Evidence map›Paper›PMID 30102720›Full record

ArticlePloS one2018

Engineered ferritin for lanthanide binding.

Lorenzo Calisti, Matilde Cardoso Trabuco, Alberto Boffi, Claudia Testi, Linda Celeste Montemiglio, Amédée des Georges, Irene Benni, Andrea Ilari, Bartłomiej Taciak, Maciej Białasek and 4 more

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

17 citing papers in PubMed, 31 citations in OpenAlex.

  1. Chemical reviews · 2026
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  13. Ferritin Nanocages for Protein Delivery to Tumor Cells.Molecules (Basel, Switzerland) · 2020
    Review
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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

14 authors at 6 institutions in 3 countries.

Lorenzo CalistiDepartment of Biochemical Sciences "Alessandro Rossi Fanelli", Sapienza University of Rome, Rome Italy.
Matilde Cardoso TrabucoMolirom srl, Rome, Italy.
Alberto BoffiCenter for Life Nano Science @ Sapienza, Istituto Italiano di Tecnologia, Rome, Italy.
Claudia TestiDepartment of Biochemical Sciences "Alessandro Rossi Fanelli", Sapienza University of Rome, Rome Italy.ORCID 0000-0003-0556-975X
Linda Celeste MontemiglioDepartment of Biochemical Sciences "Alessandro Rossi Fanelli", Sapienza University of Rome, Rome Italy.
Amédée des GeorgesThe City University of New York Advanced Science Research Center, New York, NY.
Irene BenniDepartment of Biochemical Sciences "Alessandro Rossi Fanelli", Sapienza University of Rome, Rome Italy.
Andrea IlariInstitute of Molecular Biology and Pathology, National Research Council, Rome, Italy.
Bartłomiej TaciakFaculty of Veterinary Medicine, Warsaw University of Life Sciences, ul. Nowoursynowska, Warszawa, Poland.
Maciej BiałasekFaculty of Veterinary Medicine, Warsaw University of Life Sciences, ul. Nowoursynowska, Warszawa, Poland.
Tomasz RygielCellis Ltd., Warsaw, Poland.
Magdalena KrólFaculty of Veterinary Medicine, Warsaw University of Life Sciences, ul. Nowoursynowska, Warszawa, Poland.
Paola BaioccoCenter for Life Nano Science @ Sapienza, Istituto Italiano di Tecnologia, Rome, Italy.ORCID 0000-0002-1084-5694
Alessandra BonamoreDepartment of Biochemical Sciences "Alessandro Rossi Fanelli", Sapienza University of Rome, Rome Italy.
Sapienza University of Rome · ITWarsaw University of Life Sciences · PLInstitute of Molecular Biology and Pathology · ITItalian Institute of Technology · ITMedical University of Warsaw · PLThe Graduate Center, CUNY · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ferritin H-homopolymers have been extensively used as nanocarriers for diverse applications in the targeted delivery of drugs and imaging agents, due to their unique ability to bind the transferrin receptor (CD71), highly overexpressed in most tumor cells. In order to incorporate novel fluorescence imaging properties, we have fused a lanthanide binding tag (LBT) to the C-terminal end of mouse H-chain ferritin, HFt. The HFt-LBT possesses one high affinity Terbium binding site per each of the 24 subunits provided by six coordinating aminoacid side chains and a tryptophan residue in its close proximity and is thus endowed with strong FRET sensitization properties. Accordingly, the characteristic Terbium emission band at 544 nm for the HFt-LBT Tb(III) complex was detectable upon excitation of the tag enclosed at two order of magnitude higher intensity with respect to the wtHFt protein. X-ray data at 2.9 Å and cryo-EM at 7 Å resolution demonstrated that HFt-LBT is correctly assembled as a 24-mer both in crystal and in solution. On the basis of the intrinsic Tb(III) binding properties of the wt protein, 32 additional Tb(III) binding sites, located within the natural iron binding sites of the protein, were identified besides the 24 Tb(III) ions coordinated to the LBTs. HFt-LBT Tb(III) was demonstrated to be actively uptaken by selected tumor cell lines by confocal microscopy and FACS analysis of their FITC derivatives, although direct fluorescence from Terbium emission could not be singled out with conventional, 295-375 nm, fluorescence excitation.

Indexed as

AnimalsApoferritinsBinding SitesCell Line, TumorEscherichia coliHumansLanthanoid Series ElementsMiceNeoplasmsProtein BindingProtein EngineeringApoferritinsLanthanoid Series Elements

Identifiers

PMID30102720
PMCPMC6089422
OpenAlexW2885976012

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.