Monoclonal antibody with conformational specificity for a toxic conformer of amyloid β42 and its application toward the Alzheimer’s disease diagnosis

Amyloid β-protein (Aβ42) oligomerization is an early event in Alzheimer’s disease (AD). Current diagnostic methods using sequence-specific antibodies against less toxic fibrillar and monomeric Aβ42 run the risk of overdiagnosis. Hence, conformation-specific antibodies against neurotoxic Aβ42 oligome...

Full description

Saved in:
Bibliographic Details
Published inScientific reports Vol. 6; no. 1; p. 29038
Main Authors Murakami, Kazuma, Tokuda, Maki, Suzuki, Takashi, Irie, Yumi, Hanaki, Mizuho, Izuo, Naotaka, Monobe, Yoko, Akagi, Ken-ichi, Ishii, Ryotaro, Tatebe, Harutsugu, Tokuda, Takahiko, Maeda, Masahiro, Kume, Toshiaki, Shimizu, Takahiko, Irie, Kazuhiro
Format Journal Article
LanguageEnglish
Published London Nature Publishing Group UK 04.07.2016
Nature Publishing Group
Subjects
101/1
631/378/1689
631/92/611
82
82/1
Aged
Aged, 80 and over
Alzheimer Disease - cerebrospinal fluid
Alzheimer Disease - diagnosis
Amyloid beta-Peptides - cerebrospinal fluid
Amyloid beta-Peptides - immunology
Amyloid beta-Peptides - toxicity
Animals
Antibodies, Monoclonal - cerebrospinal fluid
Antibodies, Monoclonal - chemistry
Case-Control Studies
Cell Line, Tumor
Cells, Cultured
Female
Humanities and Social Sciences
Humans
Male
Molecular Conformation
multidisciplinary
Neurons - drug effects
Neurons - metabolism
Peptide Fragments - cerebrospinal fluid
Peptide Fragments - immunology
Peptide Fragments - toxicity
Rats, Wistar
Science
Science (multidisciplinary)
Surface Plasmon Resonance
Online AccessGet full text
ISSN2045-2322
2045-2322
DOI10.1038/srep29038

Cover

Abstract Amyloid β-protein (Aβ42) oligomerization is an early event in Alzheimer’s disease (AD). Current diagnostic methods using sequence-specific antibodies against less toxic fibrillar and monomeric Aβ42 run the risk of overdiagnosis. Hence, conformation-specific antibodies against neurotoxic Aβ42 oligomers have garnered much attention for developing more accurate diagnostics. Antibody 24B3, highly specific for the toxic Aβ42 conformer that has a turn at Glu22 and Asp23, recognizes a putative Aβ42 dimer, which forms stable and neurotoxic oligomers more potently than the monomer. 24B3 significantly rescues Aβ42-induced neurotoxicity, whereas sequence-specific antibodies such as 4G8 and 82E1, which recognizes the N-terminus, do not. The ratio of toxic to total Aβ42 in the cerebrospinal fluid of AD patients is significantly higher than in control subjects as measured by sandwich ELISA using antibodies 24B3 and 82E1. Thus, 24B3 may be useful for AD diagnosis and therapy.
AbstractList Amyloid β-protein (Aβ42) oligomerization is an early event in Alzheimer’s disease (AD). Current diagnostic methods using sequence-specific antibodies against less toxic fibrillar and monomeric Aβ42 run the risk of overdiagnosis. Hence, conformation-specific antibodies against neurotoxic Aβ42 oligomers have garnered much attention for developing more accurate diagnostics. Antibody 24B3, highly specific for the toxic Aβ42 conformer that has a turn at Glu22 and Asp23, recognizes a putative Aβ42 dimer, which forms stable and neurotoxic oligomers more potently than the monomer. 24B3 significantly rescues Aβ42-induced neurotoxicity, whereas sequence-specific antibodies such as 4G8 and 82E1, which recognizes the N-terminus, do not. The ratio of toxic to total Aβ42 in the cerebrospinal fluid of AD patients is significantly higher than in control subjects as measured by sandwich ELISA using antibodies 24B3 and 82E1. Thus, 24B3 may be useful for AD diagnosis and therapy.
Amyloid β-protein (Aβ42) oligomerization is an early event in Alzheimer's disease (AD). Current diagnostic methods using sequence-specific antibodies against less toxic fibrillar and monomeric Aβ42 run the risk of overdiagnosis. Hence, conformation-specific antibodies against neurotoxic Aβ42 oligomers have garnered much attention for developing more accurate diagnostics. Antibody 24B3, highly specific for the toxic Aβ42 conformer that has a turn at Glu22 and Asp23, recognizes a putative Aβ42 dimer, which forms stable and neurotoxic oligomers more potently than the monomer. 24B3 significantly rescues Aβ42-induced neurotoxicity, whereas sequence-specific antibodies such as 4G8 and 82E1, which recognizes the N-terminus, do not. The ratio of toxic to total Aβ42 in the cerebrospinal fluid of AD patients is significantly higher than in control subjects as measured by sandwich ELISA using antibodies 24B3 and 82E1. Thus, 24B3 may be useful for AD diagnosis and therapy.Amyloid β-protein (Aβ42) oligomerization is an early event in Alzheimer's disease (AD). Current diagnostic methods using sequence-specific antibodies against less toxic fibrillar and monomeric Aβ42 run the risk of overdiagnosis. Hence, conformation-specific antibodies against neurotoxic Aβ42 oligomers have garnered much attention for developing more accurate diagnostics. Antibody 24B3, highly specific for the toxic Aβ42 conformer that has a turn at Glu22 and Asp23, recognizes a putative Aβ42 dimer, which forms stable and neurotoxic oligomers more potently than the monomer. 24B3 significantly rescues Aβ42-induced neurotoxicity, whereas sequence-specific antibodies such as 4G8 and 82E1, which recognizes the N-terminus, do not. The ratio of toxic to total Aβ42 in the cerebrospinal fluid of AD patients is significantly higher than in control subjects as measured by sandwich ELISA using antibodies 24B3 and 82E1. Thus, 24B3 may be useful for AD diagnosis and therapy.
ArticleNumber 29038
Author Suzuki, Takashi
Ishii, Ryotaro
Monobe, Yoko
Irie, Kazuhiro
Izuo, Naotaka
Irie, Yumi
Maeda, Masahiro
Akagi, Ken-ichi
Tatebe, Harutsugu
Tokuda, Takahiko
Tokuda, Maki
Murakami, Kazuma
Kume, Toshiaki
Hanaki, Mizuho
Shimizu, Takahiko
Author_xml – sequence: 1
  givenname: Kazuma
  surname: Murakami
  fullname: Murakami, Kazuma
  organization: Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University
– sequence: 2
  givenname: Maki
  surname: Tokuda
  fullname: Tokuda, Maki
  organization: Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University
– sequence: 3
  givenname: Takashi
  surname: Suzuki
  fullname: Suzuki, Takashi
  organization: Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University
– sequence: 4
  givenname: Yumi
  surname: Irie
  fullname: Irie, Yumi
  organization: Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University
– sequence: 5
  givenname: Mizuho
  surname: Hanaki
  fullname: Hanaki, Mizuho
  organization: Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University
– sequence: 6
  givenname: Naotaka
  surname: Izuo
  fullname: Izuo, Naotaka
