The DOI matches its Crossref record; 20 of the 20 references it cites were found in a registry or an index; none of the 32 sources its claims cite is checked for support yet.
Amyloid β Protein (Aβ) in Alzheimeri's Disease Brain
Open accessAbstract
Biochemical and immunocytochemical analyses were performed to evaluate the composition of the amyloid beta protein (A beta) deposited in the brains of patients with Alzheimer's disease (AD). To quantitate all A beta s present, cerebral cortex was homogenized in 70% formic acid, and the supernatant was analyzed by sandwich enzyme-linked immunoabsorbent assays specific for various forms of A beta. In 9 of 27 AD brains examined, there was minimal congophilic angiopathy and virtually all A beta (96%) ended at A beta 42(43). The other 18 AD brains contained increasing amounts of A beta ending at A beta 40. From this set, 6 brains with substantial congophilic angiopathy were separately analyzed. In these brains, the amount of A beta ending at A beta 42(43) was much the same as in brains with minimal congophilic angiopathy, but a large amount of A beta ending at A beta 40 (76% of total A beta) was also present. Immunocytochemical analysis with monoclonal antibodies selective for A beta s ending at A beta 42(43) or A beta 40 confirmed that, in brains with minimal congophilic angiopathy, virtually all A beta is A beta ending at A beta 42(43) and showed that this A beta is deposited in senile plaques of all types. In the remaining AD brains, A beta 42(43) was deposited in a similar fashion in plaques, but, in addition, widely varying amounts of A beta ending at A beta 40 were deposited, primarily in blood vessel walls, where some A beta ending at A beta 42(43) was also present. These observations indicate that A beta s ending at A beta 42(43), which are a minor component of the A beta in human cerebrospinal fluid and plasma, are critically important in AD where they deposit selectively in plaques of all kinds.
Overview
AI snapshot
Written from the paper’s full text.
TL;DR
In Alzheimer’s disease (AD) brain, Aβ ending at Aβ42(43) is the predominant deposited species in cases with minimal congophilic angiopathy, while Aβ40 becomes prominent mainly in brains with substantial vascular amyloid. The authors conclude that Aβ42(43), though a minor secreted species, is critically important in AD because it deposits selectively in senile plaques of all types.
Key findings
- In 9 of 27 AD brains with minimal congophilic angiopathy, virtually all Aβ (96%) ended at Aβ42(43); BC-05/4G8 detected 4663 ± 421 pmol/g versus BAN-50/BC-05 at 714 ± 68 pmol/g, while BA-27/4G8 detected only 216 ± 38 pmol/g.
- In 6 AD brains with substantial congophilic angiopathy, Aβ42(43) amounts were similar to minimal-angiopathy brains (BC-05/4G8: 5089 ± 409 pmol/g; BAN-50/BC-05: 826 ± 119 pmol/g), but Aβ40 was dramatically increased (BA-27/4G8: 13,607 ± 3397 pmol/g; BAN-50/BA-27: 5001 ± 2164 pmol/g). The abstract reports 76% of total Aβ ended at Aβ40 in these brains; the Results state an average of 67%.
- Total Aβ in 27 AD brains ranged from at least 500 to 4400 times that in plaque-free control brain; 98.5% of total Aβ required formic acid for solubilization and only 1.5% was extracted into Tris-saline.
- Immunocytochemistry showed BC-05 and 4G8 intensely labeled all plaque types and vascular amyloid, whereas BA-27 stained vascular amyloid well but stained plaque cores less intensely and almost failed to stain uncored plaques.
Methods
- AD and plaque-free control cerebral cortex was homogenized directly in 70% formic acid or sequentially extracted first into Tris-saline buffer with protease inhibitors and then into 70% formic acid.
- Aβ was quantitated by sandwich ELISAs specific for forms ending at Aβ40 (BA-27/4G8 or BAN-50/BA-27) or Aβ42(43) (BC-05/4G8 or BAN-50/BC-05), with some samples fractionated by Superose 12 size exclusion chromatography.
- Samples included an initial 3 AD and 3 control brains, then 27 AD and 6 plaque-free control brains; immunocytochemistry used formalin- or methacarn-fixed inferior temporal cortex with BA-27, BC-05, and 4G8 antibodies.
Limitations
- The paper does not state a formal limitations section. The authors note that BAN-50 cannot capture Aβs beginning at or beyond Aβ17, so the increased Aβ detected with 4G8 may indicate considerable amino-terminally truncated Aβ, but they caution this interpretation because other factors such as isoaspartates at Aβ1 and Aβ37 may diminish BAN-50 capture.
- The authors address the concern that BA-27 epitope destruction during fixation could distort immunocytochemistry, arguing against it because brains with minimal vascular amyloid had virtually all Aβ ending at Aβ42(43).
- Evident from the text: subgroup analyses rely on small numbers (e.g., 9 minimal and 6 substantial congophilic angiopathy cases), and no formal statistical comparisons are reported.
Model-written summary. Check it against the paper before relying on it.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
0 of 32 cited sources checked · 0 supported · 0 flagged
A result the paper reports from its own data — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“and large amounts of A{3C40 were deposited in some brains (Fig. 2).”
§ Communication Amyloid 13 Protein (Af3) in Alzheimer's Disease Brain BIOCHEMICAL AND IMMUNOCYTOCHEMICAL ANALYSIS WITH ANTIBODIES SPECIFIC FOR FORMS ENDING AT A1340 OR AI342(43)* ( > Analysis of A{3 in 27 AD and 6
Strength:plain· not yet calibratedTests✓ Asserted: passes✓ Checkable: passes? Load-bearing: unclear✓ Based: passesA result the paper reports from its own data — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“the remaining brains had increasing amounts of A{3C40'”
§ Communication Amyloid 13 Protein (Af3) in Alzheimer's Disease Brain BIOCHEMICAL AND IMMUNOCYTOCHEMICAL ANALYSIS WITH ANTIBODIES SPECIFIC FOR FORMS ENDING AT A1340 OR AI342(43)* ( > Analysis of A{3 in 27 AD and 6
Strength:plain· not yet calibratedCausal:correlational· not yet calibratedTests✓ Asserted: passes✓ Checkable: passes? Load-bearing: unclear✓ Based: passesThe paper states this without a source or data behind it here, so there is nothing to check it against. The quote shows it is in the paper.
In the paper
“Based on this upper limit, the total A{3 in the 27 AD brains ranged from at least SOO to 4400 times that in plaque-free control brain.”
§ Communication Amyloid 13 Protein (Af3) in Alzheimer's Disease Brain BIOCHEMICAL AND IMMUNOCYTOCHEMICAL ANALYSIS WITH ANTIBODIES SPECIFIC FOR FORMS ENDING AT A1340 OR AI342(43)* ( > Analysis of A{3 in 27 AD and 6
Tests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passes- Rests on an assumption: The recovery of synthetic Aβ added to control brain applies to endogenous Aβ in AD brain.
