Evidence map›Paper›PMID 20568736›Full record

ArticleBiochemistry2010

Delineating electrogenic reactions during lactose/H+ symport.

Juan J Garcia-Celma, Julian Ploch, Irina Smirnova, H Ronald Kaback, Klaus Fendler

Open access · bronzeAbstract read
In one paragraph

Article in Biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
4.1field-weighted citation impact, top 7% 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

25 citing papers in PubMed, 41 citations in OpenAlex.

  1. Article
  2. Rescue of Epilepsy-Associated Mutations of the Highly Conserved Glycine Residue 443 in the Human GABA Transporter 1.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025
    Article
  3. Article
  4. Function Trumps Form in Two Sugar Symporters,International journal of molecular sciences · 2021
    Review
  5. Article
  6. It takes two to tango: The dance of the permease.The Journal of general physiology · 2019
    Review
  7. Arg302 governs the pKProceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  8. Article
  9. Oversized galactosides as a probe for conformational dynamics in LacY.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  10. A Loose Relationship: Incomplete HBiophysical journal · 2017
    Article
  11. Article
  12. Article
  13. Structure of LacY with an α-substituted galactoside: Connecting the binding site to the protonation site.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  14. A chemiosmotic mechanism of symport.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  15. Direct observation of electrogenic NH4(+) transport in ammonium transport (Amt) proteins.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  16. Functional architecture of MFS D-glucose transporters.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  17. Structure of sugar-bound LacY.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  18. Evolutionary mix-and-match with MFS transporters II.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  19. Introduction to solid supported membrane based electrophysiology.Journal of visualized experiments : JoVE · 2013
    Article
  20. Evolutionary mix-and-match with MFS transporters.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
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 2 countries.

Juan J Garcia-CelmaDepartment of Biophysical Chemistry, Max-Planck-Institute of Biophysics, D-60438 Frankfurt/M, Germany.
Julian Ploch
Irina Smirnova
H Ronald Kaback
Klaus Fendler
Max Planck Institute of Biophysics · DEUniversity of California, Los Angeles · US

Funding

Yeast ExpressionP50GM073210 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI STROUD, ROBERT M · 2004 to 2013
$21.5M
SPECIALIZED CENTER FOR THE PROTEIN STRUCTURE INITIATIVEU54GM074929 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI STAHLBERG, HENNING · 2005 to 2009
$16.6M
NEW APPROACHES TO MEMBRANE PROTEIN STRUCTURESR01DK051131 · NIDDK · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI KABACK, HOWARD RONALD · 1996 to 2014
$5.2M
Structural Basis for Mechanism of Secondary TransportersR01DK069463 · NIDDK · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI KABACK, HOWARD RONALD · 2005 to 2013
$3.7M
Structural Basis for Mechanism of Secondary TransportersR56DK069463 · NIDDK · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI KABACK, HOWARD RONALD · 2009 to 2009
$500k
Dynamics of the Lactose Permease of Escherichia ColiR56DK051131 · NIDDK · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI KABACK, HOWARD RONALD · 2015 to 2015
$154k
NIDDK NIH HHS DK051131NIDDK NIH HHS DK069463NIDDK NIH HHS R01 DK069463NIGMS NIH HHS GM073210NIGMS NIH HHS GM074929
6 · The paper itself

Abstract

Electrogenic reactions accompanying downhill lactose/H(+) symport catalyzed by the lactose permease of Escherichia coli (LacY) have been assessed using solid-supported membrane-based electrophysiology with improved time resolution. Rates of charge translocation generated by purified LacY reconstituted into proteoliposomes were analyzed over a pH range from 5.2 to 8.5, which allows characterization of two electrogenic steps in the transport mechanism: (i) a weak electrogenic reaction triggered by sugar binding and observed under conditions where H(+) translocation is abolished either by acidic pH or by a Glu325 --> Ala mutation in the H(+) binding site (this step with a rate constant of approximately 200 s(-1) for wild-type LacY leads to an intermediate proposed to represent an "occluded" state) and (ii) a major electrogenic reaction corresponding to 94% of the total charge translocated at pH 8, which is pH-dependent with a maximum rate of approximately 30 s(-1) and a pK of 7.5. This partial reaction is assigned to rate-limiting H(+) release on the cytoplasmic side of LacY during turnover. These findings together with previous electrophysiological results and biochemical-biophysical studies are included in an overall kinetic mechanism that allows delineation of the electrogenic steps in the reaction pathway.

Indexed as

Binding SitesCell MembraneElectrophysiological PhenomenaEscherichia coliEscherichia coli ProteinsHydrogen-Ion ConcentrationLactoseMonosaccharide Transport ProteinsMutationProtonsSymportersEscherichia coli ProteinsLactoseLacY protein, E coliMonosaccharide Transport ProteinsProtonsSymporters

Identifiers

PMID20568736
PMCPMC2907097
OpenAlexW2070723646

What OpenQuestion holds

Textmetadata
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Registered trials

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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.