain - enzymology
Brain - metabolism
Cell Nucleus - enzymology
Cells, Cultured
Cricetinae
Drug Design
Female
Gene Expression - genetics
Internal Medicine
Membrane Microdomains - metabolism
Membrane Proteins - genetics
Membrane Proteins - metabolism
Mice
Mice, Knockout
Molecular Targeted Therapy
Nerve Tissue Proteins - genetics
Nerve Tissue Proteins - metabolism
Neurology
Presenilin 1
Presenilin-1 - physiology
PRiMA
γ-Secretase
Acetylcholinesterase
Presenilin 1
PRiMA
Alzheimer's disease
γ-Secretase
Online AccessGet full text
ISSN0197-4580
1558-1497
1558-1497
DOI10.1016/j.neurobiolaging.2014.01.147

Cover

Abstract Presenilin-1 (PS1) is the catalytic component of the γ-secretase complex. In this study, we explore if PS1 participates in the processing of the cholinergic acetylcholinesterase (AChE). The major AChE variant expressed in the brain is a tetramer (G4) bound to a proline-rich membrane anchor (PRiMA). Overexpression of the transmembrane PRiMA protein in Chinese hamster ovary cells expressing AChE and treated with the γ-secretase inhibitor N-[N-(3,5-difluorophenacetyl)-l-alanyl]-S-phenylglycine t-butyl ester have enabled us to study whether, through its γ-secretase activity, PS1 participates in the processing of PRiMA-linked AChE. γ-Secretase inhibition led to a notable increase in the level of PRiMA-linked AChE, suggesting that γ-secretase is involved in the cleavage of PRiMA. We demonstrate that cleavage of PRiMA by γ-secretase results in a C-terminal PRiMA fragment. Immunofluorescence labeling allowed us to identify this PRiMA fragment in the nucleus. Moreover, we have determined changes in the proportion of the raft-residing AChE-PRiMA in a PS1 conditional knockout mouse. Our results are of interest as both enzymes have therapeutic relevance for Alzheimer's disease.
AbstractList Presenilin-1 (PS1) is the catalytic component of the γ-secretase complex. In this study, we explore if PS1 participates in the processing of the cholinergic acetylcholinesterase (AChE). The major AChE variant expressed in the brain is a tetramer (G(4)) bound to a proline-rich membrane anchor (PRiMA). Overexpression of the transmembrane PRiMA protein in Chinese hamster ovary cells expressing AChE and treated with the γ-secretase inhibitor N-[N-(3,5-difluorophenacetyl)-l-alanyl]-S-phenylglycine t-butyl ester have enabled us to study whether, through its γ-secretase activity, PS1 participates in the processing of PRiMA-linked AChE. γ-Secretase inhibition led to a notable increase in the level of PRiMA-linked AChE, suggesting that γ-secretase is involved in the cleavage of PRiMA. We demonstrate that cleavage of PRiMA by γ-secretase results in a C-terminal PRiMA fragment. Immunofluorescence labeling allowed us to identify this PRiMA fragment in the nucleus. Moreover, we have determined changes in the proportion of the raft-residing AChE-PRiMA in a PS1 conditional knockout mouse. Our results are of interest as both enzymes have therapeutic relevance for Alzheimer's disease.Presenilin-1 (PS1) is the catalytic component of the γ-secretase complex. In this study, we explore if PS1 participates in the processing of the cholinergic acetylcholinesterase (AChE). The major AChE variant expressed in the brain is a tetramer (G(4)) bound to a proline-rich membrane anchor (PRiMA). Overexpression of the transmembrane PRiMA protein in Chinese hamster ovary cells expressing AChE and treated with the γ-secretase inhibitor N-[N-(3,5-difluorophenacetyl)-l-alanyl]-S-phenylglycine t-butyl ester have enabled us to study whether, through its γ-secretase activity, PS1 participates in the processing of PRiMA-linked AChE. γ-Secretase inhibition led to a notable increase in the level of PRiMA-linked AChE, suggesting that γ-secretase is involved in the cleavage of PRiMA. We demonstrate that cleavage of PRiMA by γ-secretase results in a C-terminal PRiMA fragment. Immunofluorescence labeling allowed us to identify this PRiMA fragment in the nucleus. Moreover, we have determined changes in the proportion of the raft-residing AChE-PRiMA in a PS1 conditional knockout mouse. Our results are of interest as both enzymes have therapeutic relevance for Alzheimer's disease.
Presenilin-1 (PS1) is the catalytic component of the gamma -secretase complex. In this study, we explore if PS1 participates in the processing of the cholinergic acetylcholinesterase (AChE). The major AChE variant expressed in the brain is a tetramer (G sub(4)) bound to a proline-rich membrane anchor (PRiMA). Overexpression of the transmembrane PRiMA protein in Chinese hamster ovary cells expressing AChE and treated with the gamma -secretase inhibitor N-[N-(3,5-difluorophenacetyl)-l-alanyl]-S-phenylglycine t-butyl ester have enabled us to study whether, through its gamma -secretase activity, PS1 participates in the processing of PRiMA-linked AChE. gamma -Secretase inhibition led to a notable increase in the level of PRiMA-linked AChE, suggesting that gamma -secretase is involved in the cleavage of PRiMA. We demonstrate that cleavage of PRiMA by gamma -secretase results in a C-terminal PRiMA fragment. Immunofluorescence labeling allowed us to identify this PRiMA fragment in the nucleus. Moreover, we have determined changes in the proportion of the raft-residing AChE-PRiMA in a PS1 conditional knockout mouse. Our results are of interest as both enzymes have therapeutic relevance for Alzheimer's disease.
Abstract Presenilin-1 (PS1) is the catalytic component of the γ-secretase complex. In this study, we explore if PS1 participates in the processing of the cholinergic acetylcholinesterase (AChE). The major AChE variant expressed in the brain is a tetramer (G4 ) bound to a proline-rich membrane anchor (PRiMA). Overexpression of the transmembrane PRiMA protein in Chinese hamster ovary cells expressing AChE and treated with the γ-secretase inhibitor N -[ N -(3,5-difluorophenacetyl)-l-alanyl]- S -phenylglycine t -butyl ester have enabled us to study whether, through its γ-secretase activity, PS1 participates in the processing of PRiMA-linked AChE. γ-Secretase inhibition led to a notable increase in the level of PRiMA-linked AChE, suggesting that γ-secretase is involved in the cleavage of PRiMA. We demonstrate that cleavage of PRiMA by γ-secretase results in a C-terminal PRiMA fragment. Immunofluorescence labeling allowed us to identify this PRiMA fragment in the nucleus. Moreover, we have determined changes in the proportion of the raft-residing AChE-PRiMA in a PS1 conditional knockout mouse. Our results are of interest as both enzymes have therapeutic relevance for Alzheimer's disease.
Presenilin-1 (PS1) is the catalytic component of the γ-secretase complex. In this study, we explore if PS1 participates in the processing of the cholinergic acetylcholinesterase (AChE). The major AChE variant expressed in the brain is a tetramer (G(4)) bound to a proline-rich membrane anchor (PRiMA). Overexpression of the transmembrane PRiMA protein in Chinese hamster ovary cells expressing AChE and treated with the γ-secretase inhibitor N-[N-(3,5-difluorophenacetyl)-l-alanyl]-S-phenylglycine t-butyl ester have enabled us to study whether, through its γ-secretase activity, PS1 participates in the processing of PRiMA-linked AChE. γ-Secretase inhibition led to a notable increase in the level of PRiMA-linked AChE, suggesting that γ-secretase is involved in the cleavage of PRiMA. We demonstrate that cleavage of PRiMA by γ-secretase results in a C-terminal PRiMA fragment. Immunofluorescence labeling allowed us to identify this PRiMA fragment in the nucleus. Moreover, we have determined changes in the proportion of the raft-residing AChE-PRiMA in a PS1 conditional knockout mouse. Our results are of interest as both enzymes have therapeutic relevance for Alzheimer's disease.
Presenilin-1 (PS1) is the catalytic component of the γ-secretase complex. In this study, we explore if PS1 participates in the processing of the cholinergic acetylcholinesterase (AChE). The major AChE variant expressed in the brain is a tetramer (G4) bound to a proline-rich membrane anchor (PRiMA). Overexpression of the transmembrane PRiMA protein in Chinese hamster ovary cells expressing AChE and treated with the γ-secretase inhibitor N-[N-(3,5-difluorophenacetyl)-l-alanyl]-S-phenylglycine t-butyl ester have enabled us to study whether, through its γ-secretase activity, PS1 participates in the processing of PRiMA-linked AChE. γ-Secretase inhibition led to a notable increase in the level of PRiMA-linked AChE, suggesting that γ-secretase is involved in the cleavage of PRiMA. We demonstrate that cleavage of PRiMA by γ-secretase results in a C-terminal PRiMA fragment. Immunofluorescence labeling allowed us to identify this PRiMA fragment in the nucleus. Moreover, we have determined changes in the proportion of the raft-residing AChE-PRiMA in a PS1 conditional knockout mouse. Our results are of interest as both enzymes have therapeutic relevance for Alzheimer's disease.
Author Cuchillo-Ibáñez, Inmaculada
Vidal, Cecilio J.
Tsim, Karl
Campanari, María-Letizia
Sáez-Valero, Javier
Belbin, Olivia
Montenegro, María-Fernanda
Lleó, Alberto
García-Ayllón, María-Salud
Author_xml – sequence: 1
  givenname: María-Salud
  surname: García-Ayllón
  fullname: García-Ayllón, María-Salud
  organization: Instituto de Neurociencias de Alicante, Universidad Miguel Hernández—Consejo Superior de Investigaciones Científicas (CSIC), Sant Joan d'Alacant, Spain
– sequence: 2
  givenname: María-Letizia
  surname: Campanari
  fullname: Campanari, María-Letizia
  organization: Instituto de Neurociencias de Alicante, Universidad Miguel Hernández—Consejo Superior de Investigaciones Científicas (CSIC), Sant Joan d'Alacant, Spain
– sequence: 3
  givenname: María-Fernanda
  surname: Montenegro
  fullname: Montenegro, María-Fernanda
  organization: Departamento de Bioquímica y Biología Molecular-A, Universidad de Murcia, Regional Campus of International Excellence “Campus Mare Nostrum”, Murcia, Spain
– sequence: 4
  givenname: Inmaculada
  surname: Cuchillo-Ibáñez
  fullname: Cuchillo-Ibáñez, Inmaculada
  organization: Instituto de Neurociencias de Alicante, Universidad Miguel Hernández—Consejo Superior de Investigaciones Científicas (CSIC), Sant Joan d'Alacant, Spain
– sequence: 5
  givenname: Olivia
  surname: Belbin
  fullname: Belbin, Olivia
  organization: Centro de Investigación Biomédica en Red sobre Enfermedades Neurodegenerativas (CIBERNED), Madrid, Spain
– sequence: 6
  givenname: Alberto
  surname: Lleó
  fullname: Lleó, Alberto
  organization: Centro de Investigación Biomédica en Red sobre Enfermedades Neurodegenerativas (CIBERNED), Madrid, Spain
– sequence: 7
  givenname: Karl
  surname: Tsim
  fullname: Tsim, Karl
  organization: Division of Life Science and Center for Chinese Medicine, The Hong Kong University of Science and Technology, Hong Kong, China
– sequence: 8
  givenname: Cecilio J.
