Evidence map›Paper›PMID 8804603›Full record

ArticleBiophysical journal1996

The orientation of eosin-5-maleimide on human erythrocyte band 3 measured by fluorescence polarization microscopy.

S M Blackman, C E Cobb, A H Beth, D W Piston

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in Biophysical journal, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
0.7field-weighted citation impact, top 32% 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

30 citing papers in PubMed, 54 citations in OpenAlex.

  1. Trial
  2. Review
  3. Article
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  9. Review
  10. Fluorescence linear dichroism imaging for quantifying membrane order.Methods in molecular biology (Clifton, N.J.) · 2015
    Article
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  12. Article
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  15. Article
  16. 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

4 authors at 1 institution in 1 country.

S M BlackmanDepartment of Molecular Physiology and Biophysics, Vanderbilt University, Nashville, Tennessee 37232, USA.
C E Cobb
A H Beth
D W Piston
Vanderbilt University · US

Funding

MEDICAL SCIENTIST TRAINING PROGRAMT32GM007347 · NIGMS · VANDERBILT UNIVERSITY · PI WILLIAMS, CHRISTOPHER S. · 1985 to 2023
$26.3M
EPR STUDIES OF MEMBRANE PROTEINSR37HL034737 · NHLBI · VANDERBILT UNIVERSITY · PI BETH, ALBERT H · 1998 to 2007
$2.5M
MOLECULAR PHYSIOLOGY &BIOPHYSICSR01HL034737 · NHLBI · VANDERBILT UNIVERSITY · PI BETH, ALBERT H · 1985 to 1998
–
NHLBI NIH HHS HL 34737NIGMS NIH HHS T32 GM07347
6 · The paper itself

Abstract

The dominant motional mode for membrane proteins is uniaxial rotational diffusion about the membrane normal axis, and investigations of their rotational dynamics can yield insight into both the oligomeric state of the protein and its interactions with other proteins such as the cytoskeleton. However, results from the spectroscopic methods used to study these dynamics are dependent on the orientation of the probe relative to the axis of motion. We have employed polarized fluorescence confocal microscopy to measure the orientation of eosin-5-maleimide covalently reacted with Lys-430 of human erythrocyte band 3. Steady-state polarized fluorescence images showed distinct intensity patterns, which were fit to an orientation distribution of the eosin absorption and emission dipoles relative to the membrane normal axis. This orientation was found to be unchanged by trypsin treatment, which cleaves band 3 between the integral membrane domain and the cytoskeleton-attached domain. this result suggests that phosphorescence anisotropy changes observed after trypsin treatment are due to a rotational constraint change rather than a reorientation of eosin. By coupling time-resolved prompt fluorescence anisotropy with confocal microscopy, we calculated the expected amplitudes of the e-Dt and e-4Dt terms from the uniaxial rotational diffusion model and found that the e-4Dt term should dominate the anisotropy decay. Delayed fluorescence and phosphorescence anisotropy decays of control and trypsin-treated band 3 in ghosts, analyzed as multiple uniaxially rotating populations using the amplitudes predicted by confocal microscopy, were consistent with three motional species with uniaxial correlation times ranging from 7 microseconds to 1.4 ms.

Indexed as

Anion Exchange Protein 1, ErythrocyteBiophysical PhenomenaBiophysicsDiffusionElectron Spin Resonance SpectroscopyEosine Yellowish-(YS)Erythrocyte MembraneFluorescence PolarizationFluorescent DyesHumansMicroscopy, ConfocalMicroscopy, FluorescenceModels, ChemicalRotationThermodynamicsTrypsinAnion Exchange Protein 1, ErythrocyteEosine Yellowish-(YS)eosin maleimideFluorescent DyesTrypsin

Identifiers

PMID8804603
PMCPMC1233471
OpenAlexW2005423498

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.