Evidence map›Paper›PMID 35725977›Full record

ArticleNature communications2022

Mapping the conformational energy landscape of Abl kinase using ClyA nanopore tweezers.

Fanjun Li, Monifa A Fahie, Kaitlyn M Gilliam, Ryan Pham, Min Chen

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
6.9field-weighted citation impact, top 2% 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

22 citing papers in PubMed, 46 citations in OpenAlex.

  1. Article
  2. Tyrosine kinases sample unique activation ensembles.bioRxiv : the preprint server for biology · 2026
    Article
  3. Review
  4. Article
  5. Article
  6. Purification and Oligomerization of YaxAB Nanopores.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Exploring the conformational landscape of protein kinases.Current opinion in structural biology · 2024
    Review
  17. Article
  18. Article
  19. Article
  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

5 authors at 1 institution in 1 country.

Fanjun LiDepartment of Chemistry, University of Massachusetts Amherst, Amherst, MA, 01003, USA.
Monifa A FahieMolecular and Cellular Biology Program, University of Massachusetts Amherst, Amherst, MA, 01003, USA.
Kaitlyn M GilliamMolecular and Cellular Biology Program, University of Massachusetts Amherst, Amherst, MA, 01003, USA.
Ryan PhamDepartment of Chemistry, University of Massachusetts Amherst, Amherst, MA, 01003, USA.
Min ChenDepartment of Chemistry, University of Massachusetts Amherst, Amherst, MA, 01003, USA. mchen1@chem.umass.edu.ORCID 0000-0002-7572-0761
University of Massachusetts Amherst · US

Funding

Probing Functional States and Inhibition of Flaviviral Proteases Using Nanopore TweezersR01AI156187 · NIAID · UNIVERSITY OF MASSACHUSETTS AMHERST · PI CHEN, MIN · 2021 to 2025
$2.2M
OmpG nanopore for single molecule protein sensingR01GM115442 · NIGMS · UNIVERSITY OF MASSACHUSETTS AMHERST · PI CHEN, MIN · 2016 to 2020
$1.5M
NIAID NIH HHS R01 AI156187NIGMS NIH HHS R01 GM115442
6 · The paper itself

Abstract

Protein kinases play central roles in cellular regulation by catalyzing the phosphorylation of target proteins. Kinases have inherent structural flexibility allowing them to switch between active and inactive states. Quantitative characterization of kinase conformational dynamics is challenging. Here, we use nanopore tweezers to assess the conformational dynamics of Abl kinase domain, which is shown to interconvert between two major conformational states where one conformation comprises three sub-states. Analysis of kinase-substrate and kinase-inhibitor interactions uncovers the functional roles of relevant states and enables the elucidation of the mechanism underlying the catalytic deficiency of an inactive Abl mutant G321V. Furthermore, we obtain the energy landscape of Abl kinase by quantifying the population and transition rates of the conformational states. These results extend the view on the dynamic nature of Abl kinase and suggest nanopore tweezers can be used as an efficient tool for other members of the human kinome.

Indexed as

NanoporesHumansMolecular ConformationPhosphorylationProtein ConformationProtein Kinase InhibitorsProto-Oncogene Proteins c-ablProtein Kinase InhibitorsProto-Oncogene Proteins c-abl

Identifiers

PMID35725977
PMCPMC9209526
OpenAlexW4283161671

What Socratic holds

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LicenceCC BY
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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 Socratic graph.