  surname: Vidal
  fullname: Vidal, Cecilio J.
  organization: Departamento de Bioquímica y Biología Molecular-A, Universidad de Murcia, Regional Campus of International Excellence “Campus Mare Nostrum”, Murcia, Spain
– sequence: 9
  givenname: Javier
  surname: Sáez-Valero
  fullname: Sáez-Valero, Javier
  email: j.saez@umh.es
  organization: Instituto de Neurociencias de Alicante, Universidad Miguel Hernández—Consejo Superior de Investigaciones Científicas (CSIC), Sant Joan d'Alacant, Spain
BackLink https://www.ncbi.nlm.nih.gov/pubmed/24612677$$D View this record in MEDLINE/PubMed
BookMark eNqNkk1rFEEQhhuJmE30L8gcPHiZsas_Z0CEmPgFEYPGc9PTW5P0OtMdu2cC--_tZaOgIOypDvXUWy_11gk5CjEgIS-ANkBBvdo0AZcUex9He-PDTcMoiIZCA0I_IiuQsq1BdPqIrCh0uhaypcfkJOcNpVQLrZ6QYyYUMKX1ilxfJcwY_OhDDZUPw7hgcJiruxRLyWVBFYdqvsXKOpy3o7uNhcU8Y7IZqwmnPtlQuqF0UnX11X8-e0oeD3bM-OyhnpLv799dn3-sL798-HR-dlk72am5VhoGJ23rULJiDZVeS0ElUsEpU9TytuOdtqIFtu4FF4wJ17pBcSd434Hgp-TlXreY_bkUT2by2eE4FkNxyQYkL8OScn0ACkJwqTgt6PMHdOknXJu75Cebtub30Qrweg-4FHNOOPxBgJpdRmZj_s7I7DIyFEzJqIy__Wfc-dnOPoY5WT8eKvJmL4Llvvcek3ElFu_s-AO3mDdxSaGc3oDJzFDzbfcKu08AQYt21xWBi_8LmHX0h_n4BaqmzC0
CitedBy_id crossref_primary_10_1016_j_semcdb_2020_05_019
crossref_primary_10_1007_s12031_015_0699_y
crossref_primary_10_1111_jnc_15189
crossref_primary_10_1007_s12031_015_0667_6
crossref_primary_10_3390_ijms24021437
crossref_primary_10_36290_csf_2016_011
crossref_primary_10_1016_j_cbi_2016_04_009
crossref_primary_10_1096_fj_201600609R
crossref_primary_10_3389_fncel_2019_00309
Cites_doi 10.1016/S0960-9822(01)00394-3
10.1038/nmeth.2089
10.1056/NEJMra040223
10.1074/jbc.M402752200
10.1002/ana.410190305
10.1111/j.1365-2818.1993.tb03313.x
10.1074/jbc.M607221200
10.1111/j.1365-2818.2006.01706.x
10.1021/bi002770t
10.1093/emboj/cdg005
10.1159/000095267
10.1074/jbc.M407986200
10.4161/cc.4.1.1322
10.1021/bi034904j
10.2174/156720508783954767
10.1016/j.bbrc.2009.03.070
10.1111/j.1471-4159.2009.06126.x
10.1016/0306-4522(88)90012-7
10.1016/j.bbrc.2006.11.043
10.1016/j.bbrc.2004.09.095
10.1016/S1097-2765(00)00061-7
10.1111/j.1742-4658.2009.07022.x
10.1016/S0140-6736(76)91936-X
10.1046/j.1460-9568.2003.02914.x
10.1038/35067589
10.1523/JNEUROSCI.3863-08.2009
10.1016/j.neulet.2012.06.045
10.1006/bbrc.1996.1577
10.1002/jnr.20981
10.1016/S0168-0102(02)00005-6
10.2174/156802611795861004
10.1074/jbc.M109.038711
10.1385/MN:26:1:081
10.1016/0197-0186(95)00099-2
10.1016/0197-0186(87)90029-5
10.1111/j.1471-4159.2010.07032.x
10.1128/MCB.02065-07
10.1101/cshperspect.a006270
10.3389/fphys.2012.00189
10.1046/j.1471-4159.1999.721600.x
10.1016/j.brainres.2009.07.105
10.1016/j.bbamem.2006.05.008
10.1016/S0140-6736(77)91780-9
10.1016/S0896-6273(04)00182-5
10.1124/jpet.102.048280
10.1046/j.1432-1327.1999.00693.x
10.2174/156720511795256008
10.1002/gps.935
10.1016/0306-4522(82)90111-7
10.1111/j.1600-0404.2006.00682.x
10.1016/0304-3940(83)90302-6
10.1074/jbc.272.12.7977
10.1016/j.cbi.2012.09.019
10.1046/j.1471-4159.1999.721534.x
10.1016/j.neuron.2012.10.003
10.1074/jbc.274.18.12702
10.1016/S0896-6273(01)00417-2
10.1046/j.1471-4159.1997.69052179.x
10.1006/bbrc.1996.0180
10.1093/brain/awm276
10.1016/j.brainres.2010.05.022
10.1016/j.cbi.2010.02.018
10.1074/jbc.M109119200
10.1159/000065054
10.1016/S0896-6273(01)00584-0
10.1001/archneurol.2012.540
10.1074/jbc.R800019200
10.2174/138920207783769549
10.1016/j.neurobiolaging.2011.04.006
10.1074/jbc.M111.261248
10.1002/jnr.490350610
10.1016/S0140-6736(06)69113-7
ContentType Journal Article
Copyright 2014 Elsevier Inc.
Elsevier Inc.
Copyright © 2014 Elsevier Inc. All rights reserved.
Copyright_xml – notice: 2014 Elsevier Inc.
– notice: Elsevier Inc.
– notice: Copyright © 2014 Elsevier Inc. All rights reserved.
DBID AAYXX
CITATION
CGR
CUY
CVF
ECM
EIF
NPM
7X8
7TK
DOI 10.1016/j.neurobiolaging.2014.01.147
DatabaseName CrossRef
Medline
MEDLINE
MEDLINE (Ovid)
MEDLINE
MEDLINE
PubMed
MEDLINE - Academic
Neurosciences Abstracts
DatabaseTitle CrossRef
MEDLINE
Medline Complete
MEDLINE with Full Text
PubMed
MEDLINE (Ovid)
MEDLINE - Academic
Neurosciences Abstracts
DatabaseTitleList MEDLINE - Academic
Neurosciences Abstracts

MEDLINE
Database_xml – sequence: 1
  dbid: NPM
  name: PubMed
  url: https://proxy.k.utb.cz/login?url=http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed
  sourceTypes: Index Database
– sequence: 2
  dbid: EIF
  name: MEDLINE
  url: https://proxy.k.utb.cz/login?url=https://www.webofscience.com/wos/medline/basic-search
  sourceTypes: Index Database
DeliveryMethod fulltext_linktorsrc
Discipline Anatomy & Physiology
EISSN 1558-1497
EndPage 1536
ExternalDocumentID 24612677
10_1016_j_neurobiolaging_2014_01_147
1_s2_0_S0197458014001699
S0197458014001699
Genre Research Support, Non-U.S. Gov't
Journal Article
GroupedDBID ---
--K
--M
-~X
.1-
.FO
.GJ
.~1
0R~
123
1B1
1P~
1RT
1~.
1~5
29N
4.4
457
4G.
53G
5RE
5VS
7-5
71M
8P~
9JM
9JO
AABNK
AADFP
AAEDT
AAEDW
AAGJA
AAGUQ
AAIKJ
AAKOC
AALRI
AAOAW
AAQFI
AAQXK
AATTM
AAXKI
AAXLA
AAXUO
AAYWO
ABBQC
ABCQJ
ABFNM
ABFRF
ABGSF
ABIVO
ABJNI
ABLJU
ABMAC
ABMZM
ABOYX
ABUDA
ABWVN
ABXDB
ACDAQ
ACGFO
ACGFS
ACIEU
ACIUM
ACRLP
ACRPL
ACVFH
ACXNI
ADBBV
ADCNI
ADEZE
ADMUD
ADNMO
ADUVX
AEBSH
AEFWE
AEHWI
AEIPS
AEKER
AENEX
AEUPX
AEVXI
AFJKZ
AFPUW
AFRHN
AFTJW
AFXIZ
AGCQF
AGHFR
AGQPQ
AGRDE
AGUBO
AGWIK
AGYEJ
AHHHB
AIEXJ
AIGII
AIIUN
AIKHN
AITUG
AJRQY
AJUYK
AKBMS
AKRLJ
AKRWK
AKYEP
ALMA_UNASSIGNED_HOLDINGS
AMRAJ
ANKPU
ANZVX
APXCP
ASPBG
AVWKF
AXJTR
AZFZN
BKOJK
BLXMC
BNPGV
CS3
DU5
EBS
EFJIC
EFKBS
EJD
EO8
EO9
EP2
EP3
F5P
FDB
FEDTE
FGOYB
FIRID
FNPLU
FYGXN
G-2
G-Q
GBLVA
HDW
HMK
HMO
HMQ
HVGLF
HZ~
IHE
J1W
KOM
LX8
M29
M2V
M41
MO0
MOBAO
MVM
N9A
O-L
O9-
OAUVE
OD~
OKEIE
OO0
OZT
P-8
P-9
P2P
PC.
Q38
R2-
ROL
RPZ
SAE
SCC
SDF
SDG
SDP
SEL
SES
SEW
SNS
SPCBC
SSB
SSH
SSN
SSU
SSY
SSZ
T5K
WUQ
Z5R
ZGI
~G-
AACTN
AFCTW
AFKWA
AJOXV
AMFUW
RIG
AAYXX
AGRNS
CITATION
CGR
CUY
CVF
ECM
EIF
NPM
7X8
ACLOT
EFLBG
~HD
7TK
ID FETCH-LOGICAL-c596t-671fc5a8ce52007e67d5405e0430260a389397a4812db434224c8cf63c43b9143
ISSN 0197-4580
1558-1497
IngestDate Sun Sep 28 11:16:20 EDT 2025
Sun Sep 28 03:09:41 EDT 2025
Mon Jul 21 06:02:00 EDT 2025
Tue Jul 01 01:28:10 EDT 2025
Thu Apr 24 23:08:42 EDT 2025
Sun Feb 23 10:19:35 EST 2025
Tue Aug 26 19:57:19 EDT 2025
IsDoiOpenAccess false
IsOpenAccess true
IsPeerReviewed true
IsScholarly true
Issue 7
Keywords Acetylcholinesterase
Presenilin 1
PRiMA
Alzheimer's disease
γ-Secretase
Language English
License https://www.elsevier.com/tdm/userlicense/1.0
Copyright © 2014 Elsevier Inc. All rights reserved.