A result the paper reports from its own data — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“In these brains, A{3C40' measured with BA-27/4G8 (13607 :+: 3397 pmol/g) and BAN-SOIBA-27 (SOOI :+: 2164 pmol/g) ELISAs, was dramatically increased.”
§ Communication Amyloid 13 Protein (Af3) in Alzheimer's Disease Brain BIOCHEMICAL AND IMMUNOCYTOCHEMICAL ANALYSIS WITH ANTIBODIES SPECIFIC FOR FORMS ENDING AT A1340 OR AI342(43)* ( > Analysis of A{3 in 27 AD and 6
Tests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passes- Rests on an assumption: The recovery of synthetic Aβ added to control brain applies to endogenous Aβ in AD brain.
A result the paper reports from its own data — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“In many AD brains, virtually all A{3 was A{3C42(4:Jl'”
§ Communication Amyloid 13 Protein (Af3) in Alzheimer's Disease Brain BIOCHEMICAL AND IMMUNOCYTOCHEMICAL ANALYSIS WITH ANTIBODIES SPECIFIC FOR FORMS ENDING AT A1340 OR AI342(43)* ( > Analysis of A{3 in 27 AD and 6
Tests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passesA result the paper reports from its own data — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“and showed that this Ap is deposited in senile plaques of all types.”
§ Communication Amyloid 13 Protein (Af3) in Alzheimer's Disease Brain BIOCHEMICAL AND IMMUNOCYTOCHEMICAL ANALYSIS WITH ANTIBODIES SPECIFIC FOR FORMS ENDING AT A1340 OR AI342(43)* ( > Abstract
Tests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passesA result the paper reports from its own data — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“In the remaining AD brains, Ap42(43) was deposited in a similar fashion in plaques”
§ Communication Amyloid 13 Protein (Af3) in Alzheimer's Disease Brain BIOCHEMICAL AND IMMUNOCYTOCHEMICAL ANALYSIS WITH ANTIBODIES SPECIFIC FOR FORMS ENDING AT A1340 OR AI342(43)* ( > Abstract
Tests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passesA result the paper reports from its own data — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“but, in addition, widely varying amounts of Ap ending at Ap40 were deposited, primarily in blood vessel walls”
§ Communication Amyloid 13 Protein (Af3) in Alzheimer's Disease Brain BIOCHEMICAL AND IMMUNOCYTOCHEMICAL ANALYSIS WITH ANTIBODIES SPECIFIC FOR FORMS ENDING AT A1340 OR AI342(43)* ( > Abstract
Tests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passesA result the paper reports from its own data — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“but a large amount of Ap ending at Ap40 (76% of total Am was also present.”
§ Communication Amyloid 13 Protein (Af3) in Alzheimer's Disease Brain BIOCHEMICAL AND IMMUNOCYTOCHEMICAL ANALYSIS WITH ANTIBODIES SPECIFIC FOR FORMS ENDING AT A1340 OR AI342(43)* ( > Abstract
Tests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passesA result the paper reports from its own data — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“but the total A{3 present in control brain was invariably less than 7 pmol/g.”
§ Communication Amyloid 13 Protein (Af3) in Alzheimer's Disease Brain BIOCHEMICAL AND IMMUNOCYTOCHEMICAL ANALYSIS WITH ANTIBODIES SPECIFIC FOR FORMS ENDING AT A1340 OR AI342(43)* ( > Analysis of A{3 in 27 AD and 6
Tests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passes
- It may state two separate claims as one. 14
- Probably not a substantial claim. 2
A result the paper reports from its own data — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“The BAN-50IBA-27 ELISA showed a total of 73 ± 28 pmol of A{3lg in AD brain, whereas the BAN-50/BC-05 ELISA detected 725 ± 347 pmol/g (Table I).”
§ Communication Amyloid 13 Protein (Af3) in Alzheimer's Disease Brain BIOCHEMICAL AND IMMUNOCYTOCHEMICAL ANALYSIS WITH ANTIBODIES SPECIFIC FOR FORMS ENDING AT A1340 OR AI342(43)* ( > EXPERIMENTAL PROCEDURES
Tests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passesIt may state two separate claims as one.
A result the paper reports from its own data — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“In the AD brains, 98.S% of the total A{3 present required formic acid for solubilization and only l.S9t}was extracted into Tris-saline.”
§ Communication Amyloid 13 Protein (Af3) in Alzheimer's Disease Brain BIOCHEMICAL AND IMMUNOCYTOCHEMICAL ANALYSIS WITH ANTIBODIES SPECIFIC FOR FORMS ENDING AT A1340 OR AI342(43)* ( > Analysis of A{3 in 27 AD and 6
Tests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passesIt may state two separate claims as one.
A result the paper reports from its own data — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“Both 4G8 and BC-OS intensely labeled the AD brain, whereas BA-27 showed very little labeling (Fig. 3).”
§ Communication Amyloid 13 Protein (Af3) in Alzheimer's Disease Brain BIOCHEMICAL AND IMMUNOCYTOCHEMICAL ANALYSIS WITH ANTIBODIES SPECIFIC FOR FORMS ENDING AT A1340 OR AI342(43)* ( > Sandwich ELISAs for A~Sandwich
Load-bearingStrength:plain· not yet calibratedTests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passesIt may state two separate claims as one.
A result the paper reports from its own data — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“BA-27 stained vascular amyloid quite well but, in contrast to BC-OS and 4G8, stained the cores of classic neuritic plaques less intensely and almost completely failed to stain uncored (diffuse and uncored neuritic) plaques or the region surrounding plaque cores.”
§ Communication Amyloid 13 Protein (Af3) in Alzheimer's Disease Brain BIOCHEMICAL AND IMMUNOCYTOCHEMICAL ANALYSIS WITH ANTIBODIES SPECIFIC FOR FORMS ENDING AT A1340 OR AI342(43)* ( > Sandwich ELISAs for A~Sandwich
Load-bearingStrength:plain· not yet calibratedTests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passesIt may state two separate claims as one.
A result the paper reports from its own data — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“4G8 and BC-OS labeled uncored (diffuse and uncored neuritic) plaques, the cores of classic neuritic plaques, the region surrounding plaque cores, and vascular amyloid.”
§ Communication Amyloid 13 Protein (Af3) in Alzheimer's Disease Brain BIOCHEMICAL AND IMMUNOCYTOCHEMICAL ANALYSIS WITH ANTIBODIES SPECIFIC FOR FORMS ENDING AT A1340 OR AI342(43)* ( > Sandwich ELISAs for A~Sandwich
Tests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passesIt may state two separate claims as one.
A result the paper reports from its own data — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“In 9 of 27 AD brains examined, there was minimal congophilic angiopathy and virtually all Ap (96%) ended at AP42(43).”
