Evidence map›Paper›PMID 33600794›Full record

ArticleThe Journal of biological chemistry

Conformation of the von Willebrand factor/factor VIII complex in quasi-static flow.

Ernest T Parker, Pete Lollar

Open access · goldAbstract read
In one paragraph

Article in The Journal of biological chemistry. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

17 citing papers in PubMed, 23 citations in OpenAlex.

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  9. Structural hierarchy of mechanical extensibility in human von Willebrand factor multimers.Protein science : a publication of the Protein Society · 2023
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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

2 authors at 1 institution in 1 country.

Ernest T ParkerAflac Cancer and Blood Disorders Center, Children's Healthcare of Atlanta; Department of Pediatrics, Emory University, Atlanta, Georgia, USA.
Pete LollarAflac Cancer and Blood Disorders Center, Children's Healthcare of Atlanta; Department of Pediatrics, Emory University, Atlanta, Georgia, USA. Electronic address: jlollar@emory.edu.
Emory University · US

Funding

Unraveling the immune response to factor VIIIU54HL141981 · NHLBI · EMORY UNIVERSITY · PI LOLLAR, JOHN S. · 2018 to 2022
$8.1M
NHLBI NIH HHS U54 HL141981
6 · The paper itself

Abstract

Von Willebrand factor (VWF) is a plasma glycoprotein that circulates noncovalently bound to blood coagulation factor VIII (fVIII). VWF is a population of multimers composed of a variable number of ∼280 kDa monomers that is activated in shear flow to bind collagen and platelet glycoprotein Ibα. Electron microscopy, atomic force microscopy, small-angle neutron scattering, and theoretical studies have produced a model in which the conformation of VWF under static conditions is a compact, globular "ball-of-yarn," implying strong, attractive forces between monomers. We performed sedimentation velocity (SV) analytical ultracentrifugation measurements on unfractionated VWF/fVIII complexes. There was a 20% per mg/ml decrease in the weight-average sedimentation coefficient, s

Indexed as

Blood PlateletsCollagenDrug CombinationsFactor VIIIHumansMolecular ConformationMolecular WeightPlasmaScattering, Small AngleUltracentrifugationvon Willebrand FactorCollagenDrug CombinationsFactor VIIIfactor VIII, von Willebrand factor drug combinationvon Willebrand Factoranalytical ultracentrifugationdynamic light scatteringfactor VIIIprotein conformationsize-exclusion chromatographystructural modelvon Willebrand factor

Identifiers

PMID33600794
PMCPMC8005835
OpenAlexW3129427611

What OpenQuestion holds

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LicenceCC BY
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.