GLP-1 Receptor Agonists

Amylin: indexed trial records

Records checked

Compiled and citation-checked by GLP-1 Receptor Agonists editorial desk

Qualified clinical review None on record

Withheld from the index. This page sets out the indexed clinical-record picture for Amylin.

Every compound in scope is marked high impact and none has a qualified clinical reviewer recorded, so this page is built, checked and served with a noindex directive and left out of the sitemap. Nothing on it has been removed or softened. Recording a named reviewer publishes it unchanged on the next build. How the gate works.

This page carries 12 of the 3,167 records the literature query returned for Amylin, selected by citation count and preferring records that name the compound in their title. It is a selection, not a complete index.

Every row below resolves to a real identifier and names the study model the indexer assigned. The record class is read from the publication type on the record itself. Nothing here states what a record found.

At a glance

Class
Amylin and amylin receptor agonists
Receptor targets as recorded
Amylin receptor, Calcitonin receptor
Records indexed here
12
Records returned by the query
3,167
Publication years covered
2006–2017
Query retrieved
2026-10-12

Shape of the indexed record set

Record classRecords
Review or synthesis5
Not a registered trial record7
Study model as assignedRecords
other10
rodent2

Study model is the indexer’s own assignment, taken from the MeSH population headings and the publication type. It is not a judgement about how well a record was conducted.

Endpoint coverage

EndpointRecords for this compoundRecords across all compounds in scope
Body weight and adiposity3108
Glycaemic control9117
Cardiovascular130
Renal010
Hepatic09
Neurological418

1 of the 12 records here carry no subject heading from any endpoint set used on this site, so they appear under no endpoint.

Derived record-set tier

Animal and in vitro only (INFERRED, derived from record counts)
Basis: no interventional human trial record; 2 rodent and 0 in vitro records among 12.
This label counts record types. It is not an assessment of clinical efficacy, of safety, of study quality or of consensus, and it does not rank one compound above another.

What the corpus does not carry for this compound

  • Identity fields with no source retrieved: uniprot_id, sequence.
  • Reported half-life: no source retrieved, so the value reads Unknown.
  • Amounts reported in the cited literature: no row recorded.
  • Adverse effects reported in the cited literature: no row recorded.
  • Long-form mechanism: not written, because no source was read in full.
  • Records the query returned that this corpus does not carry: 3,155.

An absent row records the absence of a retrieved report, never the absence of the thing itself.

Application register

A query of the FDA Drugs@FDA application register on 2026-10-09 returned no application records for this compound name. This compound is not approved by the FDA for human use.[2]

Scope statement: this records the result of a single automated query against the openFDA drugsfda endpoint on the stated date. It is not legal advice and is not a jurisdiction-by-jurisdiction legality assessment.

The records

Review or synthesis — 5 records

No.IdentifierYearRecordModelSubject headings
1pmid:282697852017The Link between Type 2 Diabetes and Neurodegeneration: Roles for Amyloid-β, Amylin, and Tau Proteins
Journal of Alzheimer's disease : JAD · Review
otherBrain; Animals; Humans; Neurodegenerative Diseases; Diabetes Mellitus, Type 2; tau Proteins; Amyloid beta-Peptides; Islet Amyloid Polypeptide
2pmid:266493192016Islet Amyloid Polypeptide: Structure, Function, and Pathophysiology
Journal of diabetes research · research-article, Review
otherIslets of Langerhans; Humans; Diabetes Mellitus, Type 2; Structure-Activity Relationship; Insulin-Secreting Cells; Islet Amyloid Polypeptide
3pmid:260710952015Amylin: Pharmacology, Physiology, and Clinical Potential
Pharmacological reviews · Research Support, Non-U.S. Gov't, Review
otherAnimals; Humans; Diabetes Mellitus, Type 1; Diabetes Mellitus, Type 2; Weight Loss; Hypoglycemic Agents; Energy Metabolism; Islet Amyloid Polypeptide
5pmid:217427882011Islet amyloid polypeptide, islet amyloid, and diabetes mellitus
Physiological reviews · Research Support, Non-U.S. Gov't, Review
otherPancreas; Islets of Langerhans; Secretory Vesicles; Endoplasmic Reticulum; Animals; Humans; Diabetes Mellitus; Diabetes Mellitus, Type 1
11pmid:168158002006Pancreatic signals controlling food intake; insulin, glucagon and amylin
Philosophical transactions of the Royal Society of London. Series B, Biological sciences · research-article, Review
otherPancreas; Animals; Body Weight; Amyloid; Glucagon; Insulin; Eating; Islet Amyloid Polypeptide