  organization: Department of Advanced Aging Medicine, Chiba University Graduate School of Medicine
– sequence: 7
  givenname: Yoko
  surname: Monobe
  fullname: Monobe, Yoko
  organization: National Institute of Biomedical Innovation, Health and Nutrition
– sequence: 8
  givenname: Ken-ichi
  surname: Akagi
  fullname: Akagi, Ken-ichi
  organization: National Institute of Biomedical Innovation, Health and Nutrition
– sequence: 9
  givenname: Ryotaro
  surname: Ishii
  fullname: Ishii, Ryotaro
  organization: Department of Neurology, Kyoto Prefectural University of Medicine
– sequence: 10
  givenname: Harutsugu
  surname: Tatebe
  fullname: Tatebe, Harutsugu
  organization: Department of Neurology, Kyoto Prefectural University of Medicine
– sequence: 11
  givenname: Takahiko
  surname: Tokuda
  fullname: Tokuda, Takahiko
  organization: Department of Neurology, Kyoto Prefectural University of Medicine, Department of Molecular Pathobiology of Brain Diseases, Kyoto Prefectural University of Medicine
– sequence: 12
  givenname: Masahiro
  surname: Maeda
  fullname: Maeda, Masahiro
  organization: Immuno-Biological Laboratories Co, Ltd
– sequence: 13
  givenname: Toshiaki
  surname: Kume
  fullname: Kume, Toshiaki
  organization: Department of Pharmacology, Graduate School of Pharmaceutical Sciences, Kyoto University
– sequence: 14
  givenname: Takahiko
  surname: Shimizu
  fullname: Shimizu, Takahiko
  organization: Department of Advanced Aging Medicine, Chiba University Graduate School of Medicine
– sequence: 15
  givenname: Kazuhiro
  surname: Irie
  fullname: Irie, Kazuhiro
  email: irie@kais.kyoto-u.ac.jp
  organization: Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University
BackLink https://www.ncbi.nlm.nih.gov/pubmed/27374357$$D View this record in MEDLINE/PubMed
BookMark eNp9UktuFDEQbaEgEkIWXAB5CUhD_GvcvUGKIn5SEBtYW267esaR225sd4ZmxTHgGhyEQ3ASnJlJCCjCm7Jc772qeuX71Z4PHqrqIcHPCGbNcYow0rbc7lQHFPN6QRmlezfu-9VRSue4nJq2nLT3qn0qmOCsFgfVt3fBB-2CVw4pn20XzIzWNq-QDr4PcVDZbpJpBG17q22eUXlHCuXw2eorGEQUeqSG2QVr0M8fnBY5g2xOSI2js3qjUzhrFQ3KK0An7ssKbCH--vo9IWMTqAQlqqUPyaYH1d1euQRHu3hYfXz18sPpm8XZ-9dvT0_OFrqmOC9YB0qInoABXndE9LXBWD-HruHN5byMKdYoQzjj1PCGY1ZrgklTQyt6xjU7rJ5udSc_qnmtnJNjtIOKsyRYXjosrx0u4Bdb8Dh1AxgNPkf1hxCUlX9nvF3JZbiQvGWEC1wEHu8EYvg0QcpysEmDc8pDmJIkDaaCk1q0BfroZq3rIle7K4DjLUDHkEqPvSzL2dhcSlt3a_tP_mH8b9SdL6lg_BKiPA9TLD8h3QL-DbdOzuM
CitedBy_id crossref_primary_10_1021_acscentsci_3c00592
crossref_primary_10_1002_pep2_24333
crossref_primary_10_1016_j_biopha_2021_111609
crossref_primary_10_3390_ijms232113259
crossref_primary_10_3389_fnins_2022_884667
crossref_primary_10_1042_BSR20181415
crossref_primary_10_1093_bbb_zbaa008
crossref_primary_10_1039_D0RA03429K
crossref_primary_10_1080_09168451_2019_1667222
crossref_primary_10_1248_yakushi_20_00251_5
crossref_primary_10_5059_yukigoseikyokaishi_77_1201
crossref_primary_10_1016_j_nbd_2020_104739
crossref_primary_10_1039_C7AY02918G
crossref_primary_10_1002_ptr_8006
crossref_primary_10_1039_D2CB00194B
crossref_primary_10_1186_s12951_023_01772_y
crossref_primary_10_3389_fnins_2018_00037
crossref_primary_10_1002_alz_12457
crossref_primary_10_3233_JAD_180059
crossref_primary_10_1021_acs_biochem_1c00739
crossref_primary_10_1002_ange_202002574
crossref_primary_10_1021_acsomega_0c02134
crossref_primary_10_1016_j_bbrc_2022_07_010
crossref_primary_10_3390_ijms21041179
crossref_primary_10_1021_acschemneuro_0c00331
crossref_primary_10_1039_D3OB00509G
crossref_primary_10_1016_j_bbapap_2019_03_001
crossref_primary_10_3390_ijms22115549
crossref_primary_10_1021_acschemneuro_6b00390
crossref_primary_10_1038_s41598_017_11671_6
crossref_primary_10_1016_j_snb_2019_03_049
crossref_primary_10_1021_acschemneuro_1c00416
crossref_primary_10_1074_jbc_RA119_010955
crossref_primary_10_1016_j_tibtech_2017_11_004
crossref_primary_10_1097_QAD_0000000000002336
crossref_primary_10_3233_JAD_201407
crossref_primary_10_1016_j_bbrc_2025_151655
crossref_primary_10_1016_j_bmc_2018_01_028
crossref_primary_10_1039_D0CC01053G
crossref_primary_10_1007_s12640_018_9955_6
crossref_primary_10_1002_anie_202002574
crossref_primary_10_1039_C8CC08618D
crossref_primary_10_1016_j_bbrc_2019_05_131
crossref_primary_10_1016_j_jbc_2021_101478
Cites_doi 10.1016/S0140-6736(08)61075-2
10.1113/jphysiol.2005.103754
10.1073/pnas.0408153101
10.1074/jbc.M406262200
10.1093/brain/awv355
10.1021/cn300033k
10.1126/science.1079469
10.1586/ern.10.29
10.1074/jbc.R800036200
10.1016/j.bmcl.2015.05.029
10.1016/S0896-6273(03)00367-2
10.1039/c3sc22295k
10.1021/acs.biochem.5b00318
10.1212/01.wnl.0000256043.50901.e3
10.1016/j.jalz.2010.03.006
10.1080/09168451.2014.940275
10.1016/j.tibtech.2010.09.007
10.1016/j.jneumeth.2010.12.001
10.1016/S0960-894X(99)00121-3
10.1002/cbic.200800411
10.1038/nm1782
10.1016/j.stem.2013.01.009
10.1073/pnas.95.11.6448
10.1038/nn.4163
10.1074/jbc.M110.133488
10.1074/jbc.M301874200
10.1021/cn100072e
10.1016/j.jalz.2011.03.005
10.1016/j.bbrc.2015.09.051
10.1073/pnas.0506723102
10.1038/tp.2012.109
10.1002/ana.410440108
10.1016/0006-8993(95)00282-U
10.1038/nrm2101
10.1159/000345771
10.1001/archneurol.2008.565
10.1074/jbc.M113.457739
10.1016/j.jmb.2012.11.006
10.1016/j.jmb.2015.06.008
10.1111/j.1749-6632.2009.04944.x
10.1073/pnas.82.12.4245
10.1001/archneurol.2010.138
10.1016/j.jalz.2011.03.008
10.1039/b912784d
10.4061/2011/431320
ContentType Journal Article
Copyright The Author(s) 2016
Copyright © 2016, Macmillan Publishers Limited 2016 Macmillan Publishers Limited
Copyright_xml – notice: The Author(s) 2016
– notice: Copyright © 2016, Macmillan Publishers Limited 2016 Macmillan Publishers Limited
DBID C6C
AAYXX
CITATION
CGR
CUY
CVF
ECM
EIF
NPM
7X8
5PM
ADTOC
UNPAY
DOI 10.1038/srep29038
DatabaseName Springer Nature Open Access Journals
CrossRef
Medline
MEDLINE
MEDLINE (Ovid)
MEDLINE
MEDLINE
PubMed
MEDLINE - Academic
PubMed Central (Full Participant titles)
Unpaywall for CDI: Periodical Content
Unpaywall
DatabaseTitle CrossRef
MEDLINE
Medline Complete
MEDLINE with Full Text
PubMed
MEDLINE (Ovid)
MEDLINE - Academic
DatabaseTitleList
MEDLINE - Academic
CrossRef

MEDLINE
Database_xml – sequence: 1
  dbid: C6C
  name: Springer Nature OA Free Journals
  url: http://www.springeropen.com/
  sourceTypes: Publisher
– sequence: 2
  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: 3
  dbid: EIF
  name: MEDLINE
  url: https://proxy.k.utb.cz/login?url=https://www.webofscience.com/wos/medline/basic-search
  sourceTypes: Index Database
– sequence: 4
  dbid: UNPAY
  name: Unpaywall
  url: https://proxy.k.utb.cz/login?url=https://unpaywall.org/
  sourceTypes: Open Access Repository
DeliveryMethod fulltext_linktorsrc
Discipline Biology
EISSN 2045-2322
ExternalDocumentID 10.1038/srep29038
PMC4931470
27374357
10_1038_srep29038
Genre Research Support, Non-U.S. Gov't
Journal Article
GroupedDBID 0R~
3V.
