Evidence map›Paper›PMID 25145542›Full record

ArticleGlycoconjugate journal2014

Antithrombin-binding oligosaccharides: structural diversities in a unique function?

Marco Guerrini, Pierre A J Mourier, Giangiacomo Torri, Christian Viskov

Abstract read
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Article in Glycoconjugate journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing 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

14 citing papers in PubMed.

  1. Article
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  3. Review
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  13. Article
  14. Heparan sulfate and heparin interactions with proteins.Journal of the Royal Society, Interface · 2015
    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.

Marco GuerriniIstituto di Ricerche Chimiche e Biochimiche "G. Ronzoni", via G. Colombo 81, 20133, Milan, Italy, guerrini@ronzoni.it.
Pierre A J Mourier
Giangiacomo Torri
Christian Viskov

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Heparin-antithrombin interaction is one of the most documented examples of heparin/protein complexes. The specific heparin sequence responsible for the binding corresponds to a pentasaccharide sequence with an internal 3-O-sulfated glucosamine residue. Moreover, the position of the pentasaccharide along the chain as well as the structure of the neighbor units affects the affinity to antithrombin. The development of separation and purification techniques, in conjunction with physico-chemical approaches (mostly NMR), allowed to characterize several structural variants of antithrombin-binding oligosaccharides, both in the free state and in complex with antithrombin. The article provides an overview of the studies that lead to the elucidation of the mechanism of interaction as well as acquiring new knowledge in heparin biosynthesis.

Indexed as

AntithrombinsCarbohydrate ConformationMagnetic Resonance SpectroscopyOligosaccharidesSurface Plasmon ResonanceAntithrombinsOligosaccharides

Identifiers

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.