Evidence map›Paper›PMID 32497515›Full record

ArticleBiophysical journal2020

Toxic and Physiological Metal Uptake and Release by Human Serum Transferrin.

David J Reilley, Jack T Fuller, Michael R Nechay, Marie Victor, Wei Li, Josiah D Ruberry, Jon I Mujika, Xabier Lopez, Anastassia N Alexandrova

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Biophysical journal, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
–field-weighted citation impact
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

3 citing papers in PubMed.

  1. Many-Body Study of Iron(III)-Bound Human Serum Transferrin.The journal of physical chemistry letters · 2022
    Article
  2. Article
  3. 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

9 authors.

David J ReilleyDepartment of Chemistry and Biochemistry, University of California, Los Angeles, Los Angeles, California.
Jack T FullerDepartment of Chemistry and Biochemistry, University of California, Los Angeles, Los Angeles, California.
Michael R NechayDepartment of Chemistry and Biochemistry, University of California, Los Angeles, Los Angeles, California.
Marie VictorDepartment of Chemistry and Biochemistry, University of California, Los Angeles, Los Angeles, California; Institut Lumire Matire, Villeurbanne, France.
Wei LiDepartment of Chemistry and Biochemistry, University of California, Los Angeles, Los Angeles, California; Department of Chemistry and Chemical Biology, Harvard University, Cambridge, Massachusetts.
Josiah D RuberryDepartment of Chemistry and Biochemistry, University of California, Los Angeles, Los Angeles, California.
Jon I MujikaKimika Fakultatea, Euskal Herriko Unibertsitatea (UPV/EHU) and Donostia, International Physics Center, Donostia, Euskadi, Spain.
Xabier LopezKimika Fakultatea, Euskal Herriko Unibertsitatea (UPV/EHU) and Donostia, International Physics Center, Donostia, Euskadi, Spain.
Anastassia N AlexandrovaDepartment of Chemistry and Biochemistry, University of California, Los Angeles, Los Angeles, California; California NanoSystems Institute, University of California, Los Angeles, Los Angeles, California. Electronic address: ana@chem.ucla.edu.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

An atomistic understanding of metal transport in the human body is critical to anticipate the side effects of metal-based therapeutics and holds promise for new drugs and drug delivery designs. Human serum transferrin (hTF) is a central part of the transport processes because of its ubiquitous ferrying of physiological Fe(III) and other transition metals to tightly controlled parts of the body. There is an atomistic mechanism for the uptake process with Fe(III), but not for the release process, or for other metals. This study provides initial insight into these processes for a range of transition metals-Ti(IV), Co(III), Fe(III), Ga(III), Cr(III), Fe(II), Zn(II)-through fully atomistic, extensive quantum mechanical/discrete molecular dynamics sampling and provides, to our knowledge, a new technique we developed to calculate relative binding affinities between metal cations and the protein. It identifies protonation of Tyr188 as a trigger for metal release rather than protonation of Lys206 or Lys296. The study identifies the difficulty of metal release from hTF as potentially related to cytotoxicity. Simulations identify a few critical interactions that stabilize the metal binding site in a flexible, nuanced manner.

Indexed as

Ferric CompoundsTransferrinBiological TransportHumansMetalsMolecular Dynamics SimulationFerric CompoundsMetalsTransferrin

Identifiers

PMID32497515
PMCPMC7300305

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.