Not a registered trial record — 7 records

No.IdentifierYearRecordModelSubject headings
4pmid:237944482013Amylin deposition in the brain: A second amyloid in Alzheimer disease?
Annals of neurology · Research Support, Non-U.S. Gov't, research-article
otherBrain; Humans; Alzheimer Disease; Diabetic Angiopathies; RNA, Messenger; Aged; Aged, 80 and over; Female
6pmid:207073882010The flavanol (-)-epigallocatechin 3-gallate inhibits amyloid formation by islet amyloid polypeptide, disaggregates amyloid fibrils, and protects cultured cells against IAPP-induced toxicity
Biochemistry · Comparative Study, Research Support, Non-U.S. Gov't
rodentAnimals; Rats; Diabetes Mellitus, Type 2; Phenols; Thiazoles; Catechin; Flavonoids; Amyloid
7pmid:194756632009Atomic structures of IAPP (amylin) fusions suggest a mechanism for fibrillation and the role of insulin in the process
Protein science : a publication of the Protein Society · Research Support, Non-U.S. Gov't, research-article
otherHumans; Diabetes Mellitus, Type 2; Amyloid; Insulin; Carrier Proteins; Recombinant Fusion Proteins; Crystallography, X-Ray; Binding Sites
8pmid:184583262008Leptin responsiveness restored by amylin agonism in diet-induced obesity: evidence from nonclinical and clinical studies
Proceedings of the National Academy of Sciences of the United States of America · research-article
rodentHypothalamus; Adipose Tissue; Animals; Rats; Obesity; Disease Models, Animal; Body Weight; Amyloid
9pmid:185564732008Atomic structure of the cross-beta spine of islet amyloid polypeptide (amylin)
Protein science : a publication of the Protein Society · Research Support, Non-U.S. Gov't, research-article
otherIslets of Langerhans; Humans; Diabetes Mellitus, Type 2; Disulfides; Amyloid; Histidine; Carrier Proteins; Recombinant Fusion Proteins
10pmid:179793022007Peptide conformation and supramolecular organization in amylin fibrils: constraints from solid-state NMR
Biochemistry · Research Support, N.I.H., Intramural, Comparative Study
otherAnimals; Humans; Amyloid; Peptides; Peptide Fragments; Microscopy, Electron, Scanning Transmission; Microscopy, Atomic Force; Nuclear Magnetic Resonance, Biomolecular
12pmid:168845002006The aggregation potential of human amylin determines its cytotoxicity towards islet beta-cells
The FEBS journal · Journal Article
otherIslets of Langerhans; Cell Line; Humans; Amyloid; Microscopy, Electron, Transmission; Circular Dichroism; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Amino Acid Sequence

Where this page sits

Receptor targets

All compounds in scope: the trial index. Coverage by endpoint: the endpoint index.

Review status

Review tier
High impact
State
Pending qualified review
Compiled by
automated pipeline
Qualified clinical review
None on record

Why this tier was assigned

  • the class covers weight-management and metabolic prescribing, the highest-risk consumer subject in this corpus

Checks the pipeline performed

  • every cited source id resolves to a sources[] row on the entity
  • every identifier is a well-formed PMID or DOI
  • study model derived only from assigned MeSH headings and publication types
  • banned-phrase lint over rendered HTML including title, meta, alt and JSON-LD
  • unknown values render as the literal word Unknown

Checks the pipeline did not perform

  • no full text was read
  • no clinical appraisal of any study
  • no assessment of whether the indexed set is representative of the literature

A high_impact profile with qualified_review null must not be published as indexable. Compilation and linting are not clinical validation.

Sources

  1. PubChem Compound Summary for CID 16132430, Islet Amyloid Polypeptide. PubChem, National Library of Medicine (2026). pubchem:16132430
  2. Drugs@FDA application register query for this compound, no application records returned. U.S. Food and Drug Administration, openFDA drugsfda endpoint (2026). fda:amylin
  3. Islet amyloid polypeptide, islet amyloid, and diabetes mellitus. Physiological reviews (2011). pmid:21742788
  4. International Union of Pharmacology. XXXII. The mammalian calcitonin gene-related peptides, adrenomedullin, amylin, and calcitonin receptors. Pharmacological reviews (2002). pmid:12037140
  5. Multiple amylin receptors arise from receptor activity-modifying protein interaction with the calcitonin receptor gene product. Molecular pharmacology (1999). pmid:10385705
  6. Pancreatic amylin and calcitonin gene-related peptide cause resistance to insulin in skeletal muscle in vitro. Nature (1988). pmid:3050530
  7. Islet amyloid polypeptide: pinpointing amino acid residues linked to amyloid fibril formation. Proceedings of the National Academy of Sciences of the United States of America (1990). pmid:2195544
  8. Pancreatic islet cell toxicity of amylin associated with type-2 diabetes mellitus. Nature (1994). pmid:8152488
  9. Pore formation by the cytotoxic islet amyloid peptide amylin. The Journal of biological chemistry (1996). pmid:8567648
  10. The mechanism of islet amyloid polypeptide toxicity is membrane disruption by intermediate-sized toxic amyloid particles. Diabetes (1999). pmid:10078548
  11. Peptide conformation and supramolecular organization in amylin fibrils: constraints from solid-state NMR. Biochemistry (2007). pmid:17979302
  12. Membrane damage by human islet amyloid polypeptide through fibril growth at the membrane. Proceedings of the National Academy of Sciences of the United States of America (2008). pmid:18408164
  13. Activation of the NLRP3 inflammasome by islet amyloid polypeptide provides a mechanism for enhanced IL-1β in type 2 diabetes. Nature immunology (2010). pmid:20835230