4.4
53G
5VS
7X7
88A
88E
88I
8FE
8FH
8FI
8FJ
AAFWJ
AAJSJ
AAKDD
ABDBF
ABUWG
ACGFS
ACSMW
ACUHS
ADBBV
ADRAZ
AENEX
AEUYN
AFKRA
AJTQC
ALIPV
ALMA_UNASSIGNED_HOLDINGS
AOIJS
AZQEC
BAWUL
BBNVY
BCNDV
BENPR
BHPHI
BPHCQ
BVXVI
C6C
CCPQU
DIK
DWQXO
EBD
EBLON
EBS
EJD
ESX
FYUFA
GNUQQ
GROUPED_DOAJ
GX1
HCIFZ
HH5
HMCUK
HYE
KQ8
LK8
M0L
M1P
M2P
M48
M7P
M~E
NAO
OK1
PIMPY
PQQKQ
PROAC
PSQYO
RNT
RNTTT
RPM
SNYQT
UKHRP
AASML
AAYXX
AFPKN
CITATION
PHGZM
PHGZT
PJZUB
PPXIY
PQGLB
PUEGO
CGR
CUY
CVF
ECM
EIF
NPM
7X8
5PM
ADTOC
AFFHD
IPNFZ
RIG
UNPAY
ID FETCH-LOGICAL-c520t-3bea77f1ede45b17f5d00c6eb848052933a38ad14342d484035c10185e97f34c3
IEDL.DBID M48
ISSN 2045-2322
IngestDate Wed Oct 29 12:20:34 EDT 2025
Tue Sep 30 16:50:44 EDT 2025
Wed Oct 15 13:31:57 EDT 2025
Mon Jul 21 06:00:57 EDT 2025
Thu Apr 24 22:59:37 EDT 2025
Wed Oct 01 06:03:48 EDT 2025
Fri Feb 21 02:37:25 EST 2025
IsDoiOpenAccess true
IsOpenAccess true
IsPeerReviewed true
IsScholarly true
Issue 1
Language English
License This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0
cc-by
LinkModel DirectLink
MergedId FETCHMERGED-LOGICAL-c520t-3bea77f1ede45b17f5d00c6eb848052933a38ad14342d484035c10185e97f34c3
Notes ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
OpenAccessLink https://proxy.k.utb.cz/login?url=https://www.nature.com/articles/srep29038.pdf
PMID 27374357
PQID 1802741579
PQPubID 23479
ParticipantIDs unpaywall_primary_10_1038_srep29038
pubmedcentral_primary_oai_pubmedcentral_nih_gov_4931470
proquest_miscellaneous_1802741579
pubmed_primary_27374357
crossref_citationtrail_10_1038_srep29038
crossref_primary_10_1038_srep29038
springer_journals_10_1038_srep29038
ProviderPackageCode CITATION
AAYXX
PublicationCentury 2000
PublicationDate 20160704
2016-07-04
PublicationDateYYYYMMDD 2016-07-04
PublicationDate_xml – month: 7
  year: 2016
  text: 20160704
  day: 4
PublicationDecade 2010
PublicationPlace London
PublicationPlace_xml – name: London
– name: England
PublicationTitle Scientific reports
PublicationTitleAbbrev Sci Rep
PublicationTitleAlternate Sci Rep
PublicationYear 2016
Publisher Nature Publishing Group UK
Nature Publishing Group
Publisher_xml – name: Nature Publishing Group UK
– name: Nature Publishing Group
References Roychaudhuri, Yang, Hoshi, Teplow (CR3) 2009; 284
Gu, Liu, Guo (CR11) 2013; 288
Lambert (CR39) 1998; 95
Murakami (CR13) 2010; 1
Xia (CR43) 2009; 66
Morimoto (CR8) 2004; 279
Kulic (CR15) 2012; 2
Izuo (CR21) 2012; 3
Murakami (CR24) 2015; 466
Soucek, Cumming, Dargusch, Maher, Schubert (CR31) 2003; 39
Holmes (CR32) 2008; 372
Masters (CR1) 1985; 82
Kok (CR38) 2013; 4
Klaver, Patrias, Finke, Loeffler (CR44) 2011; 195
Aisen (CR6) 2010; 6
Mattsson, Blennow, Zetterberg (CR17) 2009; 1180
Masuda (CR7) 2009; 10
Kanai (CR45) 1998; 44
Roychaudhuri (CR10) 2013; 425
Muller-Schiffmann (CR42) 2015; 139
Busche (CR33) 2015; 18
Urbanc (CR34) 2004; 101
Humpel (CR28) 2011; 29
Suzuki (CR37) 2010; 2011
McKhann (CR46) 2011; 7
Haass, Selkoe (CR2) 2007; 8
Fotuhi (CR18) 2010; 67
Fukuda, Shimizu, Nakajima, Mori, Shirasawa (CR26) 1999; 9
Luhrs (CR35) 2005; 102
Murakami (CR9) 2014; 78
Shinoda, Sohma, Kanai (CR41) 2015; 25
Albert (CR27) 2011; 7
Bateman, Wen, Morris, Holtzman (CR47) 2007; 68
CR23
Ringman (CR19) 2012; 2
Murakami (CR25) 2003; 278
Ma, Nussinov (CR20) 2010; 285
Kondo (CR16) 2013; 12
Yamin, Huynh, Teplow (CR40) 2015; 54
Shankar (CR4) 2008; 14
Soejima (CR14) 2013; 10
Luo (CR30) 1995; 681
Chemuru, Kodali, Wetzel (CR12) 2016; 428
Schenk, Basi, Pangalos (CR36) 2012; 2
Townsend, Shankar, Mehta, Walsh, Selkoe (CR5) 2006; 572
Kayed (CR22) 2003; 300
Grill, Cummings (CR29) 2010; 10
AC Klaver (BFsrep29038_CR44) 2011; 195
CL Masters (BFsrep29038_CR1) 1985; 82
R Roychaudhuri (BFsrep29038_CR10) 2013; 425
MP Lambert (BFsrep29038_CR39) 1998; 95
A Muller-Schiffmann (BFsrep29038_CR42) 2015; 139
K Murakami (BFsrep29038_CR13) 2010; 1
T Kondo (BFsrep29038_CR16) 2013; 12
M Fotuhi (BFsrep29038_CR18) 2010; 67
T Suzuki (BFsrep29038_CR37) 2010; 2011
WM Kok (BFsrep29038_CR38) 2013; 4
Y Masuda (BFsrep29038_CR7) 2009; 10
GM Shankar (BFsrep29038_CR4) 2008; 14
K Murakami (BFsrep29038_CR24) 2015; 466
R Roychaudhuri (BFsrep29038_CR3) 2009; 284
GM McKhann (BFsrep29038_CR46) 2011; 7
K Murakami (BFsrep29038_CR25) 2003; 278
N Izuo (BFsrep29038_CR21) 2012; 3
B Ma (BFsrep29038_CR20) 2010; 285
PS Aisen (BFsrep29038_CR6) 2010; 6
MS Albert (BFsrep29038_CR27) 2011; 7
C Holmes (BFsrep29038_CR32) 2008; 372
K Shinoda (BFsrep29038_CR41) 2015; 25
JD Grill (BFsrep29038_CR29) 2010; 10
T Soucek (BFsrep29038_CR31) 2003; 39
H Fukuda (BFsrep29038_CR26) 1999; 9
BFsrep29038_CR23
C Humpel (BFsrep29038_CR28) 2011; 29
D Schenk (BFsrep29038_CR36) 2012; 2
M Kanai (BFsrep29038_CR45) 1998; 44
N Soejima (BFsrep29038_CR14) 2013; 10
R Kayed (BFsrep29038_CR22) 2003; 300
JM Ringman (BFsrep29038_CR19) 2012; 2
S Chemuru (BFsrep29038_CR12) 2016; 428
L Kulic (BFsrep29038_CR15) 2012; 2
G Yamin (BFsrep29038_CR40) 2015; 54
N Mattsson (BFsrep29038_CR17) 2009; 1180
MA Busche (BFsrep29038_CR33) 2015; 18
M Townsend (BFsrep29038_CR5) 2006; 572
W Xia (BFsrep29038_CR43) 2009; 66
K Murakami (BFsrep29038_CR9) 2014; 78
A Morimoto (BFsrep29038_CR8) 2004; 279
B Urbanc (BFsrep29038_CR34) 2004; 101
L Gu (BFsrep29038_CR11) 2013; 288
C Haass (BFsrep29038_CR2) 2007; 8
T Luhrs (BFsrep29038_CR35) 2005; 102
YQ Luo (BFsrep29038_CR30) 1995; 681
RJ Bateman (BFsrep29038_CR47) 2007; 68
26551546 - Nat Neurosci. 2015 Dec;18(12):1725-7
16469784 - J Physiol. 2006 Apr 15;572(Pt 2):477-92
12848931 - Neuron. 2003 Jul 3;39(1):43-56
18845536 - J Biol Chem. 2009 Feb 20;284(8):4749-53
19826677 - Chem Commun (Camb). 2009 Nov 7;(41):6228-30
26122432 - J Mol Biol. 2016 Jan 29;428(2 Pt A):274-91
26048787 - Bioorg Med Chem Lett. 2015 Aug 1;25(15):2976-9
10230618 - Bioorg Med Chem Lett. 1999 Apr 5;9(7):953-6
16293696 - Proc Natl Acad Sci U S A. 2005 Nov 29;102(48):17342-7
18640458 - Lancet. 2008 Jul 19;372(9634):216-23
22950910 - Curr Alzheimer Res. 2013 Jan;10(1):11-20
23149447 - Transl Psychiatry. 2012 Nov 13;2:e183
20625105 - Arch Neurol. 2010 Jul;67(7):899; author reply 900-1
23341831 - Dement Geriatr Cogn Dis Extra. 2012 Jan;2(1):652-7
21514250 - Alzheimers Dement. 2011 May;7(3):263-9
19906258 - Ann N Y Acad Sci. 2009 Oct;1180:28-35
15459202 - J Biol Chem. 2004 Dec 10;279(50):52781-8
23019494 - ACS Chem Neurosci. 2012 Sep 19;3(9):674-81
19204155 - Arch Neurol. 2009 Feb;66(2):190-9
26657517 - Brain. 2016 Feb;139(Pt 2):509-25
22778811 - ACS Chem Neurosci. 2010 Nov 17;1(11):747-56
21514249 - Alzheimers Dement. 2011 May;7(3):270-9
20971518 - Trends Biotechnol. 2011 Jan;29(1):26-32
3159021 - Proc Natl Acad Sci U S A. 1985 Jun;82(12):4245-9
20451872 - Alzheimers Dement. 2010 May;6(3):239-46
21163305 - J Neurosci Methods. 2011 Feb 15;195(2):249-54
7552293 - Brain Res. 1995 May 29;681(1-2):65-74
23687299 - J Biol Chem. 2013 Jun 28;288(26):18673-83
15583128 - Proc Natl Acad Sci U S A. 2004 Dec 14;101(50):17345-50
9667589 - Ann Neurol. 1998 Jul;44(1):17-26
20847046 - J Biol Chem. 2010 Nov 19;285(47):37102-10
21234376 - Int J Alzheimers Dis. 2010 Dec 19;2011:431320
19115328 - Chembiochem. 2009 Jan 26;10(2):287-95
17245412 - Nat Rev Mol Cell Biol. 2007 Feb;8(2):101-12
18568035 - Nat Med. 2008 Aug;14(8):837-42
25130729 - Biosci Biotechnol Biochem. 2014;78(8):1293-305
17325273 - Neurology. 2007 Feb 27;68(9):666-9
26241378 - Biochemistry. 2015 Sep 1;54(34):5315-21
23434393 - Cell Stem Cell. 2013 Apr 4;12(4):487-96
26367176 - Biochem Biophys Res Commun. 2015 Oct 23;466(3):463-7
12944403 - J Biol Chem. 2003 Nov 14;278(46):46179-87
20420492 - Expert Rev Neurother. 2010 May;10(5):711-28
22951439 - Cold Spring Harb Perspect Med. 2012 Sep 01;2(9):a006387
9600986 - Proc Natl Acad Sci U S A. 1998 May 26;95(11):6448-53
23154165 - J Mol Biol. 2013 Jan 23;425(2):292-308
12702875 - Science. 2003 Apr 18;300(5618):486-9
References_xml – volume: 372
  start-page: 216
  year: 2008
  end-page: 223
  ident: CR32
  article-title: Long-term effects of Aβ42 immunisation in Alzheimer’s disease: follow-up of a randomised, placebo-controlled phase I trial
  publication-title: Lancet
  doi: 10.1016/S0140-6736(08)61075-2
– volume: 572
  start-page: 477
  year: 2006
  end-page: 492
  ident: CR5
  article-title: Effects of secreted oligomers of amyloid β-protein on hippocampal synaptic plasticity: a potent role for trimers
  publication-title: J. Physiol.
