Evidence map›Paper›PMID 25709560›Full record

ArticleCrystal growth & design2015

Effect of Otoconial Proteins Fetuin A, Osteopontin, and Otoconin 90 on the Nucleation and Growth of Calcite.

Mina Hong, K Trent Moreland, Jiajun Chen, Henry H Teng, Ruediger Thalmann, James J De Yoreo

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In one paragraph

Article in Crystal growth & design, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.6field-weighted citation impact, top 33% 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

3 citing papers in PubMed, 14 citations in OpenAlex.

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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 4 institutions in 1 country.

Mina HongPhysical Sciences Division, Pacific Northwest National Laboratory , Richland, Washington 99352, United States ; Department of Chemistry, The George Washington University , Washington, D.C. 20052, United States ; The Molecular Foundry, Lawrence Berkeley National Laboratory , Berkeley, California 94720, United States.
K Trent MorelandDepartment of Otolaryngology-Head and Neck Surgery, Washington University in St. Louis , St. Louis, Missouri 63110, United States.
Jiajun ChenThe Molecular Foundry, Lawrence Berkeley National Laboratory , Berkeley, California 94720, United States.
Henry H TengDepartment of Chemistry, The George Washington University , Washington, D.C. 20052, United States.
Ruediger ThalmannDepartment of Otolaryngology-Head and Neck Surgery, Washington University in St. Louis , St. Louis, Missouri 63110, United States.
James J De YoreoPhysical Sciences Division, Pacific Northwest National Laboratory , Richland, Washington 99352, United States.
George Washington University · USWashington University in St. Louis · USLawrence Berkeley National Laboratory · USPacific Northwest National Laboratory · US

Funding

Molecular Characterization of Key Proteins Directing Otoconial MineralizationR01DC011614 · NIDCD · WASHINGTON UNIVERSITY · PI THALMANN, RUEDIGER R · 2011 to 2013
$1.2M
NIDCD NIH HHS R01 DC011614
6 · The paper itself

Abstract

We investigated the roles of three proteins associated with the formation of otoconia including fetuin A, osteopontin (OPN), and otoconin 90 (OC90). In situ atomic force microscopy (AFM) studies of the effects of these proteins on the growth of atomic steps on calcite surfaces were performed to obtain insight into their effects on the growth kinetics. We also used scanning electron microscopy to examine the effects of these proteins on crystal morphology. All three proteins were found to be potent inhibitors of calcite growth, although fetuin A promoted growth at concentrations below about 40 nM and only became an inhibitor at higher concentrations. We then used in situ optical microscopy to observe calcite nucleation on films of these proteins adsorbed onto mica surfaces. By measuring the calcite nucleation rate as a function of supersaturation, the value of the interfacial energy that controls the free energy barrier to heterogeneous nucleation was determined for each protein. OPN and OC90 films led to significantly reduced interfacial energies as compared to the value for homogeneous calcite nucleation in bulk solution. The value for fetuin A was equal to that for bulk solution within experimental error. Zeta potential measurements showed all of the proteins possessed negative surface charge and varied in magnitude according to sequence fetuin A > OC90 > OPN. In addition, the interfacial energies exhibited an inverse scaling with the zeta potential. In analogy to previous measurements on polysaccharide films, this scaling indicates the differences between the proteins arise from the effect of protein surface charge on the solution-substrate interfacial energy.

Identifiers

PMID25709560
PMCPMC4334277
OpenAlexW1991629256

What OpenQuestion holds

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Registered trials

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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.