Evidence map›Paper›PMID 36697777›Full record

ArticleCommunications chemistry2021

Protein nanofibril design via manipulation of hydrogen bonds.

Nidhi Aggarwal, Dror Eliaz, Hagai Cohen, Irit Rosenhek-Goldian, Sidney R Cohen, Anna Kozell, Thomas O Mason, Ulyana Shimanovich

Abstract read
In one paragraph

Article in Communications chemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing 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

13 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. One- and Two-Photon Excited Autofluorescence of Lysozyme Amyloids.The journal of physical chemistry letters · 2022
    Article
  12. Article
  13. 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

8 authors.

Nidhi Aggarwal *Department of Molecular Chemistry and Materials Science, Weizmann Institute of Science, Rehovot, Israel.
Dror Eliaz *Department of Molecular Chemistry and Materials Science, Weizmann Institute of Science, Rehovot, Israel.
Hagai CohenDepartment of Chemical Research Support, Weizmann Institute of Science, Rehovot, Israel.
Irit Rosenhek-GoldianDepartment of Chemical Research Support, Weizmann Institute of Science, Rehovot, Israel.
Sidney R CohenDepartment of Chemical Research Support, Weizmann Institute of Science, Rehovot, Israel.ORCID http://orcid.org/0000-0003-4255-3351
Anna KozellDepartment of Molecular Chemistry and Materials Science, Weizmann Institute of Science, Rehovot, Israel.
Thomas O MasonDepartment of Molecular Chemistry and Materials Science, Weizmann Institute of Science, Rehovot, Israel.
Ulyana ShimanovichDepartment of Molecular Chemistry and Materials Science, Weizmann Institute of Science, Rehovot, Israel. ulyana.shimanovich@weizmann.ac.il.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The process of amyloid nanofibril formation has broad implications including the generation of the strongest natural materials, namely silk fibers, and their major contribution to the progression of many degenerative diseases. The key question that remains unanswered is whether the amyloidogenic nature, which includes the characteristic H-bonded β-sheet structure and physical characteristics of protein assemblies, can be modified via controlled intervention of the molecular interactions. Here we show that tailored changes in molecular interactions, specifically in the H-bonded network, do not affect the nature of amyloidogenic fibrillation, and even have minimal effect on the initial nucleation events of self-assembly. However, they do trigger changes in networks at a higher hierarchical level, namely enhanced 2D packaging which is rationalized by the 3D hierarchy of β-sheet assembly, leading to variations in fibril morphology, structural composition and, remarkably, nanomechanical properties. These results pave the way to a better understanding of the role of molecular interactions in sculpting the structural and physical properties of protein supramolecular constructs.

Identifiers

PMID36697777
PMCPMC9814780

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.