Concentrations of antibodies against β-amyloid 40/42 monomer and oligomers in Chinese intravenous immunoglobulins

•Anti-Aβ antibody levels in Chinese IVIgs were markedly higher than in Octagam®.•Chinese IVIgs have different antibody concentrations to different Aβ conformations.•The effects of Chinese IVIg products in AD patients should be investigated. Intravenous immunoglobulin (IVIg) preparations are being in...

Full description

Saved in:
Bibliographic Details
Published in:Journal of pharmaceutical and biomedical analysis Vol. 138; pp. 277 - 282
Main Authors: Ye, Shengliang, Zeng, Renyong, Jiang, Peng, Hou, Mingxia, Liu, Fengjuan, Wang, Zongkui, Du, Xi, Yuan, Jing, Chen, Yunhua, Cao, Haijun, Ma, Li, Li, Changqing
Format: Journal Article
Language:English
Published: England Elsevier B.V 10-05-2017
Subjects:
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Abstract •Anti-Aβ antibody levels in Chinese IVIgs were markedly higher than in Octagam®.•Chinese IVIgs have different antibody concentrations to different Aβ conformations.•The effects of Chinese IVIg products in AD patients should be investigated. Intravenous immunoglobulin (IVIg) preparations are being investigated as a potential agent for treatment or prevention of Alzheimer’s disease (AD). Antibodies towards soluble β-amyloid (Aβ) contained in IVIg were considered to be the major component contributing to the beneficial effect of the preparations in pilot studies. This study compared the antibody concentrations against Aβ in Octagam® IVIg (Octapharma) and 9 IVIg preparations from different Chinese manufacturers by ELISA, using Aβ40 monomer, Aβ40 soluble oligomers, Aβ42 monomer and Aβ42 soluble oligomers as the antigens. The results showed that each preparation contained different antibody levels against the four Aβ forms. The median values of the four antibody concentrations in Chinese IVIg preparations were 16.53, 8.47, 24.36 and 33.25μg/mL, which were remarkably higher than that in Octagam® IVIg (1.66, 2.07, 4.61 and 4.64μg/mL). Moreover, the anti-Aβ42 oligomer antibody levels in almost all IVIg preparations were higher than the anti-Aβ42 monomer antibody, and the concentrations of anti-Aβ42 antibodies in most of the IVIg preparations were significantly higher than that of anti-Aβ40 antibodies. These findings will contribute to an increased understanding of the uniqueness of Chinese IVIg preparations, and could provide support for a trial of a Chinese IVIg product in AD patients.
AbstractList •Anti-Aβ antibody levels in Chinese IVIgs were markedly higher than in Octagam®.•Chinese IVIgs have different antibody concentrations to different Aβ conformations.•The effects of Chinese IVIg products in AD patients should be investigated. Intravenous immunoglobulin (IVIg) preparations are being investigated as a potential agent for treatment or prevention of Alzheimer’s disease (AD). Antibodies towards soluble β-amyloid (Aβ) contained in IVIg were considered to be the major component contributing to the beneficial effect of the preparations in pilot studies. This study compared the antibody concentrations against Aβ in Octagam® IVIg (Octapharma) and 9 IVIg preparations from different Chinese manufacturers by ELISA, using Aβ40 monomer, Aβ40 soluble oligomers, Aβ42 monomer and Aβ42 soluble oligomers as the antigens. The results showed that each preparation contained different antibody levels against the four Aβ forms. The median values of the four antibody concentrations in Chinese IVIg preparations were 16.53, 8.47, 24.36 and 33.25μg/mL, which were remarkably higher than that in Octagam® IVIg (1.66, 2.07, 4.61 and 4.64μg/mL). Moreover, the anti-Aβ42 oligomer antibody levels in almost all IVIg preparations were higher than the anti-Aβ42 monomer antibody, and the concentrations of anti-Aβ42 antibodies in most of the IVIg preparations were significantly higher than that of anti-Aβ40 antibodies. These findings will contribute to an increased understanding of the uniqueness of Chinese IVIg preparations, and could provide support for a trial of a Chinese IVIg product in AD patients.
Intravenous immunoglobulin (IVIg) preparations are being investigated as a potential agent for treatment or prevention of Alzheimer's disease (AD). Antibodies towards soluble β-amyloid (Aβ) contained in IVIg were considered to be the major component contributing to the beneficial effect of the preparations in pilot studies. This study compared the antibody concentrations against Aβ in Octagam® IVIg (Octapharma) and 9 IVIg preparations from different Chinese manufacturers by ELISA, using Aβ40 monomer, Aβ40 soluble oligomers, Aβ42 monomer and Aβ42 soluble oligomers as the antigens. The results showed that each preparation contained different antibody levels against the four Aβ forms. The median values of the four antibody concentrations in Chinese IVIg preparations were 16.53, 8.47, 24.36 and 33.25μg/mL, which were remarkably higher than that in Octagam® IVIg (1.66, 2.07, 4.61 and 4.64μg/mL). Moreover, the anti-Aβ42 oligomer antibody levels in almost all IVIg preparations were higher than the anti-Aβ42 monomer antibody, and the concentrations of anti-Aβ42 antibodies in most of the IVIg preparations were significantly higher than that of anti-Aβ40 antibodies. These findings will contribute to an increased understanding of the uniqueness of Chinese IVIg preparations, and could provide support for a trial of a Chinese IVIg product in AD patients.
Intravenous immunoglobulin (IVIg) preparations are being investigated as a potential agent for treatment or prevention of Alzheimer's disease (AD). Antibodies towards soluble β-amyloid (Aβ) contained in IVIg were considered to be the major component contributing to the beneficial effect of the preparations in pilot studies. This study compared the antibody concentrations against Aβ in Octagam IVIg (Octapharma) and 9 IVIg preparations from different Chinese manufacturers by ELISA, using Aβ40 monomer, Aβ40 soluble oligomers, Aβ42 monomer and Aβ42 soluble oligomers as the antigens. The results showed that each preparation contained different antibody levels against the four Aβ forms. The median values of the four antibody concentrations in Chinese IVIg preparations were 16.53, 8.47, 24.36 and 33.25μg/mL, which were remarkably higher than that in Octagam IVIg (1.66, 2.07, 4.61 and 4.64μg/mL). Moreover, the anti-Aβ42 oligomer antibody levels in almost all IVIg preparations were higher than the anti-Aβ42 monomer antibody, and the concentrations of anti-Aβ42 antibodies in most of the IVIg preparations were significantly higher than that of anti-Aβ40 antibodies. These findings will contribute to an increased understanding of the uniqueness of Chinese IVIg preparations, and could provide support for a trial of a Chinese IVIg product in AD patients.
