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Amyloid Proteins

Overview of attention for book
Cover of 'Amyloid Proteins'

Table of Contents

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    Book Overview
  2. Altmetric Badge
    Chapter 1 Amyloid Proteins
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    Chapter 2 Application of Photochemical Cross-linking to the Study of Oligomerization of Amyloidogenic Proteins
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    Chapter 3 Preparation of Stable Amyloid β-Protein Oligomers of Defined Assembly Order
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    Chapter 4 Purification and Fibrillation of Full-Length Recombinant PrP
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    Chapter 5 Featuring Amyloids with Fourier Transform Infrared and Circular Dichroism Spectroscopies
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    Chapter 6 Quasielastic Light Scattering Study of Amyloid β-Protein Fibrillogenesis
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    Chapter 7 Conformations of Microtubule-Associated Protein Tau Mapped by Fluorescence Resonance Energy Transfer
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    Chapter 8 Measuring the kinetics of amyloid fibril elongation using quartz crystal microbalances.
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    Chapter 9 X-Ray Fibre Diffraction Studies of Amyloid Fibrils
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    Chapter 10 Structural Characterization of Prefibrillar Intermediates and Amyloid Fibrils by Small-Angle X-Ray Scattering
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    Chapter 11 Atomic Force Fluorescence Microscopy in the Characterization of Amyloid Fibril Assembly and Oligomeric Intermediates
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    Chapter 12 Investigating Fibrillar Aggregates of Tau Protein by Atomic Force Microscopy
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    Chapter 13 Amyloid Proteins
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    Chapter 14 Amyloid Proteins
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    Chapter 15 Search for Amyloid-Binding Proteins by Affinity Chromatography
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    Chapter 16 Establishing the Links Between Aβ Aggregation and Cytotoxicity In Vitro Using Biophysical Approaches
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    Chapter 17 Preparation of Cultured Human Vascular Cells
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    Chapter 18 Murine Cerebrovascular Cells as a Cell Culture Model for Cerebral Amyloid Angiopathy: Isolation of Smooth Muscle and Endothelial Cells from Mouse Brain
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    Chapter 19 In Vitro Assays Measuring Protection by Proteins such as Cystatin C of Primary Cortical Neuronal and Smooth Muscle Cells
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    Chapter 20 Study of Neurotoxic Intracellular Calcium Signalling Triggered by Amyloids
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    Chapter 21 Bacterial amyloids.
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    Chapter 22 Study of Amyloids Using Yeast
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    Chapter 23 Cell-to-Cell Transmission of α-Synuclein Aggregates
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    Chapter 24 Subcutaneous Adipose Tissue Biopsy for Amyloid Protein Studies
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    Chapter 25 Analysis of s100 oligomers and amyloids.
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    Chapter 26 S100A8/A9 Amyloidosis in the Ageing Prostate: Relating Ex Vivo and In Vitro Studies
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    Chapter 27 Isolation of Amyloid by Solubilization in Water
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    Chapter 28 Histological Staining of Amyloid and Pre-amyloid Peptides and Proteins in Mouse Tissue
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    Chapter 29 A Pentameric Luminescent-Conjugated Oligothiophene for Optical Imaging of In Vitro-Formed Amyloid Fibrils and Protein Aggregates in Tissue Sections
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    Chapter 30 In Vivo Magnetic Resonance Imaging of Amyloid-β Plaques in Mice.
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    Chapter 31 The Mouse Model for Scrapie: Inoculation, Clinical Scoring, and Histopathological Techniques
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    Chapter 32 Biochemical Isolation of Insoluble Tau in Transgenic Mouse Models of Tauopathies
  34. Altmetric Badge
    Chapter 33 Tissue processing prior to analysis of Alzheimer's disease associated proteins and metabolites, including aβ.
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    Chapter 34 Aβ measurement by enzyme-linked immunosorbent assay.
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    Chapter 35 Cognitive and Sensorimotor Tasks for Assessing Functional Impairments in Mouse Models of Alzheimer’s Disease and Related Disorders
Attention for Chapter 34: Aβ measurement by enzyme-linked immunosorbent assay.
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101 Mendeley
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Chapter title
Aβ measurement by enzyme-linked immunosorbent assay.
Chapter number 34
Book title
Amyloid Proteins
Published in
Methods in molecular biology, April 2012
DOI 10.1007/978-1-61779-551-0_34
Pubmed ID
Book ISBNs
978-1-61779-550-3, 978-1-61779-551-0
Authors

Schmidt SD, Mazzella MJ, Nixon RA, Mathews PM, Stephen D. Schmidt, Matthew J. Mazzella, Ralph A. Nixon, Paul M. Mathews, Schmidt, Stephen D., Mazzella, Matthew J., Nixon, Ralph A., Mathews, Paul M.

Abstract

The neuritic plaque in the brain of Alzheimer's disease patients consists of an amyloid composed primarily of Aβ, an approximately 4-kDa peptide derived from the amyloid precursor protein. Multiple lines of evidence suggest that Aβ plays a key role in the pathogenesis of the disease, and potential treatments that target Aβ production and/or Aβ accumulation in the brain as β-amyloid are being aggressively pursued. Methods to quantitate the Aβ peptide are, therefore, invaluable to most studies aimed at a better understanding of the molecular etiology of the disease and in assessing potential therapeutics. Although other techniques have been used to measure Aβ in the brains of AD patients and β-amyloid-depositing transgenic mice, the enzyme-linked immunosorbent assay (ELISA) is one of the most commonly used, reliable, and sensitive methods for quantitating the Aβ peptide. Here we describe methods for the recovery of both soluble and deposited Aβ from brain tissue and the subsequent quantitation of the peptide by sandwich ELISA.

Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 101 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
United States 1 <1%
Unknown 100 99%

Demographic breakdown

Readers by professional status Count As %
Student > Bachelor 29 29%
Student > Ph. D. Student 15 15%
Student > Master 15 15%
Researcher 5 5%
Other 4 4%
Other 13 13%
Unknown 20 20%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 20 20%
Agricultural and Biological Sciences 13 13%
Chemistry 10 10%
Engineering 8 8%
Pharmacology, Toxicology and Pharmaceutical Science 6 6%
Other 22 22%
Unknown 22 22%
Attention Score in Context

Attention Score in Context

This research output has an Altmetric Attention Score of 3. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 14 July 2023.
All research outputs
#7,453,126
of 22,785,242 outputs
Outputs from Methods in molecular biology
#2,316
of 13,094 outputs
Outputs of similar age
#54,054
of 163,478 outputs
Outputs of similar age from Methods in molecular biology
#10
of 43 outputs
Altmetric has tracked 22,785,242 research outputs across all sources so far. This one is in the 44th percentile – i.e., 44% of other outputs scored the same or lower than it.
So far Altmetric has tracked 13,094 research outputs from this source. They receive a mean Attention Score of 3.4. This one has done well, scoring higher than 76% of its peers.
Older research outputs will score higher simply because they've had more time to accumulate mentions. To account for age we can compare this Altmetric Attention Score to the 163,478 tracked outputs that were published within six weeks on either side of this one in any source. This one is in the 47th percentile – i.e., 47% of its contemporaries scored the same or lower than it.
We're also able to compare this research output to 43 others from the same source and published within six weeks on either side of this one. This one has gotten more attention than average, scoring higher than 62% of its contemporaries.