The DOI matches its Crossref record; 42 of the 42 references it cites were found in a registry or an index.
Assembly and aggregation properties of synthetic Alzheimer's A4/beta amyloid peptide analogs.
Open accessAbstract
The amyloid A4 or beta peptide is a major component of extracellular amyloid deposits that are a characteristic feature of Alzheimer's disease. We synthesized a series of peptide analogs of the A4/beta peptide which are progressively longer at their carboxyl termini, including 42- and 39-residue peptides which represent the major forms of the A4/beta peptide in senile plaque and the hereditary cerebral hemorrhage with amyloidosis form, respectively. All peptides tested, beta 1-28 through beta 1-42, formed amyloid-like fibrils and previously unreported thin sheet-like structures which stained with thioflavin T and Congo Red. The solubility of beta 1-42 and shorter peptides was pH and concentration dependent, with a broad insolubility profile in the pH range of 3.5-6.5 and at concentrations above 0.75 mg/ml. Only peptides of 42 residues or longer were significantly insoluble at pH 7.4. beta 1-47 and beta 1-52 peptides are highly insoluble in aqueous media but are soluble at 40 mg/ml in the alpha helix-promoting solvent, 1,1,1,3,3,3-hexafluoro-2-propanol. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis revealed that the beta 1-42 peptide migrates as a series of higher molecular mass aggregates whereas shorter peptides migrate as monomers. Aggregation is also dependent on pH, peptide concentration, and time of incubation in aqueous medium. These results indicate that the length of the hydrophobic carboxyl terminus of the A4/beta peptide is important in determining the s…
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
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?
In the citing paper
“A{31-42 has been shown to form insoluble amyloid fibrils more rapidly than A{31-40 (10)(11)(12)(13).”
From Amyloid β Protein (Aβ) in Alzheimeri's Disease Brain (1995) · cites this paper as [11]
Citations
Cites
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
LAEMMLI, U. K. (1970) · Nature · doi:10.1038/227680a0 · Cited by 249,961
Glenner, G. G., & Wong, C. W. (1984) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(84)80190-4 · Cited by 5,404
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 plaque core protein in Alzheimer disease and Down syndrome.
Masters, C. L., Simms, G., Weinman, N. A., Multhaup, G., McDonald, B. L., & Beyreuther, K. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.12.4245 · Cited by 4,431
Neurotrophic and Neurotoxic Effects of Amyloid β Protein: Reversal by Tachykinin Neuropeptides
Yankner, B. A., Duffy, L. K., & Kirschner, D. A. (1990) · Science · doi:10.1126/science.2218531 · Cited by 1,975
Cleavage of Amyloid β Peptide During Constitutive Processing of Its Precursor
Esch, F. S., Keim, P. S., Beattie, E. C., Blacher, R. W., Culwell, A. R., Oltersdorf, T., McClure, D., & Ward, P. J. (1990) · Science · doi:10.1126/science.2111583 · Cited by 1,403
Identification, biogenesis, and localization of precursors of Alzheimer's disease A4 amyloid protein
Weidemann, A., König, G., Bunke, D., Fischer, P. Q., Salbaum, J. M., Masters, C. L., & Beyreuther, K. T. (1989) · Cell · doi:10.1016/0092-8674(89)90177-3 · Cited by 1,233
Novel precursor of Alzheimer's disease amyloid protein shows protease inhibitory activity
Kitaguchi, N., Takahashi, Y., Tokushima, Y., Shiojiri, S., & Ito, H. (1988) · Nature · doi:10.1038/331530a0 · Cited by 1,083
Quantitative monitoring of solid-phase peptide synthesis by the ninhydrin reaction
