Evidence map›Paper›PMID 21942221›Full record

ArticleLangmuir : the ACS journal of surfaces and colloids2011

Protein assembly at the air-water interface studied by fluorescence microscopy.

Zhengzheng Liao, Joshua W Lampe, Portonovo S Ayyaswamy, David M Eckmann, Ivan J Dmochowski

Open access · greenAbstract read
In one paragraph

Article in Langmuir : the ACS journal of surfaces and colloids, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.6field-weighted citation impact, top 19% 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

10 citing papers in PubMed, 34 citations in OpenAlex.

  1. Review
  2. Review
  3. Amphiphilic proteins coassemble into multiphasic condensates and act as biomolecular surfactants.Proceedings of the National Academy of Sciences of the United States of America · 2021
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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

5 authors at 2 institutions in 1 country.

Zhengzheng LiaoDepartment of Chemistry, University of Pennsylvania, Philadelphia, Pennsylvania 19104, United States.
Joshua W Lampe
Portonovo S Ayyaswamy
David M Eckmann
Ivan J Dmochowski
University of Pennsylvania · USHospital of the University of Pennsylvania · US

Funding

INTERFACIAL MECHANICS IN INTRAVASCULAR GAS EMBOLISMR01HL060230 · NHLBI · UNIVERSITY OF PENNSYLVANIA · PI ECKMANN, DAVID M · 1999 to 2011
$3.8M
Targeted Microcarrier Design and OptimizationR01EB006818 · NIBIB · UNIVERSITY OF PENNSYLVANIA · PI ECKMANN, DAVID M · 2008 to 2016
$3.3M
Structure-Based Design of Xe-129 NMR Biosensors for Multiplexed Cancer DetectionR01GM097478 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI DMOCHOWSKI, IVAN JULIAN · 2011 to 2018
$3.1M
Oligonucleotides for turning genes on and off with lightR01GM083030 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI DMOCHOWSKI, IVAN JULIAN · 2008 to 2017
$3.0M
Activation of Clotting &cell adhesion : gas embolismR01HL067986 · NHLBI · UNIVERSITY OF PENNSYLVANIA · PI ECKMANN, DAVID M · 2002 to 2010
$2.4M
LEICA TCS SP2 AOBS UV CONFOCAL SYSTEM: EMBRYO DEVELOPMENTS10RR021113 · NCRR · UNIVERSITY OF PENNSYLVANIA · PI DMOCHOWSKI, IVAN JULIAN · 2005 to 2005
$497k
NCRR NIH HHS 1S10RR021113NCRR NIH HHS S10 RR021113NHLBI NIH HHS R01 HL060230NHLBI NIH HHS R01 HL067986NHLBI NIH HHS R01 HL60230NHLBI NIH HHS R01 HL67986NIBIB NIH HHS R01 EB006818NIGMS NIH HHS R01 GM083030NIGMS NIH HHS R01 GM097478
6 · The paper itself

Abstract

Protein assembly at the air-water interface (AWI) occurs naturally in many biological processes and provides a method for creating biomaterials. However, the factors that control protein self-assembly at the AWI and the dynamic processes that occur during adsorption are still underexplored. Using fluorescence microscopy, we investigated assembly at the AWI of a model protein, human serum albumin minimally labeled with Texas Red fluorophore. Static and dynamic information was obtained under low subphase concentrations. By varying the solution protein concentration, ionic strength, and redox state, we changed the microstructure of protein assembly at the AWI accordingly. The addition of pluronic surfactant caused phase segregation to occur at the AWI, with fluid surfactant domains and more rigid protein domains revealed by fluorescence recovery after photobleaching experiments. Protein domains were observed to coalesce during this competitive adsorption process.

Indexed as

AirAdsorptionHumansKineticsMicroscopy, FluorescenceModels, MolecularProtein ConformationProteinsSerum AlbuminWaterXanthenesProteinsSerum AlbuminTexas redWaterXanthenes

Identifiers

PMID21942221
PMCPMC3212854
OpenAlexW1993017089

What OpenQuestion holds

Textmetadata
LicenceTDM
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.