Islet Amyloid Polypeptide: Structure, Function, and Pathophysiology. - Wikidata - wikimedia - TriplyDB

Islet Amyloid Polypeptide: Structure, Function, and Pathophysiology.

Islet Amyloid Polypeptide: Structure, Function, and Pathophysiology.

http://www.wikidata.org/entity/Q36327915

about

IL-1β at the crossroad between rheumatoid arthritis and type 2 diabetes: may we kill two birds with one stone?The dye SYPRO orange binds to amylin amyloid fibrils but not pre-fibrillar intermediates.Amylin structure-function relationships and receptor pharmacology: implications for amylin mimetic drug development.Effect of Post-Translational Amidation on Islet Amyloid Polypeptide Conformational Ensemble: Implications for Its Aggregation Early Steps.Endosulfine-alpha inhibits membrane-induced α-synuclein aggregation and protects against α-synuclein neurotoxicity Transactive DNA Binding Protein 43 Rather Than Other Misfolded Proteins in the Brain is Associated with Islet Amyloid Polypeptide in Pancreas in Aged Subjects with Diabetes Mellitus.Novel insight into streptozotocin-induced diabetic rats from the protein misfolding perspective β-Hairpin mimics containing a piperidine-pyrrolidine scaffold modulate the β-amyloid aggregation process preserving the monomer species.Nucleobindin 1 binds to multiple types of pre-fibrillar amyloid and inhibits fibrillization.Peptide Conjugates of Benzene Carboxylic Acids as Agonists and Antagonists of Amylin Aggregation.Islet Amyloid Polypeptide Membrane Interactions: Effects of Membrane Composition.RAGE binds preamyloid IAPP intermediates and mediates pancreatic β cell proteotoxicity.A versatile platform for adding functional properties to amyloid fibrils.Inhibition of the Aggregation and Toxicity of the Minimal Amyloidogenic Fragment of Tau by Its Pro-Substituted Analogues.Analysis of the role of the conserved disulfide in amyloid formation by human IAPP in homogenous and heterogeneous environments.The Receptor for Advanced Glycation Endproducts is a mediator of toxicity by IAPP and other proteotoxic aggregates: Establishing and Exploiting Common Ground for Novel Amyloidosis Therapies.Comparative occurrence of diabetes in canine, feline, and few wild animals and their association with pancreatic diseases and ketoacidosis with therapeutic approach.Evolutionary Adaptation and Amyloid Formation: Does the Reduced Amyloidogenicity and Cytotoxicity of Ursine Amylin Contribute to the Metabolic Adaption of Bears and Polar Bears?mTORC1 Overactivation as a Key Aging Factor in the Progression to Type 2 Diabetes Mellitus Autophagy in Metabolic Age-Related Human Diseases

P2860

Q30251741-14512760-B702-419B-9994-6EFE080D910E Q36091684-AC8ABAEB-A407-4417-9DFA-576775F23687 Q36941265-9AA1DAC9-3EF0-4FB9-90EF-166E29638743 Q37465610-7345C010-FE45-488B-A1FB-B046E0C2F354 Q37576386-1927E7BF-A676-48D4-B9BC-4AC2447605B8 Q40966843-B3F9A13A-339F-4CD3-AB5A-B5BC4320283C Q41044393-B0C77CDD-4BFC-48D3-B928-9EC1E41CD262 Q42314973-2E306364-FD02-443B-B6E3-9BECBC440FB6 Q42320579-F6CD8609-4A5B-4C11-8ADC-ECA6C0ACEF31 Q46434649-170038E3-6139-489C-8D9C-8F1E3DADD549 Q48092573-13A19DEE-F656-4459-9273-18913618FFAF Q48536125-368246CB-A5E6-48E1-BF0A-58C5F5EEDE3B Q49994603-6385EFB3-4C5D-4A6D-B33D-A6C6614EFAAD Q50863156-D22AFA5F-124B-4AE4-9442-9F559F50EEDB Q52561860-479097E8-6A23-435D-B90A-83F43B98AD45 Q52583445-E02C5FB8-B851-43C7-A783-90357C893D1C Q55234475-90C20D37-0C50-48A5-9ED4-8C51C4F2D4DD Q55404538-BEBEAAD5-D27C-4984-A8A9-AF08C32C03BB Q58553598-E61AA232-DB51-4EF4-BB69-83FCB75C8159 Q58699659-BE4F4710-5C49-409E-AE0F-120227A75A45

