Evidence map›Paper›PMID 23393575›Full record

ArticlePloS one2013

Single particle electron microscopy analysis of the bovine anion exchanger 1 reveals a flexible linker connecting the cytoplasmic and membrane domains.

Jiansen Jiang, Nathaniel Magilnick, Kirill Tsirulnikov, Natalia Abuladze, Ivo Atanasov, Peng Ge, Mohandas Narla, Alexander Pushkin, Z Hong Zhou, Ira Kurtz

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.6field-weighted citation impact, top 18% 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

14 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
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  7. Adaptable interaction between aquaporin-1 and band 3 reveals a potential role of water channel in blood COFASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2017
    Article
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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

10 authors at 4 institutions in 1 country.

Jiansen JiangDepartment of Microbiology, Immunology and Molecular Genetics, and California NanoSystems Institute, University of California Los Angeles, Los Angeles, California, United States of America.
Nathaniel Magilnick
Kirill Tsirulnikov
Natalia Abuladze
Ivo Atanasov
Peng Ge
Mohandas Narla
Alexander Pushkin
Z Hong Zhou
Ira Kurtz
University of California, Los Angeles · USCalifornia NanoSystems Institute · USBaylor College of Medicine · USNew York Blood Center · US

Funding

The Biology of NBCe1 in Health and DiseaseR01DK077162 · NIDDK · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI IRA KURTZ · 2007 to 2026
$6.7M
High-Resolution CryoEM Reconstruction of Large ComplexesR01GM071940 · NIGMS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI ZHOU, Z HONG · 2006 to 2025
$5.0M
RED CELL DEFORMABILITY IN VITRO AND SURVIVAL IN VIVOR37DK026263 · NIDDK · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI NARLA, MOHANDAS · 1995 to 2017
$4.5M
BIOLOGY OF SODIUM BICARBONATE TRANSPORTR01DK058563 · NIDDK · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI KURTZ, IRA · 2001 to 2011
$3.1M
NIDDK NIH HHS DK058563NIDDK NIH HHS DK077162NIDDK NIH HHS R01 DK058563NIDDK NIH HHS R01 DK077162NIDDK NIH HHS R37 DK026263NIGMS NIH HHS GM071940NIGMS NIH HHS R01 GM071940
6 · The paper itself

Abstract

Anion exchanger 1 (AE1) is the major erythrocyte membrane protein that mediates chloride/bicarbonate exchange across the erythrocyte membrane facilitating CO₂ transport by the blood, and anchors the plasma membrane to the spectrin-based cytoskeleton. This multi-protein cytoskeletal complex plays an important role in erythrocyte elasticity and membrane stability. An in-frame AE1 deletion of nine amino acids in the cytoplasmic domain in a proximity to the membrane domain results in a marked increase in membrane rigidity and ovalocytic red cells in the disease Southeast Asian Ovalocytosis (SAO). We hypothesized that AE1 has a flexible region connecting the cytoplasmic and membrane domains, which is partially deleted in SAO, thus causing the loss of erythrocyte elasticity. To explore this hypothesis, we developed a new non-denaturing method of AE1 purification from bovine erythrocyte membranes. A three-dimensional (3D) structure of bovine AE1 at 2.4 nm resolution was obtained by negative staining electron microscopy, orthogonal tilt reconstruction and single particle analysis. The cytoplasmic and membrane domains are connected by two parallel linkers. Image classification demonstrated substantial flexibility in the linker region. We propose a mechanism whereby flexibility of the linker region plays a critical role in regulating red cell elasticity.

Indexed as

AnimalsAnion Exchange Protein 1, ErythrocyteCattleCytoplasmElectrophoresis, Polyacrylamide GelImmunoblottingMicroscopy, ElectronProtein Structure, TertiaryAnion Exchange Protein 1, Erythrocyte

Identifiers

PMID23393575
PMCPMC3564912
OpenAlexW2000197232

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.