Evidence map›Paper›PMID 18642799›Full record

ArticleACS chemical biology2008

Discovery of potent CLC chloride channel inhibitors.

Kimberly Matulef, Andrew E Howery, Li Tan, William R Kobertz, J Du Bois, Merritt Maduke

Open access · greenAbstract read
In one paragraph

Article in ACS chemical biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.0field-weighted citation impact, top 26% 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

24 citing papers in PubMed, 41 citations in OpenAlex.

  1. Article
  2. Chloride Homeostasis Regulates cGAS-STING Signaling.bioRxiv : the preprint server for biology · 2024
    Article
  3. Biophysical and Pharmacological Insights to CLC Chloride Channels.Handbook of experimental pharmacology · 2024
    Article
  4. Article
  5. Review
  6. Article
  7. Targeting Ion Channels for Cancer Treatment: Current Progress and Future Challenges.Reviews of physiology, biochemistry and pharmacology · 2022
    Review
  8. Article
  9. Article
  10. A selective class of inhibitors for the CLC-Ka chloride ion channel.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  11. Taming unruly chloride channel inhibitors with rational design.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Novel diuretic targets.American journal of physiology. Renal physiology · 2013
    Review
  18. Article
  19. Article
  20. Pendrin function and regulation in Xenopus oocytes.Cellular physiology and biochemistry : international journal of experimental cellular physiology, biochemistry, and pharmacology · 2011
    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

6 authors at 2 institutions in 1 country.

Kimberly MatulefDepartment of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, California 94305, USA.
Andrew E Howery
Li Tan
William R Kobertz
J Du Bois
Merritt Maduke
Stanford University · USUniversity of Massachusetts Chan Medical School · US

Funding

K+ channel protein complexes in auditory biologyR01DC007669 · NIDCD · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI KOBERTZ, WILLIAM R · 2005 to 2009
$2.1M
Mechanisms of CIC Chloride Transport ProteinsR01GM070773 · NIGMS · STANFORD UNIVERSITY · PI MADUKE, MERRITT C · 2005 to 2009
$1.5M
NIDCD NIH HHS R01 DC007669NIGMS NIH HHS R01 GM070773
6 · The paper itself

Abstract

Anion-transport proteins are central to all of physiology, for processes ranging from regulating bone-density, muscle excitability, and blood pressure, to facilitating extreme-acid survival of pathogenic bacteria. 4,4-Diisothiocyanatostilbene-2,2'-disulfonic acid (DIDS) has been used as an anion-transport inhibitor for decades. In this study, we demonstrate that polythiourea products derived from DIDS hydrolysis inhibit three different CLC chloride-transport proteins, ClC-ec1, ClC-0, and ClC-Ka, more effectively than DIDS itself. The structures of the five major products were determined by NMR spectroscopy, mass spectrometry, and chemical synthesis. These compounds bind directly to the CLC proteins, as evidenced by the fact that inhibition of ClC-0 occurs only from the intracellular side and inhibition of ClC-Ka is prevented by the point mutation N68D. These polythioureas are the highest affinity inhibitors known for the CLCs and provide a new class of chemical probes for dissecting the molecular mechanisms of chloride transport.

Indexed as

4,4'-Diisothiocyanostilbene-2,2'-Disulfonic AcidAnionsChloride ChannelsChloridesCombinatorial Chemistry TechniquesEscherichia coliGene Expression Regulation, BacterialModels, MolecularMolecular StructureThiourea4,4'-Diisothiocyanostilbene-2,2'-Disulfonic AcidAnionsChloride ChannelsChloridesThiourea

Identifiers

PMID18642799
PMCPMC2556891
OpenAlexW2050987750

What OpenQuestion holds

Textmetadata
LicenceTDM
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.