FAQ

Amylin

Known as: Islet Amyloid Polypeptide, Polypeptide, Islet Amyloid, Insulinoma Amyloid Polypeptide 
A pancreatic beta-cell hormone that is co-secreted with INSULIN. It displays an anorectic effect on nutrient metabolism by inhibiting gastric acid… (More)
National Institutes of Health

Topic mentions per year

Topic mentions per year

1959-2018
05019592018

Related topics

Related topics

20 relations

Broader (3)

Amylin Receptor AgonistsAppetite DepressantsPancreatic Polypeptide
Amyloid ProteinsDAP geneDiabetes Mellitus, Non-Insulin-DependentIAPP gene
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Narrower (2)

Islet Amyloid Polypeptide PrecursorPramlintide

Related mentions per year

Related mentions per year

1936-2018
19401960198020002020
Amylin
Diabetes Mellitus, Non-Insulin-Dependent
physiological aspects
In Blood
Appetite Depressants
chemical synthesis

Papers overview

Semantic Scholar uses AI to extract papers important to this topic.
Highly Cited
2008
Highly Cited
2008
Leptin responsiveness restored by amylin agonism in diet-induced obesity: evidence from nonclinical and clinical studies.
Body weight is regulated by complex neurohormonal interactions between endocrine signals of long-term adiposity (e.g., leptin, a… (More)
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Highly Cited
2008
Highly Cited
2008
Atomic structure of the cross-beta spine of islet amyloid polypeptide (amylin).
Human islet amyloid polypeptide (IAPP or amylin) is a 37-residue hormone found as fibrillar deposits in pancreatic extracts of… (More)
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Highly Cited
2007
Highly Cited
2007
Peptide conformation and supramolecular organization in amylin fibrils: constraints from solid-state NMR.
The 37-residue amylin peptide, also known as islet amyloid polypeptide, forms fibrils that are the main peptide or protein… (More)
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Highly Cited
2007
Highly Cited
2007
Atomic structures of amyloid cross-beta spines reveal varied steric zippers.
Amyloid fibrils formed from different proteins, each associated with a particular disease, contain a common cross-beta spine. The… (More)
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Highly Cited
2004
Highly Cited
2004
Amylin inhibits bone resorption while the calcitonin receptor controls bone formation in vivo
Amylin is a member of the calcitonin family of hormones cosecreted with insulin by pancreatic beta cells. Cell culture assays… (More)
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Highly Cited
2001
Highly Cited
2001
The anorectic effect of a chronic peripheral infusion of amylin is abolished in area postrema/nucleus of the solitary tract (AP/NTS) lesioned rats
OBJECTIVE: Neurons in the area postrema/nucleus of the solitary tract (AP/NTS) region mediate amylin's anorectic effect elicited… (More)
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Highly Cited
1998
Highly Cited
1998
Differential permeability of the blood-brain barrier to two pancreatic peptides: insulin and amylin.
Insulin and amylin are cosecreted by pancreatic B cells and have receptors within the central nervous system (CNS), where they… (More)
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Highly Cited
1996
Highly Cited
1996
Pore formation by the cytotoxic islet amyloid peptide amylin.
Amylin is a 37-amino acid cytotoxic constituent of amyloid deposits found in the islets of Langerhans of patients with type II… (More)
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Highly Cited
1994
Highly Cited
1994
Pancreatic islet cell toxicity of amylin associated with type-2 diabetes mellitus
THE 37-amino-acid polypeptide amylin is the principal constituent of the amyloid deposits that form in the islets of Langerhans… (More)
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Highly Cited
1990
Highly Cited
1990
Effects of meal ingestion on plasma amylin concentration in NIDDM and nondiabetic humans.
Recent interest has focused on the potential role of amylin in the pathogenesis of non-insulin-dependent diabetes mellitus (NIDDM… (More)
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