Evidence map›Paper›PMID 22522257›Full record

ArticleNature chemistry2012

Metal-directed, chemically tunable assembly of one-, two- and three-dimensional crystalline protein arrays.

Jeffrey D Brodin, X I Ambroggio, Chunyan Tang, Kristin N Parent, Timothy S Baker, F Akif Tezcan

Abstract read
In one paragraph

Article in Nature chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 110 papers.

0numbers the graph read from it
0cells of the map it votes in
110citing 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

110 citing papers in PubMed.

  1. Review
  2. Article
  3. Review
  4. Review
  5. Designability of α-Helical Protein Filaments.Sub-cellular biochemistry · 2026
    Review
  6. Review
  7. Article
  8. Article
  9. Assembly and Functionality of 2D Protein Arrays.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Review
  10. Article
  11. Protein Cage Directed Assembly of Binary Nanoparticle Superlattices.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024
    Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review

50 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors.

Jeffrey D BrodinDepartment of Chemistry and Biochemistry, University of California, San Diego, La Jolla, California 92093, USA.
X I Ambroggio
Chunyan Tang
Kristin N Parent
Timothy S Baker
F Akif Tezcan

Funding

VIRUS ASSEMBLY AND TRANSMISSIONP01AI045976 · NIAID · PURDUE UNIVERSITY WEST LAFAYETTE · PI KUHN, RICHARD J. · 1999 to 2008
$8.8M
Microscopy &Image Analysis of Unstained MacromoleculesR37GM033050 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI BAKER, TIMOTHY S · 2004 to 2013
$5.6M
MICROSCOPY &IMAGE ANALYSIS OF UNSTAINED MACROMOLECULESR01GM033050 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI BAKER, TIMOTHY S · 1985 to 2017
$4.3M
TRANSMISSION ELECTRON MICROSCOPE: STRUCTURAL &CELL BIOL: MEMBRANE TRANSPORT, GAS10RR020016 · NCRR · UNIVERSITY OF CALIFORNIA SAN DIEGO · PI BAKER, TIMOTHY S · 2004 to 2004
$2.0M
Electron cryo-microscopy of phage P22F32AI078624 · NIAID · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI PARENT, KRISTIN N · 2009 to 2010
$98k
NCRR NIH HHS 1S10 RR.020016NCRR NIH HHS S10 RR020016NIAID NIH HHS F32 AI078624NIAID NIH HHS P01 AI045976NIGMS NIH HHS R01 GM033050NIGMS NIH HHS R37 GM033050NIGMS NIH HHS R37GM-033050
6 · The paper itself

Abstract

Proteins represent the most sophisticated building blocks available to an organism and to the laboratory chemist. Yet, in contrast to nearly all other types of molecular building blocks, the designed self-assembly of proteins has largely been inaccessible because of the chemical and structural heterogeneity of protein surfaces. To circumvent the challenge of programming extensive non-covalent interactions to control protein self-assembly, we have previously exploited the directionality and strength of metal coordination interactions to guide the formation of closed, homoligomeric protein assemblies. Here, we extend this strategy to the generation of periodic protein arrays. We show that a monomeric protein with properly oriented coordination motifs on its surface can arrange, on metal binding, into one-dimensional nanotubes and two- or three-dimensional crystalline arrays with dimensions that collectively span nearly the entire nano- and micrometre scale. The assembly of these arrays is tuned predictably by external stimuli, such as metal concentration and pH.

Indexed as

CrystallizationHydrogen-Ion ConcentrationMetalsMethodsNanotubesProtein MultimerizationProteinsMetalsProteins

Identifiers

PMID22522257
PMCPMC3335442

What OpenQuestion holds

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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.