LinkModel OpenURL
MergedId FETCHMERGED-LOGICAL-c596t-671fc5a8ce52007e67d5405e0430260a389397a4812db434224c8cf63c43b9143
Notes ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ObjectType-Article-2
ObjectType-Feature-1
OpenAccessLink https://digital.csic.es/bitstream/10261/103460/4/Presenilin1_influences_processing_GaciaAyllon.pdf
PMID 24612677
PQID 1514435630
PQPubID 23479
PageCount 11
ParticipantIDs proquest_miscellaneous_1534815037
proquest_miscellaneous_1514435630
pubmed_primary_24612677
crossref_primary_10_1016_j_neurobiolaging_2014_01_147
crossref_citationtrail_10_1016_j_neurobiolaging_2014_01_147
elsevier_clinicalkeyesjournals_1_s2_0_S0197458014001699
elsevier_clinicalkey_doi_10_1016_j_neurobiolaging_2014_01_147
ProviderPackageCode CITATION
AAYXX
PublicationCentury 2000
PublicationDate 2014-07-01
PublicationDateYYYYMMDD 2014-07-01
PublicationDate_xml – month: 07
  year: 2014
  text: 2014-07-01
  day: 01
PublicationDecade 2010
PublicationPlace United States
PublicationPlace_xml – name: United States
PublicationTitle Neurobiology of aging
PublicationTitleAlternate Neurobiol Aging
PublicationYear 2014
Publisher Elsevier Inc
Publisher_xml – name: Elsevier Inc
References Davies, Maloney (bib14) 1976; 2
Leung, Xie, Chen, Mok, Chu, Choi, Tsim (bib38) 2009; 276
Chen, Choi, Chan, Leung, Guo, Chan, Luk, Tsim (bib12) 2011; 286
Anglade, Grassi, Motelica-Heino, Hashikawa, Tsuji (bib1) 1999; 37
Noureddine, Schmitt, Liu, Garbay, Massoulié, Bon (bib45) 2007; 282
Flores-Flores, Martinez-Martinez, Muñoz-Delgado, Vidal (bib19) 1996; 219
Lleó (bib39) 2007; 8
Riddell, Christie, Hussain, Dingwall (bib51) 2001; 11
Silveyra, García-Ayllón, Serra-Basante, Mazzoni, García-Gutierrez, Manzanares, Culvenor, Sáez-Valero (bib58) 2012; 33
Sáez-Valero, Sberna, McLean, Small (bib53) 1999; 72
Perrier, Khérif, Perrier, Dumas, Mallet, Massoulié (bib49) 2003; 18
Wolfe (bib68) 2008; 5
Vetrivel, Cheng, Lin, Sakurai, Li, Nukina, Wong, Xu, Thinakaran (bib63) 2004; 279
Xie, Liang, Leung, Chen, Zhu, Chan, Choi, Massoulié, Tsim (bib70) 2010; 285
Hicks, Nalivaeva, Turner (bib32) 2012; 3
Silveyra, Evin, Montenegro, Vidal, Martínez, Culvenor, Sáez-Valero (bib57) 2008; 28
Thinakaran, Koo (bib62) 2008; 283
Soreq, Seidman (bib60) 2001; 2
Hicks, John, Makova, Henderson, Nalivaeva, Turner (bib30) 2011; 116
Xia, Zhang, Kholodenko, Citron, Podlisny, Teplow, Haass, Seubert, Koo, Selkoe (bib69) 1997; 272
Yang, He, Zhang (bib72) 2002; 42
Suzuki, Hayashi, Nakahara, Kumazaki, Prox, Horiuchi, Zeng, Tanimura, Nishiyama, Osawa, Sehara-Fujisawa, Saftig, Yokoshima, Fukuyama, Matsuki, Koyama, Tomita, Iwatsubo (bib61) 2012; 76
Wagner, Tanzi, Mobley, Galasko (bib66) 2012; 69
Bolte, Cordelieres (bib8) 2006; 224
Hinz, Ramer, Eichele, Weinzierl, Brune (bib33) 2004; 324
Parkin, Hussain, Karran, Turner, Hooper (bib46) 1999; 72
Fishman, Siek, MacCallum, Bird, Volicer, Marquis (bib18) 1986; 19
Giacobini (bib21) 2003; 18
Chan, Chen, Luk, Choi, Tsim (bib11) 2012; 523
Hicks, Makova, Nalivaeva, Turner (bib31) 2013; 203
Cummings (bib13) 2004; 351
Lanz, Himes, Pallante, Adams, Yamazaki, Amore, Merchant (bib37) 2003; 305
Huang, Lee, Johnson, Naleway, Guzikowski, Dai, Darzynkiewicz (bib35) 2005; 4
Berson, Knobloch, Hanan, Diamant, Sharoni, Schuppli, Geyer, Ravid, Mor, Nitsch, Soreq (bib6) 2008; 131
Perrier, Massoulié, Krejci (bib48) 2002; 33
Manders, Verbeek, Aten (bib41) 1993; 169
Appleyard, Smith (bib2) 1987; 11
Capell, Meyn, Fluhrer, Teplow, Walter, Haass (bib10) 2002; 277
Saura, Choi, Beglopoulos, Malkani, Zhang, Shankaranarayana Rao, Chattarji, Kelleher, Kandel, Duff, Kirkwood, Shen (bib55) 2004; 42
Hattori, Asai, Onishi, Sasagawa, Hashimoto, Saido, Maruyama, Mizutani, Ishiura (bib28) 2006; 84
Meshorer, Toiber, Zurel, Sahly, Dori, Cagnano, Schreiber, Grisaru, Tronche, Soreq (bib44) 2004; 279
Xie, Leung, Chen, Chan, Xu, Guo, Zhu, Zheng, Bi, Zhan, Chan, Choi, Tsim (bib71) 2010; 187
Evin, Sharples, Weidemann, Reinhard, Carbone, Culvenor, Holsinger, Sernee, Beyreuther, Masters (bib17) 2001; 40
Kaether, Haass, Steiner (bib36) 2006; 3
Eckert, Müller (bib16) 2009; 382
Sáez-Valero, Tornel, Muñoz-Delgado, Vidal (bib54) 1993; 35
Small, Michaelson, Sberna (bib59) 1996; 28
Schneider, Rasband, Eliceiri (bib56) 2012; 9
Grisaru, Sternfeld, Eldor, Glick, Soreq (bib24) 1999; 264
Henderson, Matto, John, Nalivaeva, Turner (bib29) 2012; 1344
Perry, Perry, Blessed, Tomlinson (bib50) 1977; 1
Volonte, Galbiati, Li, Nishiyama, Okamoto, Lisanti (bib64) 1999; 274
Struhl, Adachi (bib74) 2000; 6
García-Marcos, Pochet, Tandel, Fontanils, Astigarraga, Fernández-González, Kumps, Marino, Dehaye (bib20) 2006; 1758
Dobbertin, Hrabovska, Dembele, Camp, Taylor, Krejci, Bernard (bib15) 2009; 29
Parkin, Hussain, Turner, Hooper (bib47) 1997; 69
Williamson, Sutherland (bib67) 2011; 8
Atack, Perry, Bonham, Perry, Tomlinson, Blessed, Fairbairn (bib5) 1983; 40
Asai, Iwata, Yoshikawa, Aizaki, Ishiura, Saido, Maruyama (bib4) 2007; 352
Bourne, Taylor, Radic, Marchot (bib9) 2003; 22
Guardia-Laguarta, Pera, Clarimón, Molinuevo, Sánchez-Valle, Lladó, Coma, Gómez-Isla, Blesa, Ferrer, Lleó (bib25) 2009; 110
Massoulié (bib43) 2002; 11
Blennow, de Leon, Zetterberg (bib7) 2006; 368
Greenfield, Shaw (bib22) 1982; 7
Lleó, Saura (bib40) 2011; 11
Yu, Saura, Choi, Sun, Yang, Handler, Kawarabayashi, Younkin, Fedeles, Wilson, Younkin, Kandel, Kirkwood, Shen (bib73) 2001; 31
Appleyard, Vercher, Greenfield (bib3) 1988; 25
Wada, Morishima-Kawashima, Qi, Misono, Shimada, Ohno-Iwashita, Ihara (bib65) 2003; 42
Harris, Pereira, Parkin (bib27) 2009; 1296
Grimm, Tschäpe, Grimm, Zinser, Hartmann (bib23) 2006; 185
Hu, Gray, Brimijoin (bib34) 2009; 1
Haass, Kaether, Thinakaran, Sisodia (bib26) 2012; 2
Rochette, Murphy (bib52) 2002; 26
Maruyama, Tomita, Shinozaki, Kume, Asada, Saido, Ishiura, Iwatsubo, Obata (bib42) 1996; 227
Meshorer (10.1016/j.neurobiolaging.2014.01.147_bib44) 2004; 279
Parkin (10.1016/j.neurobiolaging.2014.01.147_bib46) 1999; 72
Appleyard (10.1016/j.neurobiolaging.2014.01.147_bib3) 1988; 25
Massoulié (10.1016/j.neurobiolaging.2014.01.147_bib43) 2002; 11
Hinz (10.1016/j.neurobiolaging.2014.01.147_bib33) 2004; 324
Saura (10.1016/j.neurobiolaging.2014.01.147_bib55) 2004; 42
Leung (10.1016/j.neurobiolaging.2014.01.147_bib38) 2009; 276
Wada (10.1016/j.neurobiolaging.2014.01.147_bib65) 2003; 42
Bourne (10.1016/j.neurobiolaging.2014.01.147_bib9) 2003; 22
Davies (10.1016/j.neurobiolaging.2014.01.147_bib14) 1976; 2
Schneider (10.1016/j.neurobiolaging.2014.01.147_bib56) 2012; 9
Hicks (10.1016/j.neurobiolaging.2014.01.147_bib30) 2011; 116
Guardia-Laguarta (10.1016/j.neurobiolaging.2014.01.147_bib25) 2009; 110
Cummings (10.1016/j.neurobiolaging.2014.01.147_bib13) 2004; 351
Silveyra (10.1016/j.neurobiolaging.2014.01.147_bib58) 2012; 33
Evin (10.1016/j.neurobiolaging.2014.01.147_bib17) 2001; 40
Appleyard (10.1016/j.neurobiolaging.2014.01.147_bib2) 1987; 11
Flores-Flores (10.1016/j.neurobiolaging.2014.01.147_bib19) 1996; 219
Perry (10.1016/j.neurobiolaging.2014.01.147_bib50) 1977; 1
Kaether (10.1016/j.neurobiolaging.2014.01.147_bib36) 2006; 3
Yang (10.1016/j.neurobiolaging.2014.01.147_bib72) 2002; 42
Lanz (10.1016/j.neurobiolaging.2014.01.147_bib37) 2003; 305
Parkin (10.1016/j.neurobiolaging.2014.01.147_bib47) 1997; 69
Sáez-Valero (10.1016/j.neurobiolaging.2014.01.147_bib53) 1999; 72
Small (10.1016/j.neurobiolaging.2014.01.147_bib59) 1996; 28
Dobbertin (10.1016/j.neurobiolaging.2014.01.147_bib15) 2009; 29
Yu (10.1016/j.neurobiolaging.2014.01.147_bib73) 2001; 31
Eckert (10.1016/j.neurobiolaging.2014.01.147_bib16) 2009; 382
Harris (10.1016/j.neurobiolaging.2014.01.147_bib27) 2009; 1296
Anglade (10.1016/j.neurobiolaging.2014.01.147_bib1) 1999; 37
Hu (10.1016/j.neurobiolaging.2014.01.147_bib34) 2009; 1
Xie (10.1016/j.neurobiolaging.2014.01.147_bib71) 2010; 187
Fishman (10.1016/j.neurobiolaging.2014.01.147_bib18) 1986; 19