- Also stated in: § Analysis of A{3 in 27 AD and 6 · plain
“Virtually all A{3 in the formic acid extracts from these 9 brains (96%) ended at A{342(43)”
§ Communication Amyloid 13 Protein (Af3) in Alzheimer's Disease Brain BIOCHEMICAL AND IMMUNOCYTOCHEMICAL ANALYSIS WITH ANTIBODIES SPECIFIC FOR FORMS ENDING AT A1340 OR AI342(43)* ( > Abstract
Tests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passesIt may state two separate claims as one.
- Also stated in: § Analysis of A{3 in 27 AD and 6 · plain
In the paper
“The immunocytochemical results shown here and in a recent report by Iwatsubo et al. (21) demonstrate that BC-05 intensely stains all types of senile plaques, that vessels are stained by both BC-OS and BA-27, and that BA-27 stains plaques poorly, in many cases only faintly staining occasional cored plaques (Fig. 3).”
§ Communication Amyloid 13 Protein (Af3) in Alzheimer's Disease Brain BIOCHEMICAL AND IMMUNOCYTOCHEMICAL ANALYSIS WITH ANTIBODIES SPECIFIC FOR FORMS ENDING AT A1340 OR AI342(43)* ( > Sandwich ELISAs for A~Sandwich
What the sources say
- Not checked — no full text of the sourcecites [21] Iwatsubo, 1994, Neuron source
Tests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passesIt may state two separate claims as one.
A result the paper reports from its own data — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“In the 3 AD brains, the BA-27/4GB ELISA showed a total of93 ± 45 pmol of A,B/g whereas the BC-05/4G8 ELISA showed 3200 ± 1350 pmol of A,BIg (Table I).”
§ Communication Amyloid 13 Protein (Af3) in Alzheimer's Disease Brain BIOCHEMICAL AND IMMUNOCYTOCHEMICAL ANALYSIS WITH ANTIBODIES SPECIFIC FOR FORMS ENDING AT A1340 OR AI342(43)* ( > EXPERIMENTAL PROCEDURES
Tests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passesIt may state two separate claims as one.
A conclusion the paper draws from its own results — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“Thus, it a ppears t hat deposition of A{3C42(43) in senile plaq ues is fundamental to AD path ogenesis with additi ona l deposition of A{3C40' prim aril y in blood vessel wa lls, occurring in some cases.”
§ Communication Amyloid 13 Protein (Af3) in Alzheimer's Disease Brain BIOCHEMICAL AND IMMUNOCYTOCHEMICAL ANALYSIS WITH ANTIBODIES SPECIFIC FOR FORMS ENDING AT A1340 OR AI342(43)* ( > Analysis of A{3 in 27 AD and 6
Tests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passesIt may state two separate claims as one.
A claim is checked only against the cited paper’s full text, never its abstract, and none is available for its sources.
In the paper
“Th is finding is consistent with pr evious re ports (15,17,18) that most of the A{3 in AD brains is amino-ter mi na lly trunca te d or modifi ed.”
§ Communication Amyloid 13 Protein (Af3) in Alzheimer's Disease Brain BIOCHEMICAL AND IMMUNOCYTOCHEMICAL ANALYSIS WITH ANTIBODIES SPECIFIC FOR FORMS ENDING AT A1340 OR AI342(43)* ( > FIG.
What the sources say
Strength:plain· not yet calibratedn = 27Tests✓ Asserted: passes✓ Checkable: passes✗ Load-bearing: fails✓ Based: passesProbably not a substantial claim. The paper’s conclusions may not depend on it.
None of the sources cited for this claim have been checked yet.
In the paper
“The monoclonal antibodies employed were BAN-50 (anti-A{31-16), 4G8 (anti-Af3l7-24) (19), BA-27, which is specific for A{3 ending at A{340, and BC-05, which is specific for A{3 ending at A{342(43).”
§ Communication Amyloid 13 Protein (Af3) in Alzheimer's Disease Brain BIOCHEMICAL AND IMMUNOCYTOCHEMICAL ANALYSIS WITH ANTIBODIES SPECIFIC FOR FORMS ENDING AT A1340 OR AI342(43)* ( > Sandwich ELISAs for A~Sandwich
What the sources say
- Not checked — no full text of the sourcecites [9] Suzuki, 1994, Science source
- Not checked yetcites [19] Kim, 1988, Neurosci. Res. Commun.
Load-bearingStrength:plain· not yet calibratedTests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passesIt may state two separate claims as one.
None of the sources cited for this claim have been checked yet.
In the paper
“In the brains of patients with Alzheimer's disease (AD),!amyloid composed of 4-kDa amyloid {3 protein (A{3) is deposited in senile plaques and in blood vessel walls.”
§ Communication Amyloid 13 Protein (Af3) in Alzheimer's Disease Brain BIOCHEMICAL AND IMMUNOCYTOCHEMICAL ANALYSIS WITH ANTIBODIES SPECIFIC FOR FORMS ENDING AT A1340 OR AI342(43)* ( > Abstract
What the sources say
- Not checked — no full text of the sourcecites [1] Yamaguchi, 1988, Acta Neuropathol. source
- Not matchedcites [2] Masliah, 1990, Am. J. Pathol.
Couldn’t be matched to a paper in Crossref, so it can’t be checked.
Load-bearingStrength:plain· not yet calibratedTests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passesIt may state two separate claims as one.
A claim is checked only against the cited paper’s full text, never its abstract, and none is available for its sources.
In the paper
“Recently, we and others have shown that normal processing of the large amyloid f3 protein precursor ({3-APP) secretes 4-kDa A(3 that is readily detected in human cerebrospinal fluid and in medium conditioned by cultured cells (3)(4)(5)(6).”
§ Communication Amyloid 13 Protein (Af3) in Alzheimer's Disease Brain BIOCHEMICAL AND IMMUNOCYTOCHEMICAL ANALYSIS WITH ANTIBODIES SPECIFIC FOR FORMS ENDING AT A1340 OR AI342(43)* ( > Abstract
What the sources say
Strength:plain· not yet calibratedCausal:direct· not yet calibratedTests✓ Asserted: passes✓ Checkable: passes? Load-bearing: unclear✓ Based: passesIt may state two separate claims as one.
In the paper
“As t his occurred, BC-05 in varia bly showed intense staini ng of all plaq ues as well as some staining of blood ves sel wa lls whereas BA-27 intensely staine d blood vess els a nd showed increa sing stai ning of A{3C40 in plaques, par ticul a rly ma t ure cored pla qu es, a lthough it never stained plaques to t he exte nt observed with BC-05.”
§ Communication Amyloid 13 Protein (Af3) in Alzheimer's Disease Brain BIOCHEMICAL AND IMMUNOCYTOCHEMICAL ANALYSIS WITH ANTIBODIES SPECIFIC FOR FORMS ENDING AT A1340 OR AI342(43)* ( > Analysis of A{3 in 27 AD and 6
What the sources say
- Not matchedcites [22] Iwatsubo, 1995, Ann. Neurol.
