Evidence map›Paper›PMID 23548073›Full record

ReviewJournal of the American Chemical Society2013

The supramolecular chemistry of β-sheets.

Pin-Nan Cheng, Johnny D Pham, James S Nowick

Abstract readReview
In one paragraph

Review 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 68 papers.

0numbers the graph read from it
0cells of the map it votes in
68citing papers in PubMed
11.1field-weighted citation impact, top 1% 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

68 citing papers in PubMed, 209 citations in OpenAlex.

  1. Article
  2. Article
  3. A Lipocalin and a Hedgehog-related protein are partners in thebioRxiv : the preprint server for biology · 2026
    Article
  4. Water-Mediated Phosphoryl Wires Stabilize Pathological Tau Fibrils.Angewandte Chemie (International ed. in English) · 2026
    Article
  5. Article
  6. Article
  7. Article
  8. β-barrels from short macrocyclic peptides.Chemical communications (Cambridge, England) · 2026
    Article
  9. Article
  10. Article
  11. Article
  12. Kar4 acts as a Ste12 regulator inbioRxiv : the preprint server for biology · 2025
    Article
  13. Article
  14. Hydration (HJournal of the American Chemical Society · 2025
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Unravelling the Complexity of Amyloid Peptide Core Interfaces.Journal of chemical information and modeling · 2024
    Article

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

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

3 authors at 1 institution in 1 country.

Pin-Nan ChengDepartment of Chemistry, University of California, Irvine, Irvine, California 92697-2025, USA.
Johnny D Pham
James S Nowick
University of California, Irvine · US

Funding

Purchase of an Microwave Peptide SynthesizerR01GM097562 · NIGMS · UNIVERSITY OF CALIFORNIA-IRVINE · PI NOWICK, JAMES S · 2012 to 2019
$2.5M
NIGMS NIH HHS 1R01GM097562NIGMS NIH HHS R01 GM097562
6 · The paper itself

Abstract

Interactions among β-sheets occur widely in protein quaternary structure, protein-protein interaction, and protein aggregation and are central in Alzheimer's and other amyloid-related diseases. This Perspective looks at the structural biology of these important yet under-appreciated interactions from a supramolecular chemist's point of view. Common themes in the supramolecular interactions of β-sheets are identified and richly illustrated though examples from proteins, amyloids, and chemical model systems. β-Sheets interact through edge-to-edge hydrogen bonding to form extended layers and through face-to-face hydrophobic or van der Waals interactions to form layered sandwich-like structures. Side chains from adjacent layers can fit together through simple hydrophobic contacts or can participate in complementary interdigitation or knob-hole interactions. The layers can be aligned, offset, or rotated. The right-handed twist of β-sheets provides additional opportunities for stabilization of edge-to-edge contacts and rotated layered structures.

Indexed as

Protein Structure, SecondaryHumansHydrogen BondingProtein FoldingProtein MultimerizationProteinsProteins

Identifiers

PMID23548073
PMCPMC3642101
OpenAlexW2050868331

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.