Author Wang, Zongkui
Li, Changqing
Chen, Yunhua
Liu, Fengjuan
Cao, Haijun
Ma, Li
Ye, Shengliang
Jiang, Peng
Du, Xi
Yuan, Jing
Zeng, Renyong
Hou, Mingxia
Author_xml – sequence: 1
  givenname: Shengliang
  surname: Ye
  fullname: Ye, Shengliang
  email: yeshl@aliyun.com
  organization: Institute of Blood Transfusion, Chinese Academy of Medical Sciences, 26 Huacai Road, Longtan Industry Park, Chenghua District, Chengdu, 610052, China
– sequence: 2
  givenname: Renyong
  surname: Zeng
  fullname: Zeng, Renyong
  email: zengry2011@126.com
  organization: Institute of Blood Transfusion, Chinese Academy of Medical Sciences, 26 Huacai Road, Longtan Industry Park, Chenghua District, Chengdu, 610052, China
– sequence: 3
  givenname: Peng
  surname: Jiang
  fullname: Jiang, Peng
  email: pengjiang2014@163.com
  organization: Institute of Blood Transfusion, Chinese Academy of Medical Sciences, 26 Huacai Road, Longtan Industry Park, Chenghua District, Chengdu, 610052, China
– sequence: 4
  givenname: Mingxia
  surname: Hou
  fullname: Hou, Mingxia
  email: 251873769@qq.com
  organization: Institute of Blood Transfusion, Chinese Academy of Medical Sciences, 26 Huacai Road, Longtan Industry Park, Chenghua District, Chengdu, 610052, China
– sequence: 5
  givenname: Fengjuan
  surname: Liu
  fullname: Liu, Fengjuan
  email: liufengjuan110@126.com
  organization: Institute of Blood Transfusion, Chinese Academy of Medical Sciences, 26 Huacai Road, Longtan Industry Park, Chenghua District, Chengdu, 610052, China
– sequence: 6
  givenname: Zongkui
  surname: Wang
  fullname: Wang, Zongkui
  email: pumchammer@163.com
  organization: Institute of Blood Transfusion, Chinese Academy of Medical Sciences, 26 Huacai Road, Longtan Industry Park, Chenghua District, Chengdu, 610052, China
– sequence: 7
  givenname: Xi
  surname: Du
  fullname: Du, Xi
  email: shela44@163.com
  organization: Institute of Blood Transfusion, Chinese Academy of Medical Sciences, 26 Huacai Road, Longtan Industry Park, Chenghua District, Chengdu, 610052, China
– sequence: 8
  givenname: Jing
  surname: Yuan
  fullname: Yuan, Jing
  email: yuanjing@chinabiologic.com
  organization: Guizhou Taibang Biological Products Co. Ltd., 156 Daqian Road, Huaxi District, Guiyang, 550025, China
– sequence: 9
  givenname: Yunhua
  surname: Chen
  fullname: Chen, Yunhua
  email: chenyunhua@chinabiologic.com
  organization: Guizhou Taibang Biological Products Co. Ltd., 156 Daqian Road, Huaxi District, Guiyang, 550025, China
– sequence: 10
  givenname: Haijun
  surname: Cao
  fullname: Cao, Haijun
  email: chjr007@163.com
  organization: Institute of Blood Transfusion, Chinese Academy of Medical Sciences, 26 Huacai Road, Longtan Industry Park, Chenghua District, Chengdu, 610052, China
– sequence: 11
  givenname: Li
  surname: Ma
  fullname: Ma, Li
  email: mary19820225@163.com
  organization: Institute of Blood Transfusion, Chinese Academy of Medical Sciences, 26 Huacai Road, Longtan Industry Park, Chenghua District, Chengdu, 610052, China
– sequence: 12
  givenname: Changqing
  surname: Li
  fullname: Li, Changqing
  email: lichangqing268@163.com
  organization: Institute of Blood Transfusion, Chinese Academy of Medical Sciences, 26 Huacai Road, Longtan Industry Park, Chenghua District, Chengdu, 610052, China
BackLink https://www.ncbi.nlm.nih.gov/pubmed/28231531$$D View this record in MEDLINE/PubMed
BookMark eNp9kM1KJDEQx8OirKPuC-xhyXEvPSbV6U43eFkGVwXBywreQj5qZjN0J2PSLfhaPsg-02YY9SgU5INf_an6nZKjEAMS8p2zJWe8vdgutzujl8C4XDIoJb6QBe9kXUErHo_IgsmaV5J1zQk5zXnLGGt4L76SE-ig5k3NFyStYrAYpqQnH0OmcU11mLyJzmOmeqN9yBP991rp8WWI3lHBLgTQMYY4Yiqso3Hwm_0jUx_o6q8PmLFcS-QzhjiX73GcQ9wM0cxDiTsnx2s9ZPz2dp6Rh99Xf1Y31d399e3q111l66adyg6GAQfd2FabWvLWgOO8ZVrzhmMvRAfWGN50Qpq-dYwZ40CA7euOSQeuPiM_D7m7FJ9mzJMafbY4DDpgGUsVU9DItgdZUDigNsWcE67VLvlRpxfFmdq7Vlu1d632rhWDUqI0_XjLn82I7qPlXW4BLg8Ali2fPSaVrcei2_mEdlIu-s_y_wMFupNE
CitedBy_id crossref_primary_10_3390_ijms24065549
crossref_primary_10_1016_j_biologicals_2020_02_004
crossref_primary_10_2174_1567205017666200102151731
Cites_doi 10.1126/science.1072994
10.1002/ana.21475
10.1080/14737175.2016.1194203
10.1016/j.jaci.2007.11.001
10.1016/0896-6273(94)90458-8
10.1016/j.jalz.2011.02.004
10.1002/path.4491
10.1007/s10875-010-9413-6
10.1016/j.intimp.2013.04.034
10.1021/bi00139a028
10.1038/nn.4018
10.1212/WNL.0b013e3181ae7aaf
10.1038/jhg.2013.79
10.1186/alzrt272
10.1016/j.intimp.2009.10.005
10.1038/nn.3028
10.1016/S0166-2236(00)01749-5
10.1126/science.1079469
10.1016/j.intimp.2005.11.005
10.1016/j.jneuroim.2010.06.010
10.2217/imt.11.170
10.1038/nature19323
10.1002/ana.1061
10.2174/1567205011666140812113415
10.1016/j.neurobiolaging.2007.12.021
10.1126/science.1566067
10.1038/325733a0
10.3233/JAD-2010-1353
10.1016/j.neuropharm.2016.02.015
10.1016/j.jalz.2016.02.010
10.1136/jnnp.2003.033399
10.1016/j.jneumeth.2010.05.001
10.1016/j.nlm.2011.08.003
10.1074/jbc.R800016200
10.1111/j.1471-4159.1993.tb09841.x
10.1038/359325a0
10.1016/j.ebiom.2016.03.035
10.1056/NEJMra0909142
10.1016/S0923-2494(94)80072-3
10.1002/ana.10253
10.1056/NEJMoa1304839
10.1007/s10875-014-0041-4
ContentType Journal Article
Copyright 2017 Elsevier B.V.
Copyright © 2017 Elsevier B.V. All rights reserved.
Copyright_xml – notice: 2017 Elsevier B.V.
– notice: Copyright © 2017 Elsevier B.V. All rights reserved.
DBID CGR
CUY
CVF
ECM
EIF
NPM
AAYXX
CITATION
7X8
DOI 10.1016/j.jpba.2017.02.024
DatabaseName Medline
MEDLINE
MEDLINE (Ovid)
MEDLINE
MEDLINE
PubMed
CrossRef
MEDLINE - Academic
DatabaseTitle MEDLINE
Medline Complete
MEDLINE with Full Text
PubMed
MEDLINE (Ovid)
CrossRef
MEDLINE - Academic
DatabaseTitleList
MEDLINE - Academic
MEDLINE
Database_xml – sequence: 1
  dbid: ECM
  name: MEDLINE
  url: https://search.ebscohost.com/login.aspx?direct=true&db=cmedm&site=ehost-live
  sourceTypes: Index Database
DeliveryMethod fulltext_linktorsrc
Discipline Pharmacy, Therapeutics, & Pharmacology
EISSN 1873-264X
EndPage 282
ExternalDocumentID 10_1016_j_jpba_2017_02_024
28231531
S0731708516313413
Genre Journal Article
GroupedDBID ---
--K
--M
.~1
0R~
1B1
1RT
1~.