Couldn’t be matched to a paper in Crossref, so it can’t be checked.
Tests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passesIt may state two separate claims as one.
- Not matched
A claim is checked only against the cited paper’s full text, never its abstract, and none is available for its sources.
In the paper
“Recent reports using this approach, particularly those of Roher and his colleagues, indicate that the SDS-insoluble amyloid in senile plaque cores is primarily A(31-42 (15,17)”
§ Communication Amyloid 13 Protein (Af3) in Alzheimer's Disease Brain BIOCHEMICAL AND IMMUNOCYTOCHEMICAL ANALYSIS WITH ANTIBODIES SPECIFIC FOR FORMS ENDING AT A1340 OR AI342(43)* ( > Abstract
What the sources say
Load-bearingStrength:hedged· not yet calibratedTests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passesProbably not a substantial claim.
In the paper
“In th ese br ai ns, A{3C42(43l staine d by BC-05 was deposited fir st in diffu se plaq ues , an d there was esse ntia lly no staining by BA-27.”
§ Communication Amyloid 13 Protein (Af3) in Alzheimer's Disease Brain BIOCHEMICAL AND IMMUNOCYTOCHEMICAL ANALYSIS WITH ANTIBODIES SPECIFIC FOR FORMS ENDING AT A1340 OR AI342(43)* ( > Analysis of A{3 in 27 AD and 6
What the sources say
- Not matchedcites [22] Iwatsubo, 1995, Ann. Neurol.
Couldn’t be matched to a paper in Crossref, so it can’t be checked.
Load-bearingStrength:plain· not yet calibratedTests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passesIt may state two separate claims as one.
- Not matched
The paper relies on this without support.
The recovery of synthetic Aβ added to control brain applies to endogenous Aβ in AD brain.
“To assess Af3 recovery, synthetic Af3 (500 pmol of A{31-4o plus 500 pmol of Af31-42, Bachem) was added to samples of cerebral cortex (-0.5 g) from control brains prior to homogenization.”
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“and both forms continued to increase substantially from 12 to 23 months, reaching levels like those seen in the AD brain (Gravina et al., 1995).”
From Age-Dependent Changes in Brain, CSF, and Plasma Amyloid β Protein in the Tg2576 Transgenic Mouse Model of Alzheimer's Disease (2001) · cites this paper as Gravina et al., 1995
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“In our previous examination of insoluble A in 27 AD brains (Gravina et al., 1995), A42 predominated in 70% and, in 33%, there was essentially no A40 deposited.”
From Age-Dependent Changes in Brain, CSF, and Plasma Amyloid β Protein in the Tg2576 Transgenic Mouse Model of Alzheimer's Disease (2001) · cites this paper as Gravina et al., 1995
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“In the 30% in which A40 was the predominant species deposited, there was typically prominent congophilic angiopathy.”
From Age-Dependent Changes in Brain, CSF, and Plasma Amyloid β Protein in the Tg2576 Transgenic Mouse Model of Alzheimer's Disease (2001) · cites this paper as Gravina et al., 1995
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“In most AD patients, very little A40 is deposited in the brain, but in ϳ33%, extraordinary amounts of A40 are deposited, and most of these patients show substantial amyloid angiopathy (Gravina et al., 1995).”
From Age-Dependent Changes in Brain, CSF, and Plasma Amyloid β Protein in the Tg2576 Transgenic Mouse Model of Alzheimer's Disease (2001) · cites this paper as Gravina et al., 1995
Experimental — accuracy not yet measuredThe cited source says what the claim attributes to it.
In the citing paper
“accumulates to a variable degree in the human AD brain”
From Aβ40 Inhibits Amyloid Deposition In Vivo (2007) · cites this paper as Gravina et al., 1995
The cited source says what the claim attributes to it.
In the citing paper
“In our previous study (Gravina et al., 1995), ELISAs for Ax-42 (BC-05/4G8) and Ax-40 (BA-27/4G8) showed that most of the A in AD brain is N-terminally truncated or modified.”
From Age-Dependent Changes in Brain, CSF, and Plasma Amyloid β Protein in the Tg2576 Transgenic Mouse Model of Alzheimer's Disease (2001) · cites this paper as Gravina et al., 1995
The cited source says what the claim attributes to it.
In the citing paper
“In contrast, virtually all A terminated at A42 in the two AD brains examined (Fig. 5 K, L), as occurs in ϳ33% of AD cases (Gravina et al., 1995).”
From Age-Dependent Changes in Brain, CSF, and Plasma Amyloid β Protein in the Tg2576 Transgenic Mouse Model of Alzheimer's Disease (2001) · cites this paper as Gravina et al., 1995
In the citing paper
“In contrast, Aβ40, the major Aβ peptide secreted by cells, appears to be the predominant species deposited in the amyloid deposits in the cerebral vasculature (congophillic angiopathy, CAA) (Gravina et al., 1995; Iwatsubo et al., 1994).”
From Aβ42 Is Essential for Parenchymal and Vascular Amyloid Deposition in Mice (2005) · cites this paper as Gravina et al., 1995
In the citing paper
“These data provide definitive in vivo confirmation of predictions inferred from (1) in vitro studies of Aβ aggregation, (2) effects of PS and certain APP mutations on Aβ production and deposition, and (3) analyses of Aβ peptides in the human AD brain (Gravina et al., 1995; Iwatsubo et al., 1994).”
From Aβ42 Is Essential for Parenchymal and Vascular Amyloid Deposition in Mice (2005) · cites this paper as Gravina et al., 1995
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
Each contradiction between two passages listed here was confirmed by an independent check.
Conflicting percentages of Aβ ending at Aβ40
MajorFor the six brains with substantial congophilic angiopathy, the abstract states that 76% of total Aβ ended at Aβ40, while the results state that the average was 67%. Both statements describe the same six-brain group.
“In these brains, the amount of Ap ending at AP42(43) was much the same as in brains with minimal congophilic angiopathy, but a large amount of Ap ending at Ap40 (76% of total Am was also present.”
