Evidence map›Paper›PMID 41507482›Full record

ArticleBulletin of experimental biology and medicine2025

Isolation, Purification, and Structural-Functional Analysis of Recombinant Human Transferrin Produced by the Methylotrophic Yeast Strain Pichia pastoris.

R Yu Popov, E D Nikolskaya, T K Aliev, N N Kostin, T V Bobik, A G Gabibov

Abstract read
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Article in Bulletin of experimental biology and medicine, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0citing papers in PubMed
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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

6 authors.

R Yu PopovNational Research Centre "Kurchatov Institute", Moscow, Russia. poprom@outlook.com.
E D NikolskayaEmanuel Institute of Biochemical Physics, Russian Academy of Sciences, Moscow, Russia.
T K AlievShemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, Russia.
N N KostinShemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, Russia.
T V BobikShemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, Russia.
A G GabibovShemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, Russia.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A recombinant modified human transferrin (N413D and N611D) was produced by the Pichia pastoris strain pPIC9pGAPZalpha-short_hTFNG (Yst-TFNG2). A multi-step protocol for isolation and purification of recombinant transferrin was developed achieving the target protein yield of 70.29% and a purity of at least 95%. Structural correspondence of the recombinant transferrin to the natural protein was confirmed by mass spectrometry and circular dichroism analysis. Functional analysis demonstrated the protein's ability to bind and release iron ions, as well as support the proliferation of eukaryotic cells.

Indexed as

Recombinant ProteinsTransferrinCircular DichroismHumansIronPichiaSaccharomycetalesIronRecombinant ProteinsTransferrinPichia pastorisprotein purificationrecombinant transferrinstructural and functional analysis

Identifiers

PMID41507482

What OpenQuestion holds

Textmetadata
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.