Evidence map›Paper›PMID 23815081›Full record

ArticleJournal of the American Chemical Society2013

Controlling self-assembly of a peptide-based material via metal-ion induced registry shift.

Paolo Anzini, Chunfu Xu, Spencer Hughes, Elizabeth Magnotti, Tao Jiang, Lars Hemmingsen, Borries Demeler, Vincent P Conticello

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2013. 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
–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

10 citing papers in PubMed.

  1. Article
  2. Protein Assembly by Design.Chemical reviews · 2021
    Review
  3. Article
  4. Peptide Tectonics: Encoded Structural Complementarity Dictates Programmable Self-Assembly.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2019
    Review
  5. Article
  6. Article
  7. Article
  8. pH responsiveness of fibrous assemblies of repeat-sequence amphipathic α-helix polypeptides.Protein science : a publication of the Protein Society · 2015
    Article
  9. Review
  10. Review
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

8 authors.

Paolo AnziniDepartment of Chemistry, Emory University, Atlanta, Georgia 30322, United States.
Chunfu Xu
Spencer Hughes
Elizabeth Magnotti
Tao Jiang
Lars Hemmingsen
Borries Demeler
Vincent P Conticello

Funding

UltraScan Software Maintenance and DevelopmentR01RR022200 · NCRR · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI DEMELER, BORRIES · 2007 to 2010
$1.7M
NCRR NIH HHS R01 RR022200NCRR NIH HHS RR022200
6 · The paper itself

Abstract

Peptide TZ1C2 can populate two distinct orientations: a staggered (out-of-register) fibril and an aligned (in-register) coiled-coil trimer. The coordination of two cadmium ions induces a registry shift that results in a reversible transition between these structural forms. This process recapitulates the self-assembly mechanism of native protein fibrils in which a ligand binding event gates a reversible conformational transition between alternate forms of a folded peptide structure.

Indexed as

CadmiumIonsParticle SizePeptidesSurface PropertiesCadmiumIonsPeptides

Identifiers

PMID23815081
PMCPMC3786573

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.