  doi: 10.1113/jphysiol.2005.103754
– volume: 101
  start-page: 17345
  year: 2004
  end-page: 17350
  ident: CR34
  article-title: In silico study of amyloid β-protein folding and oligomerization
  publication-title: Proc. Natl. Acad. Sci. USA
  doi: 10.1073/pnas.0408153101
– volume: 279
  start-page: 52781
  year: 2004
  end-page: 52788
  ident: CR8
  article-title: Analysis of the secondary structure of β-amyloid (Aβ42) fibrils by systematic proline replacement
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M406262200
– volume: 139
  start-page: 509
  year: 2015
  end-page: 525
  ident: CR42
  article-title: Amyloid-β dimers in the absence of plaque pathology impair learning and synaptic plasticity
  publication-title: Brain
  doi: 10.1093/brain/awv355
– volume: 3
  start-page: 674
  year: 2012
  end-page: 681
  ident: CR21
  article-title: Toxicity in rat primary neurons through the cellular oxidative stress induced by the turn formation at positions 22 and 23 of Aβ42
  publication-title: ACS Chem Neurosci
  doi: 10.1021/cn300033k
– volume: 300
  start-page: 486
  year: 2003
  end-page: 489
  ident: CR22
  article-title: Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
  publication-title: Science
  doi: 10.1126/science.1079469
– volume: 10
  start-page: 711
  year: 2010
  end-page: 728
  ident: CR29
  article-title: Current therapeutic targets for the treatment of Alzheimer’s disease
  publication-title: Expert Rev. Neurother.
  doi: 10.1586/ern.10.29
– volume: 284
  start-page: 4749
  year: 2009
  end-page: 4753
  ident: CR3
  article-title: Amyloid β-protein assembly and Alzheimer disease
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.R800036200
– volume: 25
  start-page: 2976
  year: 2015
  end-page: 2979
  ident: CR41
  article-title: Synthesis of chemically-tethered amyloid-β segment trimer possessing amyloidogenic properties
  publication-title: Bioorg. Med. Chem. Lett.
  doi: 10.1016/j.bmcl.2015.05.029
– volume: 39
  start-page: 43
  year: 2003
  end-page: 56
  ident: CR31
  article-title: The regulation of glucose metabolism by HIF-1 mediates a neuroprotective response to amyloid β peptide
  publication-title: Neuron
  doi: 10.1016/S0896-6273(03)00367-2
– volume: 4
  start-page: 4449
  year: 2013
  end-page: 4454
  ident: CR38
  article-title: Synthetic dityrosine-linked β-amyloid dimers form stable, soluble, neurotoxic oligomers
  publication-title: Chemical Science
  doi: 10.1039/c3sc22295k
– volume: 10
  start-page: 11
  year: 2013
  end-page: 20
  ident: CR14
  article-title: Intracellular accumulation of toxic turn amyloid-β is associated with endoplasmic reticulum stress in Alzheimer’s disease
  publication-title: Curr. Alzheimer Res.
– volume: 54
  start-page: 5315
  year: 2015
  end-page: 5321
  ident: CR40
  article-title: Design and characterization of chemically stabilized Aβ42 oligomers
  publication-title: Biochemistry
  doi: 10.1021/acs.biochem.5b00318
– volume: 68
  start-page: 666
  year: 2007
  end-page: 669
  ident: CR47
  article-title: Fluctuations of CSF amyloid-β levels: implications for a diagnostic and therapeutic biomarker
  publication-title: Neurology
  doi: 10.1212/01.wnl.0000256043.50901.e3
– volume: 6
  start-page: 239
  year: 2010
  end-page: 246
  ident: CR6
  article-title: Clinical Core of the Alzheimer’s Disease Neuroimaging Initiative: progress and plans
  publication-title: Alzheimers Dement
  doi: 10.1016/j.jalz.2010.03.006
– volume: 78
  start-page: 1293
  year: 2014
  end-page: 1305
  ident: CR9
  article-title: Conformation-specific antibodies to target amyloid β oligomers and their application to immunotherapy for Alzheimer’s disease
  publication-title: Biosci. Biotechnol. Biochem.
  doi: 10.1080/09168451.2014.940275
– volume: 29
  start-page: 26
  year: 2011
  end-page: 32
  ident: CR28
  article-title: Identifying and validating biomarkers for Alzheimer’s disease
  publication-title: Trends Biotechnol.
  doi: 10.1016/j.tibtech.2010.09.007
– volume: 195
  start-page: 249
  year: 2011
  end-page: 254
  ident: CR44
  article-title: Specificity and sensitivity of the Aβ oligomer ELISA
  publication-title: J. Neurosci. Methods
  doi: 10.1016/j.jneumeth.2010.12.001
– ident: CR23
– volume: 9
  start-page: 953
  year: 1999
  end-page: 956
  ident: CR26
  article-title: Synthesis, aggregation, and neurotoxicity of the Alzheimer’s Aβ1-42 amyloid peptide and its isoaspartyl isomers
  publication-title: Bioorg. Med. Chem. Lett.
  doi: 10.1016/S0960-894X(99)00121-3
– volume: 10
  start-page: 287
  year: 2009
  end-page: 295
  ident: CR7
  article-title: Identification of physiological and toxic conformations in Aβ42 aggregates
  publication-title: Chem Bio Chem
  doi: 10.1002/cbic.200800411
– volume: 14
  start-page: 837
  year: 2008
  end-page: 842
  ident: CR4
  article-title: Amyloid-β protein dimers isolated directly from Alzheimer’s brains impair synaptic plasticity and memory
  publication-title: Nat. Med.
  doi: 10.1038/nm1782
– volume: 12
  start-page: 487
  year: 2013
  end-page: 496
  ident: CR16
  article-title: Modeling Alzheimer’s disease with iPSCs reveals stress phenotypes associated with intracellular Aβ and differential drug responsiveness
  publication-title: Cell Stem Cell
  doi: 10.1016/j.stem.2013.01.009
– volume: 95
  start-page: 6448
  year: 1998
  end-page: 6453
  ident: CR39
  article-title: Diffusible, nonfibrillar ligands derived from Aβ1-42 are potent central nervous system neurotoxins
  publication-title: Proc. Natl. Acad. Sci. USA
  doi: 10.1073/pnas.95.11.6448
– volume: 18
  start-page: 1725
  year: 2015
  end-page: 1727
  ident: CR33
  article-title: Decreased amyloid-β and increased neuronal hyperactivity by immunotherapy in Alzheimer’s models
  publication-title: Nat. Neurosci.
  doi: 10.1038/nn.4163
– volume: 285
  start-page: 37102
  year: 2010
  end-page: 37110
  ident: CR20
  article-title: Polymorphic C-terminal β-sheet interactions determine the formation of fibril or amyloid β-derived diffusible ligand-like globulomer for the Alzheimer Aβ42 dodecamer
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M110.133488
– volume: 278
  start-page: 46179
  year: 2003
  end-page: 46187
  ident: CR25
  article-title: Neurotoxicity and physicochemical properties of Aβ mutant peptides from cerebral amyloid angiopathy: implication for the pathogenesis of cerebral amyloid angiopathy and Alzheimer’s disease
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M301874200
– volume: 1
  start-page: 747
  year: 2010
  end-page: 756
  ident: CR13
  article-title: Monoclonal antibody against the turn of the 42-residue amyloid β protein at positions 22 and 23
  publication-title: ACS Chem Neurosci
  doi: 10.1021/cn100072e
– volume: 7
  start-page: 263
  year: 2011
  end-page: 269
  ident: CR46
  article-title: The diagnosis of dementia due to Alzheimer’s disease: recommendations from the National Institute on Aging-Alzheimer’s Association workgroups on diagnostic guidelines for Alzheimer’s disease
  publication-title: Alzheimers Dement
  doi: 10.1016/j.jalz.2011.03.005
– volume: 466
  start-page: 463
  year: 2015
  end-page: 467
  ident: CR24
  article-title: Synthesis and characterization of the amyloid β40 dimer model with a linker at position 30 adjacent to the intermolecular β-sheet region
  publication-title: Biochem. Biophys. Res. Commun.