1~5
4.4
457
4G.
5GY
5VS
7-5
71M
8P~
9JM
9JN
AABNK
AACTN
AAEDT
AAEDW
AAIAV
AAIKJ
AAKOC
AALRI
AAOAW
AAQFI
AARLI
AATCM
AAXUO
ABFRF
ABJNI
ABMAC
ABYKQ
ABZDS
ACDAQ
ACGFO
ACGFS
ACIUM
ACRLP
ADBBV
ADECG
ADEZE
AEBSH
AEFWE
AEKER
AENEX
AFKWA
AFTJW
AFXIZ
AFZHZ
AGHFR
AGUBO
AGYEJ
AIEXJ
AIKHN
AITUG
AJBFU
AJOXV
AJSZI
ALCLG
ALMA_UNASSIGNED_HOLDINGS
AMFUW
AMRAJ
AXJTR
BKOJK
BLXMC
C45
CS3
DU5
EBS
EFJIC
EFLBG
EJD
EO8
EO9
EP2
EP3
F5P
FDB
FIRID
FLBIZ
FNPLU
FYGXN
G-Q
GBLVA
IHE
J1W
KOM
M34
M36
M41
MO0
N9A
O-L
O9-
OAUVE
OGGZJ
OVD
OZT
P-8
P-9
P2P
PC.
Q38
RIG
RNS
ROL
RPZ
SCC
SCH
SDF
SDG
SDP
SES
SPC
SPCBC
SSK
SSP
SSZ
T5K
TEORI
YK3
~G-
AAXKI
AKRWK
CGR
CUY
CVF
ECM
EIF
NPM
29L
53G
AAQXK
AAYXX
ABFNM
ABXDB
ACNNM
ADMUD
AFJKZ
AHHHB
AJQLL
ASPBG
AVWKF
AZFZN
CITATION
FEDTE
FGOYB
G-2
HMT
HMU
HVGLF
HZ~
R2-
SCB
SEW
SPT
WUQ
XPP
7X8
ID FETCH-LOGICAL-c356t-26b0212a5c6ab3716b2d1160aa151e94482cbb15847b96d00bbd242c93807d2d3
ISSN 0731-7085
IngestDate Fri Oct 25 23:53:17 EDT 2024
Thu Sep 26 15:48:24 EDT 2024
Sat Sep 28 08:11:09 EDT 2024
Fri Feb 23 02:25:39 EST 2024
IsPeerReviewed true
IsScholarly true
Keywords Oligomers
amyloid
Antibody
Intravenous immunoglobulin
Monomer
Alzheimer's disease
beta
Language English
License Copyright © 2017 Elsevier B.V. All rights reserved.
LinkModel OpenURL
MergedId FETCHMERGED-LOGICAL-c356t-26b0212a5c6ab3716b2d1160aa151e94482cbb15847b96d00bbd242c93807d2d3
Notes ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
PMID 28231531
PQID 1872576927
PQPubID 23479
PageCount 6
ParticipantIDs proquest_miscellaneous_1872576927
crossref_primary_10_1016_j_jpba_2017_02_024
pubmed_primary_28231531
elsevier_sciencedirect_doi_10_1016_j_jpba_2017_02_024
PublicationCentury 2000
PublicationDate 2017-05-10
PublicationDateYYYYMMDD 2017-05-10
PublicationDate_xml – month: 05
  year: 2017
  text: 2017-05-10
  day: 10
PublicationDecade 2010
PublicationPlace England
PublicationPlace_xml – name: England
PublicationTitle Journal of pharmaceutical and biomedical analysis
PublicationTitleAlternate J Pharm Biomed Anal
PublicationYear 2017
Publisher Elsevier B.V
Publisher_xml – name: Elsevier B.V
References Balakrishnan, Andrei-Selmer, Selmer, Bacher, Dodel (bib0105) 2010; 20
Sengupta, Nilson, Kayed (bib0040) 2016; 6
Puli, Tanila, Relkin (bib0095) 2014; 11
Hardy, Higgins (bib0020) 1992; 256
Relkin, Szabo, Adamiak, Burgut, Monthe, Lent, Younkin, Younkin, Schiff, Weksler (bib0135) 2009; 30
Iwatsubo, Odaka, Suzuki, Mizusawa, Nukina, Ihara (bib0190) 1994; 13
Sun, Zhou, Huang, Liu, Lin, Yu, Huang, Chu, Yang (bib0200) 2013; 58
Relkin (bib0215) 2014; 34
Sevigny, Chiao, Bussiere, Weinreb, Williams, Maier, Dunstan, Salloway, Chen, Ling, O'Gorman, Qian, Arastu, Li, Chollate, Brennan, Quintero-Monzon, Scannevin, Arnold, Engber, Rhodes, Ferrero, Hang, Mikulskis, Grimm, Hock, Nitsch, Sandrock (bib0070) 2016; 537
Loeffler (bib0100) 2014; 11
Panza, Frisardi, Solfrizzi, Imbimbo, Logroscino, Santamato, Greco, Seripa, Pilotto (bib0065) 2012; 4
Paquet, Amin, Mouton-Liger, Nasser, Love, Gray, Pickering, Nicoll, Holmes, Hugon, Boche (bib0050) 2015; 235
Querfurth, LaFerla (bib0005) 2010; 362
Klaver, Finke, Digambaranath, Balasubramaniam, Loeffler (bib0110) 2010; 10
Wang, Xie, Ji, Wang, Zha, Zhou, Yu, Wei, Ma, Xi, Pang, Liu (bib0170) 2016; 105
Calsolaro, Edison (bib0010) 2016; 12
Hardy, Selkoe (bib0025) 2002; 297
Kayed, Head, Thompson, McIntire, Milton, Cotman, Glabe (bib0150) 2003; 300
Dodel, Du, Depboylu, Hampel, Frolich, Haag, Hemmeter, Paulsen, Teipel, Brettschneider, Spottke, Nolker, Moller, Wei, Farlow, Sommer, Oertel (bib0090) 2004; 75
Martin (bib0210) 2006; 6
Seubert, Vigo-Pelfrey, Esch, Lee, Dovey, Davis, Sinha, Schlossmacher, Whaley, Swindlehurst (bib0180) 1992; 359
O'Nuallain, Williams, McWilliams-Koeppen, Acero, Weber, Ehrlich, Schwarz, Solomon (bib0160) 2010; 30
Lejtenyi, Mazer (bib0195) 2008; 121
Amanatkar, Papagiannopoulos, Grossberg (bib0220) 2017; 17
Shingala, Rajyaguru (bib0125) 2015; 2
Goure, Krafft, Jerecic, Hefti (bib0045) 2014; 6
Salloway, Sperling, Fox, Blennow, Klunk, Raskind, Sabbagh, Honig, Porsteinsson, Ferris, Reichert, Ketter, Nejadnik, Guenzler, Miloslavsky, Wang, Lu, Lull, Tudor, Liu, Grundman, Yuen, Black, Brashear (bib0060) 2014; 370
Kellner, Matschke, Bernreuther, Moch, Ferrer, Glatzel (bib0085) 2009; 65
Smith, Coffey, Klaver, Loeffler (bib0120) 2013; 16
Zagorski, Barrow (bib0130) 1992; 31
Ryan, Narrow, Federoff, Bowers (bib0115) 2010; 190
Vigo-Pelfrey, Lee, Keim, Lieberburg, Schenk (bib0185) 1993; 61
Benilova, Karran, De Strooper (bib0035) 2012; 15
Glabe (bib0155) 2008; 283
Szabo, Mujalli, Rotondi, Sharma, Weber, Schwarz, Weksler, Relkin (bib0165) 2010; 227
Alzheimer's Association (bib0015) 2011; 7
Ferreira, Klein (bib0145) 2011; 96
Dodel, Hampel, Depboylu, Lin, Gao, Schock, Jackel, Wei, Buerger, Hoft, Hemmer, Moller, Farlow, Oertel, Sommer, Du (bib0080) 2002; 52
