Evidence map›Paper›PMID 29116774›Full record

ArticleJournal of the American Chemical Society2017

Toward a Soluble Model System for the Amyloid State.

Nicole C Thomas, Gail J Bartlett, Derek N Woolfson, Samuel H Gellman

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. 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

4 authors.

Nicole C ThomasDepartment of Chemistry, University of Wisconsin-Madison , Madison, Wisconsin 53706, United States.ORCID 0000-0002-7200-8015
Gail J BartlettSchool of Chemistry, University of Bristol , Cantock's Close, Bristol BS8 1TD, United Kingdom.
Derek N WoolfsonSchool of Chemistry, University of Bristol , Cantock's Close, Bristol BS8 1TD, United Kingdom.ORCID 0000-0002-0394-3202
Samuel H GellmanDepartment of Chemistry, University of Wisconsin-Madison , Madison, Wisconsin 53706, United States.

Funding

INTEGRATED TRAINING FOR PHYSICIAN-SCIENTISTST32GM008692 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI BURKARD, MARK E · 1998 to 2020
$10.3M
Use of designed peptides to study folding and bindingR01GM061238 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI GELLMAN, SAMUEL H. · 2000 to 2023
$7.9M
Laser-Enhanced NMR Instrumentation for Chemical and Biochemical ResearchS10OD012245 · OD · UNIVERSITY OF WISCONSIN-MADISON · PI CAVAGNERO, SILVIA · 2013 to 2013
$1.0M
ACQUISITION OF MASS SPECTROMETER FOR CORE FACILITYS10RR013790 · NCRR · UNIVERSITY OF WISCONSIN MADISON · PI RAINES, RONALD T · 1999 to 1999
–
Biotechnology and Biological Sciences Research Council BB/L01386X/1NIGMS NIH HHS R01 GM061238NIGMS NIH HHS T32 GM008692NIH HHS S10 OD012245NSF BIR-9512577
6 · The paper itself

Abstract

The formation and deposition of amyloids is associated with many diseases. β-Sheet secondary structure is a common feature of amyloids, but the packing of sheets against one another is distinctive relative to soluble proteins. Standard methods that rely on perturbing a polypeptide's sequence and evaluating impact on folding can be problematic for amyloid aggregates because a single sequence can adopt multiple conformations and diverse packing arrangements. We describe initial steps toward a minimum-sized, soluble model system for the amyloid state that supports comparisons among sequence variants. Critical to this goal is development of a new linking strategy to enable intersheet association mediated by side chain interactions, which is characteristic of the amyloid state. The linker design we identified should ultimately support exploration of relationships between sequence and amyloid state stability for specific strand-association modes.

Indexed as

AmyloidModels, MolecularProtein Structure, SecondarySolubilityAmyloid

Identifiers

PMID29116774
PMCPMC5939379

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.