Evidence map›Paper›PMID 29262364›Full record

ArticleBiophysical journal2017

pKID Binds to KIX via an Unstructured Transition State with Nonnative Interactions.

Liza Dahal, Tristan O C Kwan, Sarah L Shammas, Jane Clarke

Open access · hybridAbstract read
In one paragraph

Article in Biophysical journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
3.5field-weighted citation impact, top 6% 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

26 citing papers in PubMed, 38 citations in OpenAlex.

  1. Article
  2. Fluorine-Thiol Displacement Stapling on the Disordered αSynlett : accounts and rapid communications in synthetic organic chemistry · 2025
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  3. Article
  4. Lighting up Nobel Prize-winning studies with protein intrinsic disorder.Cellular and molecular life sciences : CMLS · 2022
    Review
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  7. Unexpected specificity within dynamic transcriptional protein-protein complexes.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  8. Article
  9. Article
  10. Review
  11. Templated folding of intrinsically disordered proteins.The Journal of biological chemistry · 2020
    Review
  12. Review
  13. Article
  14. Article
  15. Review
  16. Article
  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

4 authors at 1 institution in 1 country.

Liza DahalDepartment of Chemistry, University of Cambridge, Cambridge, United Kingdom.
Tristan O C KwanDepartment of Chemistry, University of Cambridge, Cambridge, United Kingdom.
Sarah L ShammasDepartment of Chemistry, University of Cambridge, Cambridge, United Kingdom. Electronic address: sarah.shammas@bioch.ox.ac.uk.
Jane ClarkeDepartment of Chemistry, University of Cambridge, Cambridge, United Kingdom. Electronic address: jc162@cam.ac.uk.
University of Cambridge · GB

Funding

Medical Research Council MC_U105485808Medical Research Council MR/N024168/1Wellcome Trust
6 · The paper itself

Abstract

Understanding the detailed mechanism of interaction of intrinsically disordered proteins with their partners is crucial to comprehend their functions in signaling and transcription. Through its interaction with KIX, the disordered pKID region of CREB protein is central in the transcription of cAMP responsive genes, including those involved in long-term memory. Numerous simulation studies have investigated these interactions. Combined with experimental results, these can provide valuable and comprehensive understanding of the mechanisms involved. Here, we probe the transition state of this interaction experimentally through analyzing the kinetic effect of mutating both interface and solvent exposed residues in pKID. We show that very few specific interactions between pKID and KIX are required in the initial binding process. Only a small number of weak interactions are formed at the transition state, including nonnative interactions, and most of the folding occurs after the initial binding event. These properties are consistent with computational results and also the majority of experimental studies of intrinsically disordered protein coupled folding and binding in other protein systems, suggesting that these may be common features.

Indexed as

Cyclic AMP Response Element-Binding ProteinIntrinsically Disordered ProteinsModels, MolecularMutationProtein BindingProtein DomainsProtein StabilityCyclic AMP Response Element-Binding ProteinIntrinsically Disordered Proteins

Identifiers

PMID29262364
PMCPMC5770965
OpenAlexW2778291561

What OpenQuestion holds

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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.