Labrousse, Adib-Conquy, Avrameas (bib0205) 1994; 145
Hyman, Smith, Buldyrev, Whelan, Brown, Tang, Mayeux (bib0075) 2001; 49
Fillit, Hess, Hill, Bonnet, Toso (bib0140) 2009; 73
Kang, Lemaire, Unterbeck, Salbaum, Masters, Grzeschik, Multhaup, Beyreuther, Muller-Hill (bib0175) 1987; 325
Musiek, Holtzman (bib0030) 2015; 18
Klein, Krafft, Finch (bib0055) 2001; 24
Hardy (10.1016/j.jpba.2017.02.024_bib0025) 2002; 297
Wang (10.1016/j.jpba.2017.02.024_bib0170) 2016; 105
Balakrishnan (10.1016/j.jpba.2017.02.024_bib0105) 2010; 20
Kellner (10.1016/j.jpba.2017.02.024_bib0085) 2009; 65
Shingala (10.1016/j.jpba.2017.02.024_bib0125) 2015; 2
Querfurth (10.1016/j.jpba.2017.02.024_bib0005) 2010; 362
Ferreira (10.1016/j.jpba.2017.02.024_bib0145) 2011; 96
Vigo-Pelfrey (10.1016/j.jpba.2017.02.024_bib0185) 1993; 61
Dodel (10.1016/j.jpba.2017.02.024_bib0090) 2004; 75
Goure (10.1016/j.jpba.2017.02.024_bib0045) 2014; 6
Klaver (10.1016/j.jpba.2017.02.024_bib0110) 2010; 10
Iwatsubo (10.1016/j.jpba.2017.02.024_bib0190) 1994; 13
Lejtenyi (10.1016/j.jpba.2017.02.024_bib0195) 2008; 121
Fillit (10.1016/j.jpba.2017.02.024_bib0140) 2009; 73
Smith (10.1016/j.jpba.2017.02.024_bib0120) 2013; 16
Zagorski (10.1016/j.jpba.2017.02.024_bib0130) 1992; 31
Kayed (10.1016/j.jpba.2017.02.024_bib0150) 2003; 300
Calsolaro (10.1016/j.jpba.2017.02.024_bib0010) 2016; 12
Ryan (10.1016/j.jpba.2017.02.024_bib0115) 2010; 190
Puli (10.1016/j.jpba.2017.02.024_bib0095) 2014; 11
Musiek (10.1016/j.jpba.2017.02.024_bib0030) 2015; 18
Benilova (10.1016/j.jpba.2017.02.024_bib0035) 2012; 15
Sevigny (10.1016/j.jpba.2017.02.024_bib0070) 2016; 537
Klein (10.1016/j.jpba.2017.02.024_bib0055) 2001; 24
O'Nuallain (10.1016/j.jpba.2017.02.024_bib0160) 2010; 30
Loeffler (10.1016/j.jpba.2017.02.024_bib0100) 2014; 11
Martin (10.1016/j.jpba.2017.02.024_bib0210) 2006; 6
Relkin (10.1016/j.jpba.2017.02.024_bib0215) 2014; 34
Szabo (10.1016/j.jpba.2017.02.024_bib0165) 2010; 227
Sun (10.1016/j.jpba.2017.02.024_bib0200) 2013; 58
Amanatkar (10.1016/j.jpba.2017.02.024_bib0220) 2017; 17
Glabe (10.1016/j.jpba.2017.02.024_bib0155) 2008; 283
Alzheimer's Association (10.1016/j.jpba.2017.02.024_bib0015) 2011; 7
Salloway (10.1016/j.jpba.2017.02.024_bib0060) 2014; 370
Panza (10.1016/j.jpba.2017.02.024_bib0065) 2012; 4
Relkin (10.1016/j.jpba.2017.02.024_bib0135) 2009; 30
Kang (10.1016/j.jpba.2017.02.024_bib0175) 1987; 325
Hyman (10.1016/j.jpba.2017.02.024_bib0075) 2001; 49
Seubert (10.1016/j.jpba.2017.02.024_bib0180) 1992; 359
Paquet (10.1016/j.jpba.2017.02.024_bib0050) 2015; 235
Hardy (10.1016/j.jpba.2017.02.024_bib0020) 1992; 256
Sengupta (10.1016/j.jpba.2017.02.024_bib0040) 2016; 6
Dodel (10.1016/j.jpba.2017.02.024_bib0080) 2002; 52
Labrousse (10.1016/j.jpba.2017.02.024_bib0205) 1994; 145
References_xml – volume: 227
  start-page: 167
  year: 2010
  end-page: 174
  ident: bib0165
  article-title: Measurement of anti-beta amyloid antibodies in human blood
  publication-title: J. Neuroimmunol.
  contributor:
    fullname: Relkin
– volume: 370
  start-page: 322
  year: 2014
  end-page: 333
  ident: bib0060
  article-title: Two phase 3 trials of bapineuzumab in mild-to-moderate Alzheimer's disease
  publication-title: N. Engl. J. Med.
  contributor:
    fullname: Brashear
– volume: 30
  start-page: 1728
  year: 2009
  end-page: 1736
  ident: bib0135
  article-title: 18-Month study of intravenous immunoglobulin for treatment of mild Alzheimer disease
  publication-title: Neurobiol. Aging
  contributor:
    fullname: Weksler
– volume: 256
  start-page: 184
  year: 1992
  end-page: 185
  ident: bib0020
  article-title: Alzheimer's disease: the amyloid cascade hypothesis
  publication-title: Science (New York, N.Y.)
  contributor:
    fullname: Higgins
– volume: 105
  start-page: 561
  year: 2016
  end-page: 576
  ident: bib0170
  article-title: Naturally occurring autoantibodies against Abeta oligomers exhibited more beneficial effects in the treatment of mouse model of Alzheimer's disease than intravenous immunoglobulin
  publication-title: Neuropharmacology
  contributor:
    fullname: Liu
– volume: 58
  start-page: 686
  year: 2013
  end-page: 693
  ident: bib0200
  article-title: Correlation between the linguistic affinity and genetic diversity of Chinese ethnic groups
  publication-title: J. Hum. Genet.
  contributor:
    fullname: Yang
– volume: 300
  start-page: 486
  year: 2003
  end-page: 489
  ident: bib0150
  article-title: Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
  publication-title: Science (New York, N.Y.)
  contributor:
    fullname: Glabe
– volume: 20
  start-page: 135
  year: 2010
  end-page: 143
  ident: bib0105
  article-title: Comparison of intravenous immunoglobulins for naturally occurring autoantibodies against amyloid-beta
  publication-title: J. Alzheimer's Dis.