Sarin, V. K., Kent, S. B. H., Tam, J. P., & Merrifield, R. B. (1981) · Analytical Biochemistry · doi:10.1016/0003-2697(81)90704-1 · Cited by 1,066
A new A4 amyloid mRNA contains a domain homologous to serine proteinase inhibitors
Ponte, P. A., Gonzalez‐DeWhitt, P. A., Schilling, J., Miller, J., Hsu, D. K., Greenberg, B., Davis, K. L., Wallace, W., Lieberburg, I. M., Fuller, F. H., et al. (1988) · Nature · doi:10.1038/331525a0 · Cited by 1,050
Research works printed but not linked: 4
- Beyreuther, 1986, Discoveries Neurosci., 3, 68
- Glabe, 1990, Technique, 2, 138
- Joachim, 1989, Am. J. Pathol., 135, 309
- Masters, 1987, Ciba Found. Symp., 126, 49
Cited by
Sorted by citations
Items 901–1,000 of 1,000
The Molecular Mechanism of Amyloidosis in Alzheimer’s Disease
Zagorski, M. G. (1999) · CRC Press eBooks · doi:10.1201/9780203909607.ch14 · Cited by 1
Production of Amyloid β Protein from Normal and Mutated Amyloid β Protein Precursors
Golde, T. E., Cai, X., Cheung, T. T., Shoji, M., & Younkin, S. G. (1994) · Springer eBooks · doi:10.1007/978-3-662-01135-5_4 · Cited by 1
Synthesis of Alzheimer's (1–42) Aβ-amyloid peptide with preformed Fmoc-aminoacyl fluorides
Milton, S. C. F., Milton, R. C. D. L., Kates, S. A., & Glabe, C. G. (1997) · Techniques in protein chemistry · doi:10.1016/s1080-8914(97)80083-x · Cited by 1
Self-citationMechanism of Cerebral Amyloidosis in Alzheimer’s Disease
Allsop, D., Clements, A., Kennedy, H., Walsh, D. M., & Williams, C. H. (1994) · Springer eBooks · doi:10.1007/978-3-662-01135-5_5 · Cited by 1
Hamblett, C. L., Shah, S., Heidebrecht, R. W., & Muñoz, B. (2010) · Methods and principles in medicinal chemistry · doi:10.1002/9783527630943.ch13 · Cited by 1
Jiao, Y., & Yang, P. (2007) · Science China Chemistry · doi:10.1007/s11426-007-0077-x · Cited by 1
Hood, C. A., Fuentes, G., Patel, H., Page, K., Menakuru, M., & Park, J. H. (2009) · ChemInform · doi:10.1002/chin.200932270
KÖNIG, G., GRAHAM, P., Bushnell, A. F., Webster, S. M., Wunderlich, D. A., & Perlmutter, L. S. (1996) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1996.tb34444.x · Cited by 1
Proteomic strategies for analysis of cerebrospinal fluid in neurodegenerative disorders
Hansson, S. (2008) · Gothenburg University Publications Electronic Archive (Gothenburg University) · Cited by 1
A study of b-secretase cleaved Alzheimer amyloid precursor protein
Sennvik, K. (2002) · Figshare · Cited by 1
The presenilins as potential drug targets in Alzheimer’s disease
Cupers, P., Annaert, W. G., & Strooper, B. D. (1999) · Emerging Therapeutic Targets · doi:10.1517/14728222.3.3.413 · Cited by 3
Yeast as a Model for Studying Aβ Aggregation, Toxicity and Clearance
Bharadwaj, P. (2011) · Australasian Journal of Paramedicine · Cited by 1
Riek, R., Güntert, P., Döbeli, H., Wipf, B., & Kurt Wüthrich, A. (2001) · Cited by 1
Entrada de calcio inducida por los oligómeros del péptido amiloide en la Enfermedad de Alzheimer
Ortega, E. C. (2013) · UVaDOC UVaDOC University of Valladolid Documentary Repository (University of Valladolid) · doi:10.35376/10324/3786 · Cited by 1
Structural Characterization and Membrane Interactions of the Amyloid Peptide PrP(106-126)
Walsh, P. J. (2013) · TSpace (University of Toronto) · Cited by 1
Metabolic Abnormalities in Alzheimer Disease
Gebhardt, F. M., & Dodd, P. R. (2008) · Springer eBooks · doi:10.1007/978-0-387-79112-8_22 · Cited by 1
Chemical Synthesis of Microtubule-Associated Protein Tau 2N4RPreprint
Powell, W. C., Jing, R., & Walczak, M. A. A. (2023) · ChemRxiv · doi:10.26434/chemrxiv-2023-js9bp
p53, a Molecular Bridge Between Alzheimer’s Disease Pathology and Cancers?
