The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
Blood-brain barrier uptake of the 40 and 42 amino acid sequences of circulating Alzheimer's amyloid β in guinea pigs
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
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
“Previous studies have shown that circulating free A b is also metabolized during its transport across the BBB (48, 49, 65, 66), possibly by pericytes, which represent a major enzymatic barrier for the transport of several peptides and proteins across the BBB (67).”
From Clearance of Alzheimer’s amyloid-β1-40 peptide from brain by LDL receptor–related protein-1 at the blood-brain barrier (2000) · cites this paper as [65]
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
“This makes re-entry of radiolabeled A b into the brain very unlikely, because the blood-to-brain transport of A b normally operates down the concentration gradient (39, 62-65).”
From Clearance of Alzheimer’s amyloid-β1-40 peptide from brain by LDL receptor–related protein-1 at the blood-brain barrier (2000) · cites this paper as [65]
Experimental — accuracy not yet measured
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
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
Isolation 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
Amyloid β Protein (Aβ) in Alzheimeri's Disease Brain
Gravina, S. A., Ho, L., Eckman, C. B., Long, K. E., Otvos, L., Younkin, L. H., Suzuki, N., & Younkin, S. G. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.13.7013 · Cited by 676
The role of integrins in the maintenance of endothelial monolayer integrity.
Lampugnani, M. G., Resnati, M., Dejana, E., & Marchisio, P. C. (1991) · The Journal of cell biology · doi:10.1083/jcb.112.3.479 · Cited by 292
Flagged first, then by citations
Research works printed but not linked: 13
- Ghiso, 1992, A 109-amino-acid C-terminal fragment of Alzheimer's disease amyloid precursor protein contains a sequence, RHDS, that promotes cell adhesion, Biochem. J., 288, 1053, 10.1042/bj2881053 · DOI
- Ghiso, 1994, Unifying features of systemic and cerebral amyloidosis, Mol. Neurobiol., 8, 49, 10.1007/BF02778007 · DOI
- Johnstone, 1991, Conservation of the sequence of Alzheimer's disease amyloid peptide in dog, polar bear and five other mammals by cross-species polymerase chain reaction analysis, Mol. Brain Res., 10, 299, 10.1016/0169-328X(91)90088-F · DOI
- Maness, 1994, Passage of human amyloid β-protein 1–40 across the murine blood-brain barrier, Life Sci., 55, 1643, 10.1016/0024-3205(94)00331-9 · DOI · Paper page
- Saporito-Irwin, 1995, Coagulation factor Xla cleaves the RHDS sequence and abolishes the cell adhesive properties of the amyloid β-protein, J. Biol. Chem., 270, 26265, 10.1074/jbc.270.44.26265 · DOI
- Soto, 1995, Fibrillogenesis of synthetic amyloid β peptide is dependent on the initial secondary structure, Neurosci. Lett., 200, 105, 10.1016/0304-3940(95)12089-M · DOI
- Soto, 1995, Two conformational states of amyloid β-peptide: implications for the pathogenesis of Alzheimer's disease, Neurosci. Lett., 186, 115, 10.1016/0304-3940(95)11299-C · DOI
- Suzuki, 1994, An increased percentage of long amyloid beta protein secreted by familial amyloid beta protein precursor (beta APP717) mutants, Science, 264, 1336, 10.1126/science.8191290 · DOI · Paper page
- Walker, 1995, In vivo binding of synthetic β-amyloid (Aβ) to endogenous Aβ in aged monkeys, Soc. Neurosci. Abstr., 21, 257
- Wisniewski, 1994, Alzheimer's disease and soluble Aβ, Neurobiol. Aging, 15, 143, 10.1016/0197-4580(94)90105-8 · DOI
- Zlokovic, 1995, Cerebrovascular permeability to peptides: manipulations of transport systems at the blood-brain barrier, Pharm. Res., 12, 1395, 10.1023/A:1016254514167 · DOI
- Zlokovic, 1993, Blood-brain barrier transport of circulating Alzheimer's amyloid β, Biochem. Biophys. Res. Commun., 197, 1034, 10.1006/bbrc.1993.2582 · DOI · Paper page
- Zlokovic, 1994, Brain uptake of circulating apolipoproteins J and E complexed to Alz heimer's amyloid β, Biochem. Biophys. Res. Commun., 205, 1431, 10.1006/bbrc.1994.2825 · DOI
Cited by
Sorted by citations
The Blood-Brain Barrier in Health and Chronic Neurodegenerative Disorders
Zlokovic, B. V. (2008) · Neuron · doi:10.1016/j.neuron.2008.01.003 · Cited by 3,280
Neurovascular pathways to neurodegeneration in Alzheimer’s disease and other disorders
Zlokovic, B. V. (2011) · Nature Reviews Neuroscience · doi:10.1038/nrn3114 · Cited by 2,969
RAGE mediates amyloid-β peptide transport across the blood-brain barrier and accumulation in brain
Deane, R., Du Yan, S., Submamaryan, R. K., LaRue, B., Jovanovic, S., Hogg, E., Welch, D., Manness, L., Lin, C., Yu, J., et al. (2003) · Nature Medicine · doi:10.1038/nm890 · Cited by 1,426
Self-citationShibata, M., Yamada, S., Kumar, S. R., Calero, M., Bading, J., Frangione, B., Holtzman, D. M., Miller, C. A., Strickland, D. K., Ghiso, J., et al. (2000) · Journal of Clinical Investigation · doi:10.1172/jci10498 · Cited by 1,413
Self-citationThe Blood-Brain Barrier in Brain Homeostasis and Neurological Diseases
Weiss, N., Miller, F., Cazaubon, S., & Couraud, P.-O. (2009) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2008.10.022 · Cited by 731
Metadata
- Authors
- Martel, C. L., Mackic, J. B., McComb, J. G., Ghiso, J., & Zlokovic, B. V.
- Venue
- Neuroscience Letters
- Publisher
- Elsevier BV
- Published
- 1996-03
- Volume
- 206
- Issue
- 2-3
- Pages
- 157-160
- ISSN
- 0304-3940
- Cited by
- 69
- References
- 4
- Language
- en
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.
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