  doi: 10.1016/j.bbrc.2015.09.051
– volume: 102
  start-page: 17342
  year: 2005
  end-page: 17347
  ident: CR35
  article-title: 3D structure of Alzheimer’s amyloid-β(1-42) fibrils
  publication-title: Proc. Natl. Acad. Sci. USA
  doi: 10.1073/pnas.0506723102
– volume: 2
  start-page: e183
  year: 2012
  ident: CR15
  article-title: Early accumulation of intracellular fibrillar oligomers and late congophilic amyloid angiopathy in mice expressing the Osaka intra-Aβ APP mutation
  publication-title: Transl. Psychiatry
  doi: 10.1038/tp.2012.109
– volume: 44
  start-page: 17
  year: 1998
  end-page: 26
  ident: CR45
  article-title: Longitudinal study of cerebrospinal fluid levels of tau, Aβ1-40, and Aβ1-42(43) in Alzheimer’s disease: a study in Japan
  publication-title: Ann. Neurol.
  doi: 10.1002/ana.410440108
– volume: 2011
  start-page: 431320
  year: 2010
  ident: CR37
  article-title: E22Δ mutation in amyloid β-protein promotes β-sheet transformation, radical production, and synaptotoxicity, but not neurotoxicity
  publication-title: Int J Alzheimers Dis
– volume: 681
  start-page: 65
  year: 1995
  end-page: 74
  ident: CR30
  article-title: Physiological levels of β-amyloid increase tyrosine phosphorylation and cytosolic calcium
  publication-title: Brain Res.
  doi: 10.1016/0006-8993(95)00282-U
– volume: 8
  start-page: 101
  year: 2007
  end-page: 112
  ident: CR2
  article-title: Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer’s amyloid β-peptide
  publication-title: Nat Rev Mol Cell Biol
  doi: 10.1038/nrm2101
– volume: 2
  start-page: a006387
  year: 2012
  ident: CR36
  article-title: Treatment strategies targeting amyloid β-protein.
  publication-title: Perspect Med.
– volume: 2
  start-page: 652
  year: 2012
  end-page: 657
  ident: CR19
  article-title: Conformation-dependent oligomers in cerebrospinal fluid of presymptomatic familial Alzheimer’s disease mutation carriers
  publication-title: Dement. Geriatr. Cogn. Dis. Extra
  doi: 10.1159/000345771
– volume: 66
  start-page: 190
  year: 2009
  end-page: 199
  ident: CR43
  article-title: A specific enzyme-linked immunosorbent assay for measuring β-amyloid protein oligomers in human plasma and brain tissue of patients with Alzheimer disease
  publication-title: Arch. Neurol.
  doi: 10.1001/archneurol.2008.565
– volume: 288
  start-page: 18673
  year: 2013
  end-page: 18683
  ident: CR11
  article-title: Structural insights into Aβ42 oligomers using site-directed spin labeling
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M113.457739
– volume: 425
  start-page: 292
  year: 2013
  end-page: 308
  ident: CR10
  article-title: C-terminal turn stability determines assembly differences between Aβ40 and Aβ42
  publication-title: J. Mol. Biol.
  doi: 10.1016/j.jmb.2012.11.006
– volume: 428
  start-page: 274
  year: 2016
  end-page: 291
  ident: CR12
  article-title: C-Terminal threonine reduces Aβ43 amyloidogenicity compared with Aβ42
  publication-title: J. Mol. Biol.
  doi: 10.1016/j.jmb.2015.06.008
– volume: 1180
  start-page: 28
  year: 2009
  end-page: 35
  ident: CR17
  article-title: CSF biomarkers: pinpointing Alzheimer pathogenesis
  publication-title: Ann. N. Y. Acad. Sci.
  doi: 10.1111/j.1749-6632.2009.04944.x
– volume: 82
  start-page: 4245
  year: 1985
  end-page: 4249
  ident: CR1
  article-title: Amyloid plaque core protein in Alzheimer disease and Down syndrome
  publication-title: Proc. Natl. Acad. Sci. USA
  doi: 10.1073/pnas.82.12.4245
– volume: 67
  start-page: 900
  year: 2010
  end-page: 891
  ident: CR18
  article-title: The challenge and public health implications of Alzheimer overdiagnosis in the oldest old
  publication-title: Arch. Neurol.
  doi: 10.1001/archneurol.2010.138
– volume: 7
  start-page: 270
  year: 2011
  end-page: 279
  ident: CR27
  article-title: The diagnosis of mild cognitive impairment due to Alzheimer’s disease: recommendations from the National Institute on Aging-Alzheimer’s Association workgroups on diagnostic guidelines for Alzheimer’s disease
  publication-title: Alzheimers Dement
  doi: 10.1016/j.jalz.2011.03.008
– volume: 2
  start-page: e183
  year: 2012
  ident: BFsrep29038_CR15
  publication-title: Transl. Psychiatry
  doi: 10.1038/tp.2012.109
– volume: 66
  start-page: 190
  year: 2009
  ident: BFsrep29038_CR43
  publication-title: Arch. Neurol.
  doi: 10.1001/archneurol.2008.565
– volume: 44
  start-page: 17
  year: 1998
  ident: BFsrep29038_CR45
  publication-title: Ann. Neurol.
  doi: 10.1002/ana.410440108
– ident: BFsrep29038_CR23
  doi: 10.1039/b912784d
– volume: 7
  start-page: 270
  year: 2011
  ident: BFsrep29038_CR27
  publication-title: Alzheimers Dement
  doi: 10.1016/j.jalz.2011.03.008
– volume: 68
  start-page: 666
  year: 2007
  ident: BFsrep29038_CR47
  publication-title: Neurology
  doi: 10.1212/01.wnl.0000256043.50901.e3
– volume: 3
  start-page: 674
  year: 2012
  ident: BFsrep29038_CR21
  publication-title: ACS Chem Neurosci
  doi: 10.1021/cn300033k
– volume: 14
  start-page: 837
  year: 2008
  ident: BFsrep29038_CR4
  publication-title: Nat. Med.
  doi: 10.1038/nm1782
– volume: 39
  start-page: 43
  year: 2003
  ident: BFsrep29038_CR31
  publication-title: Neuron
  doi: 10.1016/S0896-6273(03)00367-2
– volume: 300
  start-page: 486
  year: 2003
  ident: BFsrep29038_CR22
  publication-title: Science
  doi: 10.1126/science.1079469
– volume: 102
  start-page: 17342
  year: 2005
  ident: BFsrep29038_CR35
  publication-title: Proc. Natl. Acad. Sci. USA
  doi: 10.1073/pnas.0506723102
– volume: 139
  start-page: 509
  year: 2015
  ident: BFsrep29038_CR42
  publication-title: Brain
  doi: 10.1093/brain/awv355
– volume: 6
  start-page: 239
  year: 2010
  ident: BFsrep29038_CR6
  publication-title: Alzheimers Dement
  doi: 10.1016/j.jalz.2010.03.006
– volume: 2
  start-page: 652
  year: 2012
  ident: BFsrep29038_CR19
  publication-title: Dement. Geriatr. Cogn. Dis. Extra
  doi: 10.1159/000345771
– volume: 681
  start-page: 65
  year: 1995
  ident: BFsrep29038_CR30
  publication-title: Brain Res.
  doi: 10.1016/0006-8993(95)00282-U
– volume: 278
  start-page: 46179
  year: 2003
  ident: BFsrep29038_CR25
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M301874200
– volume: 466
  start-page: 463
  year: 2015
  ident: BFsrep29038_CR24
  publication-title: Biochem. Biophys. Res. Commun.
  doi: 10.1016/j.bbrc.2015.09.051
– volume: 372
  start-page: 216
  year: 2008
  ident: BFsrep29038_CR32
  publication-title: Lancet
  doi: 10.1016/S0140-6736(08)61075-2
– volume: 7
  start-page: 263
  year: 2011
  ident: BFsrep29038_CR46
  publication-title: Alzheimers Dement
  doi: 10.1016/j.jalz.2011.03.005
– volume: 18
  start-page: 1725
  year: 2015
  ident: BFsrep29038_CR33
  publication-title: Nat. Neurosci.
  doi: 10.1038/nn.4163
– volume: 9
  start-page: 953
  year: 1999
  ident: BFsrep29038_CR26
  publication-title: Bioorg. Med. Chem. Lett.
  doi: 10.1016/S0960-894X(99)00121-3
– volume: 1
  start-page: 747
  year: 2010
  ident: BFsrep29038_CR13
  publication-title: ACS Chem Neurosci
  doi: 10.1021/cn100072e
– volume: 95
  start-page: 6448
  year: 1998
  ident: BFsrep29038_CR39
  publication-title: Proc. Natl. Acad. Sci. USA
  doi: 10.1073/pnas.95.11.6448
– volume: 25
  start-page: 2976
  year: 2015
  ident: BFsrep29038_CR41
  publication-title: Bioorg. Med. Chem. Lett.
  doi: 10.1016/j.bmcl.2015.05.029
– volume: 82
  start-page: 4245
  year: 1985
  ident: BFsrep29038_CR1
  publication-title: Proc. Natl. Acad. Sci. USA
  doi: 10.1073/pnas.82.12.4245
– volume: 428
  start-page: 274
  year: 2016
  ident: BFsrep29038_CR12
  publication-title: J. Mol. Biol.
  doi: 10.1016/j.jmb.2015.06.008
– volume: 78
  start-page: 1293
  year: 2014
  ident: BFsrep29038_CR9
  publication-title: Biosci. Biotechnol. Biochem.
  doi: 10.1080/09168451.2014.940275
– volume: 425
  start-page: 292
  year: 2013
  ident: BFsrep29038_CR10
  publication-title: J. Mol. Biol.
  doi: 10.1016/j.jmb.2012.11.006
– volume: 10
  start-page: 11
  year: 2013
  ident: BFsrep29038_CR14
  publication-title: Curr. Alzheimer Res.
