Evidence map›Paper›PMID 31471497›Full record

ReviewMolecular & cellular proteomics : MCP2019

Proteomics, Glycomics, and Glycoproteomics of Matrisome Molecules.

Rekha Raghunathan, Manveen K Sethi, Joshua A Klein, Joseph Zaia

Abstract readReview
In one paragraph

Review in Molecular & cellular proteomics : MCP, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing 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

31 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Review
  7. Mechanisms of assembly and remodelling of the extracellular matrix.Nature reviews. Molecular cell biology · 2024
    Review
  8. Article
  9. Uncovering Protein Networks in Cardiovascular Proteomics.Molecular & cellular proteomics : MCP · 2023
    Review
  10. Review
  11. Article
  12. Review
  13. Article
  14. Review
  15. Article
  16. Matrisome changes in Parkinson's disease.Analytical and bioanalytical chemistry · 2022
    Article
  17. Article
  18. Review
  19. Article
  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

4 authors.

Rekha RaghunathanMolecular and Translational Medicine Program, Boston University, Boston, MA 02218; Department of Biochemistry, Boston University, Boston, MA 02218.
Manveen K SethiDepartment of Biochemistry, Boston University, Boston, MA 02218.
Joshua A KleinBioinformatics Program, Boston University, Boston, MA 02218.
Joseph ZaiaMolecular and Translational Medicine Program, Boston University, Boston, MA 02218; Department of Biochemistry, Boston University, Boston, MA 02218; Bioinformatics Program, Boston University, Boston, MA 02218. Electronic address: jzaia@bu.edu.

Funding

Mass Spectrometry Resource for Biology and MedicineP41GM104603 · NIGMS · BOSTON UNIVERSITY MEDICAL CAMPUS · PI COSTELLO, CATHERINE E. · 2012 to 2017
$10.4M
Methods for determination of glycoprotein glycosylation similarities among disease statesR01GM133963 · NIGMS · BOSTON UNIVERSITY MEDICAL CAMPUS · PI ZAIA, JOSEPH · 2019 to 2021
$1.4M
An open-source software suite for processing glycomics and glycoproteomics mass spectral dataU01CA221234 · NCI · BOSTON UNIVERSITY MEDICAL CAMPUS · PI ZAIA, JOSEPH · 2017 to 2019
$1.2M
A Thermo-Fisher Scientific Q-Exactive HF Mass Spectrometry SystemS10OD021651 · OD · BOSTON UNIVERSITY MEDICAL CAMPUS · PI ZAIA, JOSEPH · 2016 to 2016
$580k
NCI NIH HHS U01 CA221234NIGMS NIH HHS P41 GM104603NIGMS NIH HHS R01 GM133963NIH HHS S10 OD021651
6 · The paper itself

Abstract

The most straightforward applications of proteomics database searching involve intracellular proteins. Although intracellular gene products number in the thousands, their well-defined post-translational modifications (PTMs) makes database searching practical. By contrast, cell surface and extracellular matrisome proteins pass through the secretory pathway where many become glycosylated, modulating their physicochemical properties, adhesive interactions, and diversifying their functions. Although matrisome proteins number only a few hundred, their high degree of complex glycosylation multiplies the number of theoretical proteoforms by orders of magnitude. Given that extracellular networks that mediate cell-cell and cell-pathogen interactions in physiology depend on glycosylation, it is important to characterize the proteomes, glycomes, and glycoproteomes of matrisome molecules that exist in a given biological context. In this review, we summarize proteomics approaches for characterizing matrisome molecules, with an emphasis on applications to brain diseases. We demonstrate the availability of methods that should greatly increase the availability of information on matrisome molecular structure associated with health and disease.

Indexed as

AnimalsBiomarkersExtracellular MatrixExtracellular Matrix ProteinsGlycomicsGlycoproteinsGlycosylationHumansProtein Processing, Post-TranslationalProteomeProteomicsBiomarkersExtracellular Matrix ProteinsGlycoproteinsProteomeExtracellular matrixglycomicsglycoproteinsglycoproteomicsn-glycosylation

Identifiers

PMID31471497
PMCPMC6823855

What OpenQuestion holds

Textmetadata
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.