Cardioprotection by controlling hyperamylinemia in a "humanized" diabetic rat model - Wikidata - awgldk - TriplyDB

Cardioprotection by controlling hyperamylinemia in a "humanized" diabetic rat model

Cardioprotection by controlling hyperamylinemia in a "humanized" diabetic rat model

http://www.wikidata.org/entity/Q35026344

about

The 2014 Bernard B. Brodie award lecture-epoxide hydrolases: drug metabolism to therapeutics for chronic pain The Mitochondrial Peptidase Pitrilysin Degrades Islet Amyloid Polypeptide in Beta-Cells.Intracellular Na+ Concentration ([Na+]i) Is Elevated in Diabetic Hearts Due to Enhanced Na+-Glucose Cotransport.Islet Amyloid Polypeptide: Structure, Function, and Pathophysiology.Hyperamylinemia as a risk factor for accelerated cognitive decline in diabetes Intraneuronal Amylin Deposition, Peroxidative Membrane Injury and Increased IL-1β Synthesis in Brains of Alzheimer's Disease Patients with Type-2 Diabetes and in Diabetic HIP Rats.Time-resolved studies define the nature of toxic IAPP intermediates, providing insight for anti-amyloidosis therapeutics.Brain microvascular injury and white matter disease provoked by diabetes-associated hyperamylinemia.Viewing Extrinsic Proteotoxic Stress Through the Lens of Amyloid Cardiomyopathy.Target acquired: Selective autophagy in cardiometabolic disease.Amylin and its G-protein-coupled receptor: A probable pathological process and drug target for Alzheimer's disease.Hyperamylinemia Increases IL-1β Synthesis in the Heart via Peroxidative Sarcolemmal Injury Human amylin proteotoxicity impairs protein biosynthesis, and alters major cellular signaling pathways in the heart, brain and liver of humanized diabetic rat model in vivo.Amylin and diabetic cardiomyopathy - amylin-induced sarcolemmal Ca2+ leak is independent of diabetic remodeling of myocardium.Islet Amyloid Polypeptide Membrane Interactions: Effects of Membrane Composition.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.

P2860

Q28392416-8180470E-0397-45FD-BC35-6AA492FD4488 Q34485889-718B92B2-CEF5-4EE7-B4EE-F0731982BA2D Q36141842-B41ABF14-E6B3-4755-BD8A-FE5790709FE8 Q36327915-6733D02B-2B05-43EF-8A2B-4F1DEE65B3F9 Q37019858-39D2CC10-1540-40CD-B43B-374D1C4954D6 Q37037394-BE2EFAA3-0E72-4059-8CB4-2D0FF953929C Q37083241-CCC60CEE-E097-48BC-B582-80495C65BD15 Q38684307-042517FD-4C13-46A1-A103-F9A6D56FC8FD Q38851025-0F8EEF72-95C0-4E95-8193-FC89D1BBF1A9 Q39155198-79EC375E-7719-4749-8557-947F5018D387 Q39320824-5AAC5DD8-5FDE-4FA1-B535-F27BC6D808C5 Q39661461-A9CFA6A6-77F7-45A4-AE44-62BF3FE46470 Q41197182-F7DDF2A7-9122-4110-A488-A075768A024B Q46028408-4BA97982-400B-428B-98A7-26D841BD5D5A Q48092573-A1BBD61F-BFB3-4AA4-9EF1-DA8A816A19DC Q52583445-A935CAC3-36DC-4DA4-BA0C-00C719466AC8

P2860

Cardioprotection by controlling hyperamylinemia in a "humanized" diabetic rat model

http://www.wikidata.org/entity/Q35026344

description

2014 nî lūn-bûn

@nan

2014 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2014 թվականի օգոստոսին հրատարակված գիտական հոդված

@hy

2014年の論文

@ja

2014年論文

@yue

2014年論文

@zh-hant

2014年論文

@zh-hk

2014年論文

@zh-mo

2014年論文

@zh-tw

2014年论文

@wuu

name

Cardioprotection by controlling hyperamylinemia in a "humanized" diabetic rat model

@ast

Cardioprotection by controlling hyperamylinemia in a "humanized" diabetic rat model

@en

type

label

Cardioprotection by controlling hyperamylinemia in a "humanized" diabetic rat model

@ast

Cardioprotection by controlling hyperamylinemia in a "humanized" diabetic rat model

@en

prefLabel

Cardioprotection by controlling hyperamylinemia in a "humanized" diabetic rat model