Atack (10.1016/j.neurobiolaging.2014.01.147_bib5) 1983; 40
Bolte (10.1016/j.neurobiolaging.2014.01.147_bib8) 2006; 224
Lleó (10.1016/j.neurobiolaging.2014.01.147_bib40) 2011; 11
Wagner (10.1016/j.neurobiolaging.2014.01.147_bib66) 2012; 69
Huang (10.1016/j.neurobiolaging.2014.01.147_bib35) 2005; 4
Struhl (10.1016/j.neurobiolaging.2014.01.147_bib74) 2000; 6
Hicks (10.1016/j.neurobiolaging.2014.01.147_bib31) 2013; 203
Chen (10.1016/j.neurobiolaging.2014.01.147_bib12) 2011; 286
Perrier (10.1016/j.neurobiolaging.2014.01.147_bib49) 2003; 18
Greenfield (10.1016/j.neurobiolaging.2014.01.147_bib22) 1982; 7
Vetrivel (10.1016/j.neurobiolaging.2014.01.147_bib63) 2004; 279
Asai (10.1016/j.neurobiolaging.2014.01.147_bib4) 2007; 352
García-Marcos (10.1016/j.neurobiolaging.2014.01.147_bib20) 2006; 1758
Rochette (10.1016/j.neurobiolaging.2014.01.147_bib52) 2002; 26
Giacobini (10.1016/j.neurobiolaging.2014.01.147_bib21) 2003; 18
Grisaru (10.1016/j.neurobiolaging.2014.01.147_bib24) 1999; 264
Thinakaran (10.1016/j.neurobiolaging.2014.01.147_bib62) 2008; 283
Blennow (10.1016/j.neurobiolaging.2014.01.147_bib7) 2006; 368
Hicks (10.1016/j.neurobiolaging.2014.01.147_bib32) 2012; 3
Grimm (10.1016/j.neurobiolaging.2014.01.147_bib23) 2006; 185
Perrier (10.1016/j.neurobiolaging.2014.01.147_bib48) 2002; 33
Silveyra (10.1016/j.neurobiolaging.2014.01.147_bib57) 2008; 28
Volonte (10.1016/j.neurobiolaging.2014.01.147_bib64) 1999; 274
Noureddine (10.1016/j.neurobiolaging.2014.01.147_bib45) 2007; 282
Soreq (10.1016/j.neurobiolaging.2014.01.147_bib60) 2001; 2
Xie (10.1016/j.neurobiolaging.2014.01.147_bib70) 2010; 285
Berson (10.1016/j.neurobiolaging.2014.01.147_bib6) 2008; 131
Wolfe (10.1016/j.neurobiolaging.2014.01.147_bib68) 2008; 5
Manders (10.1016/j.neurobiolaging.2014.01.147_bib41) 1993; 169
Maruyama (10.1016/j.neurobiolaging.2014.01.147_bib42) 1996; 227
Capell (10.1016/j.neurobiolaging.2014.01.147_bib10) 2002; 277
Riddell (10.1016/j.neurobiolaging.2014.01.147_bib51) 2001; 11
Sáez-Valero (10.1016/j.neurobiolaging.2014.01.147_bib54) 1993; 35
Williamson (10.1016/j.neurobiolaging.2014.01.147_bib67) 2011; 8
Suzuki (10.1016/j.neurobiolaging.2014.01.147_bib61) 2012; 76
Lleó (10.1016/j.neurobiolaging.2014.01.147_bib39) 2007; 8
Henderson (10.1016/j.neurobiolaging.2014.01.147_bib29) 2012; 1344
Chan (10.1016/j.neurobiolaging.2014.01.147_bib11) 2012; 523
Haass (10.1016/j.neurobiolaging.2014.01.147_bib26) 2012; 2
Hattori (10.1016/j.neurobiolaging.2014.01.147_bib28) 2006; 84
Xia (10.1016/j.neurobiolaging.2014.01.147_bib69) 1997; 272
References_xml – volume: 276
  start-page: 3031
  year: 2009
  end-page: 3042
  ident: bib38
  article-title: Restricted localization of proline-rich membrane anchor (PRiMA) of globular form acetylcholinesterase at the neuromuscular junctions—contribution and expression from motor neurons
  publication-title: FEBS J.
– volume: 169
  start-page: 375
  year: 1993
  end-page: 382
  ident: bib41
  article-title: Measurement of co-localization of objects in dual-colour confocal images
  publication-title: J. Microsc.
– volume: 72
  start-page: 1600
  year: 1999
  end-page: 1608
  ident: bib53
  article-title: Molecular isoform distribution and glycosylation of acetylcholinesterase are altered in brain and cerebrospinal fluid of patients with Alzheimer's disease
  publication-title: J. Neurochem.
– volume: 1296
  start-page: 203
  year: 2009
  end-page: 215
  ident: bib27
  article-title: Targeting ADAM10 to lipid rafts in neuroblastoma SH-SY5Y cells impairs amyloidogenic processing of the amyloid precursor protein
  publication-title: Brain Res.
– volume: 187
  start-page: 78
  year: 2010
  end-page: 83
  ident: bib71
  article-title: PRiMA directs a restricted localization of tetrameric AChE at synapses
  publication-title: Chem. Biol. Interact
– volume: 37
  start-page: 243
  year: 1999
  end-page: 247
  ident: bib1
  article-title: Ultrastructural evidence for dendritic release of acetylcholinesterase in the rat substantia nigra
  publication-title: Folia Histochem. Cytobiol.
– volume: 324
  start-page: 621
  year: 2004
  end-page: 626
  ident: bib33
  article-title: R(+)-methanandamide-induced cyclooxygenase-2 expression in H4 human neuroglioma cells: possible involvement of membrane lipid rafts
  publication-title: Biochem. Biophys. Res. Commun.
– volume: 35
  start-page: 678
  year: 1993
  end-page: 689
  ident: bib54
  article-title: Amphiphilic and hydrophilic forms of acetyl- and butyrylcholinesterase in human brain
  publication-title: J. Neurosci. Res.
– volume: 286
  start-page: 32948
  year: 2011
  end-page: 32961
  ident: bib12
  article-title: The assembly of proline-rich membrane anchor (PRiMA)-linked acetylcholinesterase enzyme: glycosylation is required for enzymatic activity but not for oligomerization
  publication-title: J. Biol. Chem.
– volume: 18
  start-page: S1
  year: 2003
  end-page: S5
  ident: bib21
  article-title: Cholinergic function and Alzheimer's disease
  publication-title: Int. J. Geriatr. Psychiatry
– volume: 282
  start-page: 3487
  year: 2007
  end-page: 3497
  ident: bib45
  article-title: Assembly of acetylcholinesterase tetramers by peptidic motifs from the proline-rich membrane anchor, PRiMA: competition between degradation and secretion pathways of heteromeric complexes
  publication-title: J. Biol. Chem.
– volume: 1
  start-page: 189
  year: 1977
  ident: bib50
  article-title: Necropsy evidence of central cholinergic deficits in senile dementia
  publication-title: Lancet
– volume: 274
  start-page: 12702
  year: 1999
  end-page: 12709
  ident: bib64
  article-title: Flotillins/cavatellins are differentially expressed in cells and tissues and form a hetero-oligomeric complex with caveolins in vivo. Characterization and epitope-mapping of a novel flotillin-1 monoclonal antibody probe
  publication-title: J. Biol. Chem.
– volume: 40
  start-page: 8359
  year: 2001
  end-page: 8368
  ident: bib17
  article-title: Aspartyl protease inhibitor pepstatin binds to the presenilins of Alzheimer's disease
  publication-title: Biochemistry
– volume: 42
  start-page: 23
  year: 2004
  end-page: 36
  ident: bib55
  article-title: Loss of presenilin function causes impairments of memory and synaptic plasticity followed by age-dependent neurodegeneration
  publication-title: Neuron
– volume: 305
  start-page: 864
  year: 2003
  end-page: 871
  ident: bib37
  article-title: The gamma-secretase inhibitor N-[N-(3,5-difluorophenacetyl)-L-alanyl]-S-phenylglycine t-butyl ester reduces A beta levels in vivo in plasma and cerebrospinal fluid in young (plaque-free) and aged (plaque-bearing) Tg2576 mice
  publication-title: J. Pharmacol. Exp. Ther.
– volume: 4
  start-page: 140
  year: 2005
  end-page: 147
  ident: bib35
  article-title: Novel assay utilizing fluorochrome-tagged physostigmine (Ph-F) to in situ detect active acetylcholinesterase (AChE) induced during apoptosis
  publication-title: Cell Cycle
– volume: 351
  start-page: 56
  year: 2004
  end-page: 67
  ident: bib13
  article-title: Alzheimer's disease
  publication-title: N. Engl. J. Med.
– volume: 279
  start-page: 29740
  year: 2004
  end-page: 29751
  ident: bib44
  article-title: Combinatorial complexity of 5' alternative acetylcholinesterase transcripts and protein products
  publication-title: J. Biol. Chem.
– volume: 11
  start-page: 397
  year: 1987
  end-page: 406
  ident: bib2
  article-title: Spontaneous and carbachol-evoked in vivo secretion of acetylcholinesterase from the hippocampus of the rat
  publication-title: Neurochem. Int.
– volume: 272
  start-page: 7977
  year: 1997
  end-page: 7982
  ident: bib69
  article-title: Enhanced production and oligomerization of the 42-residue amyloid beta-protein by Chinese hamster ovary cells stably expressing mutant presenilins
  publication-title: J. Biol. Chem.
