Zinc and iron dynamics in human islet amyloid polypeptide-induced diabetes mouse model
- Location
-
Deutsche Nationalbibliothek Frankfurt am Main
- Extent
-
1 Online-Ressource.
- Language
-
Englisch
- Bibliographic citation
-
Zinc and iron dynamics in human islet amyloid polypeptide-induced diabetes mouse model ; volume:13 ; number:1 ; day:15 ; month:3 ; year:2023 ; pages:1-13 ; date:12.2023
Scientific reports ; 13, Heft 1 (15.3.2023), 1-13, 12.2023
- Creator
-
Fukunaka, Ayako
Shimura, Mari
Ichinose, Takayuki
Pereye, Ofejiro B.
Nakagawa, Yuko
Tamura, Yasuko
Mizutani, Wakana
Inoue, Ryota
Inoue, Takato
Tanaka, Yuto
Sato, Takashi
Saitoh, Tatsuya
Fukada, Toshiyuki
Nishida, Yuya
Miyatsuka, Takeshi
Shirakawa, Jun
Watada, Hirotaka
Matsuyama, Satoshi
Fujitani, Yoshio
- Contributor
-
SpringerLink (Online service)
- DOI
-
10.1038/s41598-023-30498-y
- URN
-
urn:nbn:de:101:1-2023120807045517495897
- Rights
-
Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
15.08.2025, 7:34 AM CEST
Data provider
This object is provided by:
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Fukunaka, Ayako
- Shimura, Mari
- Ichinose, Takayuki
- Pereye, Ofejiro B.
- Nakagawa, Yuko
- Tamura, Yasuko
- Mizutani, Wakana
- Inoue, Ryota
- Inoue, Takato
- Tanaka, Yuto
- Sato, Takashi
- Saitoh, Tatsuya
- Fukada, Toshiyuki
- Nishida, Yuya
- Miyatsuka, Takeshi
- Shirakawa, Jun
- Watada, Hirotaka
- Matsuyama, Satoshi
- Fujitani, Yoshio
- SpringerLink (Online service)
Other Objects (12)
The role of SORLA in islet amyloid polypeptide transport and islet amyloid deposition
Zinc and pH modulate the ability of insulin to inhibit aggregation of islet amyloid polypeptide
Lipid accelerating the fibril of islet amyloid polypeptide aggravated the pancreatic islet injury in vitro and in vivo
Modulation of amyloid self-assembly of ß-amyloid peptide (Aß) and islet amyloid polypeptide (IAPP) via IAPP cross-amyloid interaction surface mimics
Epigallocatechin gallate (EGCG) reduces the intensity of pancreatic amyloid fibrils in human islet amyloid polypeptide (hIAPP) transgenic mice
Contraction of human brain vascular pericytes in response to islet amyloid polypeptide is reversed by pramlintide
Dual effect of PEG-PE micelle over the oligomerization and fibrillation of human islet amyloid polypeptide
Structural characterization of recombinant fibrillar human Islet Amyloid Polypeptide by solid-state Nuclear Magnetic Resonance Spectroscopy
Islet amyloid polypeptide cross-seeds tau and drives the neurofibrillary pathology in Alzheimer’s disease
The islet tissue plasminogen activator/plasmin system is upregulated with human islet amyloid polypeptide aggregation and protects beta cells from aggregation-induced toxicity
The Human Host‐Defense Peptide Cathelicidin LL‐37 is a Nanomolar Inhibitor of Amyloid Self‐Assembly of Islet Amyloid Polypeptide (IAPP)
Human Islet Amyloid Polypeptide (hIAPP) Protofibril‐Specific Antibodies for Detection and Treatment of Type 2 Diabetes
The role of SORLA in islet amyloid polypeptide transport and islet amyloid deposition
Zinc and pH modulate the ability of insulin to inhibit aggregation of islet amyloid polypeptide
Lipid accelerating the fibril of islet amyloid polypeptide aggravated the pancreatic islet injury in vitro and in vivo
Modulation of amyloid self-assembly of ß-amyloid peptide (Aß) and islet amyloid polypeptide (IAPP) via IAPP cross-amyloid interaction surface mimics
Epigallocatechin gallate (EGCG) reduces the intensity of pancreatic amyloid fibrils in human islet amyloid polypeptide (hIAPP) transgenic mice
Contraction of human brain vascular pericytes in response to islet amyloid polypeptide is reversed by pramlintide
Dual effect of PEG-PE micelle over the oligomerization and fibrillation of human islet amyloid polypeptide
Structural characterization of recombinant fibrillar human Islet Amyloid Polypeptide by solid-state Nuclear Magnetic Resonance Spectroscopy
Islet amyloid polypeptide cross-seeds tau and drives the neurofibrillary pathology in Alzheimer’s disease
The islet tissue plasminogen activator/plasmin system is upregulated with human islet amyloid polypeptide aggregation and protects beta cells from aggregation-induced toxicity
The Human Host‐Defense Peptide Cathelicidin LL‐37 is a Nanomolar Inhibitor of Amyloid Self‐Assembly of Islet Amyloid Polypeptide (IAPP)
Human Islet Amyloid Polypeptide (hIAPP) Protofibril‐Specific Antibodies for Detection and Treatment of Type 2 Diabetes
The role of SORLA in islet amyloid polypeptide transport and islet amyloid deposition
Zinc and pH modulate the ability of insulin to inhibit aggregation of islet amyloid polypeptide
Lipid accelerating the fibril of islet amyloid polypeptide aggravated the pancreatic islet injury in vitro and in vivo
Modulation of amyloid self-assembly of ß-amyloid peptide (Aß) and islet amyloid polypeptide (IAPP) via IAPP cross-amyloid interaction surface mimics
Epigallocatechin gallate (EGCG) reduces the intensity of pancreatic amyloid fibrils in human islet amyloid polypeptide (hIAPP) transgenic mice
Contraction of human brain vascular pericytes in response to islet amyloid polypeptide is reversed by pramlintide
Dual effect of PEG-PE micelle over the oligomerization and fibrillation of human islet amyloid polypeptide
Structural characterization of recombinant fibrillar human Islet Amyloid Polypeptide by solid-state Nuclear Magnetic Resonance Spectroscopy
Islet amyloid polypeptide cross-seeds tau and drives the neurofibrillary pathology in Alzheimer’s disease
The islet tissue plasminogen activator/plasmin system is upregulated with human islet amyloid polypeptide aggregation and protects beta cells from aggregation-induced toxicity
The Human Host‐Defense Peptide Cathelicidin LL‐37 is a Nanomolar Inhibitor of Amyloid Self‐Assembly of Islet Amyloid Polypeptide (IAPP)