Evidence map›Paper›PMID 34439840›Full record

ArticleBiomolecules2021

Insight into Calcium-Binding Motifs of Intrinsically Disordered Proteins.

Estella A Newcombe, Catarina B Fernandes, Jeppe E Lundsgaard, Inna Brakti, Kresten Lindorff-Larsen, Annette E Langkilde, Karen Skriver, Birthe B Kragelund

Open access · goldAbstract read
In one paragraph

Article in Biomolecules, 2021. 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
1.5field-weighted citation impact, top 17% 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, 30 citations in OpenAlex.

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  14. Amyloid-International journal of molecular sciences · 2023
    Article
  15. Article
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  17. CaProtein science : a publication of the Protein Society · 2022
    Article
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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

8 authors at 1 institution in 1 country.

Estella A NewcombeLinderstrøm-Lang Centre for Protein Science, University of Copenhagen, 2200 Copenhagen, Denmark.ORCID 0000-0001-6132-6168
Catarina B FernandesLinderstrøm-Lang Centre for Protein Science, University of Copenhagen, 2200 Copenhagen, Denmark.ORCID 0000-0002-6198-3173
Jeppe E LundsgaardLinderstrøm-Lang Centre for Protein Science, University of Copenhagen, 2200 Copenhagen, Denmark.
Inna BraktiLinderstrøm-Lang Centre for Protein Science, University of Copenhagen, 2200 Copenhagen, Denmark.
Kresten Lindorff-LarsenLinderstrøm-Lang Centre for Protein Science, University of Copenhagen, 2200 Copenhagen, Denmark.ORCID 0000-0002-4750-6039
Annette E LangkildeDepartment of Drug Design and Pharmacology, University of Copenhagen, Universitetsparken 2, 2100 Copenhagen, Denmark.ORCID 0000-0003-2467-4205
Karen SkriverLinderstrøm-Lang Centre for Protein Science, University of Copenhagen, 2200 Copenhagen, Denmark.ORCID 0000-0003-2225-4012
Birthe B KragelundLinderstrøm-Lang Centre for Protein Science, University of Copenhagen, 2200 Copenhagen, Denmark.ORCID 0000-0002-7454-1761
University of Copenhagen · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Motifs within proteins help us categorize their functions. Intrinsically disordered proteins (IDPs) are rich in short linear motifs, conferring them many different roles. IDPs are also frequently highly charged and, therefore, likely to interact with ions. Canonical calcium-binding motifs, such as the EF-hand, often rely on the formation of stabilizing flanking helices, which are a key characteristic of folded proteins, but are absent in IDPs. In this study, we probe the existence of a calcium-binding motif relevant to IDPs. Upon screening several carefully selected IDPs using NMR spectroscopy supplemented with affinity quantification by colorimetric assays, we found calcium-binding motifs in IDPs which could be categorized into at least two groups-an Excalibur-like motif, sequentially similar to the EF-hand loop, and a condensed-charge motif carrying repetitive negative charges. The motifs show an affinity for calcium typically in the ~100 μM range relevant to regulatory functions and, while calcium binding to the condensed-charge motif had little effect on the overall compaction of the IDP chain, calcium binding to Excalibur-like motifs resulted in changes in compaction. Thus, calcium binding to IDPs may serve various structural and functional roles that have previously been underreported.

Indexed as

Intrinsically Disordered Proteinsalpha-SynucleinCalciumHumansProtein BindingProtein DomainsProtein PrecursorsProtein Structure, SecondarySodium-Hydrogen Exchanger 1Thymosinalpha-SynucleinCalciumIntrinsically Disordered ProteinsProtein Precursorsprothymosin alphaSLC9A1 protein, humanSNCA protein, humanSodium-Hydrogen Exchanger 1ThymosincalciumIDPintrinsically disordered proteinsmotifsNMRSLiM

Identifiers

PMID34439840
PMCPMC8391695
OpenAlexW3189430685

What OpenQuestion holds

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Registered trials

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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.