Evidence map›Paper›PMID 20404192›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2010

Noncanonical interactions between serum transferrin and transferrin receptor evaluated with electrospray ionization mass spectrometry.

Rachael Leverence, Anne B Mason, Igor A Kaltashov

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

28 citing papers in PubMed, 46 citations in OpenAlex.

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  14. Mass spectrometry-based methods to study protein architecture and dynamics.Protein science : a publication of the Protein Society · 2013
    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

3 authors at 2 institutions in 1 country.

Rachael LeverenceChemistry Department, University of Massachusetts, Amherst, MA 01003, USA.
Anne B Mason
Igor A Kaltashov
University of Massachusetts Amherst · USUniversity 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
PROTEIN FOLDING DYNAMICS BY MASS SPECTROMETRYR01GM061666 · NIGMS · UNIVERSITY OF MASSACHUSETTS AMHERST · PI KALTASHOV, IGOR A · 2000 to 2013
$3.4M
NIDDK NIH HHS R01 DK021739NIDDK NIH HHS R01 DK 21739NIGMS NIH HHS R01 GM061666
6 · The paper itself

Abstract

The primary route of iron acquisition in vertebrates is the transferrin receptor (TfR) mediated endocytotic pathway, which provides cellular entry to the metal transporter serum transferrin (Tf). Despite extensive research efforts, complete understanding of Tf-TfR interaction mechanism is still lacking owing to the complexity of this system. Electrospray ionization mass spectrometry (ESI MS) is used in this study to monitor the protein/receptor interaction and demonstrate the ability of metal-free Tf to associate with TfR at neutral pH. A set of Tf variants is used in a series of competition and displacement experiments to bracket TfR affinity of apo-Tf at neutral pH (0.2-0.6 microM). Consistent with current models of endosomal iron release from Tf, acidification of the protein solution results in a dramatic change of binding preferences, with apo-Tf becoming a preferred receptor binder. Contrary to the current models implying that the apo-Tf/TfR complex dissociates almost immediately upon exposure to the neutral environment at the cell surface, our data indicate that this complex remains intact. Iron-loaded Tf displaces apo-Tf from TfR, making it available for the next cycle of iron binding, transport and delivery to tissues. However, apo-Tf may still interfere with the cellular uptake of engineered Tf molecules whose TfR affinity is affected by various modifications (e.g., conjugation to cytotoxic molecules). This work also highlights the great potential of ESI MS as a tool capable of providing precise details of complex protein-receptor interactions under conditions that closely mimic the environment in which these encounters occur in physiological systems.

Indexed as

HumansHydrogen-Ion ConcentrationIronProtein BindingReceptors, TransferrinSpectrometry, Mass, Electrospray IonizationTransferrinIronReceptors, TransferrinTransferrin

Identifiers

PMID20404192
PMCPMC2889525
OpenAlexW2092055155

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.