– volume: 2011
  start-page: 431320
  year: 2010
  ident: BFsrep29038_CR37
  publication-title: Int J Alzheimers Dis
  doi: 10.4061/2011/431320
– volume: 572
  start-page: 477
  year: 2006
  ident: BFsrep29038_CR5
  publication-title: J. Physiol.
  doi: 10.1113/jphysiol.2005.103754
– volume: 4
  start-page: 4449
  year: 2013
  ident: BFsrep29038_CR38
  publication-title: Chemical Science
  doi: 10.1039/c3sc22295k
– volume: 195
  start-page: 249
  year: 2011
  ident: BFsrep29038_CR44
  publication-title: J. Neurosci. Methods
  doi: 10.1016/j.jneumeth.2010.12.001
– volume: 279
  start-page: 52781
  year: 2004
  ident: BFsrep29038_CR8
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M406262200
– volume: 8
  start-page: 101
  year: 2007
  ident: BFsrep29038_CR2
  publication-title: Nat Rev Mol Cell Biol
  doi: 10.1038/nrm2101
– volume: 10
  start-page: 287
  year: 2009
  ident: BFsrep29038_CR7
  publication-title: Chem Bio Chem
  doi: 10.1002/cbic.200800411
– volume: 288
  start-page: 18673
  year: 2013
  ident: BFsrep29038_CR11
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M113.457739
– volume: 12
  start-page: 487
  year: 2013
  ident: BFsrep29038_CR16
  publication-title: Cell Stem Cell
  doi: 10.1016/j.stem.2013.01.009
– volume: 10
  start-page: 711
  year: 2010
  ident: BFsrep29038_CR29
  publication-title: Expert Rev. Neurother.
  doi: 10.1586/ern.10.29
– volume: 1180
  start-page: 28
  year: 2009
  ident: BFsrep29038_CR17
  publication-title: Ann. N. Y. Acad. Sci.
  doi: 10.1111/j.1749-6632.2009.04944.x
– volume: 67
  start-page: 900
  year: 2010
  ident: BFsrep29038_CR18
  publication-title: Arch. Neurol.
  doi: 10.1001/archneurol.2010.138
– volume: 2
  start-page: a006387
  year: 2012
  ident: BFsrep29038_CR36
  publication-title: Perspect Med.
– volume: 284
  start-page: 4749
  year: 2009
  ident: BFsrep29038_CR3
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.R800036200
– volume: 285
  start-page: 37102
  year: 2010
  ident: BFsrep29038_CR20
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M110.133488
– volume: 54
  start-page: 5315
  year: 2015
  ident: BFsrep29038_CR40
  publication-title: Biochemistry
  doi: 10.1021/acs.biochem.5b00318
– volume: 29
  start-page: 26
  year: 2011
  ident: BFsrep29038_CR28
  publication-title: Trends Biotechnol.
  doi: 10.1016/j.tibtech.2010.09.007
– volume: 101
  start-page: 17345
  year: 2004
  ident: BFsrep29038_CR34
  publication-title: Proc. Natl. Acad. Sci. USA
  doi: 10.1073/pnas.0408153101
– reference: 26048787 - Bioorg Med Chem Lett. 2015 Aug 1;25(15):2976-9
– reference: 7552293 - Brain Res. 1995 May 29;681(1-2):65-74
– reference: 3159021 - Proc Natl Acad Sci U S A. 1985 Jun;82(12):4245-9
– reference: 20847046 - J Biol Chem. 2010 Nov 19;285(47):37102-10
– reference: 26551546 - Nat Neurosci. 2015 Dec;18(12):1725-7
– reference: 22778811 - ACS Chem Neurosci. 2010 Nov 17;1(11):747-56
– reference: 12848931 - Neuron. 2003 Jul 3;39(1):43-56
– reference: 10230618 - Bioorg Med Chem Lett. 1999 Apr 5;9(7):953-6
– reference: 20420492 - Expert Rev Neurother. 2010 May;10(5):711-28
– reference: 26241378 - Biochemistry. 2015 Sep 1;54(34):5315-21
– reference: 26122432 - J Mol Biol. 2016 Jan 29;428(2 Pt A):274-91
– reference: 9600986 - Proc Natl Acad Sci U S A. 1998 May 26;95(11):6448-53
– reference: 26367176 - Biochem Biophys Res Commun. 2015 Oct 23;466(3):463-7
– reference: 16469784 - J Physiol. 2006 Apr 15;572(Pt 2):477-92
– reference: 25130729 - Biosci Biotechnol Biochem. 2014;78(8):1293-305
– reference: 12944403 - J Biol Chem. 2003 Nov 14;278(46):46179-87
– reference: 20451872 - Alzheimers Dement. 2010 May;6(3):239-46
– reference: 21163305 - J Neurosci Methods. 2011 Feb 15;195(2):249-54
– reference: 23341831 - Dement Geriatr Cogn Dis Extra. 2012 Jan;2(1):652-7
– reference: 16293696 - Proc Natl Acad Sci U S A. 2005 Nov 29;102(48):17342-7
– reference: 18640458 - Lancet. 2008 Jul 19;372(9634):216-23
– reference: 20971518 - Trends Biotechnol. 2011 Jan;29(1):26-32
– reference: 9667589 - Ann Neurol. 1998 Jul;44(1):17-26
– reference: 17325273 - Neurology. 2007 Feb 27;68(9):666-9
– reference: 23434393 - Cell Stem Cell. 2013 Apr 4;12(4):487-96
– reference: 22950910 - Curr Alzheimer Res. 2013 Jan;10(1):11-20
– reference: 21514249 - Alzheimers Dement. 2011 May;7(3):270-9
– reference: 12702875 - Science. 2003 Apr 18;300(5618):486-9
– reference: 20625105 - Arch Neurol. 2010 Jul;67(7):899; author reply 900-1
– reference: 15459202 - J Biol Chem. 2004 Dec 10;279(50):52781-8
– reference: 22951439 - Cold Spring Harb Perspect Med. 2012 Sep 01;2(9):a006387
– reference: 19115328 - Chembiochem. 2009 Jan 26;10(2):287-95
– reference: 19204155 - Arch Neurol. 2009 Feb;66(2):190-9
– reference: 23154165 - J Mol Biol. 2013 Jan 23;425(2):292-308
– reference: 18568035 - Nat Med. 2008 Aug;14(8):837-42
– reference: 21234376 - Int J Alzheimers Dis. 2010 Dec 19;2011:431320
– reference: 19906258 - Ann N Y Acad Sci. 2009 Oct;1180:28-35
– reference: 17245412 - Nat Rev Mol Cell Biol. 2007 Feb;8(2):101-12
– reference: 21514250 - Alzheimers Dement. 2011 May;7(3):263-9
– reference: 23019494 - ACS Chem Neurosci. 2012 Sep 19;3(9):674-81
– reference: 23149447 - Transl Psychiatry. 2012 Nov 13;2:e183
– reference: 15583128 - Proc Natl Acad Sci U S A. 2004 Dec 14;101(50):17345-50
– reference: 23687299 - J Biol Chem. 2013 Jun 28;288(26):18673-83
– reference: 26657517 - Brain. 2016 Feb;139(Pt 2):509-25
– reference: 19826677 - Chem Commun (Camb). 2009 Nov 7;(41):6228-30
– reference: 18845536 - J Biol Chem. 2009 Feb 20;284(8):4749-53
SSID ssj0000529419
Score 2.3760788
Snippet Amyloid β-protein (Aβ42) oligomerization is an early event in Alzheimer’s disease (AD). Current diagnostic methods using sequence-specific antibodies against...
Amyloid β-protein (Aβ42) oligomerization is an early event in Alzheimer's disease (AD). Current diagnostic methods using sequence-specific antibodies against...
