The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Amyloidosis: a final common pathway for protein deposition in tissues
Abstract
This review summarizes recent advances in understanding of the amyloid diseases. They are of interest to hematologists for at least three reasons: (a) Many of the precursor proteins circulate in the blood, (b) one of the more common types of amyloidosis is a plasma cell dyscrasia, and (c) many patients with amyloid disorders require hematological evaluation at some time during the course of their disease
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.
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
The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor
Kang, J., Lemaire, H.-G., Unterbeck, A., Salbaum, J. M., Masters, C. L., Grzeschik, K.-H., Multhaup, G., Beyreuther, K., & Müller-Hill, B. (1987) · Nature · doi:10.1038/325733a0 · Cited by 4,619
Amyloid β Protein Gene: cDNA, mRNA Distribution, and Genetic Linkage Near the Alzheimer Locus
Tanzi, R. E., Gusella, J. F., Watkins, P. C., Bruns, G. A. P., St George-Hyslop, P., Van Keuren, M. L., Patterson, D., Pagan, S., Kurnit, D. M., & Neve, R. L. (1987) · Science · doi:10.1126/science.2949367 · Cited by 1,611
Cited by
Partial denaturation of transthyretin is sufficient for amyloid fibril formation in vitro
Colon, W., & Kelly, J. W. (1992) · Biochemistry · doi:10.1021/bi00151a036 · Cited by 573
Prolines and Aamyloidogenicity in Fragments of the Alzheimer's Peptide .beta./A4
Wood, S. J., Wetzel, R., Martin, J. D., & Hurle, M. R. (1995) · Biochemistry · doi:10.1021/bi00003a003 · Cited by 312
Elimination of prions by branched polyamines and implications for therapeutics
Supattapone, S., Nguyen, H.-O. B., Cohen, F. E., Prusiner, S. B., & Scott, M. R. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.25.14529 · Cited by 259
Metadata
- Authors
- Stone, M.
- Venue
- Blood
- Publisher
- American Society of Hematology
- Published
- 1990-02-01
- Volume
- 75
- Issue
- 3
- Pages
- 531-545
- ISSN
- 0006-4971 (ISSN-L)
- 1528-0020
- OpenAlex
- W2133783264
- Cited by
- 162
- References
- 2
- FWCI
- 4.86
- Type
- journal article
- Language
- en
- Open access
- closed
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
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: Amyloidosis: a final common pathway for protein deposition in tissues. https://app.cochat.ai/papers/10.1182/blood.v75.3.531.531
- The paper
- Stone, M. (1990). Amyloidosis: a final common pathway for protein deposition in tissues. Blood. https://doi.org/10.1182/blood.v75.3.531.531
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
