Amylin: indexed trial records
Records checked
Compiled and citation-checked by GLP-1 Receptor Agonists editorial desk
Qualified clinical review None on record
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 class | Records |
|---|---|
| Review or synthesis | 5 |
| Not a registered trial record | 7 |
| Study model as assigned | Records |
|---|---|
| other | 10 |
| rodent | 2 |
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
| Endpoint | Records for this compound | Records across all compounds in scope |
|---|---|---|
| Body weight and adiposity | 3 | 108 |
| Glycaemic control | 9 | 117 |
| Cardiovascular | 1 | 30 |
| Renal | 0 | 10 |
| Hepatic | 0 | 9 |
| Neurological | 4 | 18 |
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. | Identifier | Year | Record | Model | Subject headings |
|---|---|---|---|---|---|
| 1 | pmid:28269785 | 2017 | The Link between Type 2 Diabetes and Neurodegeneration: Roles for Amyloid-β, Amylin, and Tau Proteins Journal of Alzheimer's disease : JAD · Review | other | Brain; Animals; Humans; Neurodegenerative Diseases; Diabetes Mellitus, Type 2; tau Proteins; Amyloid beta-Peptides; Islet Amyloid Polypeptide |
| 2 | pmid:26649319 | 2016 | Islet Amyloid Polypeptide: Structure, Function, and Pathophysiology Journal of diabetes research · research-article, Review | other | Islets of Langerhans; Humans; Diabetes Mellitus, Type 2; Structure-Activity Relationship; Insulin-Secreting Cells; Islet Amyloid Polypeptide |
| 3 | pmid:26071095 | 2015 | Amylin: Pharmacology, Physiology, and Clinical Potential Pharmacological reviews · Research Support, Non-U.S. Gov't, Review | other | Animals; Humans; Diabetes Mellitus, Type 1; Diabetes Mellitus, Type 2; Weight Loss; Hypoglycemic Agents; Energy Metabolism; Islet Amyloid Polypeptide |
| 5 | pmid:21742788 | 2011 | Islet amyloid polypeptide, islet amyloid, and diabetes mellitus Physiological reviews · Research Support, Non-U.S. Gov't, Review | other | Pancreas; Islets of Langerhans; Secretory Vesicles; Endoplasmic Reticulum; Animals; Humans; Diabetes Mellitus; Diabetes Mellitus, Type 1 |
| 11 | pmid:16815800 | 2006 | Pancreatic signals controlling food intake; insulin, glucagon and amylin Philosophical transactions of the Royal Society of London. Series B, Biological sciences · research-article, Review | other | Pancreas; Animals; Body Weight; Amyloid; Glucagon; Insulin; Eating; Islet Amyloid Polypeptide |
Not a registered trial record — 7 records
| No. | Identifier | Year | Record | Model | Subject headings |
|---|---|---|---|---|---|
| 4 | pmid:23794448 | 2013 | Amylin deposition in the brain: A second amyloid in Alzheimer disease? Annals of neurology · Research Support, Non-U.S. Gov't, research-article | other | Brain; Humans; Alzheimer Disease; Diabetic Angiopathies; RNA, Messenger; Aged; Aged, 80 and over; Female |
| 6 | pmid:20707388 | 2010 | The 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 | rodent | Animals; Rats; Diabetes Mellitus, Type 2; Phenols; Thiazoles; Catechin; Flavonoids; Amyloid |
| 7 | pmid:19475663 | 2009 | Atomic 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 | other | Humans; Diabetes Mellitus, Type 2; Amyloid; Insulin; Carrier Proteins; Recombinant Fusion Proteins; Crystallography, X-Ray; Binding Sites |
| 8 | pmid:18458326 | 2008 | Leptin 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 | rodent | Hypothalamus; Adipose Tissue; Animals; Rats; Obesity; Disease Models, Animal; Body Weight; Amyloid |
| 9 | pmid:18556473 | 2008 | Atomic 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 | other | Islets of Langerhans; Humans; Diabetes Mellitus, Type 2; Disulfides; Amyloid; Histidine; Carrier Proteins; Recombinant Fusion Proteins |
| 10 | pmid:17979302 | 2007 | Peptide conformation and supramolecular organization in amylin fibrils: constraints from solid-state NMR Biochemistry · Research Support, N.I.H., Intramural, Comparative Study | other | Animals; Humans; Amyloid; Peptides; Peptide Fragments; Microscopy, Electron, Scanning Transmission; Microscopy, Atomic Force; Nuclear Magnetic Resonance, Biomolecular |
| 12 | pmid:16884500 | 2006 | The aggregation potential of human amylin determines its cytotoxicity towards islet beta-cells The FEBS journal · Journal Article | other | Islets 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
- Amylin receptor: every compound in scope acting at it
- Calcitonin receptor: every compound in scope acting at it
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
- PubChem Compound Summary for CID 16132430, Islet Amyloid Polypeptide. PubChem, National Library of Medicine (2026). pubchem:16132430
- Drugs@FDA application register query for this compound, no application records returned. U.S. Food and Drug Administration, openFDA drugsfda endpoint (2026). fda:amylin
- Islet amyloid polypeptide, islet amyloid, and diabetes mellitus. Physiological reviews (2011). pmid:21742788
- International Union of Pharmacology. XXXII. The mammalian calcitonin gene-related peptides, adrenomedullin, amylin, and calcitonin receptors. Pharmacological reviews (2002). pmid:12037140
- Multiple amylin receptors arise from receptor activity-modifying protein interaction with the calcitonin receptor gene product. Molecular pharmacology (1999). pmid:10385705
- Pancreatic amylin and calcitonin gene-related peptide cause resistance to insulin in skeletal muscle in vitro. Nature (1988). pmid:3050530
- 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
- Pancreatic islet cell toxicity of amylin associated with type-2 diabetes mellitus. Nature (1994). pmid:8152488
- Pore formation by the cytotoxic islet amyloid peptide amylin. The Journal of biological chemistry (1996). pmid:8567648
- The mechanism of islet amyloid polypeptide toxicity is membrane disruption by intermediate-sized toxic amyloid particles. Diabetes (1999). pmid:10078548
- Peptide conformation and supramolecular organization in amylin fibrils: constraints from solid-state NMR. Biochemistry (2007). pmid:17979302
- 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
- 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