Evidence map›Paper›PMID 27484630›Full record

ArticleeLife2016

The dimerization equilibrium of a ClC Cl(-)/H(+) antiporter in lipid bilayers.

Rahul Chadda, Venkatramanan Krishnamani, Kacey Mersch, Jason Wong, Marley Brimberry, Ankita Chadda, Ludmila Kolmakova-Partensky, Larry J Friedman, Jeff Gelles, Janice L Robertson

Open access · goldAbstract read
In one paragraph

Article in eLife, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

41 citing papers in PubMed, 57 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Cholesterol inhibits assembly and activation of the EphA2 receptor.bioRxiv : the preprint server for biology · 2024
    Article
  8. Review
  9. Structural basis of pH-dependent activation in a CLC transporter.Nature structural & molecular biology · 2024
    Article
  10. Article
  11. Dimerization mechanism of an inverted-topology ion channel in membranes.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  12. Membrane defects as a generalized driving force for membrane protein interactions.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  13. A thermodynamic analysis of CLC transporter dimerization in lipid bilayers.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Untangling the complexity of membrane protein folding.Current opinion in structural biology · 2022
    Review
  20. 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

10 authors at 2 institutions in 2 countries.

Rahul ChaddaDepartment of Molecular Physiology and Biophysics, University of Iowa, Iowa City, United States.
Venkatramanan KrishnamaniDepartment of Molecular Physiology and Biophysics, University of Iowa, Iowa City, United States.
Kacey MerschDepartment of Molecular Physiology and Biophysics, University of Iowa, Iowa City, United States.
Jason WongDepartment of Molecular Physiology and Biophysics, University of Iowa, Iowa City, United States.
Marley BrimberryDepartment of Molecular Physiology and Biophysics, University of Iowa, Iowa City, United States.
Ankita ChaddaDepartment of Molecular Physiology and Biophysics, University of Iowa, Iowa City, United States.
Ludmila Kolmakova-PartenskyDepartment of Biochemistry, Brandeis University, Waltham, United States.
Larry J FriedmanDepartment of Biochemistry, Brandeis University, Waltham, United States.ORCID 0000-0003-4946-8731
Jeff GellesDepartment of Biochemistry, Brandeis University, Waltham, United States.ORCID 0000-0001-7910-3421
Janice L RobertsonDepartment of Molecular Physiology and Biophysics, University of Iowa, Iowa City, United States.ORCID 0000-0002-5499-9943
University of Iowa · USBrandeis University · US

Funding

Single-molecule visualization of transcription regulation mechanismsR01GM081648 · NIGMS · BRANDEIS UNIVERSITY · PI JEFF GELLES · 2007 to 2026
$7.4M
Driving forces of membrane protein assembly in membranesR01GM120260 · NIGMS · WASHINGTON UNIVERSITY · PI ROBERTSON, JANICE L · 2016 to 2024
$3.4M
Reversible dimerization of a CLC transporter: A model for membrane protein foldinR00GM101016 · NIGMS · UNIVERSITY OF IOWA · PI ROBERTSON, JANICE L · 2013 to 2015
$727k
Reversible dimerization of a CLC transporter: A model for membrane protein foldinK99GM101016 · NIGMS · BRANDEIS UNIVERSITY · PI ROBERTSON, JANICE L · 2012 to 2013
$105k
NIGMS NIH HHS K99 GM101016NIGMS NIH HHS R00 GM101016NIGMS NIH HHS R01 GM081648NIGMS NIH HHS R01 GM120260
6 · The paper itself

Abstract

Interactions between membrane protein interfaces in lipid bilayers play an important role in membrane protein folding but quantification of the strength of these interactions has been challenging. Studying dimerization of ClC-type transporters offers a new approach to the problem, as individual subunits adopt a stable and functionally verifiable fold that constrains the system to two states - monomer or dimer. Here, we use single-molecule photobleaching analysis to measure the probability of ClC-ec1 subunit capture into liposomes during extrusion of large, multilamellar membranes. The capture statistics describe a monomer to dimer transition that is dependent on the subunit/lipid mole fraction density and follows an equilibrium dimerization isotherm. This allows for the measurement of the free energy of ClC-ec1 dimerization in lipid bilayers, revealing that it is one of the strongest membrane protein complexes measured so far, and introduces it as new type of dimerization model to investigate the physical forces that drive membrane protein association in membranes.

Indexed as

Lipid BilayersProtein MultimerizationChloride ChannelsSingle Molecule ImagingChloride ChannelsCLC-1 channelLipid BilayersbiochemistrybiophysicsE. coliequilibriumlipid bilayermembrane proteinprotein foldingsingle-moleculestructural biologyTIRF

Identifiers

PMID27484630
PMCPMC5010387
OpenAlexW2475459768

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.