P2860

Islet Amyloid Polypeptide: Structure, Function, and Pathophysiology.

http://www.wikidata.org/entity/Q36327915

description

2015 nî lūn-bûn

@nan

2015年の論文

@ja

2015年学术文章

@wuu

2015年学术文章

@zh-cn

2015年学术文章

@zh-hans

2015年学术文章

@zh-my

2015年学术文章

@zh-sg

2015年學術文章

@yue

2015年學術文章

@zh

2015年學術文章

@zh-hant

name

Islet Amyloid Polypeptide: Structure, Function, and Pathophysiology.

@ast

Islet Amyloid Polypeptide: Structure, Function, and Pathophysiology.

@en

type

label

Islet Amyloid Polypeptide: Structure, Function, and Pathophysiology.

@ast

Islet Amyloid Polypeptide: Structure, Function, and Pathophysiology.

@en

prefLabel

Islet Amyloid Polypeptide: Structure, Function, and Pathophysiology.

@ast

Islet Amyloid Polypeptide: Structure, Function, and Pathophysiology.

@en

P1433

Q36327915-E8AC5121-9CB0-42DF-8236-7710FA3892D6

P1476

Q36327915-9558FBCC-DF4C-4343-AB4D-38BBC12969A2

P2093

Q36327915-14E2170F-B7DD-4B4E-9970-7F6296AFF431

Q36327915-185CE4E0-2922-4004-BEB4-9A10589CE14C

Q36327915-447D455D-8C8F-412E-B669-40D0A712206B

Q36327915-796C3378-3C98-411E-B3D1-C376A5AB1EE7

Q36327915-99A0E2A0-9975-4484-98BE-E4A1F76ED8FF

Q36327915-B2C8538A-84EA-4D12-86D8-4C6AA28E420A

Q36327915-BA168945-4D82-4958-8E89-4D42D2C0FD1B

Q36327915-EC6051A3-AA78-4498-A0CD-055979FAC721

P275

Q36327915-83CBE95C-40AE-483F-8555-0468BC04D2C6

P2860

Q36327915-062B6674-4159-42C5-AEC4-90BD87D6589F

Q36327915-06DB4C8F-76A1-4330-8968-8B52BB7D05DB

Q36327915-08E4D92D-B500-4D97-86CD-2AEEE2A404F4

Q36327915-09B482FC-B3B4-4EF2-A2DF-D4581BCE8DDB

Q36327915-09FFCE72-51D0-43FE-9039-766AE6E2F924

Q36327915-0D1D9C22-4B3F-4848-B153-E5E89874DA5A

Q36327915-10161913-1942-4EEB-9744-41A3AF3A7384

Q36327915-104403A8-E87A-4E08-8A8C-D1A502A48BF7

Q36327915-11D91954-2673-42CE-9E6F-8AE1D03BC8ED

Q36327915-146356BD-29FF-49F4-A007-03FE47DC74B0

P304

Q36327915-20ED655B-392A-4CF0-86EC-D70D875011D4

P31

Q36327915-200122D9-1810-4F25-901D-7DA0D57B2393

Q36327915-3067C7A0-0A27-4F13-977A-FF36E80B24AA

P356

Q36327915-FCA1EC20-AD8C-42B1-94BA-D5A484898287

P478

Q36327915-B34AC726-1F79-47A8-AF1B-9DF4F233A30A

P50

Q36327915-08D450EE-F3A5-4A0B-B0E1-147512ADED71

Q36327915-B2842B5B-809B-488D-9EF4-7C5FFDCE4DA6

Q36327915-D78B3612-D605-4395-91ED-1BF8E5BA6020

P5008

Q36327915-630C6FE3-94BB-4A7F-B846-8ECDEA1A9B60

P577

Q36327915-508CB5C8-A975-49F2-A1B3-F765D73D74B2

P5875

Q36327915-C84A1B19-3D10-4121-BCCF-0440EEE6207C

P698

Q36327915-0CD93AC3-0C2D-4B8F-80CE-A065B5473729

P921

Q36327915-25FE013E-0A28-4629-9EC8-6B2D4626078C

Q36327915-3E84EBF3-0FF7-4EEF-AFC0-701EB2CFEFC9