Checler, F., Dunys, J., Pardossi‐Piquard, R., & da Costa, C. A. (2010) · Research and perspectives in Alzheimer's disease · doi:10.1007/978-3-642-16602-0_8
Gandy, S. (2002) · Handbook of experimental pharmacology · doi:10.1007/978-3-662-06274-6_15
Cotman, C. W., Cribbs, D. H., & Su, J. H. (1997) · Birkhäuser Boston eBooks · doi:10.1007/978-1-4612-4116-4_16
Self-citationMicroglial involvement in brain physiopathology: in vitro studies using rat primary cultures
Mengoni, I. (2014) · AMS Dottorato Institutional Doctoral Theses Repository (University of Bologna) · doi:10.6092/unibo/amsdottorato/6466
Barkóczi, B. (2013) · SZTE Repository of Dissertations (University of Szeged) · doi:10.14232/phd.1769
Neurobiologic Basis of Age-Related Dementing Disorders
Hof, P. R., Bussière, T., Buxbaum, J. D., & Morrison, J. H. (2006) · Springer eBooks · doi:10.1007/0-387-22621-4_76
Mechanisms of Brain Region-Specific Amyloid-beta Deposition
Bero, A. W. (2011) · Open Scholarship Institutional Repository (Washington University in St. Louis) · doi:10.7936/k7cj8bh2
Haass, C. (2000) · Handbook of experimental pharmacology · doi:10.1007/978-3-642-57092-6_20
Biophysical Investigations of the Aβ Aggregation Process
Muni, S. C. (2014) · D-Scholarship@Pitt (University of Pittsburgh)
Transgenic Models of Amyotrophic Lateral Sclerosis and Alzheimer's Disease
Wong, P. C., Borchelt, D., Lee, M. K., Thinakaran, G., Sisodia, S. S., & Price, D. L. (1998) · Elsevier eBooks · doi:10.1016/b978-012734610-6/50008-7
Regulierung und Verfügbarkeit von Apolipoprotein E in Astrozyten
Hamker, U. (2005) · edoc Publication server (Humboldt University of Berlin) · doi:10.18452/15272
Adlerz, L. (2007) · KTH Publication Database DiVA (KTH Royal Institute of Technology)
A Mini Review on Aβ Oligomers and its Pathogencity
Tuyet, P. T. D. (2014) · Journal of the Chosun Natural Science · doi:10.13160/ricns.2014.7.2.79
Agnes Henschen-Edman, M.D., Ph.D. April 1, 1935 to October 23, 2011
Blombäck, M., & Lord, S. T. (2012) · Thrombosis Research · doi:10.1016/j.thromres.2012.06.019
Jayalal, L. P. M. (2013) · Journal of the Chosun Natural Science · doi:10.13160/ricns.2013.6.1.021
Panegyres, P. K., & Atkins, E. (2011) · Neuroscience & Medicine · doi:10.4236/nm.2011.23033
SPECIFIC AMYLOID-BETA OLIGOMERS IN HUMAN CEREBROSPINAL FLUID
Handoko, M. (2012) · University of Minnesota Digital Conservancy (University of Minnesota)
New Structural View on How Amyloid Beta Production Hints Alzheimer’s Disease Pathology
Yan, X., Yang, Q., Howe, J., Fu, Q., & Wang, L. (2014) · Postdoc Journal · doi:10.14304/surya.jpr.v2n9.7
Die Molekularbiologie der Alzheimer-Krankheit
Urmoneit, B. (1999) · Springer eBooks · doi:10.1007/978-3-642-60231-3_11
Fibrillar aggregations of pathogenic pro-vasopressin mutants
Birk, J. (2009) · edoc (University of Basel) · doi:10.5451/unibas-005148703
Targeting cytotoxic species in amyloid diseases
Persson, M. (2012)
Na,K-ATPase α Subunit-like Immunoreactive Proteins in Human Body Fluids
Peng, J. F. (2006) · American Journal of Immunology · doi:10.3844/ajisp.2006.8.11
Dumanchin‐Njock, C., Lopez‐Perez, E., Marambaud, P., Paitel, E., Petit-Paitel, A., & Vincent, B. (2002)
Garzon, D. J., & Mount, J. (2009)
Studies on -secretase activity and products
