journal cover

Real-Time Monitoring of Self-Aggregation of β-Amyloid by a Fluorescent Probe based on Ruthenium Complex

Analytical Chemistry

Jan 17, 2020

Hui-Juan YuLin Yu

Abstract

Self-accumulation of amyloid-β protein (Aβ) into insoluble fibrils is the major hallmark of Alzheimer's disease. Real-time monitoring of fibril growth is essential for clarifying the mechanism underlying aggregation and discovering therapeutic targets. A variety of approaches including ...read more

Mentioned in this Paper

Electron Microscopy
Neurotoxicity Syndromes
Neurodegenerative Disorders
Growth Factor
Microscopy, Atomic Force
Pathogenesis
Morg1 protein, human
Alzheimer's Disease
PGE1 oligomer
Thioflavin T
1
1
Paper Details
References
  • References
  • Citations
  • finger pointing at paper

    References currently unavailable

    We're still populating references for this paper, please check back later.
  • References
  • Citations
  • quote and clock

    No citations available

    This paper may not have been cited yet.

Similar Papers Found In These Feeds

Proteostasis

Proteostasis enables the maintenance of protein homeostasis via modulation of protein translation, enhancement of chaperone capacity and the prompt clearance of misfolded proteins. It is affected in several neurodegenerative diseases. Here is the latest research.

Misfolding & Aggregation Diseases

Misfolding and aggregation of proteins can lead to several diseases. For instance, misfolding of prion or tau proteins are associated with several neurodegenerative diseases. Here is the latest research on diseases caused by protein misfolding and aggregation.

Neurotoxicity, Inflammation & Neuroprotection

The end result of the inflammatory process, neurotoxicity and/or neuroprotection, is a function of the fine balance between the two cellular systems, i.e., of the complex signaling relationships between anti-inflammatory neuroprotective factors (neurotrophins and other chemical mediators) and proinflammatory neurotoxic factors (tnf, free radicals, certain cytokines, etc). Here are the latest discoveries pertaining to neurotoxicity, inflammation and neuroprotection.

Misfolded Proteins: ND

Protein misfolding is the primary cause of several neurodegenerative disease, including Alzheimer’s and Parkinson’s disease. Here is the latest research.

Alzheimer's Disease: Abeta

Alzheimer's disease (AD) is a chronic neurodegenerative disease associated with accumulation of amyloid plaques, which are comprised of amyloid beta. Here is the latest research in this field.

Related Papers

Journal of Molecular Biology

Single fibril growth kinetics of α-synuclein

Journal of Molecular BiologyFebruary 11, 2015
Michael M WördehoffEva Birkmann
The Journal of Biological Chemistry

Direct observation of amyloid fibril growth monitored by thioflavin T fluorescence

The Journal of Biological ChemistryMarch 21, 2003
Tadato BanYuji Goto
© 2020 Meta ULC. All rights reserved

Real-Time Monitoring of Self-Aggregation of β-Amyloid by a Fluorescent Probe based on Ruthenium Complex

Analytical Chemistry

Jan 17, 2020

Hui-Juan YuLin Yu

PMID: 31941275

DOI: 10.1021/acs.analchem.9b03566

Abstract

Self-accumulation of amyloid-β protein (Aβ) into insoluble fibrils is the major hallmark of Alzheimer's disease. Real-time monitoring of fibril growth is essential for clarifying the mechanism underlying aggregation and discovering therapeutic targets. A variety of approaches including ...read more

Mentioned in this Paper

Electron Microscopy
Neurotoxicity Syndromes
Neurodegenerative Disorders
Growth Factor
Microscopy, Atomic Force
Pathogenesis
Morg1 protein, human
Alzheimer's Disease
PGE1 oligomer
Thioflavin T
1
1

Similar Papers Found In These Feeds

Proteostasis

Proteostasis enables the maintenance of protein homeostasis via modulation of protein translation, enhancement of chaperone capacity and the prompt clearance of misfolded proteins. It is affected in several neurodegenerative diseases. Here is the latest research.

Misfolding & Aggregation Diseases

Misfolding and aggregation of proteins can lead to several diseases. For instance, misfolding of prion or tau proteins are associated with several neurodegenerative diseases. Here is the latest research on diseases caused by protein misfolding and aggregation.

Related Papers

Journal of Molecular Biology

Single fibril growth kinetics of α-synuclein

Journal of Molecular BiologyFebruary 11, 2015
Michael M WördehoffEva Birkmann
The Journal of Biological Chemistry

Direct observation of amyloid fibril growth monitored by thioflavin T fluorescence

The Journal of Biological ChemistryMarch 21, 2003
Tadato BanYuji Goto
Paper Details
References
  • References
  • Citations
  • finger pointing at paper

    References currently unavailable

    We're still populating references for this paper, please check back later.
  • References
  • Citations
  • quote and clock

    No citations available

    This paper may not have been cited yet.
/papers/real-time-monitoring-of-self-aggregation-of--amylo/31941275