Journal Article FZJ-2021-04251

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png
Amyloid Oligomers: A Joint Experimental/Computational Perspective on Alzheimer’s Disease, Parkinson’s Disease, Type II Diabetes, and Amyotrophic Lateral Sclerosis

 ;  ;  ;  ;  ;  ;  ;  ;  ;  ;  ;  ;  ;  ;  ;  ;  ;  ;  ;  ;  ;  ;  ;  ;  ;  ;  ;  ;  ;  ;  ;  ;  ;

2021
ACS Publ. Washington, DC

Chemical reviews 121(4), 2545 - 2647 () [10.1021/acs.chemrev.0c01122]

This record in other databases:      

Please use a persistent id in citations:   doi:

Abstract: Protein misfolding and aggregation is observed in many amyloidogenic diseases affecting either the central nervous system or a variety of peripheral tissues. Structural and dynamic characterization of all species along the pathways from monomers to fibrils is challenging by experimental and computational means because they involve intrinsically disordered proteins in most diseases. Yet understanding how amyloid species become toxic is the challenge in developing a treatment for these diseases. Here we review what computer, in vitro, in vivo, and pharmacological experiments tell us about the accumulation and deposition of the oligomers of the (Aβ, tau), α-synuclein, IAPP, and superoxide dismutase 1 proteins, which have been the mainstream concept underlying Alzheimer’s disease (AD), Parkinson’s disease (PD), type II diabetes (T2D), and amyotrophic lateral sclerosis (ALS) research, respectively, for many years.

Classification:

Contributing Institute(s):
  1. Strukturbiochemie (IBI-7)
Research Program(s):
  1. 5244 - Information Processing in Neuronal Networks (POF4-524) (POF4-524)

Appears in the scientific report 2021
Database coverage:
Medline ; OpenAccess ; Clarivate Analytics Master Journal List ; Current Contents - Physical, Chemical and Earth Sciences ; Ebsco Academic Search ; Essential Science Indicators ; IF >= 50 ; JCR ; NationallizenzNationallizenz ; SCOPUS ; Science Citation Index Expanded ; Web of Science Core Collection
Click to display QR Code for this record

The record appears in these collections:
Dokumenttypen > Aufsätze > Zeitschriftenaufsätze
Institutssammlungen > IBI > IBI-7
Workflowsammlungen > Öffentliche Einträge
Publikationsdatenbank
Open Access

 Datensatz erzeugt am 2021-11-14, letzte Änderung am 2022-02-24


OpenAccess:
Volltext herunterladen PDF
Externer link:
Volltext herunterladenFulltext by OpenAccess repository
Dieses Dokument bewerten:

Rate this document:
1
2
3
 
(Bisher nicht rezensiert)