Frånberg, J. (2010)
Xie, H. (2014) · HKBU Institutional Repository (Hong Kong Baptist University)
Bush, A. I., Pettingell, W. H., & Tanzi, R. E. (1994) · Research and perspectives in Alzheimer's disease · doi:10.1007/978-3-662-01135-5_16
Merlin, J. L. P. (2013) · Journal of the Chosun Natural Science · doi:10.13160/ricns.2013.6.4.220
IMMUNOCYTOCHEMICAL STUDY OF AMYLOID β PROTEIN PRECURSOR IN MOUSE AND RAT BRAINS
Kawarabayashi, T. (1993) · Kitakantou igaku/Kitakantō Igaku · doi:10.2974/kmj1951.43.11
Tuyet, P. T. D. (2014) · Journal of the Chosun Natural Science · doi:10.13160/ricns.2014.7.1.11
Gomes, S. M. (2017) · TSpace (University of Toronto)
The microrna-mediated regulation of proteins implicated in the pathogenesis of Alzheimer's Disease
Chopra, N. (2016) · IUScholarWorks (Indiana University) · doi:10.7912/c28019
Alpha-synuclein expression influences the processing of the amyloid precursor protein
Hall‐Roberts, H. (2016) · The University of Bath Online Publications Store (The University of Bath)
Cognitive and Non-Cognitive Dysfunction in a Mouse Model of Alzheimer's Disease
Lee, W.-J. (2017) · Scholarship@Western (Western University)
Liu, A. W. K. (2015) · TSpace (University of Toronto)
Polymorphism of Alzheimer’s Aβ Amyloid Fibrils and Oligomers
Antzutkin, O. N. (2018) · Springer eBooks · doi:10.1007/978-3-319-28388-3_31
Mechanisms of Memory Deficits in Mouse Models of Alzheimer's Disease
Yiu, A. P. (2012) · TSpace (University of Toronto)
Charakterisierung von Prädiktoren rapid-progressiver Verläufe des M. Alzheimer
Bartlau, T. (2016) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-5745
Amyloid aggregates: detection and interaction
Rahman, M. M. (2018) · Epsilon Open Archive (Sveriges lantbruksuniversitet biblioteket (Swedish University of Agricultural Sciences))
THE CONTRIBUTION OF MOSAIC MUTATION TO AUTISM SPECTRUM DISORDER
Freed, D. N. (2017)
Feng, L. (2019) · Research Online (University of Wollongong)
JAMISON, J. (2003) · Elsevier eBooks · doi:10.1016/b978-0-443-07193-5.50014-5
Feng, L., Watanabe, H., Molino, P. J., Wallace, G. G., Phung, S. L., Uchihashi, T., & Higgins, M. J. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.10.17.343830
Strain-specific profiling of Amyloid-β in Alzheimer´s disease: functional and clinical signature
Noor, A. (2020) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-7997
βAPP Metabolites, Radicals, Calcium, and Neurodegeneration: Novel Neuroprotective Strategies
Mattson, M. P., Barger, S. W., Furukawa, K., Mark, R. J., Smith‐Swintosky, V. L., Pettigrew, L. C., & Bruce‐Keller, A. J. (1996) · Springer eBooks · doi:10.1007/978-1-4899-0209-2_38
Characterisation of the ghrelinergic system in human models of neurodegenerative diseases
Carisi, M. C. (2021) · Cronfa (Swansea University) · doi:10.23889/suthesis.58915
Siman, R., & Greenberg, B. (1996) · Humana Press eBooks · doi:10.1007/978-1-59259-466-5_10
Improved synthesis and purification of Alzheimer's Aβ 1–42 and analogs
Milton, S. C. F., Milton, R. C. D. L., Kates, S. A., & Glabe, C. G. (1999) · Letters in Peptide Science · doi:10.1023/a:1008858416745
Self-citationNicht-VSEPR-Strukturen und chemische Bindung in d0-Systemen