Q36327915-4DA9F281-E64B-47E6-8A9D-DA859BF534EE

Q36327915-88DB18B6-8E93-4CBE-A277-6FE6B9ECC0B0

Q36327915-B5B2CBC2-EA21-4825-9DD6-027A2799048D

Q36327915-D7909B58-1E72-464E-8ECF-74BF454FD104

Q36327915-E2184F05-3B93-4441-8C91-DC8B8FAC3449

Q36327915-FF098F58-E3E4-46D9-8861-19AB4E08BF04

P932

Q36327915-C503527E-66B4-411E-BB5F-2BD88F0E502D

P356

P1433

Journal of Diabetes Research

P1476

Islet Amyloid Polypeptide: Structure, Function, and Pathophysiology.

@en

P2093

Amy G Wong

http://www.w3.org/2001/XMLSchema#string

Ann Marie Schmidt

http://www.w3.org/2001/XMLSchema#string

Harris Noor

http://www.w3.org/2001/XMLSchema#string

Hui Wang

http://www.w3.org/2001/XMLSchema#string

Ping Cao

http://www.w3.org/2001/XMLSchema#string

Rehana Akter

http://www.w3.org/2001/XMLSchema#string

Xiaoxue Zhang

http://www.w3.org/2001/XMLSchema#string

Zachary Ridgway

http://www.w3.org/2001/XMLSchema#string

P275

Creative Commons Attribution 3.0 Unported

P2860

An amylin receptor is revealed following co-transfection of a calcitonin receptor with receptor activity modifying proteins-1 or -3

RAMPs regulate the transport and ligand specificity of the calcitonin-receptor-like receptor

Amyloid fibrils in human insulinoma and islets of Langerhans of the diabetic cat are derived from a neuropeptide-like protein also present in normal islet cells

Purification and characterization of a peptide from amyloid-rich pancreases of type 2 diabetic patients

Structures of rat and human islet amyloid polypeptide IAPP(1-19) in micelles by NMR spectroscopy

Macromolecular crowding and confinement: biochemical, biophysical, and potential physiological consequences

A single mutation in the nonamyloidogenic region of islet amyloid polypeptide greatly reduces toxicity

Leptin responsiveness restored by amylin agonism in diet-induced obesity: evidence from nonclinical and clinical studies

Recent advances in understanding leptin signaling and leptin resistance

Mechanisms of islet amyloidosis toxicity in type 2 diabetes

P304

2798269

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1155/2016/2798269

http://www.w3.org/2001/XMLSchema#string

P478

2016

http://www.w3.org/2001/XMLSchema#string

P50

Daniel P Raleigh

Andisheh Abedini

P5008

P577

2015-11-15T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

284139474

http://www.w3.org/2001/XMLSchema#string

P698

26649319

http://www.w3.org/2001/XMLSchema#string

P921

endocrine system

type-2 diabetes

maturity-onset diabetes of the young

Aizkuņģa dziedzeris

P932

4662979

http://www.w3.org/2001/XMLSchema#string