Evidence map›Paper›PMID 31006963›Full record

ArticleJournal of thrombosis and haemostasis : JTH2019

Temperature-dependent irreversible conformational change of recombinant ADAMTS13 upon metal ion chelation.

Hanspeter Rottensteiner, Stefan Kaufmann, Anna Rathgeb, Barbara Kink, Barbara Plaimauer, Peter Matthiessen, Stephan Hann, Friedrich Scheiflinger

Open access · bronzeAbstract read
In one paragraph

Article in Journal of thrombosis and haemostasis : JTH, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.3field-weighted citation impact, top 41% 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

5 citing papers in PubMed, 9 citations in OpenAlex.

  1. Article
  2. Analysis of the sensitization activity ofFrontiers in nutrition · 2024
    Article
  3. ADAMTS13 Activity: Screening Test Protocol.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  4. Article
  5. 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

8 authors at 2 institutions in 1 country.

Hanspeter RottensteinerBaxalta Innovations GmbH, a member of the Takeda group of companies, Vienna, Austria.
Stefan KaufmannBaxalta Innovations GmbH, a member of the Takeda group of companies, Vienna, Austria.
Anna RathgebDepartment of Chemistry, University of Natural Resources and Life Sciences (BOKU), Vienna, Austria.
Barbara KinkBaxalta Innovations GmbH, a member of the Takeda group of companies, Vienna, Austria.
Barbara PlaimauerBaxalta Innovations GmbH, a member of the Takeda group of companies, Vienna, Austria.
Peter MatthiessenBaxalta Innovations GmbH, a member of the Takeda group of companies, Vienna, Austria.
Stephan HannDepartment of Chemistry, University of Natural Resources and Life Sciences (BOKU), Vienna, Austria.
Friedrich ScheiflingerBaxalta Innovations GmbH, a member of the Takeda group of companies, Vienna, Austria.
Takeda (Austria) · ATBOKU University · AT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundThe catalytic domain of ADAMTS13 possesses one Zn

objectivesTo address the stability of ADAMTS13 in citrated human plasma.

methodsADAMTS13 activity was measured using the FRETS-VWF73 fluorogenic assay. The molar ratio of metals bound to ADAMTS13 was determined by size exclusion chromatography inductively coupled plasma mass spectrometry (SEC-ICP-MS). Higher-order structural changes were analyzed using Fourier-transformed infrared spectroscopy and dynamic light scattering.

resultsADAMTS13 was stable at room temperature for up to 24 hours irrespective of the presence of citrate (0.38%). However, at 37°C, citrate caused a time-dependent activity decrease. No ADAMTS13 activity decrease was seen in heparinized plasma, but the addition of citrate again caused ADAMTS13 instability at 37°C. Scavenging of citrate by the addition of Ca

conclusionsZn

Indexed as

ADAMTS13 ProteinCalciumCatalytic DomainChelating AgentsCitric AcidDynamic Light ScatteringEnzyme StabilityFluorescence Resonance Energy TransferHumansIn Vitro TechniquesMass SpectrometryProtein ConformationPurpura, Thrombotic ThrombocytopenicRecombinant ProteinsSpectroscopy, Fourier Transform InfraredTemperatureADAMTS13 ProteinADAMTS13 protein, humanCalciumChelating AgentsCitric AcidRecombinant ProteinsZincADAMTS13 proteinblood plasmaprotein conformationprotein stabilityzinc

Identifiers

PMID31006963
PMCPMC6850365
OpenAlexW2940827195

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.