– volume: 203
  start-page: 302
  year: 2013
  end-page: 308
  ident: bib31
  article-title: Characterisation of acetylcholinesterase release from neuronal cells
  publication-title: Chem. Biol. Interact
– volume: 219
  start-page: 53
  year: 1996
  end-page: 58
  ident: bib19
  article-title: Conversion of acetylcholinesterase hydrophilic tetramers into amphiphilic dimers and monomers
  publication-title: Biochem. Biophys. Res. Commun.
– volume: 224
  start-page: 213
  year: 2006
  end-page: 232
  ident: bib8
  article-title: A guided tour into subcellular colocalization analysis in light microscopy
  publication-title: J. Microsc.
– volume: 69
  start-page: 2179
  year: 1997
  end-page: 2188
  ident: bib47
  article-title: The amyloid precursor protein is not enriched in caveolae-like, detergent-insoluble membrane microdomains
  publication-title: J. Neurochem.
– volume: 279
  start-page: 44945
  year: 2004
  end-page: 44954
  ident: bib63
  article-title: Association of gamma-secretase with lipid rafts in post-Golgi and endosome membranes
  publication-title: J. Biol. Chem.
– volume: 33
  start-page: 275
  year: 2002
  end-page: 285
  ident: bib48
  article-title: PRiMA: the membrane anchor of acetylcholinesterase in the brain
  publication-title: Neuron
– volume: 29
  start-page: 4519
  year: 2009
  end-page: 4530
  ident: bib15
  article-title: Targeting of acetylcholinesterase in neurons in vivo: a dual processing function for the proline-rich membrane anchor subunit and the attachment domain on the catalytic subunit
  publication-title: J. Neurosci.
– volume: 3
  start-page: 189
  year: 2012
  ident: bib32
  article-title: Lipid rafts and Alzheimer's disease: protein-lipid interactions and perturbation of signaling
  publication-title: Front. Physiol.
– volume: 283
  start-page: 29615
  year: 2008
  end-page: 29619
  ident: bib62
  article-title: Amyloid precursor protein trafficking, processing, and function
  publication-title: J. Biol. Chem.
– volume: 33
  start-page: 627.e27
  year: 2012
  end-page: 627.e37
  ident: bib58
  article-title: Changes in acetylcholinesterase expression are associated with altered presenilin-1 levels
  publication-title: Neurobiol. Aging
– volume: 2
  start-page: 1403
  year: 1976
  ident: bib14
  article-title: Selective loss of central cholinergic neurons in Alzheimer's disease
  publication-title: Lancet
– volume: 40
  start-page: 199
  year: 1983
  end-page: 204
  ident: bib5
  article-title: Molecular forms of acetylcholinesterase in senile dementia of Alzheimer type: selective loss of the intermediate (10S) form
  publication-title: Neurosci. Lett.
– volume: 264
  start-page: 672
  year: 1999
  end-page: 686
  ident: bib24
  article-title: Structural roles of acetylcholinesterase variants in biology and pathology
  publication-title: Eur. J. Biochem.
– volume: 18
  start-page: 1837
  year: 2003
  end-page: 1847
  ident: bib49
  article-title: Expression of PRiMA in the mouse brain: membrane anchoring and accumulation of 'tailed' acetylcholinesterase
  publication-title: Eur. J. Neurosci.
– volume: 22
  start-page: 1
  year: 2003
  end-page: 12
  ident: bib9
  article-title: Structural insights into ligand interactions at the acetylcholinesterase peripheral anionic site
  publication-title: EMBO J.
– volume: 28
  start-page: 2908
  year: 2008
  end-page: 2919
  ident: bib57
  article-title: Presenilin 1 interacts with acetylcholinesterase and alters its enzymatic activity and glycosylation
  publication-title: Mol. Cell. Biol.
– volume: 6
  start-page: 625
  year: 2000
  end-page: 636
  ident: bib74
  article-title: Requirements for presenilin-dependent cleavage of notch and other transmembrane proteins
  publication-title: Mol. Cell.
– volume: 69
  start-page: 1255
  year: 2012
  end-page: 1258
  ident: bib66
  article-title: Potential use of γ-secretase modulators in the treatment of Alzheimer disease
  publication-title: Arch. Neurol.
– volume: 42
  start-page: 261
  year: 2002
  end-page: 268
  ident: bib72
  article-title: Increased expression of intranuclear AChE involved in apoptosis of SK-N-SH cells
  publication-title: Neurosci. Res.
– volume: 28
  start-page: 453
  year: 1996
  end-page: 483
  ident: bib59
  article-title: Non-classical actions of cholinesterases: role in cellular differentiation, tumorigenesis and Alzheimer's disease
  publication-title: Neurochem. Int.
– volume: 42
  start-page: 13977
  year: 2003
  end-page: 13986
  ident: bib65
  article-title: Gamma-secretase activity is present in rafts but is not cholesterol-dependent
  publication-title: Biochemistry
– volume: 2
  start-page: a006270
  year: 2012
  ident: bib26
  article-title: Trafficking and proteolytic processing of APP
  publication-title: Cold Spring Harb. Perspect. Med.
– volume: 9
  start-page: 671
  year: 2012
  end-page: 675
  ident: bib56
  article-title: NIH Image to ImageJ: 25 years of image analysis
  publication-title: Nat. Methods
– volume: 26
  start-page: 81
  year: 2002
  end-page: 95
  ident: bib52
  article-title: Gamma-secretase: substrates and inhibitors
  publication-title: Mol. Neurobiol.
– volume: 382
  start-page: 673
  year: 2009
  end-page: 677
  ident: bib16
  article-title: Presenilin 1 modifies lipid raft composition of neuronal membranes
  publication-title: Biochem. Biophys. Res. Commun.
– volume: 352
  start-page: 498
  year: 2007
  end-page: 502
  ident: bib4
  article-title: Berberine alters the processing of Alzheimer's amyloid precursor protein to decrease Abeta secretion
  publication-title: Biochem. Biophys. Res. Commun.
– volume: 1758
  start-page: 796
  year: 2006
  end-page: 806
  ident: bib20
  article-title: Characterization and comparison of raft-like membranes isolated by two different methods from rat submandibular gland cells
  publication-title: Biochim. Biophys. Acta
– volume: 131
  start-page: 109
  year: 2008
  end-page: 119
  ident: bib6
  article-title: Changes in readthrough acetylcholinesterase expression modulate amyloid-beta pathology
  publication-title: Brain
– volume: 7
  start-page: 2883
  year: 1982
  end-page: 2893
  ident: bib22
  article-title: Release of acetylcholinesterase and aminopeptidase in vivo following infusion of amphetamine into the substantia nigra
  publication-title: Neuroscience
– volume: 84
  start-page: 912
  year: 2006
  end-page: 917
  ident: bib28
  article-title: BACE1 interacts with lipid raft proteins
  publication-title: J. Neurosci. Res.
– volume: 1344
  start-page: 34
  year: 2012
  end-page: 42
  ident: bib29
  article-title: Co-localization of PRiMA with acetylcholinesterase in cholinergic neurons of rat brain: an immunocytochemical study
  publication-title: Brain Res.
– volume: 11
  start-page: 1288
  year: 2001
  end-page: 1293
  ident: bib51
  article-title: Compartmentalization of beta-secretase (Asp2) into low-buoyant density, noncaveolar lipid rafts
  publication-title: Curr. Biol.
– volume: 2
  start-page: 294
  year: 2001
  end-page: 302
  ident: bib60
  article-title: Acetylcholinesterase—new roles for an old actor
  publication-title: Nat. Rev. Neurosci.
– volume: 523
  start-page: 71
  year: 2012
  end-page: 75
  ident: bib11
  article-title: N-linked glycosylation of proline-rich membrane anchor (PRiMA) is not required for assembly and trafficking of globular tetrameric acetylcholinesterase
  publication-title: Neurosci. Lett.
– volume: 110
  start-page: 220
  year: 2009
  end-page: 230
  ident: bib25
  article-title: Mild cholesterol depletion reduces amyloid-beta production by impairing APP trafficking to the cell surface
  publication-title: J. Neurochem.
– volume: 11
  start-page: 130
  year: 2002
  end-page: 143
  ident: bib43
  article-title: The origin of the molecular diversity and functional anchoring of cholinesterases
  publication-title: Neurosignals
– volume: 25
  start-page: 133
  year: 1988
  end-page: 138
  ident: bib3
  article-title: Release of acetylcholinesterase from the guinea-pig cerebellum in vivo
  publication-title: Neuroscience
– volume: 1
  start-page: 15
  year: 2009
  end-page: 24
  ident: bib34
  article-title: Amyloid-beta alters trafficking of internalized acetylcholinesterase and dextran
  publication-title: Int. J. Physiol. Pathophysiol. Pharmacol.
– volume: 3
  start-page: 275
  year: 2006
  end-page: 283
  ident: bib36
  article-title: Assembly, trafficking and function of gamma-secretase
  publication-title: Neurodegener. Dis.
– volume: 8
  start-page: 550
  year: 2007
  end-page: 558
  ident: bib39
  article-title: Current therapeutic options for Alzheimer's disease
  publication-title: Curr. Genomics
– volume: 72
  start-page: 1534
  year: 1999
  end-page: 1543
  ident: bib46
  article-title: Characterization of detergent-insoluble complexes containing the familial Alzheimer's disease-associated presenilins
  publication-title: J. Neurochem.
– volume: 11
  start-page: 1513
  year: 2011
  end-page: 1527
  ident: bib40
  article-title: γ-Secretase substrates and their implications for drug development in Alzheimer's disease
  publication-title: Curr. Top. Med. Chem.
– volume: 31
  start-page: 713
  year: 2001
  end-page: 726
  ident: bib73
  article-title: APP processing and synaptic plasticity in presenilin-1 conditional knockout mice
  publication-title: Neuron
– volume: 277
  start-page: 5637
  year: 2002
  end-page: 5643
  ident: bib10
  article-title: Apical sorting of beta-secretase limits amyloid beta-peptide production
  publication-title: J. Biol. Chem.
– volume: 227
  start-page: 730
  year: 1996
  end-page: 735
  ident: bib42
  article-title: Familial Alzheimer's disease-linked mutations at Val717 of amyloid precursor protein are specific for the increased secretion of A beta 42(43)
  publication-title: Biochem. Biophys. Res. Commun.
– volume: 5
  start-page: 158
  year: 2008
  end-page: 164
  ident: bib68
  article-title: Gamma-secretase inhibition and modulation for Alzheimer's disease
  publication-title: Curr. Alzheimer Res.
– volume: 19
  start-page: 246
  year: 1986
  end-page: 252
  ident: bib18
  article-title: Distribution of the molecular forms of acetylcholinesterase in human brain: alterations in dementia of the Alzheimer type
  publication-title: Ann. Neurol.
