Evidence map›Paper›PMID 30621325›Full record

ReviewMolecules (Basel, Switzerland)2019

Vibrational Approach to the Dynamics and Structure of Protein Amyloids.

Haoqian Li, Richard Lantz, Deguo Du

Abstract readReview
In one paragraph

Review in Molecules (Basel, Switzerland), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

27 citing papers in PubMed.

  1. Article
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  9. Communications chemistry · 2023
    Article
  10. Characterization of Uranyl (UOACS chemical neuroscience · 2023
    Article
  11. Article
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  13. Article
  14. Raman Spectroscopy as a Tool to Study the Pathophysiology of Brain Diseases.International journal of molecular sciences · 2023
    Review
  15. Article
  16. Article
  17. Review
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  20. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors.

Haoqian LiQueen Mary School, Medical School, Nanchang University, Nanchang 330031, China. 6303415034@email.ncu.edu.cn.
Richard LantzDepartment of Chemistry and Biochemistry, Florida Atlantic University, Boca Raton, FL 33431, USA. rlantz@my.fau.edu.
Deguo DuDepartment of Chemistry and Biochemistry, Florida Atlantic University, Boca Raton, FL 33431, USA. ddu@fau.edu.

Funding

Role of the N-terminal Region in Abeta Oligomer and Fibril FormationR15GM116006 · NIGMS · FLORIDA ATLANTIC UNIVERSITY · PI DU, DEGUO · 2015 to 2020
$735k
Alzheimer's Association AARG-17-531423National Institutes of Health R15GM116006NIGMS NIH HHS R15 GM116006
6 · The paper itself

Abstract

Amyloid diseases, including neurodegenerative diseases such as Alzheimer's and Parkinson's, are linked to a poorly understood progression of protein misfolding and aggregation events that culminate in tissue-selective deposition and human pathology. Elucidation of the mechanistic details of protein aggregation and the structural features of the aggregates is critical for a comprehensive understanding of the mechanisms of protein oligomerization and fibrillization. Vibrational spectroscopies, such as Fourier transform infrared (FTIR) and Raman, are powerful tools that are sensitive to the secondary structure of proteins and have been widely used to investigate protein misfolding and aggregation. We address the application of the vibrational approaches in recent studies of conformational dynamics and structural characteristics of protein oligomers and amyloid fibrils. In particular, introduction of isotope labelled carbonyl into a peptide backbone, and incorporation of the extrinsic unnatural amino acids with vibrational moieties on the side chain, have greatly expanded the ability of vibrational spectroscopy to obtain site-specific structural and dynamic information. The applications of these methods in recent studies of protein aggregation are also reviewed.

Indexed as

Alzheimer DiseaseAmyloidAmyloid beta-PeptidesHumansIslet Amyloid PolypeptideIsotope LabelingModels, MolecularParkinson DiseaseProtein MultimerizationProtein Structure, SecondarySpectrum AnalysisVibrationAmyloidAmyloid beta-PeptidesIslet Amyloid Polypeptideamyloidinfraredisotopic labellingoligomersprotein aggregationRamansite-specific probevibrational spectroscopy

Identifiers

PMID30621325
PMCPMC6337179

What OpenQuestion holds

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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.