scholarly journals Chaperoned amyloid proteins for immune manipulation: α‐Synuclein/Hsp70 shifts immunity toward a modulatory phenotype

2014 ◽  
Vol 2 (4) ◽  
pp. 226-238 ◽  
Author(s):  
Adahir Labrador‐Garrido ◽  
Marta Cejudo‐Guillén ◽  
Rebecca Klippstein ◽  
Erwin J. De Genst ◽  
Laura Tomas‐Gallardo ◽  
...  
Keyword(s):  
Amyloid Proteins ◽  
Immune Manipulation

Role of the Structural Characteristics of Dendrimers in the Manifestation of the Antiamyloid Properties

INEOS OPEN ◽  
2020 ◽  
Vol 3 ◽  
Author(s):  
S. A. Sorokina ◽  
◽  
Yu. Yu. Stroilova ◽  
V. I. Muronets ◽  
Z. B. Shifrina ◽  
...  
Keyword(s):  
Neurodegenerative Diseases ◽  
Structural Characteristics ◽  
Short Review ◽  
External Factors ◽  
Amyloid Aggregation ◽  
Amyloid Proteins ◽  
Molecular Parameters ◽  
Amyloid Aggregates ◽  
Aggregation Processes

Among the compounds able to efficiently inhibit the amyloid aggregation of proteins and decompose the amyloid aggregates that cause neurodegenerative diseases, of particular interest are dendrimers, which represent individual macromolecules with the hypercrosslinked architectures and given molecular parameters. This short review outlines the peculiarities of the antiamyloid activity of dendrimers and discusses the effect of dendrimer structures and external factors on their antiamyloid properties. The potential of application of dendrimers in further investigations on the aggregation processes of amyloid proteins as the compounds that exhibit the remarkable antiamyloid activity is evaluated.

scholarly journals Autophagy Modulation as a Treatment of Amyloid Diseases

Molecules ◽  
2019 ◽  
Vol 24 (18) ◽  
pp. 3372 ◽  
Author(s):  
Zoe Mputhia ◽  
Eugene Hone ◽  
Timir Tripathi ◽  
Tim Sargeant ◽  
Ralph Martins ◽  
...  
Keyword(s):  
Protein Misfolding ◽  
Metabolic Diseases ◽  
Physiological Role ◽  
Cell Loss ◽  
Amyloid Proteins ◽  
Tissue Degeneration ◽  
Polyglutamine Disorders ◽  
Amyloid Accumulation ◽  
Causative Factors ◽  
Amyloid Diseases

Amyloids are fibrous proteins aggregated into toxic forms that are implicated in several chronic disorders. More than 30 diseases show deposition of fibrous amyloid proteins associated with cell loss and degeneration in the affected tissues. Evidence demonstrates that amyloid diseases result from protein aggregation or impaired amyloid clearance, but the connection between amyloid accumulation and tissue degeneration is not clear. Common examples of amyloid diseases are Alzheimer’s disease (AD), Parkinson’s disease (PD) and tauopathies, which are the most common forms of neurodegenerative diseases, as well as polyglutamine disorders and certain peripheral metabolic diseases. In these diseases, increased accumulation of toxic amyloid proteins is suspected to be one of the main causative factors in the disease pathogenesis. It is therefore important to more clearly understand how these toxic amyloid proteins accumulate as this will aide in the development of more effective preventive and therapeutic strategies. Protein homeostasis, or proteostasis, is maintained by multiple cellular pathways—including protein synthesis, quality control, and clearance—which are collectively responsible for preventing protein misfolding or aggregation. Modulating protein degradation is a very complex but attractive treatment strategy used to remove amyloid and improve cell survival. This review will focus on autophagy, an important clearance pathway of amyloid proteins, and strategies for using it as a potential therapeutic target for amyloid diseases. The physiological role of autophagy in cells, pathways for its modulation, its connection with apoptosis, cell models and caveats in developing autophagy as a treatment and as a biomarker is discussed.

Beyond amyloid proteins: Thioflavin T in nucleic acid recognition

Biochimie ◽  
2021 ◽  
Author(s):  
Smita Verma ◽  
Velayutham Ravichandiran ◽  
Nihar Ranjan
Keyword(s):  
Nucleic Acid ◽  
Thioflavin T ◽  
Amyloid Proteins

Screening for amyloid proteins in the yeast proteome

2017 ◽  
Vol 64 (2) ◽  
pp. 469-478 ◽  
Author(s):  
Tatyana A. Ryzhova ◽  
Julia V. Sopova ◽  
Sergey P. Zadorsky ◽  
Vera A. Siniukova ◽  
Aleksandra V. Sergeeva ◽  
...  
Keyword(s):  
Amyloid Proteins ◽  
Yeast Proteome

scholarly journals Implications of peptide assemblies in amyloid diseases

2017 ◽  
Vol 46 (21) ◽  
pp. 6492-6531 ◽  
Author(s):  
Pu Chun Ke ◽  
Marc-Antonie Sani ◽  
Feng Ding ◽  
Aleksandr Kakinen ◽  
Ibrahim Javed ◽  
...  
Keyword(s):  
Self Assembly ◽  
Amyloid Proteins ◽  
Amyloid Diseases

We highlight the role of molecular self-assembly in eliciting the mesoscopic and pathological properties of amyloid proteins. This knowledge is pivotal for the development of theranostics against amyloid diseases.

scholarly journals High Selectivity and Sensitivity of Oligomeric P-Phenylene Ethynylenes for Detecting Amyloid Proteins In-Vitro

2018 ◽  
Vol 114 (3) ◽  
pp. 358a
Author(s):  
Adeline M. Fanni ◽  
Florencia A. Monge ◽  
Arjun Thapa ◽  
David G. Whitten ◽  
Eva Y. Chi
Keyword(s):  
High Selectivity ◽  
Amyloid Proteins ◽  
Phenylene Ethynylenes

Pindborg Tumor-Associated Amyloid Proteins

2004 ◽  
pp. 468-470
Author(s):  
S Macy ◽  
S Wang ◽  
E Carlson ◽  
D Kestler ◽  
A Solomon ◽  
...  
Keyword(s):  
Amyloid Proteins ◽  
Pindborg Tumor
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