“On average, 67% of the A{3 in brains with substantial congophilic angiopathy ended at A{340”
Citations
Cites
Jarrett, J. T., & Lansbury, P. T. (1993) · Cell · doi:10.1016/0092-8674(93)90635-4 · Cited by 2,178
Jarrett, J. T., Berger, E. P., & Lansbury, P. T. (1993) · Biochemistry · doi:10.1021/bi00069a001 · Cited by 2,022
Amyloid β-peptide is produced by cultured cells during normal metabolism
Haass, C., Schlossmacher, M. G., Hung, A. Y., Vigo-Pelfrey, C., Mellon, A., Ostaszewski, B. L., Lieberburg, I., Koo, E. H., Schenk, D., Teplow, D. B., et al. (1992) · Nature · doi:10.1038/359322a0 · Cited by 1,921
Iwatsubo, T., Odaka, A., Suzuki, N., Mizusawa, H., Nukina, N., & Ihara, Y. (1994) · Neuron · doi:10.1016/0896-6273(94)90458-8 · Cited by 1,774
Self-citationIsolation and quantification of soluble Alzheimer's β-peptide from biological fluids
Seubert, P., Vigo-Pelfrey, C., Esch, F., Lee, M., Dovey, H., Davis, D., Sinha, S., Schiossmacher, M., Whaley, J., Swindlehurst, C., et al. (1992) · Nature · doi:10.1038/359325a0 · Cited by 1,731
Suzuki, N., Cheung, T. T., Cai, X.-D., Odaka, A., Otvos, L., Eckman, C., Golde, T. E., & Younkin, S. G. (1994) · Science · doi:10.1126/science.8191290 · Cited by 1,471
Self-citationProduction of the Alzheimer Amyloid β Protein by Normal Proteolytic Processing
Shoji, M., Golde, T. E., Ghiso, J., Cheung, T. T., Estus, S., Shaffer, L. M., Cai, X.-D., McKay, D. M., Tintner, R., Frangione, B., et al. (1992) · Science · doi:10.1126/science.1439760 · Cited by 1,447
Self-citationAssembly and aggregation properties of synthetic Alzheimer's A4/beta amyloid peptide analogs.
Burdick, D., Soreghan, B., Kwon, M., Kosmoski, J., Knauer, M., Henschen, A., Yates, J., Cotman, C., & Glabe, C. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)48529-8 · Cited by 1,014
Roher, A. E., Lowenson, J. D., Clarke, S., Wolkow, C., Wang, R., Cotter, R. J., Reardon, I. M., Zürcher-Neely, H. A., Heinrikson, R. L., & Ball, M. J. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)53661-9 · Cited by 799
Roher, A. E., Lowenson, J. D., Clarke, S., Woods, A. S., Cotter, R. J., Gowing, E., & Ball, M. J. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.22.10836 · Cited by 740
Flagged first, then by citations
Research works printed but not linked: 4
- Masliah, 1990, Am. J. Pathol., 137, 1293
- Kim, 1988, Neurosci. Res. Commun., 2, 121
- Suzuki, 1994, Am. J. Pathol., 145, 452
- Iwatsubo, 1995, Ann. Neurol.
Cited by
Sorted by citations
Items 201–300 of 674
Mutant Presenilin 2 Transgenic Mice
Sawamura, N., Morishima‐Kawashima, M., Waki, H., Kobayashi, K., Kuramochi, T., Frosch, M. P., Ding, K., Ito, M., Kim, T., Tanzi, R. E., et al. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m004308200 · Cited by 89
Lidocaine attenuates cognitive impairment after isoflurane anesthesia in old rats
Lin, D., Cao, L., Wang, Z., Li, J., Washington, J. M., & Zuo, Z. (2011) · Behavioural Brain Research · doi:10.1016/j.bbr.2011.12.010 · Cited by 87
Mutations in the Transmembrane Domain of APP Altering γ-Secretase Specificity
Lichtenthaler, S. F., Ida, N., Multhaup, G., Masters, C. L., & Beyreuther, K. T. (1997) · Biochemistry · doi:10.1021/bi971071m · Cited by 86
Transgenic C. elegans as a Model in Alzheimers Research
Wu, Y., & Luo, Y. (2005) · Current Alzheimer Research · doi:10.2174/1567205052772768 · Cited by 88
Decreased Neprilysin Immunoreactivity in Alzheimer Disease, but Not in Pathological Aging
Wang, D.-S., Lipton, R. B., Katz, M. J., Davies, P. J., Herman Buschke, L., Kuslansky, G., Verghese, J., Younkin, S. G., Eckman, C., & Dickson, D. W. (2005) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/64.5.378 · Cited by 85
Self-citationMolecular Structure of Aggregated Amyloid-β: Insights from Solid-State Nuclear Magnetic ResonancePreprint
Tycko, R. (2016) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a024083 · Cited by 89
Natural Compounds May Open New Routes to Treatment of Amyloid Diseases
Bieschke, J. (2013) · Neurotherapeutics · doi:10.1007/s13311-013-0192-7 · Cited by 85
Surface chemistry of Alzheimer's disease: A Langmuir monolayer approach
Thakur, G., Mićić, M., & Leblanc, R. M. (2009) · Colloids and Surfaces B Biointerfaces · doi:10.1016/j.colsurfb.2009.07.043 · Cited by 85
Svedberg, M. M., Hall, H., Hellström‐Lindahl, E., Estrada, S., Guan, Z.-Z., Nordberg, A. K., & Långström, B. (2008) · Neurochemistry International · doi:10.1016/j.neuint.2008.12.016 · Cited by 85
Receptor-Mediated Transport of Human Amyloid β-Protein 1–40 and 1–42 at the Blood–Brain Barrier
Poduslo, J. F., Curran, G. L., Sanyal, B., & Selkoe, D. J. (1999) · Neurobiology of Disease · doi:10.1006/nbdi.1999.0238 · Cited by 83
Bourassa, P., Tremblay, C., Schneider, J. A., Bennett, D. A., & Calon, F. (2019) · Acta Neuropathologica · doi:10.1007/s00401-019-01967-4 · Cited by 80
Apolipoprotein E4 promotes the early deposition of Aβ42 and then Aβ40 in the elderly
Walker, L. C., Pahnke, J., Madauss, M., Vogelgesang, S., Pahnke, A., Herbst, E. W., Stausske, D., Walther, R., Kessler, C., & Warzok, R. (2000) · Acta Neuropathologica · doi:10.1007/s004010051190 · Cited by 81
Intramembrane proteolysis by presenilin and presenilin-like proteases
Xia, W., & Wolfe, M. S. (2003) · Journal of Cell Science · doi:10.1242/jcs.00651 · Cited by 83
Martel, C. L., Mackic, J. B., McComb, J. G., Ghiso, J., & Zlokovic, B. V. (1996) · Neuroscience Letters · doi:10.1016/s0304-3940(96)12462-9 · Cited by 69
Inhibition of Alzheimer β-Peptide Fibril Formation by Serum Amyloid P Component
Janciauskiene, S. M., de Frutos, P. G., Carlemalm, E., Dahlbäck, B., & Eriksson, S. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.44.26041 · Cited by 82
C-Terminal Turn Stability Determines Assembly Differences between Aβ40 and Aβ42