  contributor:
    fullname: Dodel
– volume: 73
  start-page: 180
  year: 2009
  end-page: 185
  ident: bib0140
  article-title: IV immunoglobulin is associated with a reduced risk of Alzheimer disease and related disorders
  publication-title: Neurology
  contributor:
    fullname: Toso
– volume: 145
  start-page: 541
  year: 1994
  end-page: 552
  ident: bib0205
  article-title: Effects of pH or ionic strength on the reactivities of mono- and polyspecific IgG antibodies
  publication-title: Res. Immunol.
  contributor:
    fullname: Avrameas
– volume: 11
  start-page: 198
  year: 2014
  ident: bib0100
  article-title: Should development of Alzheimer's disease-specific intravenous immunoglobulin be considered?
  publication-title: J. Neuroinflamm.
  contributor:
    fullname: Loeffler
– volume: 75
  start-page: 1472
  year: 2004
  end-page: 1474
  ident: bib0090
  article-title: Intravenous immunoglobulins containing antibodies against beta-amyloid for the treatment of Alzheimer's disease
  publication-title: J. Neurol. Neurosurg. Psychiatry
  contributor:
    fullname: Oertel
– volume: 96
  start-page: 529
  year: 2011
  end-page: 543
  ident: bib0145
  article-title: The Abeta oligomer hypothesis for synapse failure and memory loss in Alzheimer's disease
  publication-title: Neurobiol. Learn. Mem.
  contributor:
    fullname: Klein
– volume: 283
  start-page: 29639
  year: 2008
  end-page: 29643
  ident: bib0155
  article-title: Structural classification of toxic amyloid oligomers
  publication-title: J. Biol. Chem.
  contributor:
    fullname: Glabe
– volume: 190
  start-page: 171
  year: 2010
  end-page: 179
  ident: bib0115
  article-title: An improved method for generating consistent soluble amyloid-beta oligomer preparations for in vitro neurotoxicity studies
  publication-title: J. Neurosci. Methods
  contributor:
    fullname: Bowers
– volume: 297
  start-page: 353
  year: 2002
  end-page: 356
  ident: bib0025
  article-title: The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics
  publication-title: Science (New York, N.Y.)
  contributor:
    fullname: Selkoe
– volume: 325
  start-page: 733
  year: 1987
  end-page: 736
  ident: bib0175
  article-title: The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor
  publication-title: Nature
  contributor:
    fullname: Muller-Hill
– volume: 16
  start-page: 424
  year: 2013
  end-page: 428
  ident: bib0120
  article-title: Intravenous immunoglobulin products contain specific antibodies to recombinant human tau protein
  publication-title: Int. Immunopharmacol.
  contributor:
    fullname: Loeffler
– volume: 2
  start-page: 22
  year: 2015
  end-page: 33
  ident: bib0125
  article-title: Comparison of post hoc tests for unequal variance
  publication-title: Int. J. New Technol. Sci. Eng.
  contributor:
    fullname: Rajyaguru
– volume: 34
  start-page: S74
  year: 2014
  end-page: 79
  ident: bib0215
  article-title: Clinical trials of intravenous immunoglobulin for Alzheimer's disease
  publication-title: J. Clin. Immunol.
  contributor:
    fullname: Relkin
– volume: 15
  start-page: 349
  year: 2012
  end-page: 357
  ident: bib0035
  article-title: The toxic Abeta oligomer and Alzheimer's disease: an emperor in need of clothes
  publication-title: Nat. Neurosci.
  contributor:
    fullname: De Strooper
– volume: 235
  start-page: 721
  year: 2015
  end-page: 730
  ident: bib0050
  article-title: Effect of active Abeta immunotherapy on neurons in human Alzheimer's disease
  publication-title: J. Pathol.
  contributor:
    fullname: Boche
– volume: 537
  start-page: 50
  year: 2016
  end-page: 56
  ident: bib0070
  article-title: The antibody aducanumab reduces Abeta plaques in Alzheimer's disease
  publication-title: Nature
  contributor:
    fullname: Sandrock
– volume: 6
  start-page: 42
  year: 2016
  end-page: 49
  ident: bib0040
  article-title: The role of amyloid-beta oligomers in toxicity, propagation, and immunotherapy
  publication-title: EBioMedicine
  contributor:
    fullname: Kayed
– volume: 6
  start-page: 42
  year: 2014
  ident: bib0045
  article-title: Targeting the proper amyloid-beta neuronal toxins: a path forward for Alzheimer's disease immunotherapeutics
  publication-title: Alzheimer's Res. Therapy
  contributor:
    fullname: Hefti
– volume: 30
  start-page: S37
  year: 2010
  end-page: 42
  ident: bib0160
  article-title: Anti-amyloidogenic activity of IgGs contained in normal plasma
  publication-title: J. Clin. Immunol.
  contributor:
    fullname: Solomon
– volume: 6
  start-page: 517
  year: 2006
  end-page: 522
  ident: bib0210
  article-title: IGIV: contents, properties, and methods of industrial production-evolving closer to a more physiologic product
  publication-title: Int. Immunopharmacol.
  contributor:
    fullname: Martin
– volume: 12
  start-page: 719
  year: 2016
  end-page: 732
  ident: bib0010
  article-title: Neuroinflammation in Alzheimer's disease: current evidence and future directions
  publication-title: Alzheimer's Dement.: J. Alzheimer's Assoc.
  contributor:
    fullname: Edison
– volume: 11
  start-page: 626
  year: 2014
  end-page: 636
  ident: bib0095
  article-title: Intravenous immunoglobulins for Alzheimer's disease
  publication-title: Curr. Alzheimer Res.
  contributor:
    fullname: Relkin
– volume: 359
  start-page: 325
  year: 1992
  end-page: 327
  ident: bib0180
  article-title: Isolation and quantification of soluble Alzheimer's beta-peptide from biological fluids
  publication-title: Nature
  contributor:
    fullname: Swindlehurst
– volume: 31
  start-page: 5621
  year: 1992
  end-page: 5631
  ident: bib0130
  article-title: NMR studies of amyloid beta-peptides: proton assignments, secondary structure, and mechanism of an alpha-helix--beta-sheet conversion for a homologous, 28-residue, N-terminal fragment
  publication-title: Biochemistry
  contributor:
    fullname: Barrow
– volume: 24
  start-page: 219
  year: 2001
  end-page: 224
  ident: bib0055
  article-title: Targeting small Abeta oligomers: the solution to an Alzheimer's disease conundrum?
  publication-title: Trends Neurosci.
  contributor:
    fullname: Finch
– volume: 49
  start-page: 808
  year: 2001
  end-page: 810
  ident: bib0075
  article-title: Autoantibodies to amyloid-beta and Alzheimer's disease
  publication-title: Ann. Neurol.
  contributor:
    fullname: Mayeux
– volume: 65
  start-page: 24
  year: 2009
  end-page: 31
  ident: bib0085
  article-title: Autoantibodies against beta-amyloid are common in Alzheimer's disease and help control plaque burden
  publication-title: Ann. Neurol.
  contributor:
    fullname: Glatzel
– volume: 52
  start-page: 253
  year: 2002
  end-page: 256
  ident: bib0080
  article-title: Human antibodies against amyloid beta peptide: a potential treatment for Alzheimer's disease
  publication-title: Ann. Neurol.