SourceID unpaywall
pubmedcentral
proquest
pubmed
crossref
springer
SourceType Open Access Repository
Aggregation Database
Index Database
Enrichment Source
Publisher
StartPage 29038
SubjectTerms 101/1
631/378/1689
631/92/611
82
82/1
Aged
Aged, 80 and over
Alzheimer Disease - cerebrospinal fluid
Alzheimer Disease - diagnosis
Amyloid beta-Peptides - cerebrospinal fluid
Amyloid beta-Peptides - immunology
Amyloid beta-Peptides - toxicity
Animals
Antibodies, Monoclonal - cerebrospinal fluid
Antibodies, Monoclonal - chemistry
Case-Control Studies
Cell Line, Tumor
Cells, Cultured
Female
Humanities and Social Sciences
Humans
Male
Molecular Conformation
multidisciplinary
Neurons - drug effects
Neurons - metabolism
Peptide Fragments - cerebrospinal fluid
Peptide Fragments - immunology
Peptide Fragments - toxicity
Rats, Wistar
Science
Science (multidisciplinary)
Surface Plasmon Resonance
SummonAdditionalLinks – databaseName: Springer Nature HAS Fully OA
  dbid: AAJSJ
  link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwjV3NbtQwEB6VrRBwQPwT_mRYDlwiktiOneMKUVUrwQUq9RbZsaNGSpNVk1W7nHgMeA0ehIfgSRhnE6urFolTonhsJZkZ-bNn_A3A20iYrJSZDEvJTciEiEKNZhImwiZCWBabIXn80-f08Igtj_nxHsynszA78fuBuhtnilWS4f0N2Jdoj3IG-4vF8svSb6W4YBWLs4k3iMr3vs_ubHMFQl7NhPTh0Dtwa92s1OZc1fWlGefgHtwdoSJZbHV7H_Zs8wBubotHbh7CD3THtqgdkib4eyrdmg1x26oEl7j-TCI2usOULiEI8TbB50SRvr2oiknMnpG2JOoUV-6VIb9_sQSHM6TqO3Ipuo19XH4tQbxIFvW3E1thxz_ff3ZkDPHgdUjaq7pHcHTw8euHw3CssxAWPIn6kGqrhChjayzjOhYlN1FUpFZL5goeZJQqKhUqjbLEMFwRUl44oi9uM1FSVtDHMGvaxj4FYrlNdap1EYmUxZFSsdsyQRSkU2ZtrAN4N-kjL0YSclcLo86HYDiVuVddAG-86GrLvHGd0OtJqTn6hQt2qMa26y53zHYOLYksgCdbJfthELIhcOIiALGjfi_gOLd3W5rqZODeZhmNmYgCmE-Gko9O3133dnNvQ__-hmf_NdZzuI1YLR0yhdkLmPVna_sS8VCvX43-8Bc9cQ99
  priority: 102
  providerName: Springer Nature
– databaseName: Unpaywall
  dbid: UNPAY
  link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwjV3NbtQwEB7BVgj1QPknqCBDOXDJksR2nBxXFVWFxIoDK5VTZMeOGjUkqyarsj3xGPAaPAgPwZN0nD-6tEg9RUrGUeyM7c-ez98AvPGEjrMojtws4tplQniuQjdxA2ECIQzzdUse_zgPDxfswxE_6g-r1z2tspO0bIfpgR32DueLZRB7NJoudXYbtkKO0HsCW4v5p9kXm0AOoYmL6CAY1INo9LfM5pxzBUhe5UOOQdFtuLsql3J9Jovi0rxzsAPz4Ys7usnJdNWoaXr-j5jjjat0H-71CJTMOoMHcMuUD-FOl5Ny_Qh-YC-v0sICdIKtnqtKr4ndrSW4ch6POuJDe0bT8owQxhO8TyRpqm95OpiZU1JlRH5dF1Wuye9fLMDXaZI3NbkUNMcylrZLEIaSWXF-bHIs-Of7z5r0kSO8tlzAvH4Mi4P3n_cP3T59g5vywGtcqowUIvONNowrX2Rce14aGhUxm0chplTSSKIvUBZohgtNylOrH8ZNLDLKUvoEJmVVmmdADDehCpVKPREy35PStzsxCK5UyIzxlQNvhx-cpL22uU2xUSRtjJ1GydjYDrweTZedoMd1Rq8GL0mwu9kYiixNtaoTK5hnQZiIHXjaec34GkSCiMe4cEBs-NNoYKW8N5-U-XEr6c1i6jPhObA3eF7SjyX1dV-3Nzrl_-vw_EZWuzBpTlfmBSKrRr3s-9MFYT0u3g
  priority: 102
  providerName: Unpaywall
Title Monoclonal antibody with conformational specificity for a toxic conformer of amyloid β42 and its application toward the Alzheimer’s disease diagnosis
URI https://link.springer.com/article/10.1038/srep29038
https://www.ncbi.nlm.nih.gov/pubmed/27374357
https://www.proquest.com/docview/1802741579
https://pubmed.ncbi.nlm.nih.gov/PMC4931470
https://www.nature.com/articles/srep29038.pdf
UnpaywallVersion publishedVersion
Volume 6
hasFullText 1
inHoldings 1
isFullTextHit
isPrint
journalDatabaseRights – providerCode: PRVFSB
  databaseName: Free Full-Text Journals in Chemistry
  customDbUrl:
  eissn: 2045-2322
  dateEnd: 99991231
  omitProxy: true
  ssIdentifier: ssj0000529419
  issn: 2045-2322
  databaseCode: HH5
  dateStart: 20110101
  isFulltext: true
  titleUrlDefault: http://abc-chemistry.org/
  providerName: ABC ChemistRy
– providerCode: PRVAFT
  databaseName: Open Access Digital Library
  customDbUrl:
  eissn: 2045-2322
  dateEnd: 99991231
  omitProxy: true
  ssIdentifier: ssj0000529419
  issn: 2045-2322
  databaseCode: KQ8
  dateStart: 20110101
  isFulltext: true
  titleUrlDefault: http://grweb.coalliance.org/oadl/oadl.html
  providerName: Colorado Alliance of Research Libraries
– providerCode: PRVAON
  databaseName: DOAJ Directory of Open Access Journals
  customDbUrl:
  eissn: 2045-2322
  dateEnd: 99991231
  omitProxy: true
  ssIdentifier: ssj0000529419
  issn: 2045-2322
  databaseCode: DOA
  dateStart: 20110101
  isFulltext: true
  titleUrlDefault: https://www.doaj.org/
  providerName: Directory of Open Access Journals
– providerCode: PRVEBS
  databaseName: EBSCOhost Academic Search Ultimate
  customDbUrl: https://search.ebscohost.com/login.aspx?authtype=ip,shib&custid=s3936755&profile=ehost&defaultdb=asn
  eissn: 2045-2322
  dateEnd: 99991231
  omitProxy: true
  ssIdentifier: ssj0000529419
  issn: 2045-2322
  databaseCode: ABDBF
  dateStart: 20121221
  isFulltext: true
  titleUrlDefault: https://search.ebscohost.com/direct.asp?db=asn
  providerName: EBSCOhost
– providerCode: PRVBFR
  databaseName: Free Medical Journals
  customDbUrl:
  eissn: 2045-2322
  dateEnd: 99991231
  omitProxy: true
  ssIdentifier: ssj0000529419
  issn: 2045-2322
  databaseCode: DIK
  dateStart: 20110101
  isFulltext: true
  titleUrlDefault: http://www.freemedicaljournals.com
  providerName: Flying Publisher
– providerCode: PRVFQY
  databaseName: GFMER Free Medical Journals
  customDbUrl:
  eissn: 2045-2322
  dateEnd: 99991231
  omitProxy: true
  ssIdentifier: ssj0000529419
  issn: 2045-2322
  databaseCode: GX1
  dateStart: 0
  isFulltext: true
  titleUrlDefault: http://www.gfmer.ch/Medical_journals/Free_medical.php
  providerName: Geneva Foundation for Medical Education and Research
– providerCode: PRVHPJ
  databaseName: ROAD: Directory of Open Access Scholarly Resources
  customDbUrl:
  eissn: 2045-2322
  dateEnd: 99991231
  omitProxy: true
  ssIdentifier: ssj0000529419
  issn: 2045-2322
  databaseCode: M~E
  dateStart: 20110101
  isFulltext: true
  titleUrlDefault: https://road.issn.org
  providerName: ISSN International Centre
– providerCode: PRVAQN
  databaseName: PubMed Central
  customDbUrl:
  eissn: 2045-2322
  dateEnd: 99991231
  omitProxy: true
  ssIdentifier: ssj0000529419
  issn: 2045-2322
  databaseCode: RPM
  dateStart: 20110101
  isFulltext: true
  titleUrlDefault: https://www.ncbi.nlm.nih.gov/pmc/
  providerName: National Library of Medicine
– providerCode: PRVAQT