Roychaudhuri, R., Yang, M., Deshpande, A. M., Cole, G. M., Frautschy, S. A., Lomakin, A., Benedek, G. B., & Teplow, D. B. (2012) · Journal of Molecular Biology · doi:10.1016/j.jmb.2012.11.006 · Cited by 82
Clusterin levels are increased in A lzheimer's disease and influence the regional distribution of Aβ
Miners, J. S., Clarke, P., & Love, S. (2016) · Brain Pathology · doi:10.1111/bpa.12392 · Cited by 83
Ertekin-Taner, N. (2003) · Human Molecular Genetics · doi:10.1093/hmg/ddg343 · Cited by 80
Key Residue for Aggregation of Amyloid-β Peptides
Itoh, S., Yagi‐Utsumi, M., Kato, K., & Okumura, H. (2022) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.2c00358 · Cited by 81
Uekawa, K., Hattori, Y., Ahn, S. J., Seo, J., Casey, N., Anfray, A., Zhou, P., Luo, W., Anrather, J., Park, L., et al. (2023) · Molecular Neurodegeneration · doi:10.1186/s13024-023-00660-1 · Cited by 80
Aleksis, R., Oleskovs, F., Jaudzems, K., Pahnke, J., & Biverstål, H. (2017) · Biochimie · doi:10.1016/j.biochi.2017.07.011 · Cited by 80
Marotta, N. P., Ara, J. E., Uemura, N., Lougee, M. G., Meymand, E. S., Zhang, B., Petersson, E. J., Trojanowski, J. Q., & Lee, V. M. ‐. (2021) · Acta Neuropathologica Communications · doi:10.1186/s40478-021-01288-2 · Cited by 84
Soluble amyloid-β, effect on cerebral arteriolar regulation and vascular cells
Dietrich, H. H., Xiang, C., Han, B. H., Zipfel, G. J., & Holtzman, D. M. (2010) · Molecular Neurodegeneration · doi:10.1186/1750-1326-5-15 · Cited by 81
Behavioral and neurobiological markers of Alzheimer’s disease in Ts65Dn mice: effects of estrogen
Hunter, C. L., Bimonte‐Nelson, H. A., Nelson, M., Eckman, C. B., & Granholm, A. (2004) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2003.10.010 · Cited by 77
Self-citationYokoyama, H., Okazaki, K., Imai, D., Yamashina, Y., Takeda, R., Naghavi, N., Ota, A., Hirasawa, Y., & Miyagawa, T. (2015) · BMC Geriatrics · doi:10.1186/s12877-015-0058-4 · Cited by 76
Dickson, D. W. (2005) · Acta Neuropathologica · doi:10.1007/s00401-004-0950-z · Cited by 77
Liu, L., Zhao, F., Ma, F., Zhang, L., Yang, S., & Xia, N. (2013) · Biosensors and Bioelectronics · doi:10.1016/j.bios.2013.05.028 · Cited by 76
Tam, J. H. K., Seah, C., & Pasternak, S. (2014) · Molecular Brain · doi:10.1186/s13041-014-0054-1 · Cited by 83
Yu, W., Jin, H., & Huang, Y. (2021) · Clinical Science · doi:10.1042/cs20200844 · Cited by 75
Viles, J. H. (2023) · Angewandte Chemie International Edition · doi:10.1002/anie.202215785 · Cited by 74
Comparison of Aβ levels in the brain of familial and sporadic Alzheimer's disease
Hellström‐Lindahl, E., Viitanen, M. H., & Marutle, A. (2009) · Neurochemistry International · doi:10.1016/j.neuint.2009.03.007 · Cited by 78
Maddalena, A. S., Papassotiropoulos, A., Gonzalez-Agosti, C., Signorell, A., Hegi, T., Pasch, T., Nitsch, R. M., & Höck, C. (2004) · Neurodegenerative Diseases · doi:10.1159/000080991 · Cited by 75
Ogi, H. (2013) · Proceedings of the Japan Academy Series B · doi:10.2183/pjab.89.401 · Cited by 78
Jew, S., Yoo, C., Lim, D., Kim, H., Mook‐Jung, I., Jung, M. W., Choi, H., Jung, Y. H., Kim, H., & Park, H. (2000) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/s0960-894x(99)00658-7 · Cited by 74
Davis-Salinas, J., & Nostrand, W. E. V. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.36.20887 · Cited by 74
Dorey, A., Perret‐Liaudet, A., Tholance, Y., Fourier, A., & Quadrio, I. (2015) · Frontiers in Neurology · doi:10.3389/fneur.2015.00247 · Cited by 74
Age-related toxicity to lactate, glutamate, and β-amyloid in cultured adult neurons
Brewer, G. J. (1998) · Neurobiology of Aging · doi:10.1016/s0197-4580(98)00091-8 · Cited by 73
Fukuchi, K., Ho, L., Younkin, S. G., Kunkel, D. D., Ogburn, C. E., LeBoeuf, R. C., Furlong, C. E., Deeb, S. S., Nochlin, D., Węgiel, J., et al. (1996) · Europe PMC (PubMed Central) · Cited by 69
Self-citationLi, S., Lin, C.-W., Wei, K., Huang, C.-Y., Hsu, P., Liu, H.-L., Lin, Y.-J., Lin, S.-C., Yang, H., & Ma, C.-C. M. (2016) · Scientific Reports · doi:10.1038/srep25155 · Cited by 71
The Pathogenic Aβ43 Is Enriched in Familial and Sporadic Alzheimer Disease
Matton, A., Welander, H., Winblad, B. G., Graff, C., & Tjernberg, L. O. (2013) · PLoS ONE · doi:10.1371/journal.pone.0055847 · Cited by 69
Increased amyloid β protein levels in children and adolescents with Down syndrome
Mehta, P. D., Capone, G. T., Jewell, A., & Freedland, R. L. (2007) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2006.12.010 · Cited by 72
do Nascimento, K. K. F., Silva, K. P., Malloy‐Diniz, L. F., Butters, M. A., & Diniz, B. S. (2015) · Journal of Psychiatric Research · doi:10.1016/j.jpsychires.2015.07.024 · Cited by 72
Ertekin‐Taner, N., Ronald, J., Feuk, L., Prince, J. A., Tucker, M., Younkin, L. H., Hella, M., Jain, S., Hackett, A. M., Scanlin, L., et al. (2004) · Human Molecular Genetics · doi:10.1093/hmg/ddi041 · Cited by 66
Self-citationHashimoto, M., Bogdanovic, N., Volkmann, I., Aoki, M., Winblad, B., & Tjernberg, L. O. (2010) · Acta Neuropathologica · doi:10.1007/s00401-010-0661-6 · Cited by 69
Quantitative analysis of co-oligomer formation by amyloid-beta peptide isoforms.
Iljina, M., Garcia, G. A., Dear, A. J., Flint, J., Narayan, P., Michaels, T. C. T., Dobson, C. M., Frenkel, D., Knowles, T. P. J., & Klenerman, D. (2016) · Scientific Reports · doi:10.1038/srep28658 · Cited by 68
Human apolipoprotein E4 accelerates β‐amyloid deposition in APPsw transgenic mouse brain
Carter, D. B., Dunn, E., McKinley, D. D., Stratman, N. C., Boyle, T. P., Kuiper, S. L., Oostveen, J. A., Weaver, R. J., Boller, J. A., & Gurney, M. E. (2001) · Annals of Neurology · doi:10.1002/ana.1134 · Cited by 70
Beta amyloid effects on expression of multidrug efflux transporters in brain endothelial cells.
