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Protein Amyloid Aggregation

Overview of attention for book
Cover of 'Protein Amyloid Aggregation'

Table of Contents

  1. Altmetric Badge
    Book Overview
  2. Altmetric Badge
    Chapter 1 Semisynthesis and Enzymatic Preparation of Post-translationally Modified α-Synuclein.
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    Chapter 2 Isotope-Labeled Amyloids via Synthesis, Expression, and Chemical Ligation for Use in FTIR, 2D IR, and NMR Studies.
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    Chapter 3 Intermolecular Paramagnetic Relaxation Enhancement (PRE) Studies of Transient Complexes in Intrinsically Disordered Proteins.
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    Chapter 4 Detection of Helical Intermediates During Amyloid Formation by Intrinsically Disordered Polypeptides and Proteins.
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    Chapter 5 Fluorescence Correlation Spectroscopy: A Tool to Study Protein Oligomerization and Aggregation In Vitro and In Vivo.
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    Chapter 6 Deep UV Resonance Raman Spectroscopy for Characterizing Amyloid Aggregation
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    Chapter 7 Analyzing Tau Aggregation with Electron Microscopy.
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    Chapter 8 Characterization of Amyloid Oligomers by Electrospray Ionization-Ion Mobility Spectrometry-Mass Spectrometry (ESI-IMS-MS).
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    Chapter 9 Formation and Characterization of α-Synuclein Oligomers.
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    Chapter 10 Fluorescence Methods for Unraveling Oligomeric Amyloid Intermediates
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    Chapter 11 Preparation of Amyloid Fibrils for Magic-Angle Spinning Solid-State NMR Spectroscopy
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    Chapter 12 Spin Labeling and Characterization of Tau Fibrils Using Electron Paramagnetic Resonance (EPR).
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    Chapter 13 Preparation of Crystalline Samples of Amyloid Fibrils and Oligomers
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    Chapter 14 Quenched Hydrogen Exchange NMR of Amyloid Fibrils
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    Chapter 15 Studying the Early Stages of Protein Aggregation Using Replica Exchange Molecular Dynamics Simulations
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    Chapter 16 Computational Methods for Structural and Functional Studies of Alzheimer's Amyloid Ion Channels.
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    Chapter 17 Analyzing Ensembles of Amyloid Proteins Using Bayesian Statistics
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    Chapter 18 In Vitro Studies of Membrane Permeability Induced by Amyloidogenic Polypeptides Using Large Unilamellar Vesicles
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    Chapter 19 Cell Models to Study Cell-to-Cell Transmission of α-Synuclein.
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    Chapter 20 Preparation of Amyloid Fibrils Seeded from Brain and Meninges.
Attention for Chapter 4: Detection of Helical Intermediates During Amyloid Formation by Intrinsically Disordered Polypeptides and Proteins.
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About this Attention Score

  • In the top 25% of all research outputs scored by Altmetric
  • High Attention Score compared to outputs of the same age (80th percentile)
  • High Attention Score compared to outputs of the same age and source (87th percentile)

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Chapter title
Detection of Helical Intermediates During Amyloid Formation by Intrinsically Disordered Polypeptides and Proteins.
Chapter number 4
Book title
Protein Amyloid Aggregation
Published in
Methods in molecular biology, January 2016
DOI 10.1007/978-1-4939-2978-8_4
Pubmed ID
26453205
Book ISBNs
978-1-4939-2977-1, 978-1-4939-2978-8
Authors

Abedini, Andisheh, Cao, Ping, Raleigh, Daniel P, Andisheh Abedini, Ping Cao, Daniel P. Raleigh

Abstract

Amyloid formation and aberrant protein aggregation are hallmarks of more than 30 different human diseases. The proteins that form amyloid can be divided into two structural classes: those that form compact, well-ordered, globular structures in their unaggregated state and those that are intrinsically disordered in their unaggregated states. The latter include the Aβ peptide of Alzheimer's disease, islet amyloid polypeptide (IAPP, amylin) implicated in type 2 diabetes and α-synuclein, which is linked to Parkinson's disease. Work in the last 10 years has highlighted the potential role of pre-amyloid intermediates in cytotoxicity and has focused attention on their properties. A number of intrinsically disordered proteins appear to form helical intermediates during amyloid formation. We discuss the spectroscopic methods employed to detect and characterize helical intermediates in homogenous solution and in membrane-catalyzed amyloid formation, with the emphasis on the application of circular dichroism (CD). IAPP is used as an example, but the methods are generally applicable.

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Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 16 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 16 100%

Demographic breakdown

Readers by professional status Count As %
Student > Bachelor 4 25%
Student > Doctoral Student 2 13%
Student > Ph. D. Student 2 13%
Professor 1 6%
Student > Master 1 6%
Other 2 13%
Unknown 4 25%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 4 25%
Agricultural and Biological Sciences 3 19%
Medicine and Dentistry 2 13%
Pharmacology, Toxicology and Pharmaceutical Science 1 6%
Nursing and Health Professions 1 6%
Other 3 19%
Unknown 2 13%
Attention Score in Context

Attention Score in Context

This research output has an Altmetric Attention Score of 7. 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 16 October 2015.
All research outputs
#4,180,871
of 22,834,308 outputs
Outputs from Methods in molecular biology
#1,132
of 13,126 outputs
Outputs of similar age
#71,813
of 393,581 outputs
Outputs of similar age from Methods in molecular biology
#168
of 1,470 outputs
Altmetric has tracked 22,834,308 research outputs across all sources so far. Compared to these this one has done well and is in the 80th percentile: it's in the top 25% of all research outputs ever tracked by Altmetric.
So far Altmetric has tracked 13,126 research outputs from this source. They receive a mean Attention Score of 3.4. This one has done particularly well, scoring higher than 90% 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 393,581 tracked outputs that were published within six weeks on either side of this one in any source. This one has done well, scoring higher than 80% of its contemporaries.
We're also able to compare this research output to 1,470 others from the same source and published within six weeks on either side of this one. This one has done well, scoring higher than 87% of its contemporaries.

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