Evidence map›Paper›PMID 36551315›Full record

ArticleBiomolecules2022

Portability of a Small-Molecule Binding Site between Disordered Proteins.

Rajesh Jaiprashad, Sachith Roch De Silva, Lisette M Fred Lucena, Ella Meyer, Steven J Metallo

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Biomolecules, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.2field-weighted citation impact, top 50% 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

2 citing papers in PubMed, 2 citations in OpenAlex.

  1. Review
  2. 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.

Rajesh JaiprashadDepartment of Chemistry, Georgetown University, Washington, DC 20057, USA.ORCID 0000-0003-0250-0829
Sachith Roch De SilvaDepartment of Chemistry, Georgetown University, Washington, DC 20057, USA.ORCID 0000-0002-9055-8846
Lisette M Fred LucenaDepartment of Chemistry, Georgetown University, Washington, DC 20057, USA.
Ella MeyerDepartment of Chemistry, Georgetown University, Washington, DC 20057, USA.
Steven J MetalloDepartment of Chemistry, Georgetown University, Washington, DC 20057, USA.
Georgetown University · US

Funding

The binding of small molecules to disordered proteins: specificity, affinity, and portabilityR15GM120698 · NIGMS · GEORGETOWN UNIVERSITY · PI METALLO, STEVEN J. · 2016 to 2016
$453k
NIGMS NIH HHS 1R15GM120698
6 · The paper itself

Abstract

Intrinsically disordered proteins (IDPs) are important in both normal and disease states. Small molecules can be targeted to disordered regions, but we currently have only a limited understanding of the nature of small-molecule binding sites in IDPs. Here, we show that a minimal small-molecule binding sequence of eight contiguous residues derived from the Myc protein can be ported into a different disordered protein and recapitulate small-molecule binding activity in the new context. We also find that the residue immediately flanking the binding site can have opposing effects on small-molecule binding in the different disordered protein contexts. The results demonstrate that small-molecule binding sites can act modularly and are portable between disordered protein contexts but that residues outside of the minimal binding site can modulate binding affinity.

Indexed as

Intrinsically Disordered ProteinsBinding SitesBiophysical PhenomenaProtein BindingIntrinsically Disordered Proteinsdrug targetsintrinsically disordered proteinsMycprotein-protein interactionSLiMsmall-molecule inhibitors

Identifiers

PMID36551315
PMCPMC9775153
OpenAlexW4313236911

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.