Kaupp, M. (2001) · Angewandte Chemie · doi:10.1002/1521-3757(20011001)113:19 · Cited by 50
Gandy, S., & Greengard, P. (1994) · Springer eBooks · doi:10.1007/978-3-662-01135-5_10
Targeting Various Pathogenic Pathways for the Development of Anti-alzheimer’s Drugs: An Update
Ambreen, S., Fatima, N., Umar, M., Shaququzzaman, M., Alam, M. M., & Ali, R. (2023) · Current Topics in Medicinal Chemistry · doi:10.2174/0115680266274924231002110733
Bubeníková, A., Máčová, L., Skalický, P., Mládek, A., & Bradáč, O. (2023) · Springer eBooks · doi:10.1007/978-3-031-36522-5_15
The nature of tyrosine-aminated amyloid-βPreprint
Gao, Z., Hu, T., Wu, J., Fu, S., & Li, H. (2024) · Research Square · doi:10.21203/rs.3.rs-3752850/v1
Paterno, G., Moore, B. D., Bell, B. M., Gorion, K.-M. M., Ran, Y., Prokop, S., Golde, T. E., & Giasson, B. I. (2024) · Antibodies · doi:10.3390/antib13030068
Microglial glutathione and glutamate: regulation mechanisms
Fry, V. A. H. (2009) · UCL Discovery (University College London)
Aß Toxicity in Alzheimer’s Disease
Klein, W. L. (2001) · Humana Press eBooks · doi:10.1007/978-1-59259-006-3_1 · Cited by 14
Ahmed, S., Barale, S. S., Kamble, R. S., Fatema, K., Sonawane, K. D., Hefferon, K. L., Paek, K., & Shohael, A. M. (2026) · Network Modeling Analysis in Health Informatics and Bioinformatics · doi:10.1007/s13721-025-00729-5
Boudet-Devaud, F. (2018) · theses.fr (ABES) · doi:10.70675/111341b9z5eeez4531z8f07zcb44d6f469a0
Arnould, H. (2019) · theses.fr (ABES) · doi:10.70675/9f070729z72aez4fccz9604z8c52be1a62e6
Tomadesso, C. (2018) · theses.fr (ABES) · doi:10.70675/7fad6418zff81z49c7z984dz63aa2e44d7fc
Salin (1998) · doi:10.1002/(sici)1096-9861(19980720)397:1
Self-citation
Metadata
- Authors
- Burdick, D., Soreghan, B., Kwon, M., Kosmoski, J., Knauer, M., Henschen, A., Yates, J., Cotman, C., & Glabe, C.
- Affiliations
- University of California, Irvine (US)
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1992-01
- Volume
- 267
- Issue
- 1
- Pages
- 546-554
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2130144581
- Cited by
- 1,014
- References
- 42
- Citations by year
- 2026: 7 · 2025: 8 · 2024: 14 · 2023: 21 · 2022: 14 · 2021: 29 · 2020: 20 · 2019: 22 · 2018: 28 · 2017: 27 · 2016: 30 · 2015: 29 · 2014: 37 · 2013: 29 · 2012: 31
- FWCI
- 28.77
- 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 (1r35ag007918-01, 5r01hd021379-14)
- National Institute on Aging (AG07918)
- Eunice Kennedy Shriver National Institute of Child Health and Human Development (HD21379)
- 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 › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Prion Diseases and Protein Misfolding
- Keywords
- amyloid-beta, Alzheimer's disease, peptide analogues, amyloid fibril formation, peptide aggregation, solubility, pH dependence, Congo red staining, thioflavin T staining, amyloid plaques, hexafluoroisopropanol, amyloid deposition
- MeSH terms
- Alzheimer Disease, Amino Acid Sequence, Amyloid, Chromatography, High Pressure Liquid, Electrophoresis, Polyacrylamide Gel, Hydrogen-Ion Concentration, Kinetics, Microscopy, Electron, Molecular Sequence Data, Peptides, Mass Spectrometry, 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.
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