Evidence map›Paper›PMID 32706257›Full record

ArticleThe journal of physical chemistry letters2020

A Different hIAPP Polymorph Is Observed in Human Serum Than in Aqueous Buffer: Demonstration of a New Method for Studying Amyloid Fibril Structure Using Infrared Spectroscopy.

Caitlyn R Fields, Sidney S Dicke, Megan K Petti, Martin T Zanni, Justin P Lomont

Open access · greenAbstract read
In one paragraph

Article in The journal of physical chemistry letters, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

9 citing papers in PubMed, 17 citations in OpenAlex.

  1. Review
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  8. Protein Dynamics by Two-Dimensional Infrared Spectroscopy.Annual review of analytical chemistry (Palo Alto, Calif.) · 2021
    Article
  9. 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

5 authors at 1 institution in 1 country.

Caitlyn R FieldsDepartment of Chemistry, University of Wisconsin-Madison, Madison, Wisconsin 53706, United States.ORCID http://orcid.org/0000-0003-0565-0646
Sidney S DickeDepartment of Chemistry, University of Wisconsin-Madison, Madison, Wisconsin 53706, United States.
Megan K PettiDepartment of Chemistry, University of Wisconsin-Madison, Madison, Wisconsin 53706, United States.ORCID http://orcid.org/0000-0001-7381-9701
Martin T ZanniDepartment of Chemistry, University of Wisconsin-Madison, Madison, Wisconsin 53706, United States.ORCID http://orcid.org/0000-0001-7191-9768
Justin P LomontDepartment of Chemistry, University of Wisconsin-Madison, Madison, Wisconsin 53706, United States.ORCID http://orcid.org/0000-0003-1106-3683
University of Wisconsin–Madison · US

Funding

Structural mechanism of diabetic amyloid formationR01DK079895 · NIDDK · UNIVERSITY OF WISCONSIN-MADISON · PI Martin T Zanni · 2008 to 2026
$7.7M
Examining Amyloid-β Structure During the Progression of Alzheimer’s Disease using an Immuno-2DIR-SensorR21AG061602 · NIA · UNIVERSITY OF WISCONSIN-MADISON · PI ZANNI, MARTIN T · 2019 to 2020
$409k
NIA NIH HHS R21 AG061602NIDDK NIH HHS R01 DK079895
6 · The paper itself

Abstract

There is enormous interest in measuring amyloid fibril structures, but most structural studies measure fibril formation

Indexed as

Amino Acid SequenceAmyloidHumansIsotope LabelingPeptide FragmentsProtein AggregatesProtein ConformationSerumSpectrophotometry, InfraredWaterAmyloidPeptide FragmentsProtein AggregatesWater

Identifiers

PMID32706257
PMCPMC7968077
OpenAlexW3045318217

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.