  databaseName: Springer Nature - nature.com Journals - Fully Open Access
  customDbUrl:
  eissn: 2045-2322
  dateEnd: 99991231
  omitProxy: true
  ssIdentifier: ssj0000529419
  issn: 2045-2322
  databaseCode: NAO
  dateStart: 20111201
  isFulltext: true
  titleUrlDefault: https://www.nature.com/siteindex/index.html
  providerName: Nature Publishing
– providerCode: PRVPQU
  databaseName: Health & Medical Collection
  customDbUrl:
  eissn: 2045-2322
  dateEnd: 20191231
  omitProxy: true
  ssIdentifier: ssj0000529419
  issn: 2045-2322
  databaseCode: 7X7
  dateStart: 20110101
  isFulltext: true
  titleUrlDefault: https://search.proquest.com/healthcomplete
  providerName: ProQuest
– providerCode: PRVPQU
  databaseName: ProQuest Central
  customDbUrl: http://www.proquest.com/pqcentral?accountid=15518
  eissn: 2045-2322
  dateEnd: 20191231
  omitProxy: true
  ssIdentifier: ssj0000529419
  issn: 2045-2322
  databaseCode: BENPR
  dateStart: 20110101
  isFulltext: true
  titleUrlDefault: https://www.proquest.com/central
  providerName: ProQuest
– providerCode: PRVFZP
  databaseName: Scholars Portal Journals: Open Access
  customDbUrl:
  eissn: 2045-2322
  dateEnd: 20250131
  omitProxy: true
  ssIdentifier: ssj0000529419
  issn: 2045-2322
  databaseCode: M48
  dateStart: 20110801
  isFulltext: true
  titleUrlDefault: http://journals.scholarsportal.info
  providerName: Scholars Portal
– providerCode: PRVAVX
  databaseName: Springer Nature HAS Fully OA
  customDbUrl:
  eissn: 2045-2322
  dateEnd: 99991231
  omitProxy: true
  ssIdentifier: ssj0000529419
  issn: 2045-2322
  databaseCode: AAJSJ
  dateStart: 20111201
  isFulltext: true
  titleUrlDefault: https://www.springernature.com
  providerName: Springer Nature
– providerCode: PRVAVX
  databaseName: Springer Nature OA Free Journals
  customDbUrl:
  eissn: 2045-2322
  dateEnd: 99991231
  omitProxy: true
  ssIdentifier: ssj0000529419
  issn: 2045-2322
  databaseCode: C6C
  dateStart: 20111201
  isFulltext: true
  titleUrlDefault: http://www.springeropen.com/
  providerName: Springer Nature
link http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwjV1bi9QwFD7sBXF9EO_WyxBd0X2ptk3atA8iddhlGdhhUQfGp5K0KVvotrMzHdzxh_hD_CH-Jk96Y4YdwaeWJg1Nzwn5knPyfQBvLJ4EqR_4Zuq7ick4t0yJbmI6XDmcK2YndfL42dg7nbDR1J3uQJfW3P7AxdalndaTmszz99dXq0844D82R8b9DziXzJwA797OrkytJ6Xjrq24xi7s45wVaFGHsxb4N6zfTsBq1Q9Nx24irHA62qH1BjcnqxsI9GYiZR9NvQO3l8VMrH6IPF-bsE7uwd0WaZKwcY37sKOKB3Cr0Z5cPYRfOJrLONdAnODfzWSZrIjelSW4Qu6PNGKhPoup84kQrhN8TgSpyuss7qqpOSlTIi5x4Z8l5M9v5mBzCcmqBVkLjuM7Oj2XINwkYf7zQmX44rsFaeNDeK0z_rLFI5icHH8bnpqtSIMZu45VmVQqwXlqq0QxV9o8dRPLij0lfabVEgJKBfUFWpwyJ2G4nKRurFnCXBXwlLKYPoa9oizUUyDKVZ70pIwt7jHbEsLW-y0IoaTHlLKlAUedNaK4ZTDXQhp5VEfSqR_1hjPgdV911tB2bKv0qjNphINKR0pEocrlItK0eBpq8cCAJ42J-2YQ7yHqcrkBfMP4fQVN2L1ZUmQXNXE3C6jNuGXAYecmUefw277usPegf_fh2X_04TkcIMzz6iRj9gL2qvlSvUQoVckB7PIpH8B-GI6-jvD6-Xh8_gWfDr3hoN6eGNTjBksm4_Pw-1-4qCrB
linkProvider Scholars Portal
linkToHtml http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwjV3NbpwwEB6lqaokh6r_ob9ut4deUAHbGI7RqtG2TXJKpNyQjY2CRGEVWLWbUx4jfY0-SB-iT9IxC1ZWSaWeQHhsAeORv_GMvwF4HwidFkma-EXCtc-ECHyF08SPhImEMCzUffL44VE8O2FfTvnpBkzGszBr8fueuhtXinmU4v0duJugI2cJ8qfx1G2k2FAVC9ORNYgmH12P9bXmBoC8mQfpgqE7sLWo53L5XVbVtfVm_wHcH4Ai2Vtp9iFsmPoR3FuVjlw-his0xiavLI4m-HNK1eglsZuqBB1cdyIRG-1RSpsOhGib4HMiSdf8KPNRzJyTpiDyG_rtpSa_f7EIh9Ok7FpyLbaNfWx2LUG0SPaqizNTYsc_lz9bMgR48Nqn7JXtEzjZ_3Q8nflDlQU_51HQ-VQZKUQRGm0YV6EouA6CPDYqYbbcQUqppIlElVEWaYb-IOW5pfniJhUFZTl9Cpt1U5tdIIabWMVK5YGIWRhIGdoNE8RAKmbGhMqDD6M-snygILeVMKqsD4XTJHOq8-CdE52veDduE3o7KjVDq7ChDlmbZtFmltfOYiWRevBspWQ3DAI2hE1ceCDW1O8ELOP2ektdnvXM2yylIROBB5NxomSDybe3vd3EzaF_f8Pz_xrrDWzNjg8PsoPPR19fwDaitrjPGWYvYbM7X5hXiIw69bq3jL-e1BEI
linkToPdf http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwjV3NbtQwEB5BK_4OiH_Cr6EcuASS2I6d4wpYlQUqJKjUW2THjhopJKsmK1hOPAa8Bg_CQ_AkjPNHVy0Sp0jx2EoyM_Fnz-cZgCeBMEkuE-nnkhufCRH4Gs3Ej4SNhLAsNB15_N1evLvPFgf8YDis3gy0yj6lZfebHtlhz3G-WEZJQOWzpcnPwrYUNEYj3p7NFh8W06aKC1uxMBkzCFH5t9_mvHMCTJ7kRE6B0UtwYVUt1fqzKstjc8_8ClweQCOZ9Y95Fc7Y6hqc68tIrq_Dd3TMOisdpib4oQpdmzVxG6wEF7vT6URsdMcqHTUIkTfB-0SRtv5SZKOYPSJ1TtQnXMMXhvz6ySIczpCibcixODf2cUxbgsiRzMqvh7bAjr-__WjIEOzBa0ffK5obsD9_9fHFrj9UXPAzHgWtT7VVQuShNZZxHYqcmyDIYqslc6UPEkoVlQrVR1lkGK4NKc9cyi9uE5FTltGbsFXVlb0NxHIb61jrLBAxCwOlQrd5gnhIx8zaUHvwdNRHmg3pyF1VjDLtwuJUppPqPHg8iS77HBynCT0alZqih7iwh6psvWpSl-PO4SaReHCrV_I0DII3hFBceCA21D8JuOzbmy1Vcdhl4WYJDZkIPNgZDSUd3L857el2Jhv69zvc-a-xHsL59y_n6dvXe2_uwkUEcHFHH2b3YKs9Wtn7CJJa_WBwjT_bWRfv
linkToUnpaywall http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwjV3NbtQwEB7BVgj1QPknqCBDOXDJksR2nBxXFVWFxIoDK5VTZMeOGjUkqyarsj3xGPAaPAgPwZN0nD-6tEg9RUrGUeyM7c-ez98AvPGEjrMojtws4tplQniuQjdxA2ECIQzzdUse_zgPDxfswxE_6g-r1z2tspO0bIfpgR32DueLZRB7NJoudXYbtkKO0HsCW4v5p9kXm0AOoYmL6CAY1INo9LfM5pxzBUhe5UOOQdFtuLsql3J9Jovi0rxzsAPz4Ys7usnJdNWoaXr-j5jjjat0H-71CJTMOoMHcMuUD-FOl5Ny_Qh-YC-v0sICdIKtnqtKr4ndrSW4ch6POuJDe0bT8owQxhO8TyRpqm95OpiZU1JlRH5dF1Wuye9fLMDXaZI3NbkUNMcylrZLEIaSWXF-bHIs-Of7z5r0kSO8tlzAvH4Mi4P3n_cP3T59g5vywGtcqowUIvONNowrX2Rce14aGhUxm0chplTSSKIvUBZohgtNylOrH8ZNLDLKUvoEJmVVmmdADDehCpVKPREy35PStzsxCK5UyIzxlQNvhx-cpL22uU2xUSRtjJ1GydjYDrweTZedoMd1Rq8GL0mwu9kYiixNtaoTK5hnQZiIHXjaec34GkSCiMe4cEBs-NNoYKW8N5-U-XEr6c1i6jPhObA3eF7SjyX1dV-3Nzrl_-vw_EZWuzBpTlfmBSKrRr3s-9MFYT0u3g
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=Monoclonal+antibody+with+conformational+specificity+for+a+toxic+conformer+of+amyloid+%CE%B242+and+its+application+toward+the+Alzheimer%27s+disease+diagnosis&rft.jtitle=Scientific+reports&rft.au=Murakami%2C+Kazuma&rft.au=Tokuda%2C+Maki&rft.au=Suzuki%2C+Takashi&rft.au=Irie%2C+Yumi&rft.date=2016-07-04&rft.issn=2045-2322&rft.eissn=2045-2322&rft.volume=6&rft.spage=29038&rft_id=info:doi/10.1038%2Fsrep29038&rft.externalDBID=NO_FULL_TEXT
thumbnail_l http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=2045-2322&client=summon
thumbnail_m http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=2045-2322&client=summon
thumbnail_s http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=2045-2322&client=summon