Evidence map›Paper›PMID 29971927›Full record

ArticleAngewandte Chemie (International ed. in English)2018

Selection of Secondary Structures of Heterotypic Supramolecular Peptide Assemblies by an Enzymatic Reaction.

Jie Li, Ziqing Zhan, Xuewen Du, Jiaqing Wang, Brandon Hong, Bing Xu

Abstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing 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

15 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Assemblies of Peptides in a Complex Environment and their Applications.Angewandte Chemie (International ed. in English) · 2019
    Review
  14. Article
  15. 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.

Jie LiDepartment of Chemistry, Brandeis University, 415 South Street, Waltham, MA, 02454, USA.
Ziqing ZhanDepartment of Chemistry, Brandeis University, 415 South Street, Waltham, MA, 02454, USA.
Xuewen DuDepartment of Chemistry, Brandeis University, 415 South Street, Waltham, MA, 02454, USA.
Jiaqing WangDepartment of Chemistry, Brandeis University, 415 South Street, Waltham, MA, 02454, USA.
Brandon HongDepartment of Chemistry, Brandeis University, 415 South Street, Waltham, MA, 02454, USA.
Bing XuDepartment of Chemistry, Brandeis University, 415 South Street, Waltham, MA, 02454, USA.ORCID 0000-0002-4639-387X

Funding

Subcellular Enzyme-instructed self-assembly for molecular anticancer nanomedicinesR01CA142746 · NCI · BRANDEIS UNIVERSITY · PI Bing Xu · 2010 to 2026
$6.4M
Enzyme-instructed nanoscale assemblies for killing multidrug resistant bacteriaR21AI130560 · NIAID · BRANDEIS UNIVERSITY · PI XU, BING · 2017 to 2018
$447k
NCI NIH HHS R01 CA142746NIAID NIH HHS R21 AI130560
6 · The paper itself

Abstract

In a model study to investigate the consequence of reactions of intrinsically disordered regions (IDRs) of proteins in the context of the formation of highly ordered structures, we found that enzymatic reactions control the secondary structures of peptides during assembly. Specifically, phosphorylation of an α-helix-dominant peptide results in mostly disordered conformations, which become β-strand-dominant after enzymatic dephosphorylation to regenerate the peptide. In the presence of another peptide largely with a β-strand conformation, direct coassembly of the peptides results in amorphous aggregates consisting of α-helix and β-strand peptides, but the enzymatically generated peptide coassemblies (from the phosphopeptide) mainly adopt a β-strand conformation and form ordered structures (e.g., nanofibers). These results indicate that enzymatic dephosphorylation instructs conformationally flexible peptides to adopt thermodynamically favorable conformations in homotypic or heterotypic supramolecular assemblies.

Indexed as

BiocatalysisIntrinsically Disordered ProteinsModels, MolecularNanofibersPeptidesPhosphopeptidesPhosphorylationProtein AggregatesProtein Structure, SecondaryThermodynamicsIntrinsically Disordered ProteinsPeptidesPhosphopeptidesProtein Aggregatesenzymesheterotypic assembliespeptidessecondary structuresupramolecular assemblies

Identifiers

PMID29971927
PMCPMC6400471

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Registered trials

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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.