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...
Saved in:
Published in: | Journal of pharmaceutical and biomedical analysis Vol. 138; pp. 277 - 282 |
---|---|
Main Authors: | , , , , , , , , , , , |
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 |