– volume: 8
  start-page: 213
  year: 2011
  end-page: 221
  ident: bib67
  article-title: Neuronal membranes are key to the pathogenesis of Alzheimer's disease: the role of both raft and non-raft membrane domains
  publication-title: Curr. Alzheimer Res.
– volume: 76
  start-page: 410
  year: 2012
  end-page: 422
  ident: bib61
  article-title: Activity-dependent proteolytic cleavage of neuroligin-1
  publication-title: Neuron
– volume: 368
  start-page: 387
  year: 2006
  end-page: 403
  ident: bib7
  article-title: Alzheimer's disease
  publication-title: Lancet
– volume: 185
  start-page: 27
  year: 2006
  end-page: 32
  ident: bib23
  article-title: Altered membrane fluidity and lipid raft composition in presenilin-deficient cells
  publication-title: Acta Neurol. Scand. Suppl.
– volume: 116
  start-page: 742
  year: 2011
  end-page: 746
  ident: bib30
  article-title: Membrane targeting, shedding and protein interactions of brain acetylcholinesterase
  publication-title: J. Neurochem.
– volume: 285
  start-page: 11537
  year: 2010
  end-page: 11546
  ident: bib70
  article-title: Targeting acetylcholinesterase to membrane rafts: a function mediated by the proline-rich membrane anchor (PRiMA) in neurons
  publication-title: J. Biol. Chem.
– volume: 11
  start-page: 1288
  year: 2001
  ident: 10.1016/j.neurobiolaging.2014.01.147_bib51
  article-title: Compartmentalization of beta-secretase (Asp2) into low-buoyant density, noncaveolar lipid rafts
  publication-title: Curr. Biol.
  doi: 10.1016/S0960-9822(01)00394-3
– volume: 9
  start-page: 671
  year: 2012
  ident: 10.1016/j.neurobiolaging.2014.01.147_bib56
  article-title: NIH Image to ImageJ: 25 years of image analysis
  publication-title: Nat. Methods
  doi: 10.1038/nmeth.2089
– volume: 351
  start-page: 56
  year: 2004
  ident: 10.1016/j.neurobiolaging.2014.01.147_bib13
  article-title: Alzheimer's disease
  publication-title: N. Engl. J. Med.
  doi: 10.1056/NEJMra040223
– volume: 279
  start-page: 29740
  year: 2004
  ident: 10.1016/j.neurobiolaging.2014.01.147_bib44
  article-title: Combinatorial complexity of 5' alternative acetylcholinesterase transcripts and protein products
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M402752200
– volume: 19
  start-page: 246
  year: 1986
  ident: 10.1016/j.neurobiolaging.2014.01.147_bib18
  article-title: Distribution of the molecular forms of acetylcholinesterase in human brain: alterations in dementia of the Alzheimer type
  publication-title: Ann. Neurol.
  doi: 10.1002/ana.410190305
– volume: 169
  start-page: 375
  year: 1993
  ident: 10.1016/j.neurobiolaging.2014.01.147_bib41
  article-title: Measurement of co-localization of objects in dual-colour confocal images
  publication-title: J. Microsc.
  doi: 10.1111/j.1365-2818.1993.tb03313.x
– volume: 282
  start-page: 3487
  year: 2007
  ident: 10.1016/j.neurobiolaging.2014.01.147_bib45
  article-title: Assembly of acetylcholinesterase tetramers by peptidic motifs from the proline-rich membrane anchor, PRiMA: competition between degradation and secretion pathways of heteromeric complexes
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M607221200
– volume: 224
  start-page: 213
  year: 2006
  ident: 10.1016/j.neurobiolaging.2014.01.147_bib8
  article-title: A guided tour into subcellular colocalization analysis in light microscopy
  publication-title: J. Microsc.
  doi: 10.1111/j.1365-2818.2006.01706.x
– volume: 40
  start-page: 8359
  year: 2001
  ident: 10.1016/j.neurobiolaging.2014.01.147_bib17
  article-title: Aspartyl protease inhibitor pepstatin binds to the presenilins of Alzheimer's disease
  publication-title: Biochemistry
  doi: 10.1021/bi002770t
– volume: 22
  start-page: 1
  year: 2003
  ident: 10.1016/j.neurobiolaging.2014.01.147_bib9
  article-title: Structural insights into ligand interactions at the acetylcholinesterase peripheral anionic site
  publication-title: EMBO J.
  doi: 10.1093/emboj/cdg005
– volume: 3
  start-page: 275
  year: 2006
  ident: 10.1016/j.neurobiolaging.2014.01.147_bib36
  article-title: Assembly, trafficking and function of gamma-secretase
  publication-title: Neurodegener. Dis.
  doi: 10.1159/000095267
– volume: 279
  start-page: 44945
  year: 2004
  ident: 10.1016/j.neurobiolaging.2014.01.147_bib63
  article-title: Association of gamma-secretase with lipid rafts in post-Golgi and endosome membranes
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M407986200
– volume: 4
  start-page: 140
  year: 2005
  ident: 10.1016/j.neurobiolaging.2014.01.147_bib35
  article-title: Novel assay utilizing fluorochrome-tagged physostigmine (Ph-F) to in situ detect active acetylcholinesterase (AChE) induced during apoptosis
  publication-title: Cell Cycle
  doi: 10.4161/cc.4.1.1322
– volume: 42
  start-page: 13977
  year: 2003
  ident: 10.1016/j.neurobiolaging.2014.01.147_bib65
  article-title: Gamma-secretase activity is present in rafts but is not cholesterol-dependent
  publication-title: Biochemistry
  doi: 10.1021/bi034904j
– volume: 5
  start-page: 158
  year: 2008
  ident: 10.1016/j.neurobiolaging.2014.01.147_bib68
  article-title: Gamma-secretase inhibition and modulation for Alzheimer's disease
  publication-title: Curr. Alzheimer Res.
  doi: 10.2174/156720508783954767
– volume: 382
  start-page: 673
  year: 2009
  ident: 10.1016/j.neurobiolaging.2014.01.147_bib16
  article-title: Presenilin 1 modifies lipid raft composition of neuronal membranes
  publication-title: Biochem. Biophys. Res. Commun.
  doi: 10.1016/j.bbrc.2009.03.070
– volume: 110
  start-page: 220
  year: 2009
  ident: 10.1016/j.neurobiolaging.2014.01.147_bib25
  article-title: Mild cholesterol depletion reduces amyloid-beta production by impairing APP trafficking to the cell surface
  publication-title: J. Neurochem.
  doi: 10.1111/j.1471-4159.2009.06126.x
– volume: 25
  start-page: 133
  year: 1988
  ident: 10.1016/j.neurobiolaging.2014.01.147_bib3
  article-title: Release of acetylcholinesterase from the guinea-pig cerebellum in vivo
  publication-title: Neuroscience
  doi: 10.1016/0306-4522(88)90012-7
– volume: 352
  start-page: 498
  year: 2007
  ident: 10.1016/j.neurobiolaging.2014.01.147_bib4
  article-title: Berberine alters the processing of Alzheimer's amyloid precursor protein to decrease Abeta secretion
  publication-title: Biochem. Biophys. Res. Commun.
  doi: 10.1016/j.bbrc.2006.11.043
– volume: 324
  start-page: 621
  year: 2004
  ident: 10.1016/j.neurobiolaging.2014.01.147_bib33
  article-title: R(+)-methanandamide-induced cyclooxygenase-2 expression in H4 human neuroglioma cells: possible involvement of membrane lipid rafts
  publication-title: Biochem. Biophys. Res. Commun.
  doi: 10.1016/j.bbrc.2004.09.095
– volume: 6
  start-page: 625
  year: 2000
  ident: 10.1016/j.neurobiolaging.2014.01.147_bib74
  article-title: Requirements for presenilin-dependent cleavage of notch and other transmembrane proteins
  publication-title: Mol. Cell.
  doi: 10.1016/S1097-2765(00)00061-7
– volume: 276
  start-page: 3031
  year: 2009
  ident: 10.1016/j.neurobiolaging.2014.01.147_bib38
  article-title: Restricted localization of proline-rich membrane anchor (PRiMA) of globular form acetylcholinesterase at the neuromuscular junctions—contribution and expression from motor neurons
  publication-title: FEBS J.
  doi: 10.1111/j.1742-4658.2009.07022.x
– volume: 2
  start-page: 1403
  year: 1976
  ident: 10.1016/j.neurobiolaging.2014.01.147_bib14
  article-title: Selective loss of central cholinergic neurons in Alzheimer's disease
  publication-title: Lancet
  doi: 10.1016/S0140-6736(76)91936-X
– volume: 18
  start-page: 1837
  year: 2003
  ident: 10.1016/j.neurobiolaging.2014.01.147_bib49
  article-title: Expression of PRiMA in the mouse brain: membrane anchoring and accumulation of 'tailed' acetylcholinesterase
  publication-title: Eur. J. Neurosci.
  doi: 10.1046/j.1460-9568.2003.02914.x
– volume: 2
  start-page: 294
  year: 2001
  ident: 10.1016/j.neurobiolaging.2014.01.147_bib60
  article-title: Acetylcholinesterase—new roles for an old actor
  publication-title: Nat. Rev. Neurosci.
  doi: 10.1038/35067589
– volume: 29
  start-page: 4519
  year: 2009
  ident: 10.1016/j.neurobiolaging.2014.01.147_bib15
  article-title: Targeting of acetylcholinesterase in neurons in vivo: a dual processing function for the proline-rich membrane anchor subunit and the attachment domain on the catalytic subunit
  publication-title: J. Neurosci.
  doi: 10.1523/JNEUROSCI.3863-08.2009
– volume: 523
  start-page: 71
  year: 2012
  ident: 10.1016/j.neurobiolaging.2014.01.147_bib11
  article-title: N-linked glycosylation of proline-rich membrane anchor (PRiMA) is not required for assembly and trafficking of globular tetrameric acetylcholinesterase
  publication-title: Neurosci. Lett.
  doi: 10.1016/j.neulet.2012.06.045
– volume: 227
  start-page: 730
  year: 1996
  ident: 10.1016/j.neurobiolaging.2014.01.147_bib42
  article-title: Familial Alzheimer's disease-linked mutations at Val717 of amyloid precursor protein are specific for the increased secretion of A beta 42(43)
  publication-title: Biochem. Biophys. Res. Commun.
  doi: 10.1006/bbrc.1996.1577
– volume: 84
  start-page: 912
  year: 2006
  ident: 10.1016/j.neurobiolaging.2014.01.147_bib28
  article-title: BACE1 interacts with lipid raft proteins
  publication-title: J. Neurosci. Res.
  doi: 10.1002/jnr.20981
– volume: 42
  start-page: 261
  year: 2002
  ident: 10.1016/j.neurobiolaging.2014.01.147_bib72
  article-title: Increased expression of intranuclear AChE involved in apoptosis of SK-N-SH cells
  publication-title: Neurosci. Res.
  doi: 10.1016/S0168-0102(02)00005-6
– volume: 11
  start-page: 1513
  year: 2011
  ident: 10.1016/j.neurobiolaging.2014.01.147_bib40
  article-title: γ-Secretase substrates and their implications for drug development in Alzheimer's disease
  publication-title: Curr. Top. Med. Chem.
  doi: 10.2174/156802611795861004
– volume: 285
  start-page: 11537
  year: 2010
  ident: 10.1016/j.neurobiolaging.2014.01.147_bib70
  article-title: Targeting acetylcholinesterase to membrane rafts: a function mediated by the proline-rich membrane anchor (PRiMA) in neurons
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M109.038711
– volume: 26
  start-page: 81
  year: 2002
  ident: 10.1016/j.neurobiolaging.2014.01.147_bib52
  article-title: Gamma-secretase: substrates and inhibitors
  publication-title: Mol. Neurobiol.
  doi: 10.1385/MN:26:1:081
– volume: 37
  start-page: 243
  year: 1999
  ident: 10.1016/j.neurobiolaging.2014.01.147_bib1
  article-title: Ultrastructural evidence for dendritic release of acetylcholinesterase in the rat substantia nigra
  publication-title: Folia Histochem. Cytobiol.
