Evidence map›Paper›PMID 32123337›Full record

ArticleNature chemistry2020

Heteromeric three-stranded coiled coils designed using a Pb(II)(Cys)

Audrey E Tolbert, Catherine S Ervin, Leela Ruckthong, Thomas J Paul, Vindi M Jayasinghe-Arachchige, Kosh P Neupane, Jeanne A Stuckey, Rajeev Prabhakar, Vincent L Pecoraro

Abstract read
In one paragraph

Article in Nature chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing 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

14 citing papers in PubMed.

  1. Article
  2. Chemical science · 2025
    Article
  3. Review
  4. Article
  5. Article
  6. Review
  7. Catalysis and Electron Transfer inChemical reviews · 2022
    Review
  8. De novo metalloprotein design.Nature reviews. Chemistry · 2022
    Article
  9. Protein Assembly by Design.Chemical reviews · 2021
    Review
  10. Article
  11. Article
  12. Article
  13. Synergistic Interactions Are Prevalent in Catalytic Amyloids.Chembiochem : a European journal of chemical biology · 2020
    Article
  14. Catalysis and Electron Transfer in De Novo Designed Helical Scaffolds.Angewandte Chemie (International ed. in English) · 2020
    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

9 authors.

Audrey E Tolbert *Department of Chemistry, University of Michigan, Ann Arbor, MI, USA.ORCID http://orcid.org/0000-0003-0936-8568
Catherine S Ervin *Department of Chemistry, University of Michigan, Ann Arbor, MI, USA.
Leela RuckthongDepartment of Chemistry, Faculty of Science, King Mongkut's University of Technology, Thonburi (KMUTT), Bangkok, Thailand.
Thomas J PaulDepartment of Chemistry, University of Miami, Coral Gables, FL, USA.
Vindi M Jayasinghe-ArachchigeDepartment of Chemistry, University of Miami, Coral Gables, FL, USA.
Kosh P NeupaneDepartment of Chemistry, University of Michigan, Ann Arbor, MI, USA.
Jeanne A StuckeyLife Sciences Institute, University of Michigan, Ann Arbor, MI, USA.
Rajeev PrabhakarDepartment of Chemistry, University of Miami, Coral Gables, FL, USA.ORCID http://orcid.org/0000-0003-1137-1272
Vincent L PecoraroDepartment of Chemistry, University of Michigan, Ann Arbor, MI, USA. vlpec@umich.edu.ORCID http://orcid.org/0000-0002-1540-5735

Funding

Toxic Metal Complexation By de Novo Designed PeptidesR01ES012236 · NIEHS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI PECORARO, VINCENT L · 2003 to 2018
$4.4M
NIEHS NIH HHS R01 ES012236
6 · The paper itself

Abstract

Three-stranded coiled coils are peptide structures constructed from amphipathic heptad repeats. Here we show that it is possible to form pure heterotrimeric three-stranded coiled coils by combining three distinct characteristics: (1) a cysteine sulfur layer for metal coordination, (2) a thiophilic, trigonal pyramidal metalloid (Pb(II)) that binds to these sulfurs and (3) an adjacent layer of reduced steric bulk generating a cavity where water can hydrogen bond to the cysteine sulfur atoms. Cysteine substitution in an a site yields Pb(II)A

Indexed as

Coordination ComplexesCysteineHydrogen BondingLeadPeptidesProtein Conformation, alpha-HelicalProtein MultimerizationProtein Structure, QuaternaryWaterCoordination ComplexesCysteineLeadPeptidesWater

Identifiers

PMID32123337
PMCPMC7169047

What OpenQuestion holds

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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.