  contributor:
    fullname: Du
– volume: 61
  start-page: 1965
  year: 1993
  end-page: 1968
  ident: bib0185
  article-title: Characterization of beta-amyloid peptide from human cerebrospinal fluid
  publication-title: J. Neurochem.
  contributor:
    fullname: Schenk
– volume: 121
  start-page: 254
  year: 2008
  end-page: 255
  ident: bib0195
  article-title: Consistency of protective antibody levels across lots of intravenous immunoglobulin preparations
  publication-title: J. Allergy Clin. Immunol.
  contributor:
    fullname: Mazer
– volume: 18
  start-page: 800
  year: 2015
  end-page: 806
  ident: bib0030
  article-title: Three dimensions of the amyloid hypothesis: time, space and ‘wingmen'
  publication-title: Nat. Neurosci.
  contributor:
    fullname: Holtzman
– volume: 17
  start-page: 7
  year: 2017
  end-page: 16
  ident: bib0220
  article-title: Analysis of recent failures of disease modifying therapies in Alzheimer's disease suggesting a new methodology for future studies
  publication-title: Expert Rev. Neurother.
  contributor:
    fullname: Grossberg
– volume: 4
  start-page: 213
  year: 2012
  end-page: 238
  ident: bib0065
  article-title: Immunotherapy for Alzheimer's disease: from anti-beta-amyloid to tau-based immunization strategies
  publication-title: Immunotherapy
  contributor:
    fullname: Pilotto
– volume: 13
  start-page: 45
  year: 1994
  end-page: 53
  ident: bib0190
  article-title: Visualization of A beta 42(43) and A beta 40 in senile plaques with end-specific A beta monoclonals: evidence that an initially deposited species is A beta 42(43)
  publication-title: Neuron
  contributor:
    fullname: Ihara
– volume: 362
  start-page: 329
  year: 2010
  end-page: 344
  ident: bib0005
  article-title: Alzheimer's disease
  publication-title: N. Engl. J. Med.
  contributor:
    fullname: LaFerla
– volume: 7
  start-page: 208
  year: 2011
  end-page: 244
  ident: bib0015
  article-title: Alzheimer's disease facts and figures
  publication-title: Alzheimer's Dement.: J. Alzheimer's Assoc.
  contributor:
    fullname: Alzheimer's Association
– volume: 10
  start-page: 115
  year: 2010
  end-page: 119
  ident: bib0110
  article-title: Antibody concentrations to Abeta1-42 monomer and soluble oligomers in untreated and antibody-antigen-dissociated intravenous immunoglobulin preparations
  publication-title: Int. Immunopharmacol.
  contributor:
    fullname: Loeffler
– volume: 297
  start-page: 353
  year: 2002
  ident: 10.1016/j.jpba.2017.02.024_bib0025
  article-title: The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics
  publication-title: Science (New York, N.Y.)
  doi: 10.1126/science.1072994
  contributor:
    fullname: Hardy
– volume: 65
  start-page: 24
  year: 2009
  ident: 10.1016/j.jpba.2017.02.024_bib0085
  article-title: Autoantibodies against beta-amyloid are common in Alzheimer's disease and help control plaque burden
  publication-title: Ann. Neurol.
  doi: 10.1002/ana.21475
  contributor:
    fullname: Kellner
– volume: 17
  start-page: 7
  year: 2017
  ident: 10.1016/j.jpba.2017.02.024_bib0220
  article-title: Analysis of recent failures of disease modifying therapies in Alzheimer's disease suggesting a new methodology for future studies
  publication-title: Expert Rev. Neurother.
  doi: 10.1080/14737175.2016.1194203
  contributor:
    fullname: Amanatkar
– volume: 121
  start-page: 254
  year: 2008
  ident: 10.1016/j.jpba.2017.02.024_bib0195
  article-title: Consistency of protective antibody levels across lots of intravenous immunoglobulin preparations
  publication-title: J. Allergy Clin. Immunol.
  doi: 10.1016/j.jaci.2007.11.001
  contributor:
    fullname: Lejtenyi
– volume: 13
  start-page: 45
  year: 1994
  ident: 10.1016/j.jpba.2017.02.024_bib0190
  article-title: Visualization of A beta 42(43) and A beta 40 in senile plaques with end-specific A beta monoclonals: evidence that an initially deposited species is A beta 42(43)
  publication-title: Neuron
  doi: 10.1016/0896-6273(94)90458-8
  contributor:
    fullname: Iwatsubo
– volume: 7
  start-page: 208
  issue: 2011
  year: 2011
  ident: 10.1016/j.jpba.2017.02.024_bib0015
  article-title: Alzheimer's disease facts and figures
  publication-title: Alzheimer's Dement.: J. Alzheimer's Assoc.
  doi: 10.1016/j.jalz.2011.02.004
  contributor:
    fullname: Alzheimer's Association
– volume: 235
  start-page: 721
  year: 2015
  ident: 10.1016/j.jpba.2017.02.024_bib0050
  article-title: Effect of active Abeta immunotherapy on neurons in human Alzheimer's disease
  publication-title: J. Pathol.
  doi: 10.1002/path.4491
  contributor:
    fullname: Paquet
– volume: 30
  start-page: S37
  issue: Suppl. 1
  year: 2010
  ident: 10.1016/j.jpba.2017.02.024_bib0160
  article-title: Anti-amyloidogenic activity of IgGs contained in normal plasma
  publication-title: J. Clin. Immunol.
  doi: 10.1007/s10875-010-9413-6
  contributor:
    fullname: O'Nuallain
– volume: 16
  start-page: 424
  year: 2013
  ident: 10.1016/j.jpba.2017.02.024_bib0120
  article-title: Intravenous immunoglobulin products contain specific antibodies to recombinant human tau protein
  publication-title: Int. Immunopharmacol.
  doi: 10.1016/j.intimp.2013.04.034
  contributor:
    fullname: Smith
– volume: 31
  start-page: 5621
  year: 1992
  ident: 10.1016/j.jpba.2017.02.024_bib0130
  article-title: NMR studies of amyloid beta-peptides: proton assignments, secondary structure, and mechanism of an alpha-helix--beta-sheet conversion for a homologous, 28-residue, N-terminal fragment
  publication-title: Biochemistry
  doi: 10.1021/bi00139a028
  contributor:
    fullname: Zagorski
– volume: 18
  start-page: 800
  year: 2015
  ident: 10.1016/j.jpba.2017.02.024_bib0030
  article-title: Three dimensions of the amyloid hypothesis: time, space and ‘wingmen'
  publication-title: Nat. Neurosci.
  doi: 10.1038/nn.4018
  contributor:
    fullname: Musiek
– volume: 73
  start-page: 180
  year: 2009
  ident: 10.1016/j.jpba.2017.02.024_bib0140
  article-title: IV immunoglobulin is associated with a reduced risk of Alzheimer disease and related disorders
  publication-title: Neurology
  doi: 10.1212/WNL.0b013e3181ae7aaf
  contributor:
    fullname: Fillit
– volume: 58
  start-page: 686
  year: 2013
  ident: 10.1016/j.jpba.2017.02.024_bib0200
  article-title: Correlation between the linguistic affinity and genetic diversity of Chinese ethnic groups
  publication-title: J. Hum. Genet.
