Evidence map›Paper›PMID 22513887›Full record

ReviewMolecular bioSystems2012

Proteoglycan sequence.

Lingyun Li, Mellisa Ly, Robert J Linhardt

Abstract readReview
In one paragraph

Review in Molecular bioSystems, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
60citing 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

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

  1. Pooled it
  2. Endothelial Exostosin-1 Is Needed for Glycocalyx Integrity and Inflammatory Resolution in Acute Lung Injury.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026
    Article
  3. Article
  4. Manuscript DMD-D-25-00346 The impact of glycocalyx on partitioning and distribution of basic drugs.Drug metabolism and disposition: the biological fate of chemicals · 2026
    Article
  5. Article
  6. Understanding Viral-Glycocalyx Interactions Using Brush-Linked to Cross-Linked Models.Langmuir : the ACS journal of surfaces and colloids · 2025
    Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Synthesis of a Systematic 64-Membered Heparan Sulfate Tetrasaccharide Library.Angewandte Chemie (International ed. in English) · 2023
    Article
  14. Article
  15. Review
  16. Review
  17. Article
  18. Article
  19. Analysis of the Glycosaminoglycan Chains of Proteoglycans.The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society · 2021
    Review
  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.

Lingyun LiDepartments of Chemistry and Chemical Biology, Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, New York 12180, USA.
Mellisa Ly
Robert J Linhardt

Funding

In vitro synthesis of recombinant heparan sulfateR01HL094463 · NHLBI · UNIV OF NORTH CAROLINA CHAPEL HILL · PI LIU, JIAN, PAWLINSKI, RAFAL L · 2009 to 2021
$5.2M
Development of a Bioengineered Heparin from a Non-Animal SourceR01HL096972 · NHLBI · RENSSELAER POLYTECHNIC INSTITUTE · PI DORDICK, JONATHAN S., LINHARDT, ROBERT J · 2009 to 2013
$3.9M
SEQUENCING THE POLYSACCHARIDE COMPONENT OF PROTEOGLYCANSR01GM038060 · NIGMS · UNIVERSITY OF IOWA · PI LINHARDT, ROBERT J · 1988 to 2012
$2.8M
Metabolic Engineering of Chinese Hamster Ovary Cells for Production of HeparinR01GM090127 · NIGMS · STATE UNIVERSITY OF NEW YORK AT ALBANY · PI SHARFSTEIN, SUSAN T · 2009 to 2011
$1.0M
NHLBI NIH HHS HL094463NHLBI NIH HHS HL096972NHLBI NIH HHS R01 HL094463NHLBI NIH HHS R01 HL096972NIGMS NIH HHS GM090127NIGMS NIH HHS GM38060NIGMS NIH HHS R01 GM038060NIGMS NIH HHS R01 GM090127
6 · The paper itself

Abstract

Proteoglycans (PGs) are among the most structurally complex biomacromolecules in nature. They are present in all animal cells and frequently exert their critical biological functions through interactions with protein ligands and receptors. PGs are comprised of a core protein to which one or multiple, heterogeneous, and polydisperse glycosaminoglycan (GAG) chains are attached. Proteins, including the protein core of PGs, are now routinely sequenced either directly using proteomics or indirectly using molecular biology through their encoding DNA. The sequencing of the GAG component of PGs poses a considerably more difficult challenge because of the relatively underdeveloped state of glycomics and because the control of their biosynthesis in the endoplasmic reticulum and the Golgi is poorly understood and not believed to be template driven. Recently, the GAG chain of the simplest PG has been suggested to have a defined sequence based on its top-down Fourier transform mass spectral sequencing. This review examines the advances made over the past decade in the sequencing of GAG chains and the challenges the field face in sequencing complex PGs having critical biological functions in developmental biology and pathogenesis.

Indexed as

AnimalsCarbohydrate SequenceComputer SimulationCrystallography, X-RayHumansMass SpectrometryModels, MolecularMolecular Sequence DataNuclear Magnetic Resonance, BiomolecularProteoglycansSequence AnalysisProteoglycans

Identifiers

PMID22513887
PMCPMC3425375

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.