Evidence map›Paper›PMID 9675213›Full record

ArticleBiophysical journal1998

Oligomeric state of human erythrocyte band 3 measured by fluorescence resonance energy homotransfer.

S M Blackman, D W Piston, A H Beth

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.5field-weighted citation impact, top 11% 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

28 citing papers in PubMed, 68 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

3 authors at 1 institution in 1 country.

S M BlackmanDepartment of Molecular Physiology and Biophysics, Vanderbilt University, Nashville, Tennessee 37232-0615 USA.
D W Piston
A H Beth
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
–
NCRR NIH HHS RRO3155-01NHLBI NIH HHS HL34737NIGMS NIH HHS T32GM07347
6 · The paper itself

Abstract

The oligomeric state of the erythrocyte anion exchange protein, band 3, has been assayed by resonance energy homotransfer. Homotransfer between oligomeric subunits, labeled with eosin-5-maleimide at Lys430 in the transmembrane domain, has been demonstrated by steady-state and time-resolved fluorescence spectroscopy, and is readily observed by its depolarization of the eosin fluorescence. Polarized fluorescence measurements of HPLC-purified band 3 oligomers indicate that eosin homotransfer increases progressively with increasing species size. This shows that homotransfer also occurs between labeled band 3 dimers as well as within the dimers, making fluorescence anisotropy measurements sensitive to band 3 self-association. Treatment of ghost membranes with either Zn2+ or melittin, agents that cluster band 3, significantly decreases the anisotropy as a result of the increased homotransfer within the band 3 clusters. By comparison with the anisotropy of species of known oligomeric state, the anisotropy of erythrocyte ghost membranes at 37 degrees C is consistent with dimeric and/or tetrameric band 3, and does not require postulation of a fraction of large clusters. Proteolytic removal of the cytoplasmic domain of band 3, which significantly increases the rotational mobility of the transmembrane domain, does not affect its oligomeric state, as reported by eosin homotransfer. These results support a model in which interaction with the membrane skeleton restricts the mobility of band 3 without significantly altering its self-association state.

Indexed as

Anion Exchange Protein 1, ErythrocyteChromatography, High Pressure LiquidChromatography, Ion ExchangeDimerizationElectrophoresis, Polyacrylamide GelEosine Yellowish-(YS)Erythrocyte MembraneHumansLysineMacromolecular SubstancesMelittenModels, ChemicalSpectrometry, FluorescenceSpectroscopy, Fourier Transform InfraredZincAnion Exchange Protein 1, ErythrocyteEosine Yellowish-(YS)eosin maleimideLysineMacromolecular SubstancesMelittenZinc

Identifiers

PMID9675213
PMCPMC1299786
OpenAlexW2045423678

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.