Evidence map›Paper›PMID 40869329›Full record

ArticleInternational journal of molecular sciences2025

Adaptation of the Protocol for the Isolation of Biotinylated Protein Complexes for

Igor A Shokodko, Rustam H Ziganshin, Nadezhda E Vorobyeva

Abstract read
In one paragraph

Article in International journal of molecular sciences, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

3 authors.

Igor A ShokodkoInstitute of Gene Biology Russian Academy of Sciences, 119334 Moscow, Russia.
Rustam H ZiganshinShemyakin-Ovchinnikov Institute of Bioorganic Chemistry Russian Academy of Sciences, 117997 Moscow, Russia.ORCID 0000-0002-7931-519X
Nadezhda E VorobyevaInstitute of Gene Biology Russian Academy of Sciences, 119334 Moscow, Russia.ORCID 0000-0003-4293-834X

Funding

Russian Science Foundation 23-14-00184
6 · The paper itself

Abstract

Proximity biotinylation, which utilizes various biotin ligating enzymes (BioID, TurboID, etc.), is widely used as a powerful tool for identifying novel protein-protein interactions. However, this method has a significant limitation: the use of streptavidin on beads for enriching biotinylated proteins often results in a high background of peptides from streptavidin itself, which interferes with identification by peptide mass fingerprinting. This limitation makes it practically impossible to study samples containing a small amount of material, such as individual insect tissues. In this study, we compared different precipitation and elution conditions for the purification of biotinylated proteins from protein extracts of

Indexed as

Drosophila melanogasterDrosophila ProteinsAnimalsBiotinBiotinylationCell LineFemaleOvaryProtein BindingStreptavidinBiotinDrosophila ProteinsStreptavidinbiotinecdysoneecdysone receptorEcRLC-MS/MSmass spectrometrymodified streptavidinproximal biotinylationproximal labelingstreptavidintranscription regulationTurboID

Identifiers

PMID40869329
PMCPMC12386920

What Socratic 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 Socratic graph.