– volume: 28
  start-page: 453
  year: 1996
  ident: 10.1016/j.neurobiolaging.2014.01.147_bib59
  article-title: Non-classical actions of cholinesterases: role in cellular differentiation, tumorigenesis and Alzheimer's disease
  publication-title: Neurochem. Int.
  doi: 10.1016/0197-0186(95)00099-2
– volume: 11
  start-page: 397
  year: 1987
  ident: 10.1016/j.neurobiolaging.2014.01.147_bib2
  article-title: Spontaneous and carbachol-evoked in vivo secretion of acetylcholinesterase from the hippocampus of the rat
  publication-title: Neurochem. Int.
  doi: 10.1016/0197-0186(87)90029-5
– volume: 116
  start-page: 742
  year: 2011
  ident: 10.1016/j.neurobiolaging.2014.01.147_bib30
  article-title: Membrane targeting, shedding and protein interactions of brain acetylcholinesterase
  publication-title: J. Neurochem.
  doi: 10.1111/j.1471-4159.2010.07032.x
– volume: 28
  start-page: 2908
  year: 2008
  ident: 10.1016/j.neurobiolaging.2014.01.147_bib57
  article-title: Presenilin 1 interacts with acetylcholinesterase and alters its enzymatic activity and glycosylation
  publication-title: Mol. Cell. Biol.
  doi: 10.1128/MCB.02065-07
– volume: 2
  start-page: a006270
  year: 2012
  ident: 10.1016/j.neurobiolaging.2014.01.147_bib26
  article-title: Trafficking and proteolytic processing of APP
  publication-title: Cold Spring Harb. Perspect. Med.
  doi: 10.1101/cshperspect.a006270
– volume: 3
  start-page: 189
  year: 2012
  ident: 10.1016/j.neurobiolaging.2014.01.147_bib32
  article-title: Lipid rafts and Alzheimer's disease: protein-lipid interactions and perturbation of signaling
  publication-title: Front. Physiol.
  doi: 10.3389/fphys.2012.00189
– volume: 72
  start-page: 1600
  year: 1999
  ident: 10.1016/j.neurobiolaging.2014.01.147_bib53
  article-title: Molecular isoform distribution and glycosylation of acetylcholinesterase are altered in brain and cerebrospinal fluid of patients with Alzheimer's disease
  publication-title: J. Neurochem.
  doi: 10.1046/j.1471-4159.1999.721600.x
– volume: 1296
  start-page: 203
  year: 2009
  ident: 10.1016/j.neurobiolaging.2014.01.147_bib27
  article-title: Targeting ADAM10 to lipid rafts in neuroblastoma SH-SY5Y cells impairs amyloidogenic processing of the amyloid precursor protein
  publication-title: Brain Res.
  doi: 10.1016/j.brainres.2009.07.105
– volume: 1758
  start-page: 796
  year: 2006
  ident: 10.1016/j.neurobiolaging.2014.01.147_bib20
  article-title: Characterization and comparison of raft-like membranes isolated by two different methods from rat submandibular gland cells
  publication-title: Biochim. Biophys. Acta
  doi: 10.1016/j.bbamem.2006.05.008
– volume: 1
  start-page: 189
  year: 1977
  ident: 10.1016/j.neurobiolaging.2014.01.147_bib50
  article-title: Necropsy evidence of central cholinergic deficits in senile dementia
  publication-title: Lancet
  doi: 10.1016/S0140-6736(77)91780-9
– volume: 42
  start-page: 23
  year: 2004
  ident: 10.1016/j.neurobiolaging.2014.01.147_bib55
  article-title: Loss of presenilin function causes impairments of memory and synaptic plasticity followed by age-dependent neurodegeneration
  publication-title: Neuron
  doi: 10.1016/S0896-6273(04)00182-5
– volume: 305
  start-page: 864
  year: 2003
  ident: 10.1016/j.neurobiolaging.2014.01.147_bib37
  article-title: The gamma-secretase inhibitor N-[N-(3,5-difluorophenacetyl)-L-alanyl]-S-phenylglycine t-butyl ester reduces A beta levels in vivo in plasma and cerebrospinal fluid in young (plaque-free) and aged (plaque-bearing) Tg2576 mice
  publication-title: J. Pharmacol. Exp. Ther.
  doi: 10.1124/jpet.102.048280
– volume: 264
  start-page: 672
  year: 1999
  ident: 10.1016/j.neurobiolaging.2014.01.147_bib24
  article-title: Structural roles of acetylcholinesterase variants in biology and pathology
  publication-title: Eur. J. Biochem.
  doi: 10.1046/j.1432-1327.1999.00693.x
– volume: 8
  start-page: 213
  year: 2011
  ident: 10.1016/j.neurobiolaging.2014.01.147_bib67
  article-title: Neuronal membranes are key to the pathogenesis of Alzheimer's disease: the role of both raft and non-raft membrane domains
  publication-title: Curr. Alzheimer Res.
  doi: 10.2174/156720511795256008
– volume: 18
  start-page: S1
  year: 2003
  ident: 10.1016/j.neurobiolaging.2014.01.147_bib21
  article-title: Cholinergic function and Alzheimer's disease
  publication-title: Int. J. Geriatr. Psychiatry
  doi: 10.1002/gps.935
– volume: 7
  start-page: 2883
  year: 1982
  ident: 10.1016/j.neurobiolaging.2014.01.147_bib22
  article-title: Release of acetylcholinesterase and aminopeptidase in vivo following infusion of amphetamine into the substantia nigra
  publication-title: Neuroscience
  doi: 10.1016/0306-4522(82)90111-7
– volume: 185
  start-page: 27
  year: 2006
  ident: 10.1016/j.neurobiolaging.2014.01.147_bib23
  article-title: Altered membrane fluidity and lipid raft composition in presenilin-deficient cells
  publication-title: Acta Neurol. Scand. Suppl.
  doi: 10.1111/j.1600-0404.2006.00682.x
– volume: 40
  start-page: 199
  year: 1983
  ident: 10.1016/j.neurobiolaging.2014.01.147_bib5
  article-title: Molecular forms of acetylcholinesterase in senile dementia of Alzheimer type: selective loss of the intermediate (10S) form
  publication-title: Neurosci. Lett.
  doi: 10.1016/0304-3940(83)90302-6
– volume: 272
  start-page: 7977
  year: 1997
  ident: 10.1016/j.neurobiolaging.2014.01.147_bib69
  article-title: Enhanced production and oligomerization of the 42-residue amyloid beta-protein by Chinese hamster ovary cells stably expressing mutant presenilins
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.272.12.7977
– volume: 203
  start-page: 302
  year: 2013
  ident: 10.1016/j.neurobiolaging.2014.01.147_bib31
  article-title: Characterisation of acetylcholinesterase release from neuronal cells
  publication-title: Chem. Biol. Interact
  doi: 10.1016/j.cbi.2012.09.019
– volume: 72
  start-page: 1534
  year: 1999
  ident: 10.1016/j.neurobiolaging.2014.01.147_bib46
  article-title: Characterization of detergent-insoluble complexes containing the familial Alzheimer's disease-associated presenilins
  publication-title: J. Neurochem.
  doi: 10.1046/j.1471-4159.1999.721534.x
– volume: 76
  start-page: 410
  year: 2012
  ident: 10.1016/j.neurobiolaging.2014.01.147_bib61
  article-title: Activity-dependent proteolytic cleavage of neuroligin-1
  publication-title: Neuron
  doi: 10.1016/j.neuron.2012.10.003
– volume: 274
  start-page: 12702
  year: 1999
  ident: 10.1016/j.neurobiolaging.2014.01.147_bib64
  article-title: Flotillins/cavatellins are differentially expressed in cells and tissues and form a hetero-oligomeric complex with caveolins in vivo. Characterization and epitope-mapping of a novel flotillin-1 monoclonal antibody probe
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.274.18.12702
– volume: 31
  start-page: 713
  year: 2001
  ident: 10.1016/j.neurobiolaging.2014.01.147_bib73
  article-title: APP processing and synaptic plasticity in presenilin-1 conditional knockout mice
  publication-title: Neuron
  doi: 10.1016/S0896-6273(01)00417-2
– volume: 69
  start-page: 2179
  year: 1997
  ident: 10.1016/j.neurobiolaging.2014.01.147_bib47
  article-title: The amyloid precursor protein is not enriched in caveolae-like, detergent-insoluble membrane microdomains
  publication-title: J. Neurochem.
  doi: 10.1046/j.1471-4159.1997.69052179.x
– volume: 219
  start-page: 53
  year: 1996
  ident: 10.1016/j.neurobiolaging.2014.01.147_bib19
  article-title: Conversion of acetylcholinesterase hydrophilic tetramers into amphiphilic dimers and monomers
  publication-title: Biochem. Biophys. Res. Commun.
  doi: 10.1006/bbrc.1996.0180
– volume: 131
  start-page: 109
  year: 2008
  ident: 10.1016/j.neurobiolaging.2014.01.147_bib6
  article-title: Changes in readthrough acetylcholinesterase expression modulate amyloid-beta pathology
  publication-title: Brain
  doi: 10.1093/brain/awm276
– volume: 1344
  start-page: 34
  year: 2012
  ident: 10.1016/j.neurobiolaging.2014.01.147_bib29
  article-title: Co-localization of PRiMA with acetylcholinesterase in cholinergic neurons of rat brain: an immunocytochemical study
  publication-title: Brain Res.
  doi: 10.1016/j.brainres.2010.05.022
– volume: 187
  start-page: 78
  year: 2010
  ident: 10.1016/j.neurobiolaging.2014.01.147_bib71
  article-title: PRiMA directs a restricted localization of tetrameric AChE at synapses
  publication-title: Chem. Biol. Interact
  doi: 10.1016/j.cbi.2010.02.018
– volume: 277
  start-page: 5637
  year: 2002
  ident: 10.1016/j.neurobiolaging.2014.01.147_bib10
  article-title: Apical sorting of beta-secretase limits amyloid beta-peptide production
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M109119200
– volume: 1
  start-page: 15
  year: 2009
  ident: 10.1016/j.neurobiolaging.2014.01.147_bib34
  article-title: Amyloid-beta alters trafficking of internalized acetylcholinesterase and dextran
  publication-title: Int. J. Physiol. Pathophysiol. Pharmacol.
