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Protein Aggregation

Overview of attention for book
Cover of 'Protein Aggregation'

Table of Contents

  1. Altmetric Badge
    Book Overview
  2. Altmetric Badge
    Chapter 1 Early Aggregation of Amyloid-β(1–42) Studied by Fluorescence Correlation Spectroscopy
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    Chapter 2 Preparation and Investigation of Crucial Oligomers in the Early Stages of Aβ40 and Aβ42 Aggregation
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    Chapter 3 Preparation and Fractionation of Heterogeneous Aβ42 Oligomers with Different Aggregation Properties
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    Chapter 4 An Efficient Method of Expression and Purification of Amyloid-Beta (Aβ1–42) Peptide from E. coli
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    Chapter 5 Solid-State NMR Structure of Amyloid-β Fibrils
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    Chapter 6 Time-Resolved In Situ AFM Measurement of Growth Rates of Aβ40 Fibrils
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    Chapter 7 Monitoring Kinetics of pH-Dependent Aggregation and Disaggregation of the Pmel17 Repeat Domain
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    Chapter 8 Analysis of Tau/Nucleoporin Interactions by Surface Plasmon Resonance Spectroscopy
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    Chapter 9 Microfluidic Chamber Technology to Study Missorting and Spreading of Tau Protein in Alzheimer’s Disease
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    Chapter 10 Using FRET-Based Biosensor Cells to Study the Seeding Activity of Tau and α-Synuclein
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    Chapter 11 Functional Applications of Stable Tau Oligomers in Cell Biology and Electrophysiology Studies
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    Chapter 12 An Additive-Free Model for Tau Self-Assembly
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    Chapter 13 Cross-Linking Mass Spectrometry Analysis of Metastable Compact Structures in Intrinsically Disordered Proteins
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    Chapter 14 A Validated Method to Prepare Stable Tau Oligomers
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    Chapter 15 Light Microscopy and Dynamic Light Scattering to Study Liquid-Liquid Phase Separation of Tau Proteins In Vitro
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    Chapter 16 Study of Tau Liquid-Liquid Phase Separation In Vitro
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    Chapter 17 Liquid-Liquid Phase Separation to Study the Association of Proteins in Solution
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    Chapter 18 Mapping Phase Diagram of Tau-RNA LLPS Under Live Cell Coculturing Conditions
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    Chapter 19 The Role of Buffers in Wild-Type HEWL Amyloid Fibril Formation Mechanism: A Methodological Approach
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    Chapter 20 Reproducible Formation of Insulin Superstructures: Amyloid-Like Fibrils, Spherulites, and Particulates
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    Chapter 21 CD and Solid-State NMR Studies of Low-Order Oligomers of Transthyretin
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    Chapter 22 Identifying Biological and Biophysical Features of Different Maturation States of α-Synuclein Amyloid Fibrils
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    Chapter 23 α-Synuclein Fibril, Ribbon and Fibril-91 Amyloid Polymorphs Generation for Structural Studies
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    Chapter 24 Propagation of Distinct α-Synuclein Strains Within Human Reconstructed Neuronal Network and Associated Neuronal Dysfunctions
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    Chapter 25 Single-Particle Analysis of the Interaction Between Molecules and Protein Aggregated Species by Dual-Color Time-Resolved Fluorescence Spectroscopy
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    Chapter 26 FRAP and FRET Investigation of α-Synuclein Fibrillization via Liquid-Liquid Phase Separation In Vitro and in HeLa Cells
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    Chapter 27 Spectrally Resolved FRET Microscopy of α-Synuclein Phase-Separated Liquid Droplets
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    Chapter 28 Combined H-N Cross-Polarization and Carbonyl Detection NMR Spectroscopy Allow to Record High-Resolution, High-Sensitivity Spectra of Alpha-Synuclein in Bacterial Cells
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    Chapter 29 Identification of Distinct Soluble States During Fibril Formation Using Multilinear Analysis of NMR Diffusion Data
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    Chapter 30 Structural Analysis of SOD1 Fibrils with Mass Spectrometry, Limited Proteolysis, and Atomic Force Microscopy (AFM)
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    Chapter 31 Biophysical Studies of LLPS and Aggregation of TDP-43 LCD
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    Chapter 32 A Spectrophotometric Turbidity Assay to Study Liquid-Liquid Phase Separation of UBQLN2 In Vitro
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    Chapter 33 An Optimized Stress Granule Detection Method: Investigation of UBQLN2 Effect on Stress Granule Formation
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    Chapter 34 Neuronal Puncta/Aggregate Formation by WT and Mutant UBQLN2
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    Chapter 35 In Vivo Analysis of a Biomolecular Condensate in the Nervous System of C. elegans
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    Chapter 36 FLIM-FRET Investigation of Heterogeneous Huntingtin Aggregation in HeLa Cells
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    Chapter 37 In Vitro Characterization of Protein:Nucleic Acid Liquid–Liquid Phase Separation by Microscopy Methods and Nanoparticle Tracking Analysis
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    Chapter 38 Cross-Seeding Assay in the Investigation of the Amyloid Core of Prion Fibrils
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    Chapter 39 Mapping the Domain Structure and Aggregation Propensity of Proteins Using a Gateway Plasmid Vector System
Attention for Chapter 10: Using FRET-Based Biosensor Cells to Study the Seeding Activity of Tau and α-Synuclein
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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 (86th percentile)
  • High Attention Score compared to outputs of the same age and source (98th percentile)

Mentioned by

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1 news outlet
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4 X users

Citations

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1 Dimensions

Readers on

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4 Mendeley
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Chapter title
Using FRET-Based Biosensor Cells to Study the Seeding Activity of Tau and α-Synuclein
Chapter number 10
Book title
Protein Aggregation
Published in
Methods in molecular biology, October 2022
DOI 10.1007/978-1-0716-2597-2_10
Pubmed ID
Book ISBNs
978-1-07-162596-5, 978-1-07-162597-2
Authors

Maina, Katherine N., Smet-Nocca, Caroline, Bitan, Gal, Katherine N. Maina, Caroline Smet-Nocca, Gal Bitan

X Demographics

X Demographics

The data shown below were collected from the profiles of 4 X users who shared this research output. Click here to find out more about how the information was compiled.
Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 4 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 4 100%

Demographic breakdown

Readers by professional status Count As %
Student > Ph. D. Student 2 50%
Student > Bachelor 1 25%
Unknown 1 25%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 2 50%
Neuroscience 1 25%
Unknown 1 25%
Attention Score in Context

Attention Score in Context

This research output has an Altmetric Attention Score of 11. 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 04 November 2022.
All research outputs
#2,847,917
of 23,285,523 outputs
Outputs from Methods in molecular biology
#555
of 13,326 outputs
Outputs of similar age
#58,722
of 445,615 outputs
Outputs of similar age from Methods in molecular biology
#6
of 348 outputs
Altmetric has tracked 23,285,523 research outputs across all sources so far. Compared to these this one has done well and is in the 87th percentile: it's in the top 25% of all research outputs ever tracked by Altmetric.
So far Altmetric has tracked 13,326 research outputs from this source. They receive a mean Attention Score of 3.4. This one has done particularly well, scoring higher than 95% 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 445,615 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 86% of its contemporaries.
We're also able to compare this research output to 348 others from the same source and published within six weeks on either side of this one. This one has done particularly well, scoring higher than 98% of its contemporaries.