Evidence map›Paper›PMID 26990516›Full record

ReviewJournal of thrombosis and haemostasis : JTH2016

The design and synthesis of new synthetic low-molecular-weight heparins.

K Chandarajoti, J Liu, R Pawlinski

Open access · bronzeAbstract readReview
In one paragraph

Review in Journal of thrombosis and haemostasis : JTH, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed, 1 pooled it
1.9field-weighted citation impact, top 17% 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, 1 synthesis or guideline pooled it, 38 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Review
  4. Article
  5. Heparan sulfate selectively inhibits the collagenase activity of cathepsin K.Matrix biology : journal of the International Society for Matrix Biology · 2024
    Article
  6. Article
  7. Article
  8. Review
  9. Heparin and Derivatives for Advanced Cell Therapies.International journal of molecular sciences · 2021
    Review
  10. Article
  11. Heparins: A Shift of Paradigm.Frontiers in medicine · 2019
    Article
  12. 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 at 1 institution in 2 countries.

K ChandarajotiDivision of Hematology and Oncology, McAllister Heart Institute, Department of Medicine, University of North Carolina at Chapel Hill, Chapel Hill, NC, USA.
J LiuDivision of Chemical Biology and Medicinal Chemistry, Eshelman School of Pharmacy, University of North Carolina at Chapel Hill, Chapel Hill, NC, USA.
R PawlinskiDivision of Hematology and Oncology, McAllister Heart Institute, Department of Medicine, University of North Carolina at Chapel Hill, Chapel Hill, NC, USA.
University of North Carolina at Chapel Hill · US

Funding

Targeted Anticoagulant Therapy for Sickle Cell DiseaseU01HL117659 · NHLBI · UNIV OF NORTH CAROLINA CHAPEL HILL · PI KEY, NIGEL S., MACKMAN, NIGEL · 2013 to 2017
$7.6M
The Role of Tissue Factor: FVIIa-PAR-2 Signaling in Heart Ischemia/ReperfusionR01HL096679 · NHLBI · UNIV OF NORTH CAROLINA CHAPEL HILL · PI PAWLINSKI, RAFAL L · 2011 to 2015
$1.8M
NHLBI NIH HHS R01 HL096679NHLBI NIH HHS U01 HL117659
6 · The paper itself

Abstract

Low-molecular-weight heparin (LMWH) has remained the most favorable form of heparin in clinics since the 1990s owing to its predictable pharmacokinetic properties. However, LMWH is mainly eliminated through the kidney, which limits its use in renal-impaired patients. In addition, the anticoagulant activity of LMWH is only partially neutralized by protamine. LMWH is obtained from a full-length, highly sulfated polysaccharide harvested from porcine mucosal tissue. The depolymerization involved in LMWH production generates a broad distribution of LMWH fragments (6-22 sugar residues). This, combined with the various methods used to produce commercial LMWHs, results in variable pharmacological and pharmacokinetic properties. An alternative chemoenzymatic approach offers a method for the synthesis of LMWH that has the potential to overcome the limitations of current LMWHs. This review summarizes the application of a chemoenzymatic approach to generate LMWH and the rationale for development of a synthetic LMWH.

Indexed as

Drug DesignAnimalsAnticoagulantsBlood CoagulationCarbohydratesHeparin, Low-Molecular-WeightHumansKidneyMiceMolecular WeightMucous MembranePolymerizationPolysaccharidesProtaminesProtein BindingSwineAnticoagulantsCarbohydratesHeparin, Low-Molecular-WeightPolysaccharidesProtaminesanticoagulantsenzymesheparinlow molecular weightprotaminessynthetic

Identifiers

PMID26990516
PMCPMC4907857
OpenAlexW2296337693

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.