Evidence map›Paper›PMID 35719114›Full record

ReviewMass spectrometry reviews

Mass spectrometry methods for analysis of extracellular matrix components in neurological diseases.

Margaret Downs, Joseph Zaia, Manveen K Sethi

Open access · greenAbstract readReview
In one paragraph

Review in Mass spectrometry reviews. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.0field-weighted citation impact, top 15% 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

12 citing papers in PubMed, 19 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Mechanisms of assembly and remodelling of the extracellular matrix.Nature reviews. Molecular cell biology · 2024
    Review
  9. Mechanobiological Modulation ofACS biomaterials science & engineering · 2024
    Article
  10. Review
  11. Review
  12. 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

3 authors at 1 institution in 1 country.

Margaret DownsDepartment of Biochemistry, Center for Biomedical Mass Spectrometry, Boston University, Boston, Massachusetts, USA.
Joseph ZaiaDepartment of Biochemistry, Center for Biomedical Mass Spectrometry, Boston University, Boston, Massachusetts, USA.
Manveen K SethiDepartment of Biochemistry, Center for Biomedical Mass Spectrometry, Boston University, Boston, Massachusetts, USA.
Boston University · US

Funding

Project-005UL1TR001430 · NCATS · BOSTON UNIVERSITY MEDICAL CAMPUS · PI BAIR-MERRITT, MEGAN H, CENTER, DAVID M. · 2015 to 2024
$52.3M
Cerebrovascular Remodeling and Neurodegenerative Changes in Alzheimer's DiseaseR01AG075876 · NIA · BOSTON UNIVERSITY (CHARLES RIVER CAMPUS) · PI Thor Stein, JOSEPH ZAIA · 2022 to 2026
$3.9M
Methods for measuring matrisome molecule similarity during disease processesR35GM144090 · NIGMS · BOSTON UNIVERSITY MEDICAL CAMPUS · PI JOSEPH ZAIA · 2022 to 2026
$2.1M
Methods for determination of glycoprotein glycosylation similarities among disease statesR01GM133963 · NIGMS · BOSTON UNIVERSITY MEDICAL CAMPUS · PI ZAIA, JOSEPH · 2019 to 2021
$1.4M
NCATS NIH HHS UL1 TR001430NIA NIH HHS R01 AG075876NIGMS NIH HHS R01 GM133963NIGMS NIH HHS R35 GM144090
6 · The paper itself

Abstract

The brain extracellular matrix (ECM) is a highly glycosylated environment and plays important roles in many processes including cell communication, growth factor binding, and scaffolding. The formation of structures such as perineuronal nets (PNNs) is critical in neuroprotection and neural plasticity, and the formation of molecular networks is dependent in part on glycans. The ECM is also implicated in the neuropathophysiology of disorders such as Alzheimer's disease (AD), Parkinson's disease (PD), and Schizophrenia (SZ). As such, it is of interest to understand both the proteomic and glycomic makeup of healthy and diseased brain ECM. Further, there is a growing need for site-specific glycoproteomic information. Over the past decade, sample preparation, mass spectrometry, and bioinformatic methods have been developed and refined to provide comprehensive information about the glycoproteome. Core ECM molecules including versican, hyaluronan and proteoglycan link proteins, and tenascin are dysregulated in AD, PD, and SZ. Glycomic changes such as differential sialylation, sulfation, and branching are also associated with neurodegeneration. A more thorough understanding of the ECM and its proteomic, glycomic, and glycoproteomic changes in brain diseases may provide pathways to new therapeutic options.

Indexed as

Alzheimer's diseasechondroitin sulfateextracellular matrixglycomicsglycoproteomicsglycosaminoglycansglycosylationheparan sulfatemass-spectrometryParkinson's diseaseproteoglycansproteomicsSchizophrenia

Identifiers

PMID35719114
PMCPMC9763553
OpenAlexW4283210257

What OpenQuestion holds

Textmetadata
LicenceTDM
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.