Kania, K., Wijesuriya, H. C., Hladky, S., & Barrand, M. (2011) · Brain Research · doi:10.1016/j.brainres.2011.08.044 · Cited by 63
Accumulation of β-Amyloid fibrils in pancreas of transgenic mice
Kawarabayashi, T., Shoji, M., Sato, M., Sasaki, A., Ho, L., Eckman, C. B., Prada, C.-M., Younkin, S. G., Kobayashi, T., Tada, N., et al. (1996) · Neurobiology of Aging · doi:10.1016/0197-4580(95)02061-6 · Cited by 66
Self-citationHo, L., Fukuchi, K.-I., & Younkin, S. G. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.48.30929 · Cited by 66
Self-citationThe Interaction of Amyloid-β with ApoE
Carter, D. B. (2005) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/0-387-23226-5_13 · Cited by 68
Mitigating Alzheimer’s Disease with Natural Polyphenols: A Review
Gaudreault, R., & Mousseau, N. (2019) · Current Alzheimer Research · doi:10.2174/1567205016666190315093520 · Cited by 65
McConlogue, L., Castellano, F., deWit, C., Schenk, D., & Maltese, W. A. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.3.1343 · Cited by 65
Roks, G. (2000) · Brain · doi:10.1093/brain/123.10.2130 · Cited by 65
Sordo, L., & Gunn-Moore, D. A. (2021) · Veterinary Record · doi:10.1002/vetr.3 · Cited by 69
β-Amyloid (1–40) Peptide Interactions with Supported Phospholipid Membranes: A Single-Molecule Study
Ding, H., Schauerte, J. A., Steel, D. G., & Gafni, A. (2012) · Biophysical Journal · doi:10.1016/j.bpj.2012.08.051 · Cited by 61
Qosa, H., LeVine, H., Keller, J. N., & Kaddoumi, A. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2014.06.029 · Cited by 64
Döbeli, H., Draeger, N., Huber, G., Jakob, P., Schmidt, D., Seilheimer, B., Stüber, D., Wipf, B., & Zulauf, M. (1995) · Nature Biotechnology · doi:10.1038/nbt0995-988 · Cited by 60
Beher, D., Elle, C., Underwood, J. R., Davis, J. B., Ward, R., Karran, E. H., Masters, C. L., Beyreuther, K. T., & Multhaup, G. (1999) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1999.721564.x · Cited by 60
Bohrmann, B., Adrian, M., Dubochet, J., Kuner, P., Müller, F., Huber, W., Nordstedt, C., & Döbeli, H. (2000) · Journal of Structural Biology · doi:10.1006/jsbi.2000.4241 · Cited by 58
Strazielle, N., Ghersi‐Egea, J., Ghiso, J. A., Dehouck, M., Frangione, B., Patlak, C. S., Fenstermacher, J. D., & Gorevic, P. D. (2000) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/59.1.29 · Cited by 60
Maltese, W. A., Wilson, S. E., Tan, Y., Suomensaari, S., Sinha, S., Barbour, R., & McConlogue, L. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m007238200 · Cited by 60
Differentiating Aβ40 and Aβ42 in amyloid plaques with a small molecule fluorescence probe
Yang, J., Zhu, B., Yin, W. H., Han, Z., Zheng, C., Wang, P., & Ran, C. (2020) · Chemical Science · doi:10.1039/d0sc02060e · Cited by 58
Amyloid-beta isoform metabolism quantitation by stable isotope-labeled kinetics
Mawuenyega, K. G., Kasten, T. P., Sigurdson, W. C., & Bateman, R. J. (2013) · Analytical Biochemistry · doi:10.1016/j.ab.2013.04.031 · Cited by 58
Photo-degradation of amyloid β by a designed fullerene–sugar hybrid
Ishida, Y., Tanimoto, S., Takahashi, D., & Toshima, K. (2010) · MedChemComm · doi:10.1039/c0md00075b · Cited by 58
Blood‐based neurochemical diagnosis of vascular dementia: a pilot study
Bibl, M., Esselmann, H., Mollenhauer, B., Weniger, G., Welge, V., Liess, M., Lewczuk, P., Otto, M., Schulz, J. B., Trenkwalder, C., et al. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.04763.x · Cited by 57
Plasma amyloid-β oligomers level is a biomarker for Alzheimer’s disease diagnosis
Zhou, L., Chan, K. H., Chu, L., Kwan, J., Song, Y., Chen, L. H., Ho, P. W., Cheng, O., Ho, J. W.-M., & Lam, K. S. L. (2012) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2012.06.017 · Cited by 59
Yamada, A., Akimoto, H., Kagawa, S., Guillemin, G. J., & Takikawa, O. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06175.x · Cited by 58
Cerebrospinal fluid Ab40 and Ab42 natural course and clinical usefulness
Shoji, M. (2002) · Frontiers in bioscience · doi:10.2741/a826 · Cited by 59
Genetics of Early-Onset Alzheimer Dementia
Rademakers, R., Cruts, M., & Broeckhoven, C. V. (2003) · The Scientific World JOURNAL · doi:10.1100/tsw.2003.39 · Cited by 58
The Use of Antimicrobial and Antiviral Drugs in Alzheimer’s Disease
Iqbal, U., Zeng, E., & Pasinetti, G. M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21144920 · Cited by 55
Cao, Y., Zhu, X., Li, J., & Shi, R. (2010) · Journal of Molecular Modeling · doi:10.1007/s00894-009-0594-y · Cited by 55
Gu, L., Tran, J., Jiang, L., & Guo, Z. (2016) · Journal of Structural Biology · doi:10.1016/j.jsb.2016.01.013 · Cited by 56
Li, J., & Wang, H. (2018) · Bioscience Reports · doi:10.1042/bsr20180051 · Cited by 55
Hirabayashi, A., Shindo, Y., Oka, K., Takahashi, D., & Toshima, K. (2014) · Chemical Communications · doi:10.1039/c4cc03791j · Cited by 55
β-Amyloid 42/40 ratio and kalirin expression in Alzheimer disease with psychosis
Murray, P. S., Kirkwood, C. M., Gray, M. C., Ikonomović, M. D., Paljug, W. R., Abrahamson, E. E., Henteleff, R. A., Hamilton, R. L., Kofler, J., Klunk, W. E., et al. (2012) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2012.02.015 · Cited by 58
Partial loss of endothelial nitric oxide leads to increased cerebrovascular beta amyloid
Austin, S. A., & Katusic, Z. S. (2020) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1177/0271678x18822474 · Cited by 52
Amyloid-β peptide structure in aqueous solution varies with fragment size