– volume: 11
  start-page: 130
  year: 2002
  ident: 10.1016/j.neurobiolaging.2014.01.147_bib43
  article-title: The origin of the molecular diversity and functional anchoring of cholinesterases
  publication-title: Neurosignals
  doi: 10.1159/000065054
– volume: 33
  start-page: 275
  year: 2002
  ident: 10.1016/j.neurobiolaging.2014.01.147_bib48
  article-title: PRiMA: the membrane anchor of acetylcholinesterase in the brain
  publication-title: Neuron
  doi: 10.1016/S0896-6273(01)00584-0
– volume: 69
  start-page: 1255
  year: 2012
  ident: 10.1016/j.neurobiolaging.2014.01.147_bib66
  article-title: Potential use of γ-secretase modulators in the treatment of Alzheimer disease
  publication-title: Arch. Neurol.
  doi: 10.1001/archneurol.2012.540
– volume: 283
  start-page: 29615
  year: 2008
  ident: 10.1016/j.neurobiolaging.2014.01.147_bib62
  article-title: Amyloid precursor protein trafficking, processing, and function
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.R800019200
– volume: 8
  start-page: 550
  year: 2007
  ident: 10.1016/j.neurobiolaging.2014.01.147_bib39
  article-title: Current therapeutic options for Alzheimer's disease
  publication-title: Curr. Genomics
  doi: 10.2174/138920207783769549
– volume: 33
  start-page: 627.e27
  year: 2012
  ident: 10.1016/j.neurobiolaging.2014.01.147_bib58
  article-title: Changes in acetylcholinesterase expression are associated with altered presenilin-1 levels
  publication-title: Neurobiol. Aging
  doi: 10.1016/j.neurobiolaging.2011.04.006
– volume: 286
  start-page: 32948
  year: 2011
  ident: 10.1016/j.neurobiolaging.2014.01.147_bib12
  article-title: The assembly of proline-rich membrane anchor (PRiMA)-linked acetylcholinesterase enzyme: glycosylation is required for enzymatic activity but not for oligomerization
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M111.261248
– volume: 35
  start-page: 678
  year: 1993
  ident: 10.1016/j.neurobiolaging.2014.01.147_bib54
  article-title: Amphiphilic and hydrophilic forms of acetyl- and butyrylcholinesterase in human brain
  publication-title: J. Neurosci. Res.
  doi: 10.1002/jnr.490350610
– volume: 368
  start-page: 387
  year: 2006
  ident: 10.1016/j.neurobiolaging.2014.01.147_bib7
  article-title: Alzheimer's disease
  publication-title: Lancet
  doi: 10.1016/S0140-6736(06)69113-7
SSID ssj0007476
Score 2.163552
Snippet Presenilin-1 (PS1) is the catalytic component of the γ-secretase complex. In this study, we explore if PS1 participates in the processing of the cholinergic...
Abstract Presenilin-1 (PS1) is the catalytic component of the γ-secretase complex. In this study, we explore if PS1 participates in the processing of the...
Presenilin-1 (PS1) is the catalytic component of the gamma -secretase complex. In this study, we explore if PS1 participates in the processing of the...
SourceID proquest
pubmed
crossref
elsevier
SourceType Aggregation Database
Index Database
Enrichment Source
Publisher
StartPage 1526
SubjectTerms Acetylcholinesterase
Acetylcholinesterase - metabolism
Acetylcholinesterase - physiology
Acetylcholinesterase - therapeutic use
Alzheimer Disease - drug therapy
Alzheimer Disease - etiology
Alzheimer's disease
Amyloid Precursor Protein Secretases - physiology
Amyloid Precursor Protein Secretases - therapeutic use
Animals
Brain - enzymology
Brain - metabolism
Cell Nucleus - enzymology
Cells, Cultured
Cricetinae
Drug Design
Female
Gene Expression - genetics
Internal Medicine
Membrane Microdomains - metabolism
Membrane Proteins - genetics
Membrane Proteins - metabolism
Mice
Mice, Knockout
Molecular Targeted Therapy
Nerve Tissue Proteins - genetics
Nerve Tissue Proteins - metabolism
Neurology
Presenilin 1
Presenilin-1 - physiology
PRiMA
γ-Secretase
Title Presenilin-1 influences processing of the acetylcholinesterase membrane anchor PRiMA
URI https://www.clinicalkey.com/#!/content/1-s2.0-S0197458014001699
https://www.clinicalkey.es/playcontent/1-s2.0-S0197458014001699
https://www.ncbi.nlm.nih.gov/pubmed/24612677
https://www.proquest.com/docview/1514435630
https://www.proquest.com/docview/1534815037
Volume 35
hasFullText 1
inHoldings 1
isFullTextHit
isPrint
journalDatabaseRights – providerCode: PRVESC
  databaseName: Baden-Württemberg Complete Freedom Collection (Elsevier)
  customDbUrl:
  eissn: 1558-1497
  dateEnd: 99991231
  omitProxy: true
  ssIdentifier: ssj0007476
  issn: 0197-4580
  databaseCode: GBLVA
  dateStart: 20110101
  isFulltext: true
  titleUrlDefault: https://www.sciencedirect.com
  providerName: Elsevier
– providerCode: PRVESC
  databaseName: Elsevier SD Complete Freedom Collection (subscription)
  customDbUrl:
  eissn: 1558-1497
  dateEnd: 99991231
  omitProxy: true
  ssIdentifier: ssj0007476
  issn: 0197-4580
  databaseCode: ACRLP
  dateStart: 19950101
  isFulltext: true
  titleUrlDefault: https://www.sciencedirect.com
  providerName: Elsevier
– providerCode: PRVESC
  databaseName: ScienceDirect Freedom Collection 2013
  customDbUrl:
  eissn: 1558-1497
  dateEnd: 99991231
  omitProxy: true
  ssIdentifier: ssj0007476
  issn: 0197-4580
  databaseCode: .~1
  dateStart: 19950101
  isFulltext: true
  titleUrlDefault: https://www.sciencedirect.com
  providerName: Elsevier
– providerCode: PRVESC
  databaseName: ScienceDirect Freedom Collection Journals
  customDbUrl:
  eissn: 1558-1497
  dateEnd: 99991231
  omitProxy: true
  ssIdentifier: ssj0007476
  issn: 0197-4580
  databaseCode: AIKHN
  dateStart: 19950101
  isFulltext: true
  titleUrlDefault: https://www.sciencedirect.com
  providerName: Elsevier
– providerCode: PRVLSH
  databaseName: Elsevier Journals
  customDbUrl:
  mediaType: online
  eissn: 1558-1497
  dateEnd: 99991231
  omitProxy: true
  ssIdentifier: ssj0007476
  issn: 0197-4580
  databaseCode: AKRWK
  dateStart: 19800601
  isFulltext: true
  providerName: Library Specific Holdings
link http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV3da9swEBdZB2MvY1v3kX3hQelLcYhtWYoZe8i2lnak3WAJ9E3IslwSHCdrnIf0YX_c_rLdWfLHIIFsL8bYUuzofj7dSb-7I-SIhtTzfR25aRxFLk0D5Uo_SN0BTRKmYi5DjoHCl1fsfEK_XofXnc7vFmtpXcQ9dbc1ruR_pArXQK4YJfsPkq1_FC7AOcgXjiBhOO4l4-9l7NAULEXXQ1qVKTeyOlka9r8lNKNpKZUuNhmqOqS5Y9TxSp_M9Rx85Rw3EODOLUhjajXwrMrptG7SNCFh4Kaa6JCxA59Iuc3-RbrDTZbh-acgtwFA1Z0fMlsn7Y0OmUsT3N5qNNLF9G5aTxCXmDEr1zcmBKfVzi56N-QirOSSZQv3Ii6beOU7eGZR_CKfSyTZ2uZ2ZcOjNQu2VsYheLjU8Hd7ess1q8FNwhOLVN5Sx2CcsK3zhFmymPXyahzLAUSmH8Usrh7lzfxYcQKuvomzyWgkxqfX4-PlTxcrl-EOvy3jco_c9zljWEWj96uhGYG7Vka4Ve_9gBw1HMPdj99lJu1yg0pzaPyYPLJ-jDM0oHxCOjp_Sg6HuSwW841z7JTM4hI4h2TcxqnT4NRpcOosUgdw6mzDqVPh1DE4dUqcPiOTs9Px53PXVvNwVRixwmXcS1UoB0pjpi-uGU_QW9CYdA6caomWc8QlBYsziWlAwbZUA5WyQNEgjsCsf04O8kWuXxJHAXR4P1IBBVUDBnqcaD1IUpWGAYtk0O-SD9XgCWVT3WPFlUxUnMaZ-HvoBQ696HvgCfMuCeveS5PyZc9-Hys5iSqsGSZiAZjbsz_f1l-vrMZZCU-sfNFHQmbEaYh5n9Bji6IueV_BQsDsgFt-IJTFGnqAPwQOEcMx2d0Gg_HDfgBv8MJgqv7fmG3SZ5y_2uMJr8nD5it-Qw6K27V-CxZ7Eb8rP4k_GLHtxQ
linkProvider Elsevier
openUrl ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Presenilin-1+influences+processing+of+the+acetylcholinesterase+membrane+anchor+PRiMA&rft.jtitle=Neurobiology+of+aging&rft.au=Garc%C3%ADa-Ayll%C3%B3n%2C+Mar%C3%ADa-Salud&rft.au=Campanari%2C+Mar%C3%ADa-Letizia&rft.au=Montenegro%2C+Mar%C3%ADa-Fernanda&rft.au=Cuchillo-Ib%C3%A1%C3%B1ez%2C+Inmaculada&rft.date=2014-07-01&rft.issn=1558-1497&rft.eissn=1558-1497&rft.volume=35&rft.issue=7&rft.spage=1526&rft_id=info:doi/10.1016%2Fj.neurobiolaging.2014.01.147&rft.externalDBID=NO_FULL_TEXT
thumbnail_m http://utb.summon.serialssolutions.com/2.0.0/image/custom?url=https%3A%2F%2Fcdn.clinicalkey.com%2Fck-thumbnails%2F01974580%2FS0197458014X00047%2Fcov150h.gif