Evidence map›Paper›PMID 35011704›Full record

ReviewCells2022

Structural Aspects of LIMK Regulation and Pharmacology.

Deep Chatterjee, Franziska Preuss, Verena Dederer, Stefan Knapp, Sebastian Mathea

Open access · goldAbstract readReview
In one paragraph

Review in Cells, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
3.4field-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

18 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Regulation and signaling of the LIM domain kinases.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025
    Review
  10. Review
  11. Article
  12. Article
  13. Review
  14. Review
  15. Article
  16. Article
  17. Review
  18. Review
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 1 institution in 1 country.

Deep ChatterjeeStructural Genomics Consortium, Buchmann Institute for Molecular Life Sciences, Max-von-Laue-Str 15, 60438 Frankfurt am Main, Germany.ORCID 0000-0001-8190-9213
Franziska PreussStructural Genomics Consortium, Buchmann Institute for Molecular Life Sciences, Max-von-Laue-Str 15, 60438 Frankfurt am Main, Germany.
Verena DedererStructural Genomics Consortium, Buchmann Institute for Molecular Life Sciences, Max-von-Laue-Str 15, 60438 Frankfurt am Main, Germany.
Stefan KnappStructural Genomics Consortium, Buchmann Institute for Molecular Life Sciences, Max-von-Laue-Str 15, 60438 Frankfurt am Main, Germany.ORCID 0000-0001-5995-6494
Sebastian MatheaStructural Genomics Consortium, Buchmann Institute for Molecular Life Sciences, Max-von-Laue-Str 15, 60438 Frankfurt am Main, Germany.
Goethe University Frankfurt · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Malfunction of the actin cytoskeleton is linked to numerous human diseases including neurological disorders and cancer. LIMK1 (LIM domain kinase 1) and its paralogue LIMK2 are two closely related kinases that control actin cytoskeleton dynamics. Consequently, they are potential therapeutic targets for the treatment of such diseases. In the present review, we describe the LIMK conformational space and its dependence on ligand binding. Furthermore, we explain the unique catalytic mechanism of the kinase, shedding light on substrate recognition and how LIMK activity is regulated. The structural features are evaluated for implications on the drug discovery process. Finally, potential future directions for targeting LIMKs pharmacologically, also beyond just inhibiting the kinase domain, are discussed.

Indexed as

Actin Depolymerizing FactorsActinsHumansLim KinasesModels, MolecularPhosphorylationActin Depolymerizing FactorsActinsLIMK1 protein, humanLIMK2 protein, humanLim Kinasesactin cytoskeleton dynamicscatalytic mechanismcofilinkinaseLIMK1LIMK2phosphorylationsmall-molecule inhibitor

Identifiers

PMID35011704
PMCPMC8750758
OpenAlexW4205373279

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.