Wise-Scira, O., Xu, L., Kitahara, T., Perry, G. L., & Coskuner‐Weber, O. (2011) · The Journal of Chemical Physics · doi:10.1063/1.3662490 · Cited by 53
Bleiholder, C., & Bowers, M. T. (2017) · Annual Review of Analytical Chemistry · doi:10.1146/annurev-anchem-071114-040304 · Cited by 54
Morató, X., Pytel, V., Jofresa, S., Ruiz, A., & Boada, M. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23169305 · Cited by 53
Hsu, P. J., Shou, H., Benzinger, T. L. S., Marcus, D., Durbin, T. J., Morris, J. C., & Sheline, Y. I. (2015) · Journal of Alzheimer s Disease · doi:10.3233/jad-141743 · Cited by 53
Cross‐seeding between Aβ40 and Aβ42 in Alzheimer's disease
Tran, J., Chang, D., Hsu, F., Wang, H., & Guo, Z. (2016) · FEBS Letters · doi:10.1002/1873-3468.12526 · Cited by 53
Brain Amyloid — A Physicochemical Perspective
Maggie, J. E., & Mantyh, P. W. (1996) · Brain Pathology · doi:10.1111/j.1750-3639.1996.tb00797.x · Cited by 51
Chen, J., Fears, S. C., Jasinska, A. J., Huang, A., Al‐Sharif, N., Scheibel, K. E., Dyer, T. D., Fagan, A. M., Blangero, J., Woods, R. P., et al. (2018) · Brain and Behavior · doi:10.1002/brb3.903 · Cited by 52
Aβ Measurement by Enzyme-Linked Immunosorbent Assay
Schmidt, S. D., Mazzella, M. J., Nixon, R. A., & Mathews, P. M. (2012) · Methods in molecular biology · doi:10.1007/978-1-61779-551-0_34 · Cited by 54
Targeting Post-translational Modifications on Tau as a Therapeutic Strategy for Alzheimer's Disease
Marcus, J., & Schachter, J. B. (2011) · Journal of Neurogenetics · doi:10.3109/01677063.2011.626471 · Cited by 51
Ishida, Y., Fujii, T., Oka, K., Takahashi, D., & Toshima, K. (2011) · Chemistry - An Asian Journal · doi:10.1002/asia.201100421 · Cited by 49
Verbeek, M. M., Ruiter, D. J., & de Waal, R. M. W. (1997) · Biological Chemistry · doi:10.1515/bchm.1997.378.9.937 · Cited by 49
Suh, J., Kim, M., Yoo, J., Han, J., Paulina, C., & Lim, M. H. (2022) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2022.214978 · Cited by 49
Mehta, P. D., Mehta, S. P., Fedor, B. L., Patrick, B. A., Emmerling, M. R., & Dalton, A. J. (2003) · Neuroscience Letters · doi:10.1016/s0304-3940(03)00275-1 · Cited by 50
Oxidative Stress in Alzheimer’s Disease: Molecular Hallmarks of Underlying Vulnerability
Uddin, M. S., & Kabir, M. T. (2019) · Springer eBooks · doi:10.1007/978-981-13-9636-6_5 · Cited by 50
Biophysical Comparison of Soluble Amyloid-β(1–42) Protofibrils, Oligomers, and Protofilaments
Nichols, M. R., Colvin, B. A., Hood, E. A., Paranjape, G. S., Osborn, D. C., & Terrill, S. E. (2015) · Biochemistry · doi:10.1021/bi500957g · Cited by 45
Comparison of neurotoxicity of different aggregated forms of Aβ40, Aβ42 and Aβ43 in cell cultures
Fu, L., Sun, Y., Guo, Y., Chen, Y., Yu, B., Zhang, H., Wu, J., Yu, X., Kong, W., & Wu, H. (2017) · Journal of Peptide Science · doi:10.1002/psc.2975 · Cited by 47
Miners, J., Kehoe, P., & Love, S. (2011) · Brain Pathology · doi:10.1111/j.1750-3639.2011.00486.x · Cited by 44
Alcendor, D. J. (2020) · Journal of Clinical Medicine · doi:10.3390/jcm9051490 · Cited by 47
Craft, D. (2002) · Bulletin of Mathematical Biology · doi:10.1006/bulm.2002.0304 · Cited by 64
Kato, A., Fukunari, A., Sakai, Y., & Nakajima, T. (1997) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1016/s0022-3565(24)37017-x · Cited by 45
Amyloid β‐protein deposition in the leptomeninges and cerebral cortex
Shinkai, Y., Morishima-kawashima, M., Ihara, Y., Yoshimura, M., Shimada, H., Ito, Y., & Yanagisawa, K. (1997) · Annals of Neurology · doi:10.1002/ana.410420612 · Cited by 44
Lesuisse, C. (2001) · Human Molecular Genetics · doi:10.1093/hmg/10.22.2525 · Cited by 45
Aspects of Neurodegeneration in the Canine Brain
Dimakopoulos, A. C., & Mayer, R. J. (2002) · Journal of Nutrition · doi:10.1093/jn/132.6.1579s · Cited by 46
Direct electrochemical and AFM detection of amyloid-β peptide aggregation on basal plane HOPG
Lopes, P., Xu, M., Zhang, M., Zhou, T., Yang, Y., Wang, C., & Ferapontova, E. E. (2014) · Nanoscale · doi:10.1039/c4nr02413c · Cited by 45
Metadata
- Authors
- Gravina, S. A., Ho, L., Eckman, C. B., Long, K. E., Otvos, L., Younkin, L. H., Suzuki, N., & Younkin, S. G.
- Affiliations
- Case Western Reserve University (US)
- Takeda (Japan) (JP)
- Corresponding author
- Younkin, Steven G.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1995-03
- Volume
- 270
- Issue
- 13
- Pages
- 7013-7016
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1618236677
- Cited by
- 676
- References
- 20
- Citations by year
- 2026: 8 · 2025: 16 · 2024: 19 · 2023: 21 · 2022: 23 · 2021: 33 · 2020: 33 · 2019: 22 · 2018: 18 · 2017: 22 · 2016: 27 · 2015: 20 · 2014: 22 · 2013: 24 · 2012: 24
- FWCI
- 17.94
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (5r01ag012685-04)
- National Institute on Aging (AG06656, R01AG006656, AG12685)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- amyloid-beta, Alzheimer's disease, amyloid-beta 42, Aβ40, cerebral amyloid angiopathy, amyloid plaques, cerebral cortex, vascular wall, amyloid deposition, cerebrospinal fluid
- MeSH terms
- Alzheimer Disease, Cerebral Cortex, Chromatography, Gel, Enzyme-Linked Immunosorbent Assay, Humans, Immunohistochemistry, Reference Values, Temporal Lobe, Amyloid beta-Peptides
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
A language model drew the claims from the paper on 2026-10-27, under version 3 of the claim definition (model deepseek-v4.1-flash, prompt extract-v3).
A second model labelled each claim on 2026-10-27 (model jev-1.13-20260917, definition revision gold-guideline-v0.2).
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
