Evidence map›Paper›PMID 15596535›Full record

ArticleThe Journal of general physiology2005

Perturbation analysis of the voltage-sensitive conformational changes of the Na+/glucose cotransporter.

Donald D F Loo, Bruce A Hirayama, Albert Cha, Francisco Bezanilla, Ernest M Wright

Erratum issuedOpen access · bronzeAbstract read
In one paragraph

Article in The Journal of general physiology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing 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

27 citing papers in PubMed, 41 citations in OpenAlex.

  1. Article
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  4. Active site voltage clamp fluorometry of the sodium glucose cotransporter hSGLT1.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  5. Epithelial transport inThe Journal of general physiology · 2017
    Review
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  8. Article
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  10. Article
  11. The SLC34 family of sodium-dependent phosphate transporters.Pflugers Archiv : European journal of physiology · 2014
    Review
  12. Functional identification and characterization of sodium binding sites in Na symporters.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  13. Article
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4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Donald D F LooDepartment of Physiology, David Geffen School of Medicine at UCLA, Los Angeles, CA 90095, USA. dloo@mednet.ucla.edu
Bruce A Hirayama
Albert Cha
Francisco Bezanilla
Ernest M Wright
University of California, Los Angeles · US

Funding

MOLECULAR MECHANISMS OF INTESTINAL TRANSPORTR01DK019567 · NIDDK · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI WRIGHT, ERNEST M · 1986 to 2013
$4.3M
NIDDK NIH HHS DK19567NIDDK NIH HHS R01 DK019567
6 · The paper itself

Abstract

Conformational changes of the human Na(+)/glucose cotransporter (hSGLT1) were studied using voltage-jump methods. The cotransporter was expressed in Xenopus laevis oocytes, and SGLT1 charge movements were measured in the micro- to millisecond time scale using the cut-open oocyte preparation and in the millisecond to second time scale using the two-electrode voltage clamp method. Simultaneous charge and fluorescence changes were studied using tetramethylrhodamine-6-maleimide-labeled hSGLT1 Q457C. In 100 mM external [Na(+)], depolarizing voltage steps evoked a charge movement that rose initially to a peak (with time constant tau = 0.17 ms) before decaying to steady state with two time constants (tau = 2-30 and 25-150 ms). The time to peak (0.9 ms) decreased with [Na(+)], and was not observed in 0 mM [Na(+)]. In absence of Na(+), charge movement decayed monotonically to steady state with three time constants (0.2, 2, and 150 ms). Charge movement was accompanied by fluorescence changes with similar time courses, indicating that global conformational changes monitored by charge movement are reflected by local environmental changes at or near Q457C. Our results indicate that the major voltage-dependent step of the Na(+)/glucose transport cycle is the return of the empty carrier from inward to outward facing conformations. Finally, we observed subtle differences between time constants for charge movement and for optical changes, suggesting that optical recordings can be used to monitor local conformational changes that underlie the global conformational changes of cotransporters.

Indexed as

Models, BiologicalAnimalsCells, CulturedComputer SimulationHumansKineticsMembrane GlycoproteinsMembrane PotentialsMonosaccharide Transport ProteinsOocytesProtein ConformationSodium-Glucose Transporter 1Static ElectricityStructure-Activity RelationshipXenopus laevisMembrane GlycoproteinsMonosaccharide Transport ProteinsSLC5A1 protein, humanSodium-Glucose Transporter 1

Identifiers

PMID15596535
PMCPMC2217483
OpenAlexW2117052585

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.