Evidence map›Paper›PMID 24560806›Full record

ArticleStructure (London, England : 1993)2014

High-affinity gold nanoparticle pin to label and localize histidine-tagged protein in macromolecular assemblies.

Kelsey C Anthony, Changjiang You, Jacob Piehler, Daniel A Pomeranz Krummel

RetractedAbstract readRetracted Publication
PubMed Full text at PMC Publisher
In one paragraph

Article in Structure (London, England : 1993), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It has been retracted, and should not be counted. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
2.8field-weighted citation impact, top 8% 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

2 citing papers in PubMed, 8 citations in OpenAlex.

  1. Article
  2. Analysing the nanoparticle-protein corona for potential molecular target identification.Journal of controlled release : official journal of the Controlled Release Society · 2020
    Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Kelsey C AnthonyDepartment of Biochemistry, Brandeis University, 415 South Street, Waltham, MA 02454, USA.
Changjiang YouDepartment of Biology, University of Osnabrück, Barbarastraße 11, Osnabrück 49076, Germany.
Jacob PiehlerDepartment of Biology, University of Osnabrück, Barbarastraße 11, Osnabrück 49076, Germany. Electronic address: piehler@uos.de.
Daniel A Pomeranz KrummelDepartment of Biochemistry, Brandeis University, 415 South Street, Waltham, MA 02454, USA. Electronic address: dapk@brandeis.edu.
Brandeis University · US

Funding

Single particle reconstructionP01GM062580 · NIGMS · HARVARD MEDICAL SCHOOL · PI HARRISON, STEPHEN COPLAN · 2001 to 2016
$23.7M
Quantitative Biology: a Graduate Curriculum Linking the Physical and Biomedical ST32EB009419 · NIBIB · BRANDEIS UNIVERSITY · PI GELLES, JEFF, KONDEV, JANE · 2009 to 2018
$2.8M
NIBIB NIH HHS T32 EB009419NIGMS NIH HHS GM62580NIGMS NIH HHS P01 GM062580
6 · The paper itself

Abstract

There is significant demand for experimental approaches to aid protein localization in electron microscopy micrographs and ultimately in three-dimensional reconstructions of macromolecular assemblies. We report preparation and use of a reagent consisting of tris-nitrilotriacetic acid (tris-NTA) conjugated with a monofunctional gold nanoparticle ((AuNP)tris-NTA) for site-specific, non-covalent labeling of protein termini fused to a histidine-tag (His-tag). Multivalent binding of tris-NTA to a His-tag via complexed Ni(II) ions results in subnanomolar affinity and a defined 1:1 stoichiometry. Precise localization of (AuNP)tris-NTA labeled proteins by electron microscopy is further ensured by the reagent's short conformationally restricted linker. We used (AuNP)tris-NTA to localize His-tagged proteins in an oligomeric ATPase and in the bacterial 50S ribosomal subunit. (AuNP)tris-NTA can specifically bind to the target proteins in these assemblies and is clearly discernible. Our labeling reagent should find broad application in noncovalent, site-specific labeling of protein termini to pinpoint their location in macromolecular assemblies.

Indexed as

Adenosine TriphosphatasesBacterial ProteinsEscherichia coliGoldHistidineIndicators and ReagentsMetal NanoparticlesMicroscopy, ElectronNitrilotriacetic AcidRecombinant Fusion ProteinsRibosome Subunits, Large, BacterialStaining and LabelingThermus thermophilusTromethamineAdenosine TriphosphatasesBacterial ProteinsGoldHistidineIndicators and ReagentsNitrilotriacetic AcidRecombinant Fusion ProteinsTromethamine

Identifiers

PMID24560806
PMCPMC3984384
OpenAlexW2123939722

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.