Evidence mapPaperPMID 41008617Full record

ReviewBiomolecules2025

Overview of Proteomic Analysis of Amyloid Plaques and Neurofibrillary Tangles in Alzheimer's Disease.

Amber Grewal, Simran Raikundalia, Joseph Zaia, Manveen K Sethi

Abstract readReview
In one paragraph

Review in Biomolecules, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed, 1 pooled it
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

5 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. Review
  3. Review
  4. Review
  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.

Amber GrewalCenter for Biomedical Mass Spectrometry, Department of Biochemistry and Cell Biology, Boston University Chobanian and Avedisian School of Medicine, Boston, MA 02118, USA.
Simran RaikundaliaCenter for Biomedical Mass Spectrometry, Department of Biochemistry and Cell Biology, Boston University Chobanian and Avedisian School of Medicine, Boston, MA 02118, USA.
Joseph ZaiaCenter for Biomedical Mass Spectrometry, Department of Biochemistry and Cell Biology, Boston University Chobanian and Avedisian School of Medicine, Boston, MA 02118, USA.ORCID 0000-0001-9497-8701
Manveen K SethiCenter for Biomedical Mass Spectrometry, Department of Biochemistry and Cell Biology, Boston University Chobanian and Avedisian School of Medicine, Boston, MA 02118, USA.ORCID 0000-0001-8276-6728

Funding

Project-005UL1TR001430 · NCATS · BOSTON UNIVERSITY MEDICAL CAMPUS · PI BAIR-MERRITT, MEGAN H, CENTER, DAVID M. · 2015 to 2024
$52.3M
Methods for measuring matrisome molecule similarity during disease processesR35GM144090 · NIGMS · BOSTON UNIVERSITY MEDICAL CAMPUS · PI JOSEPH ZAIA · 2022 to 2026
$2.1M
Boston University Clinical Translational Science Institute Pilot Grant Award 1UL1TR001430BrightFocus Foundation A2020687FNCATS NIH HHS UL1 TR001430NIGMS NIH HHS R35 GM144090NIGMS NIH HHS R35GM144090
6 · The paper itself

Abstract

In this review, we describe the methods used for the extraction and mass spectrometry proteomics analysis of amyloid plaques and neurofibrillary tangles (NFTs), the two primary pathological hallmarks of Alzheimer's disease (AD). We also provide a comprehensive overview of the mass spectrometry-based studies conducted to analyze these pathological features. AD is the most prevalent form of dementia and the sixth leading cause of death in the United States. While the current treatments can alleviate early-stage memory and cognitive symptoms, they do not offer a cure. Thus, there is a pressing need to deepen our understanding of the neuropathological mechanisms underlying AD and to develop more effective therapeutics. In-depth mass spectrometry-based proteomics analyses of AD pathology-specifically, extracellular the Aβ plaques found in extracellular spaces and blood vessel walls and intraneuronal NFTs composed of the microtubule-associated protein tau-may offer molecular-level observations that contribute to the understanding of the biological context of plaque and NFT formation and support the discovery of potential biomarkers and therapeutic targets for AD.

Indexed as

Alzheimer DiseaseNeurofibrillary TanglesPlaque, AmyloidProteomicsAmyloid beta-PeptidesAnimalsBiomarkersHumansMass Spectrometrytau ProteinsAmyloid beta-PeptidesBiomarkerstau ProteinsAlzheimer’s diseaseamyloid plaqueslaser microdissectionmass spectrometryneurofibrillary tangles

Identifiers

PMID41008617
PMCPMC12467479

What Socratic 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 Socratic graph.