Evidence map›Paper›PMID 33917853›Full record

ArticleBiomolecules2021

Investigation of the Differences in Antithrombin to Heparin Binding among Antithrombin Budapest 3, Basel, and Padua Mutations by Biochemical and In Silico Methods.

Réka Gindele, Krisztina Pénzes-Daku, Gábor Balogh, Judit Kállai, Réka Bogáti, Bálint Bécsi, Ferenc Erdődi, Éva Katona, Zsuzsanna Bereczky

Open access · goldAbstract read
In one paragraph

Article in Biomolecules, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed, 1 pooled it
1.6field-weighted citation impact, top 16% 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

13 citing papers in PubMed, 1 synthesis or guideline pooled it, 17 citations in OpenAlex.

  1. Pooled it
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  12. Review
  13. Antithrombin Therapy: Current State and Future Outlook.Clinical and applied thrombosis/hemostasis : official journal of the International Academy of Clinical and Applied Thrombosis/Hemostasis
    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

9 authors at 1 institution in 1 country.

Réka GindeleDivision of Clinical Laboratory Science, Department of Laboratory Medicine, Faculty of Medicine, University of Debrecen, 4032 Debrecen, Hungary.
Krisztina Pénzes-DakuDivision of Clinical Laboratory Science, Department of Laboratory Medicine, Faculty of Medicine, University of Debrecen, 4032 Debrecen, Hungary.
Gábor BaloghDivision of Clinical Laboratory Science, Department of Laboratory Medicine, Faculty of Medicine, University of Debrecen, 4032 Debrecen, Hungary.
Judit KállaiDivision of Clinical Laboratory Science, Department of Laboratory Medicine, Faculty of Medicine, University of Debrecen, 4032 Debrecen, Hungary.
Réka BogátiDivision of Clinical Laboratory Science, Department of Laboratory Medicine, Faculty of Medicine, University of Debrecen, 4032 Debrecen, Hungary.
Bálint BécsiDepartment of Medical Chemistry, Faculty of Medicine, University of Debrecen, 4032 Debrecen, Hungary.
Ferenc ErdődiDepartment of Medical Chemistry, Faculty of Medicine, University of Debrecen, 4032 Debrecen, Hungary.
Éva KatonaDivision of Clinical Laboratory Science, Department of Laboratory Medicine, Faculty of Medicine, University of Debrecen, 4032 Debrecen, Hungary.ORCID 0000-0003-3476-794X
Zsuzsanna BereczkyDivision of Clinical Laboratory Science, Department of Laboratory Medicine, Faculty of Medicine, University of Debrecen, 4032 Debrecen, Hungary.ORCID 0000-0002-1483-3703
University of Debrecen · HU

Funding

European Union under European Regional Development Fund GINOP-2.3.2-15-2016-00039European Union under European Regional Development Fund GINOP-2.3.2–15-2016–00044European Union under European Regional Development Fund GINOP-2.3.3–15-2016–00020National Research, Development and Innovation Office, Hungarian Ministry of Innovation and Technology OTKA K116228
6 · The paper itself

Abstract

Antithrombin (AT) is a serine protease inhibitor, its activity is highly accelerated by heparin. Mutations at the heparin-binding region lead to functional defect, type II heparin-binding site (IIHBS) AT deficiency. The aim of this study was to investigate and compare the molecular background of AT Budapest 3 (p.Leu131Phe, ATBp3), AT Basel (p.Pro73Leu), and AT Padua (p.Arg79His) mutations. Advanced in silico methods and heparin-binding studies of recombinant AT proteins using surface plasmon resonance method were used. Crossed immunoelectrophoresis and Differential Scanning Fluorimetry (NanoDSF) were performed in plasma samples. Heparin affinity of AT Padua was the lowest (KD = 1.08 × 10

Indexed as

Antithrombin IIIBinding SitesFemaleHeparinHumansImmunoelectrophoresisKineticsMaleMolecular Dynamics SimulationPolymorphism, Single NucleotideProtein BindingRecombinant ProteinsSurface Plasmon ResonanceAntithrombin IIIantithrombin III Baselantithrombin III PaduaHeparinRecombinant ProteinsantithrombinAntithrombin BaselAntithrombin Budapest 3Antithrombin Paduaheparin-binding sitemolecular modellingsurface plasmon resonance

Identifiers

PMID33917853
PMCPMC8068293
OpenAlexW3156466452

What OpenQuestion holds

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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.