Evidence map›Paper›PMID 21322478›Full record

ArticleFaraday discussions2011

Relating dynamic protein interactions of metallochaperones with metal transfer at the single-molecule level.

Jaime J Benítez, Aaron M Keller, David L Huffman, Liliya A Yatsunyk, Amy C Rosenzweig, Peng Chen

Abstract read
In one paragraph

Article in Faraday discussions, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

10 citing papers in PubMed, 24 citations in OpenAlex.

  1. A primer on copper biology in the brain.Neurobiology of disease · 2025
    Review
  2. Breakdown of Langmuir Adsorption Isotherm in Small Closed Systems.Langmuir : the ACS journal of surfaces and colloids · 2024
    Article
  3. Review
  4. Article
  5. Article
  6. The six metal binding domains in human copper transporter, ATP7B: molecular biophysics and disease-causing mutations.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2017
    Review
  7. Histidine residues are important for preserving the structure and heme binding to the C. elegans HRG-3 heme-trafficking protein.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2015
    Article
  8. Review
  9. Synthetic fluorescent probes for monovalent copper.Current opinion in chemical biology · 2013
    Review
  10. 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

6 authors at 3 institutions in 1 country.

Jaime J BenítezDepartment of Chemistry and Chemical Biology, Cornell University, Ithaca, New York 14853, USA.
Aaron M Keller
David L Huffman
Liliya A Yatsunyk
Amy C Rosenzweig
Peng Chen
Cornell University · USNorthwestern University · USWestern Michigan University · US

Funding

Structure and Specificity in Metal Ion HomeostasisR01GM058518 · NIGMS · NORTHWESTERN UNIVERSITY · PI ROSENZWEIG, AMY C. · 1999 to 2015
$4.4M
Single-Molecule Study of Dynamics and Mechanisms of Biomacromolecule InteractionsR01GM082939 · NIGMS · CORNELL UNIVERSITY · PI CHEN, PENG · 2008 to 2012
$1.3M
NIGMS NIH HHS GM082939NIGMS NIH HHS R01 GM058518NIGMS NIH HHS R01 GM082939
6 · The paper itself

Abstract

Metallochaperones undertake specific interactions with their target proteins to deliver metal ions inside cells. Understanding how these protein interactions are coupled with the underlying metal transfer process is important, but challenging because they are weak and dynamic. Here we use a nanovesicle trapping scheme to enable single-molecule FRET measurements of the weak, dynamic interactions between the copper chaperone Hahl and the fourth metal binding domain (MBD4) of WDP. By monitoring the behaviors of single interacting pairs, we visualize their interactions in real time in both the absence and the presence of various equivalents of Cu(1+). Regardless of the proteins' metallation state, we observe multiple, interconverting interaction complexes between Hah1 and MBD4. Within our experimental limit, the overall interaction geometries of these complexes appear invariable, but their stabilities are dependent on the proteins' metallation state. In apo-holo Hah1-MBD4 interactions, the complexes are stabilized relative to that observed in the apo-apo interactions. This stabilization is indiscernible when Hah1's Cu(1+)-binding is eliminated or when both proteins have Cu(1+) loaded. The nature of this Cu(1+)-induced complex stabilization and of the interaction complexes are discussed. These Cu(1+)-induced effects on the Hah1-MBD4 interactions provide a step toward understanding how the dynamic protein interactions of copper chaperones are coupled with their metal transfer function.

Indexed as

CopperFluorescence Resonance Energy TransferMagnetic Resonance SpectroscopyMetallochaperonesCopperMetallochaperones

Identifiers

PMID21322478
PMCPMC3059128
OpenAlexW2045366741

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.