Evidence map›Paper›PMID 26840340›Full record

ArticlePloS one2016

Identification of Human Islet Amyloid Polypeptide as a BACE2 Substrate.

Ingrid C Rulifson, Ping Cao, Li Miao, David Kopecky, Linda Huang, Ryan D White, Kim Samayoa, Jonitha Gardner, Xiaosu Wu, Kui Chen and 7 more

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

20 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
  2. The human endogenous retroviral envelope HEMO protein interacts with BACE2: Novel partnership acquired in the primate lineage.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
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  9. The emerging role of β-secretases in cancer.Journal of experimental & clinical cancer research : CR · 2021
    Review
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  11. Article
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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

17 authors at 1 institution in 1 country.

Ingrid C RulifsonAmgen, Cardiometabolic Disorders, South San Francisco, California, United States of America.
Ping CaoAmgen, Molecular Structure and Characterization, South San Francisco, California, United States of America.
Li MiaoAmgen, Cardiometabolic Disorders, South San Francisco, California, United States of America.
David KopeckyAmgen, Medicinal Chemistry, Thousand Oaks, California, United States of America.
Linda HuangAmgen, Molecular Structure and Characterization, South San Francisco, California, United States of America.
Ryan D WhiteAmgen, Medicinal Chemistry, Cambridge, Massachusetts, United States of America.
Kim SamayoaAmgen, Pathology, South San Francisco, California, United States of America.
Jonitha GardnerAmgen, Cardiometabolic Disorders, South San Francisco, California, United States of America.
Xiaosu WuAmgen, Cardiometabolic Disorders, South San Francisco, California, United States of America.
Kui ChenAmgen, Discovery Technologies, Thousand Oaks, California, United States of America.
Trace TsurudaAmgen, Biologics, Thousand Oaks, California, United States of America.
Oliver HomannAmgen, Genome Analysis Unit, South San Francisco, California, United States of America.
Helene BaribaultAmgen, Cardiometabolic Disorders, South San Francisco, California, United States of America.
Harvey YamaneAmgen, Biologics, Thousand Oaks, California, United States of America.
Tim CarlsonAmgen, Pharmacokinetics and Drug Metabolism, South San Francisco, California, United States of America.
Jed WiltziusAmgen, Genome Analysis Unit, South San Francisco, California, United States of America.
Yang LiAmgen, Cardiometabolic Disorders, South San Francisco, California, United States of America.
Amgen (United States) · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Pancreatic amyloid formation by islet amyloid polypeptide (IAPP) is a hallmark pathological feature of type 2 diabetes. IAPP is stored in the secretory granules of pancreatic beta-cells and co-secreted with insulin to maintain glucose homeostasis. IAPP is innocuous under homeostatic conditions but imbalances in production or processing of IAPP may result in homodimer formation leading to the rapid production of cytotoxic oligomers and amyloid fibrils. The consequence is beta-cell dysfunction and the accumulation of proteinaceous plaques in and around pancreatic islets. Beta-site APP-cleaving enzyme 2, BACE2, is an aspartyl protease commonly associated with BACE1, a related homolog responsible for amyloid processing in the brain and strongly implicated in Alzheimer's disease. Herein, we identify two distinct sites of the mature human IAPP sequence that are susceptible to BACE2-mediated proteolytic activity. The result of proteolysis is modulation of human IAPP fibrillation and human IAPP protein degradation. These results suggest a potential therapeutic role for BACE2 in type 2 diabetes-associated hyperamylinaemia.

Indexed as

Amino Acid SequenceAmyloid Precursor Protein SecretasesAnimalsAspartic Acid EndopeptidasesCell LineDiabetes Mellitus, Type 2HumansInsulinInsulin-Secreting CellsIslet Amyloid PolypeptideMass SpectrometryMiceMolecular Sequence DataMutationPlaque, AmyloidProteolysisAmyloid Precursor Protein SecretasesAspartic Acid EndopeptidasesBACE1 protein, humanBACE2 protein, humanInsulinIslet Amyloid PolypeptideRecombinant Proteins

Identifiers

PMID26840340
PMCPMC4739698
OpenAlexW2270495172

What Socratic 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 Socratic graph.