Evidence map›Paper›PMID 34365921›Full record

ArticleProtein and peptide letters2021

Nonhuman IAPP Variants Inhibit Human IAPP Aggregation.

Alissa Oakes, Kate Menefee, Arleen Lamba, Larry M Palato, Dillon J Rinauro, Angela Tun, Betssy Jauregui, Kevin Chang, Luiza A Nogaj, David A Moffet

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Protein and peptide letters, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.1field-weighted citation impact, top 53% 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

1 citing paper in PubMed, 2 citations in OpenAlex.

  1. 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

10 authors at 2 institutions in 1 country.

Alissa OakesDepartment of Biology, Mount Saint Mary's University, Los Angeles, CA 90049, United States.
Kate MenefeeDepartment of Chemistry and Biochemistry, Loyola Marymount University, Los Angeles, CA 90045, United States.
Arleen LambaDepartment of Biology, Mount Saint Mary's University, Los Angeles, CA 90049, United States.
Larry M PalatoDepartment of Chemistry and Biochemistry, Loyola Marymount University, Los Angeles, CA 90045, United States.
Dillon J RinauroDepartment of Chemistry and Biochemistry, Loyola Marymount University, Los Angeles, CA 90045, United States.
Angela TunDepartment of Chemistry and Biochemistry, Loyola Marymount University, Los Angeles, CA 90045, United States.
Betssy JaureguiDepartment of Chemistry and Biochemistry, Loyola Marymount University, Los Angeles, CA 90045, United States.
Kevin ChangDepartment of Chemistry and Biochemistry, Loyola Marymount University, Los Angeles, CA 90045, United States.
Luiza A NogajDepartment of Biology, Mount Saint Mary's University, Los Angeles, CA 90049, United States.
David A MoffetDepartment of Chemistry and Biochemistry, Loyola Marymount University, Los Angeles, CA 90045, United States.
Loyola Marymount University · USMount St. Mary's University · US

Funding

Optimizing Peptide Inhibitors of Human Iapp Amyloidogenicity and Identifying their Effects on the Unfolded Protein Response SystemR15DK112172 · NIDDK · LOYOLA MARYMOUNT UNIVERSITY · PI MOFFET, DAVID AARON, NOGAJ, LUIZA ANNA · 2016 to 2019
$800k
National Institutes of Health, USA 1R15DK112172-02NIDDK NIH HHS R15 DK112172
6 · The paper itself

Abstract

aimTo identify naturally occurring variants of IAPP capable of inhibiting the aggregation of human IAPP and protecting living cells from the toxic effects of human IAPP.

backgroundThe loss of insulin-producing β-cells and the overall progression of type 2 diabetes appears to be linked to the formation of toxic human IAPP (hIAPP, Islet Amyloid Polypeptide, amylin) amyloid in the pancreas. Inhibiting the initial aggregation of hIAPP has the potential to slow, if not stop entirely, the loss of β-cells and halt the progression of the disease.

objectiveTo identify and characterize naturally occurring variants of IAPP capable of inhibiting human IAPP aggregation.

methodsSynthetic human IAPP was incubated with synthetic IAPP variants identified from natural sources under conditions known to promote amyloid-based aggregation. To identify IAPP variants capable of inhibiting human IAPP aggregation, Thioflavin T-binding fluorescence, atomic force microscopy, and cell-rescue assays were performed.

resultsWhile most IAPP variants showed little to no ability to inhibit human IAPP aggregation, several variants showed some ability to inhibit aggregation, with two variants showing substantial inhibitory potential.

conclusionSeveral naturally occurring IAPP variants capable of inhibiting human IAPP aggregation were identified and characterized.

Indexed as

Protein AggregatesAnimalsHumansIslet Amyloid PolypeptideSpecies SpecificityIslet Amyloid PolypeptideProtein AggregatesamylinamyloidIslet amyloid polypeptidepancreas.protein aggregationtype 2 diabetes

Identifiers

PMID34365921
PMCPMC10712300
OpenAlexW3192492277

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.