Evidence map›Paper›PMID 23183585›Full record

ReviewAdvanced drug delivery reviews2013

Structure and dynamics of drug carriers and their interaction with cellular receptors: focus on serum transferrin.

Ashley N Luck, Anne B Mason

Abstract readReview
In one paragraph

Review in Advanced drug delivery reviews, 2013. 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
1.7field-weighted citation impact, top 16% 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, 41 citations in OpenAlex.

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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

2 authors at 1 institution in 1 country.

Ashley N LuckDepartment of Biochemistry, University of Vermont, College of Medicine, 89 Beaumont Avenue, Burlington, VT 05405, USA.
Anne B Mason
University of Vermont · US

Funding

Iron Delivery via Blood; Structure Role of TransferrinR01DK021739 · NIDDK · UNIVERSITY OF VERMONT &ST AGRIC COLLEGE · PI MASON, ANNE B. · 1987 to 2011
$3.4M
NIDDK NIH HHS R01 DK021739NIDDK NIH HHS R01 DK21739
6 · The paper itself

Abstract

Highly proliferative cells have a dramatically increased need for iron which results in the expression of an increased number of transferrin receptors (TFR). This insight makes the transferrin receptor on these cells an excellent candidate for targeted therapeutics. In this regard, it is critical to understand at a molecular level exactly how the TFR interacts with its ligand, hTF. Understanding of the hTF/TFR pathway could, in theory, maximize the use of this system for development of more effective small molecules or toxin-conjugates to specifically target cancer cells. Many strategies have been attempted with the objective of utilizing the hTF/TFR system to deliver drugs; these include conjugation of a toxin or drug to hTF or direct targeting of the TFR by antibodies. To date, in spite of all of the effort, there is a conspicuous absence of any successful candidate drugs reaching the clinic. We suggest that a lack of quantitative data to determine the basic biochemical properties of the drug carrier and the effects of drug-conjugation on the hTF-TFR interaction may have contributed to the failure to realize the full potential of this system. This review provides some guidelines for developing a more quantitative approach for evaluation of current and future hTF-drug conjugates.

Indexed as

AnimalsAntineoplastic AgentsDrug CarriersHumansReceptors, TransferrinTransferrinAntineoplastic AgentsDrug CarriersReceptors, TransferrinTransferrinapoTFBBBblood brain barrierChemotherapyelectron microscopyEMFe(2)hTFFe(C)hTFFe(N)hTFglycosylated N-terminal hexa-His tagged soluble recombinant transferrin receptor (residues 121–760)HFEhTFhuman serum transferrinisothermal titration calorimetryITCrecombinant N-terminal hexa-His tagged non-glycosylated diferric hTFrecombinant N-terminal hexa-His tagged non-glycosylated monoferric hTF that binds iron only in the C-loberecombinant N-terminal hexa-His tagged non-glycosylated monoferric hTF that binds iron only in the N-lobescFvserum transferrin that is iron freesingle chain antibody variable regionSPRsTFRsurface plasmon resonanceTFRthe hemochromatosis proteinTransferrintransferrin receptorTransferrin receptorTrojan horse

Identifiers

PMID23183585
PMCPMC3602139
OpenAlexW1979565147

What OpenQuestion holds

Textmetadata
LicenceTDM
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.