  doi: 10.1038/jhg.2013.79
  contributor:
    fullname: Sun
– volume: 6
  start-page: 42
  year: 2014
  ident: 10.1016/j.jpba.2017.02.024_bib0045
  article-title: Targeting the proper amyloid-beta neuronal toxins: a path forward for Alzheimer's disease immunotherapeutics
  publication-title: Alzheimer's Res. Therapy
  doi: 10.1186/alzrt272
  contributor:
    fullname: Goure
– volume: 10
  start-page: 115
  year: 2010
  ident: 10.1016/j.jpba.2017.02.024_bib0110
  article-title: Antibody concentrations to Abeta1-42 monomer and soluble oligomers in untreated and antibody-antigen-dissociated intravenous immunoglobulin preparations
  publication-title: Int. Immunopharmacol.
  doi: 10.1016/j.intimp.2009.10.005
  contributor:
    fullname: Klaver
– volume: 15
  start-page: 349
  year: 2012
  ident: 10.1016/j.jpba.2017.02.024_bib0035
  article-title: The toxic Abeta oligomer and Alzheimer's disease: an emperor in need of clothes
  publication-title: Nat. Neurosci.
  doi: 10.1038/nn.3028
  contributor:
    fullname: Benilova
– volume: 24
  start-page: 219
  year: 2001
  ident: 10.1016/j.jpba.2017.02.024_bib0055
  article-title: Targeting small Abeta oligomers: the solution to an Alzheimer's disease conundrum?
  publication-title: Trends Neurosci.
  doi: 10.1016/S0166-2236(00)01749-5
  contributor:
    fullname: Klein
– volume: 300
  start-page: 486
  year: 2003
  ident: 10.1016/j.jpba.2017.02.024_bib0150
  article-title: Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
  publication-title: Science (New York, N.Y.)
  doi: 10.1126/science.1079469
  contributor:
    fullname: Kayed
– volume: 2
  start-page: 22
  year: 2015
  ident: 10.1016/j.jpba.2017.02.024_bib0125
  article-title: Comparison of post hoc tests for unequal variance
  publication-title: Int. J. New Technol. Sci. Eng.
  contributor:
    fullname: Shingala
– volume: 6
  start-page: 517
  year: 2006
  ident: 10.1016/j.jpba.2017.02.024_bib0210
  article-title: IGIV: contents, properties, and methods of industrial production-evolving closer to a more physiologic product
  publication-title: Int. Immunopharmacol.
  doi: 10.1016/j.intimp.2005.11.005
  contributor:
    fullname: Martin
– volume: 227
  start-page: 167
  year: 2010
  ident: 10.1016/j.jpba.2017.02.024_bib0165
  article-title: Measurement of anti-beta amyloid antibodies in human blood
  publication-title: J. Neuroimmunol.
  doi: 10.1016/j.jneuroim.2010.06.010
  contributor:
    fullname: Szabo
– volume: 4
  start-page: 213
  year: 2012
  ident: 10.1016/j.jpba.2017.02.024_bib0065
  article-title: Immunotherapy for Alzheimer's disease: from anti-beta-amyloid to tau-based immunization strategies
  publication-title: Immunotherapy
  doi: 10.2217/imt.11.170
  contributor:
    fullname: Panza
– volume: 537
  start-page: 50
  year: 2016
  ident: 10.1016/j.jpba.2017.02.024_bib0070
  article-title: The antibody aducanumab reduces Abeta plaques in Alzheimer's disease
  publication-title: Nature
  doi: 10.1038/nature19323
  contributor:
    fullname: Sevigny
– volume: 49
  start-page: 808
  issue: 6
  year: 2001
  ident: 10.1016/j.jpba.2017.02.024_bib0075
  article-title: Autoantibodies to amyloid-beta and Alzheimer's disease
  publication-title: Ann. Neurol.
  doi: 10.1002/ana.1061
  contributor:
    fullname: Hyman
– volume: 11
  start-page: 626
  year: 2014
  ident: 10.1016/j.jpba.2017.02.024_bib0095
  article-title: Intravenous immunoglobulins for Alzheimer's disease
  publication-title: Curr. Alzheimer Res.
  doi: 10.2174/1567205011666140812113415
  contributor:
    fullname: Puli
– volume: 30
  start-page: 1728
  year: 2009
  ident: 10.1016/j.jpba.2017.02.024_bib0135
  article-title: 18-Month study of intravenous immunoglobulin for treatment of mild Alzheimer disease
  publication-title: Neurobiol. Aging
  doi: 10.1016/j.neurobiolaging.2007.12.021
  contributor:
    fullname: Relkin
– volume: 256
  start-page: 184
  year: 1992
  ident: 10.1016/j.jpba.2017.02.024_bib0020
  article-title: Alzheimer's disease: the amyloid cascade hypothesis
  publication-title: Science (New York, N.Y.)
  doi: 10.1126/science.1566067
  contributor:
    fullname: Hardy
– volume: 325
  start-page: 733
  year: 1987
  ident: 10.1016/j.jpba.2017.02.024_bib0175
  article-title: The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor
  publication-title: Nature
  doi: 10.1038/325733a0
  contributor:
    fullname: Kang
– volume: 11
  start-page: 198
  year: 2014
  ident: 10.1016/j.jpba.2017.02.024_bib0100
  article-title: Should development of Alzheimer's disease-specific intravenous immunoglobulin be considered?
  publication-title: J. Neuroinflamm.
  contributor:
    fullname: Loeffler
– volume: 20
  start-page: 135
  year: 2010
  ident: 10.1016/j.jpba.2017.02.024_bib0105
  article-title: Comparison of intravenous immunoglobulins for naturally occurring autoantibodies against amyloid-beta
  publication-title: J. Alzheimer's Dis.
  doi: 10.3233/JAD-2010-1353
  contributor:
    fullname: Balakrishnan
– volume: 105
  start-page: 561
  year: 2016
  ident: 10.1016/j.jpba.2017.02.024_bib0170
  article-title: Naturally occurring autoantibodies against Abeta oligomers exhibited more beneficial effects in the treatment of mouse model of Alzheimer's disease than intravenous immunoglobulin
  publication-title: Neuropharmacology
  doi: 10.1016/j.neuropharm.2016.02.015
  contributor:
    fullname: Wang
– volume: 12
  start-page: 719
  issue: 6
  year: 2016
  ident: 10.1016/j.jpba.2017.02.024_bib0010
  article-title: Neuroinflammation in Alzheimer's disease: current evidence and future directions
  publication-title: Alzheimer's Dement.: J. Alzheimer's Assoc.
  doi: 10.1016/j.jalz.2016.02.010
  contributor:
    fullname: Calsolaro
– volume: 75
  start-page: 1472
  year: 2004
  ident: 10.1016/j.jpba.2017.02.024_bib0090
  article-title: Intravenous immunoglobulins containing antibodies against beta-amyloid for the treatment of Alzheimer's disease
  publication-title: J. Neurol. Neurosurg. Psychiatry
  doi: 10.1136/jnnp.2003.033399
  contributor:
    fullname: Dodel
– volume: 190
  start-page: 171
  year: 2010
  ident: 10.1016/j.jpba.2017.02.024_bib0115
  article-title: An improved method for generating consistent soluble amyloid-beta oligomer preparations for in vitro neurotoxicity studies
  publication-title: J. Neurosci. Methods
  doi: 10.1016/j.jneumeth.2010.05.001
  contributor:
    fullname: Ryan
– volume: 96
  start-page: 529
  year: 2011
  ident: 10.1016/j.jpba.2017.02.024_bib0145
  article-title: The Abeta oligomer hypothesis for synapse failure and memory loss in Alzheimer's disease
  publication-title: Neurobiol. Learn. Mem.