@ast

Cardioprotection by controlling hyperamylinemia in a "humanized" diabetic rat model

@en

P1433

Q35026344-DFD1CC21-68C1-4A20-8295-5AB92F6338D5

P1476

Q35026344-4B0CC0CC-9F2D-4582-A715-FB015938DD9B

P2093

Q35026344-26D8EF71-F3EB-40CA-9ECC-CBB0B643F043

Q35026344-29DD4D62-6C26-4EC8-929B-4D8B7FBD81A5

Q35026344-35B25027-0981-4D1D-8DB1-0ED2603745CF

Q35026344-5CF446AC-D2A8-46BD-8F67-AD8B10B365F9

Q35026344-6936B31C-B507-430C-9639-ECF7FD7F0E44

Q35026344-749B6D69-922F-4CD8-8E18-4D71C62BD2E5

Q35026344-90AF7D6B-9BBD-435A-8651-57A9B137B8C6

Q35026344-9E0C7CB7-6BC9-4864-9E0A-1FF0368AA08B

Q35026344-BF121DEB-5070-4B30-90F4-337955354205

Q35026344-D35D1806-B3E5-4293-A3EA-620D6D7C1493

P2860

Q35026344-0C61AD48-6E58-4926-8E08-3ACF7D6035BC

Q35026344-0DEDC613-6B2F-4FDE-8959-AE9678413333

Q35026344-0E611C00-5873-4F65-B922-4881DD0A945E

Q35026344-0F7B3F97-994E-416B-B5AA-33EFEAF26FD3

Q35026344-28FCCF3B-7743-42ED-89CD-D7A1CEAB1B40

Q35026344-2CD0431B-F7B0-49ED-8849-C539B7E6C252

Q35026344-2F08E8C7-02B7-4D47-A072-E60581ADD1E8

Q35026344-3636853D-FB2C-42AE-B1C1-151ABFDD4CF4

Q35026344-3CA72131-99E7-4D69-9619-E33E02FC3920

Q35026344-4145C203-3302-4568-A51B-F9AA8FBF1D58

P31

Q35026344-7ED8F4E9-8A7A-46BB-BB8B-C40AEE4E2F21

P356

Q35026344-ED0B6514-4995-4CBF-B554-B56FA6045910

P433

Q35026344-120EB166-8AB3-458F-A92F-94475495ED68

P478

Q35026344-380EF6F4-4409-4DE9-9FF5-B82E1DE5448E

P577

Q35026344-ACE52ADB-D207-454C-BD3D-09C9620336E1

P698

Q35026344-F11F5C3C-DCC7-47CC-93B8-DE45263716DF

P932

Q35026344-D41E7836-063D-403D-9B20-090FBE781413

P356

JAHA.114.001015

P1433

Journal of the American Heart Association: Cardiovascular and Cerebrovascular Disease

P1476

Cardioprotection by controlling hyperamylinemia in a "humanized" diabetic rat model

@en

P2093

Bruce D Hammock

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

Florin Despa

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

Heinrich Taegtmeyer

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

Hua Dong

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

Kenneth B Margulies

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

Ning Li

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

Nipavan Chiamvimonvat

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

Sanda Despa

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

Savita Sharma

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

Todd R Harris

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

P2860

Atomic structures of IAPP (amylin) fusions suggest a mechanism for fibrillation and the role of insulin in the process

Protein misfolding, functional amyloid, and human disease

Epoxyeicosatrienoic acids (EETs): metabolism and biochemical function

Epoxide hydrolases: their roles and interactions with lipid metabolism

Soluble epoxide hydrolase deficiency alters pancreatic islet size and improves glucose homeostasis in a model of insulin resistance

Epoxides and soluble epoxide hydrolase in cardiovascular physiology

Islet amyloid polypeptide: pinpointing amino acid residues linked to amyloid fibril formation

Cardiac outcomes after screening for asymptomatic coronary artery disease in patients with type 2 diabetes: the DIAD study: a randomized controlled trial

Protein aggregates and novel presenilin gene variants in idiopathic dilated cardiomyopathy

Evidence for proteotoxicity in beta cells in type 2 diabetes: toxic islet amyloid polypeptide oligomers form intracellularly in the secretory pathway.

P31

scholarly article

P356

10.1161/JAHA.114.001015

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

P433

4

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

P478

3

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

P577

2014-08-21T00:00:00Z

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

P698

25146704

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

P932

4310392

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