Evidence map›Paper›PMID 19883600›Full record

ArticleBiophysical journal2009

Application of fluorescence spectroscopy to quantify shear-induced protein conformation change.

Efrosyni Themistou, Indrajeet Singh, Chengwei Shang, Sathy V Balu-Iyer, Paschalis Alexandridis, Sriram Neelamegham

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.9field-weighted citation impact, top 25% 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, 32 citations in OpenAlex.

  1. Review
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  5. Evaluation of fluorescent dyes to measure protein aggregation within mammalian cell culture supernatants.Journal of chemical technology and biotechnology (Oxford, Oxfordshire : 1986) · 2018
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  7. Review
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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

6 authors at 1 institution in 1 country.

Efrosyni ThemistouDepartment of Chemical and Biological Engineering, University at Buffalo, State University of New York, Buffalo, New York, USA.
Indrajeet Singh
Chengwei Shang
Sathy V Balu-Iyer
Paschalis Alexandridis
Sriram Neelamegham
University at Buffalo, State University of New York · US

Funding

VON WILLEBRAND FACTOR STRUCTURE-FUNCTION UNDE FLUID FLOWR01HL077258 · NHLBI · STATE UNIVERSITY OF NEW YORK AT BUFFALO · PI NEELAMEGHAM, SRIRAM · 2006 to 2015
$3.0M
NHLBI NIH HHS HL77258NHLBI NIH HHS R01 HL077258
6 · The paper itself

Abstract

Rapid and robust methods are required to quantify the effect of hydrodynamic shear on protein conformation change. We evaluated such strategies in this work and found that the binding of the fluorescent probe 4,4'-dianilino-1,1'-binaphthyl-5,5'-disulfonic acid (bis-ANS) to hydrophobic pockets in the blood protein von Willebrand factor (VWF) is enhanced upon the application of fluid shear to the isolated protein. Significant structural changes were observed when the protein was sheared at shear rates >or= 6000/s for approximately 3.5 min. The binding of bis-ANS to multimeric VWF, but not dimeric VWF or control protein bovine serum albumin, was enhanced upon fluid shear application. Thus, high-molecular-weight VWF is more susceptible to conformation change upon tensile loading. Although bis-ANS itself did not alter the conformation of VWF, it stabilized protein conformation once it bound the sheared molecule. Bis-ANS binding to VWF was reduced when the sheared protein was allowed to relax before dye addition. Taken together with functional data in the literature, our results suggest that shear-induced conformation changes in VWF reported by bis-ANS correlate well with the normal function of the protein under physiological/pathological fluid flow conditions. Further, this study introduces the fluorescent dye bis-ANS as a tool that may be useful in studies of shear-induced protein conformation change.

Indexed as

Anilino NaphthalenesulfonatesBiophysicsDimerizationFluorescent DyesHumansModels, MolecularMolecular ConformationMolecular WeightProtein ConformationSilver StainingSpectrometry, FluorescenceStress, MechanicalTensile Strengthvon Willebrand Factor5,5'-bis(8-(phenylamino)-1-naphthalenesulfonate)Anilino NaphthalenesulfonatesFluorescent Dyesvon Willebrand Factor

Identifiers

PMID19883600
PMCPMC2770613
OpenAlexW2012091107

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.