Evidence map›Paper›PMID 33153223›Full record

ReviewBrain sciences2020

Contributions of Molecular and Optical Techniques to the Clinical Diagnosis of Alzheimer's Disease.

Edoardo Bistaffa, Fabrizio Tagliavini, Paolo Matteini, Fabio Moda

Open access · goldAbstract readReview
In one paragraph

Review in Brain sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.8field-weighted citation impact, top 27% of its field
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

5 citing papers in PubMed, 12 citations in OpenAlex.

  1. Article
  2. Exploring the AβFrontiers in molecular biosciences · 2024
    Article
  3. Review
  4. Article
  5. Article
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

4 authors at 2 institutions in 1 country.

Edoardo BistaffaFondazione IRCCS Istituto Neurologico Carlo Besta, Division of Neurology 5 and Neuropathology, 20133 Milan, Italy.
Fabrizio TagliaviniFondazione IRCCS Istituto Neurologico Carlo Besta, Scientific Directorate, 20133 Milan, Italy.
Paolo MatteiniIFAC-CNR, Institute of Applied Physics "Nello Carrara", National Research Council, 50019 Sesto Fiorentino, Italy.ORCID 0000-0002-8488-5867
Fabio ModaFondazione IRCCS Istituto Neurologico Carlo Besta, Division of Neurology 5 and Neuropathology, 20133 Milan, Italy.ORCID 0000-0002-2820-9880
Fondazione IRCCS Istituto Neurologico Carlo Besta · ITNello Carrara Institute of Applied Physics · IT

Funding

European Community and the Italian Ministry of Health within the EuroNanoMed3 ERANET SPEEDYMinistero della Salute GR-2013-02355724Ministero della Salute NET-2011-02346784Ministero della Salute Ricerca CorrenteMJFF, ALZ, Alzheimer's Research UK and the Weston Brain Institute BAND2015
6 · The paper itself

Abstract

Alzheimer's disease (AD) is the most common neurodegenerative disorder worldwide. The distinctive neuropathological feature of AD is the intracerebral accumulation of two abnormally folded proteins: β-amyloid (Aβ) in the form of extracellular plaques, and tau in the form of intracellular neurofibrillary tangles. These proteins are considered disease-specific biomarkers, and the definite diagnosis of AD relies on their post-mortem identification in the brain. The clinical diagnosis of AD is challenging, especially in the early stages. The disease is highly heterogeneous in terms of clinical presentation and neuropathological features. This phenotypic variability seems to be partially due to the presence of distinct Aβ conformers, referred to as strains. With the development of an innovative technique named Real-Time Quaking-Induced Conversion (RT-QuIC), traces of Aβ strains were found in the cerebrospinal fluid of AD patients. Emerging evidence suggests that different conformers may transmit their strain signature to the RT-QuIC reaction products. In this review, we describe the current challenges for the clinical diagnosis of AD and describe how the RT-QuIC products could be analyzed by a surface-enhanced Raman spectroscopy (SERS)-based systems to reveal the presence of strain signatures, eventually leading to early diagnosis of AD with the recognition of individual disease phenotype.

Indexed as

Alzheimer’s diseaseclinical diagnosisoptical techniquesprotein misfoldingRT-QuICsurface-enhanced Raman spectroscopy

Identifiers

PMID33153223
PMCPMC7692713
OpenAlexW3096804668

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

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.