  doi: 10.1016/j.nlm.2011.08.003
  contributor:
    fullname: Ferreira
– volume: 283
  start-page: 29639
  year: 2008
  ident: 10.1016/j.jpba.2017.02.024_bib0155
  article-title: Structural classification of toxic amyloid oligomers
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.R800016200
  contributor:
    fullname: Glabe
– volume: 61
  start-page: 1965
  year: 1993
  ident: 10.1016/j.jpba.2017.02.024_bib0185
  article-title: Characterization of beta-amyloid peptide from human cerebrospinal fluid
  publication-title: J. Neurochem.
  doi: 10.1111/j.1471-4159.1993.tb09841.x
  contributor:
    fullname: Vigo-Pelfrey
– volume: 359
  start-page: 325
  year: 1992
  ident: 10.1016/j.jpba.2017.02.024_bib0180
  article-title: Isolation and quantification of soluble Alzheimer's beta-peptide from biological fluids
  publication-title: Nature
  doi: 10.1038/359325a0
  contributor:
    fullname: Seubert
– volume: 6
  start-page: 42
  year: 2016
  ident: 10.1016/j.jpba.2017.02.024_bib0040
  article-title: The role of amyloid-beta oligomers in toxicity, propagation, and immunotherapy
  publication-title: EBioMedicine
  doi: 10.1016/j.ebiom.2016.03.035
  contributor:
    fullname: Sengupta
– volume: 362
  start-page: 329
  year: 2010
  ident: 10.1016/j.jpba.2017.02.024_bib0005
  article-title: Alzheimer's disease
  publication-title: N. Engl. J. Med.
  doi: 10.1056/NEJMra0909142
  contributor:
    fullname: Querfurth
– volume: 145
  start-page: 541
  year: 1994
  ident: 10.1016/j.jpba.2017.02.024_bib0205
  article-title: Effects of pH or ionic strength on the reactivities of mono- and polyspecific IgG antibodies
  publication-title: Res. Immunol.
  doi: 10.1016/S0923-2494(94)80072-3
  contributor:
    fullname: Labrousse
– volume: 52
  start-page: 253
  year: 2002
  ident: 10.1016/j.jpba.2017.02.024_bib0080
  article-title: Human antibodies against amyloid beta peptide: a potential treatment for Alzheimer's disease
  publication-title: Ann. Neurol.
  doi: 10.1002/ana.10253
  contributor:
    fullname: Dodel
– volume: 370
  start-page: 322
  year: 2014
  ident: 10.1016/j.jpba.2017.02.024_bib0060
  article-title: Two phase 3 trials of bapineuzumab in mild-to-moderate Alzheimer's disease
  publication-title: N. Engl. J. Med.
  doi: 10.1056/NEJMoa1304839
  contributor:
    fullname: Salloway
– volume: 34
  start-page: S74
  issue: Suppl. 1
  year: 2014
  ident: 10.1016/j.jpba.2017.02.024_bib0215
  article-title: Clinical trials of intravenous immunoglobulin for Alzheimer's disease
  publication-title: J. Clin. Immunol.
  doi: 10.1007/s10875-014-0041-4
  contributor:
    fullname: Relkin
SSID ssj0005194
Score 2.258266
Snippet •Anti-Aβ antibody levels in Chinese IVIgs were markedly higher than in Octagam®.•Chinese IVIgs have different antibody concentrations to different Aβ...
Intravenous immunoglobulin (IVIg) preparations are being investigated as a potential agent for treatment or prevention of Alzheimer's disease (AD). Antibodies...
SourceID proquest
crossref
pubmed
elsevier
SourceType Aggregation Database
Index Database
Publisher
StartPage 277
SubjectTerms Alzheimer Disease - immunology
Alzheimer's disease
amyloid
Amyloid beta-Peptides - immunology
Antibodies - immunology
Antibody
beta
China
Enzyme-Linked Immunosorbent Assay - methods
Immunoglobulins, Intravenous - immunology
Intravenous immunoglobulin
Monomer
Oligomers
Peptide Fragments - immunology
Title Concentrations of antibodies against β-amyloid 40/42 monomer and oligomers in Chinese intravenous immunoglobulins
URI https://dx.doi.org/10.1016/j.jpba.2017.02.024
https://www.ncbi.nlm.nih.gov/pubmed/28231531
https://search.proquest.com/docview/1872576927
Volume 138
hasFullText 1
inHoldings 1
isFullTextHit
isPrint
link http://sdu.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwtV3da9swEBdp-7KXse9lX2iw9sV1Z8uyHT92WUbXhxHWDPJmJEtOHVo7NAks_9b-kP1Nu7PkuEnJ2AaDYGzhD6Hf5XQ63f2OkHc8ynkW-JmbB0ng8iiL3USHgRv2tK88pZGCD10XF_GXce_jgA86naZGXdv2X5GGNsAaM2f_Au31S6EBzgFzOALqcPwj3PuYh1haMtw6TgPGrpAVRgs6YiIKsAedw_7g8ANzxTUs1wvlcIz_48y5xgwHbaIqq6tighd1vCxW2dZz5BdZYLmimta1wMySCglFMJh9vsPKnV1u-MzxzSbj314aSpTWc1t7Yy81JhcLO6miW1sblfRVl6uqbT4vrLd7qNvGs2pp8gHKyfdC3PZqwExZE6K2rrY76Ta1RowD3409U-PnRBuN3YsDDNMbb6h0wxjTKGVbKMbM78wUO7ozdRgvxvRkOpPIR-XHNZerSfDeouS-wI5gP8CYRUK8YI8cMFB0oGcPTj8PxudtkJFfl-Jcd9ymbZkIw-0v7TKNdi19ahNo9IDct6jSUyN0D0lHl4_I0dAgvDqmozaXb35Mj-iwpUVfPSY3m5JJq5y2kkmtZNKfPxqppNx7zxm1Mgn3KrqWSVqU1MokvSWTdEsmn5Bvnwaj_plrK364WRBGC8BRYskBEWaRkAEs5SVTvh95QoBhqhPOeyyT0setfZlEyvOkVGBjZgmWTVBMBU_JflmV-jmhkWbC93JfhZxzMIMFPJhkeaZiJiM47xKnGex0Zohd0ibicZoiNClCk3oMfrxLwgaP1JqmxuRMQXx--9zbBrwU9DZuxolSw4CkILe41k9Y3CXPDKrrfjDcm4fJ8cU_fvUludf-p16R_cXNUr8me3O1fGMF9Bdh8Mim
link.rule.ids 315,782,786,27933,27934
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=Concentrations+of+antibodies+against+%CE%B2-amyloid+40%2F42+monomer+and+oligomers+in+Chinese+intravenous+immunoglobulins&rft.jtitle=Journal+of+pharmaceutical+and+biomedical+analysis&rft.au=Ye%2C+Shengliang&rft.au=Zeng%2C+Renyong&rft.au=Jiang%2C+Peng&rft.au=Hou%2C+Mingxia&rft.date=2017-05-10&rft.pub=Elsevier+B.V&rft.issn=0731-7085&rft.eissn=1873-264X&rft.volume=138&rft.spage=277&rft.epage=282&rft_id=info:doi/10.1016%2Fj.jpba.2017.02.024&rft.externalDocID=S0731708516313413
thumbnail_l http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0731-7085&client=summon
thumbnail_m http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0731-7085&client=summon
thumbnail_s http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0731-7085&client=summon