Evidence map›Paper›PMID 22136342›Full record

ArticleMicrobial cell factories2011

Biological activities of histidine-rich peptides; merging biotechnology and nanomedicine.

Neus Ferrer-Miralles, José Luis Corchero, Pradeep Kumar, Juan A Cedano, Kailash C Gupta, Antonio Villaverde, Esther Vazquez

Open access · goldAbstract read
In one paragraph

Article in Microbial cell factories, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.3field-weighted citation impact, top 21% 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

22 citing papers in PubMed, 56 citations in OpenAlex.

  1. Article
  2. Protease-Catalyzed Synthesis of Water-Soluble Oligohistidine.Industrial biotechnology (New Rochelle, N.Y.) · 2025
    Article
  3. Review
  4. Article
  5. Review
  6. Enhancement of the Water Affinity of Histidine by Zinc and Copper Ions.International journal of molecular sciences · 2022
    Article
  7. Article
  8. Article
  9. Article
  10. Coiled coil exposure and histidine tags drive function of an intracellular protein drug carrier.Journal of controlled release : official journal of the Controlled Release Society · 2021
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Inhibition of regulated cell death by cell-penetrating peptides.Cellular and molecular life sciences : CMLS · 2016
    Review
  19. Multifunctional spider silk polymers for gene delivery to human mesenchymal stem cells.Journal of biomedical materials research. Part B, Applied biomaterials · 2015
    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

7 authors at 5 institutions in 3 countries.

Neus Ferrer-MirallesInstitut de Biotecnologia i de Biomedicina, Universitat Autònoma de Barcelona, Bellaterra, Barcelona, Spain.
José Luis Corchero
Pradeep Kumar
Juan A Cedano
Kailash C Gupta
Antonio Villaverde
Esther Vazquez
Universitat Autònoma de Barcelona · ESBiomedical Research Networking Center in Bioengineering, Biomaterials and Nanomedicine · ESIndian Institute of Toxicology Research · INInstitute of Genomics and Integrative Biology · INUniversidad de la República · UY

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Histidine-rich peptides are commonly used in recombinant protein production as purification tags, allowing the one-step affinity separation of the His-tagged proteins from the extracellular media or cell extracts. Genetic engineering makes feasible the post-purification His-tag removal by inserting, between the tag and the main protein body, a target site for trans-acting proteases or a self-proteolytic peptide with regulatable activities. However, for technical ease, His tags are often not removed and the fusion proteins eventually used in this form. In this commentary, we revise the powerful biological properties of histidine-rich peptides as endosomolytic agents and as architectonic tags in nanoparticle formation, for which they are exploited in drug delivery and other nanomedical applications. These activities, generally unknown to biotechnologists, can unwillingly modulate the functionality and biotechnological performance of recombinant proteins in which they remain trivially attached.

Indexed as

Amino Acid SequenceBiotechnologyHistidineHumansMolecular Sequence DataNanomedicinePeptidesProtein EngineeringHistidinePeptides

Identifiers

PMID22136342
PMCPMC3339332
OpenAlexW2025722048

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.