Is DAPI assay of cellular nucleic acid reliable in the presence of protein aggregates?

2020 ◽  
Vol 56 (89) ◽  
pp. 13844-13847
Author(s):  
Aruna K. Mora ◽  
Sufiyan Khan ◽  
Birija S. Patro ◽  
Sukhendu Nath
Keyword(s):  
Nucleic Acid ◽  
Amyloid Fibrils ◽  
Protein Aggregates

Intracellular amyloid fibrils prevent exclusive staining of nuclei by DAPI.

Dynamics and Fluidity of Amyloid Fibrils:  A Model of Fibrous Protein Aggregates

2002 ◽  
Vol 124 (51) ◽  
pp. 15150-15151 ◽  
Author(s):  
Ami S. Lakdawala ◽  
David M. Morgan ◽  
Dennis C. Liotta ◽  
David G. Lynn ◽  
James P. Snyder
Keyword(s):  
Amyloid Fibrils ◽  
Protein Aggregates ◽  
Fibrous Protein

scholarly journals RETRACTED: Peptide-induced formation of protein aggregates and amyloid fibrils in human and guinea pig αA-crystallins under physiological conditions of temperature and pH

2019 ◽  
Vol 179 ◽  
pp. 193-205 ◽  
Author(s):  
Anbarasu Kumarasamy ◽  
Sivakumar Jeyarajan ◽  
Jonathan Cheon ◽  
Anthony Premceski ◽  
Eric Seidel ◽  
...  
Keyword(s):  
Guinea Pig ◽  
Amyloid Fibrils ◽  
Protein Aggregates ◽  
Physiological Conditions

scholarly journals Full-length prion protein aggregates to amyloid fibrils and spherical particles by distinct pathways

FEBS Journal ◽  
2008 ◽  
Vol 275 (9) ◽  
pp. 2021-2031 ◽  
Author(s):  
Driss El Moustaine ◽  
Veronique Perrier ◽  
Laszlo Smeller ◽  
Reinhard Lange ◽  
Joan Torrent
Keyword(s):  
Prion Protein ◽  
Amyloid Fibrils ◽  
Protein Aggregates ◽  
Full Length ◽  
Spherical Particles

scholarly journals Nucleic acid-containing amyloid fibrils potently induce type I interferon and stimulate systemic autoimmunity

2012 ◽  
Vol 109 (36) ◽  
pp. 14550-14555 ◽  
Author(s):  
J. Di Domizio ◽  
S. Dorta-Estremera ◽  
M. Gagea ◽  
D. Ganguly ◽  
S. Meller ◽  
...  
Keyword(s):  
Nucleic Acid ◽  
Amyloid Fibrils ◽  
Type I Interferon ◽  
Type I ◽  
Systemic Autoimmunity

scholarly journals Cryo-EM structure of disease-related prion fibrils provides insights into seeding barriers

2021 ◽  
Author(s):  
Qiuye Li ◽  
Christopher P. Jaroniec ◽  
Witold K. Surewicz
Keyword(s):  
High Resolution ◽  
Prion Protein ◽  
Prion Disease ◽  
Amyloid Fibrils ◽  
Prion Diseases ◽  
Protein Aggregates ◽  
Direct Support ◽  
Human Prion Protein ◽  
Structural Insight

One of the least understood aspects of prion diseases is the structure of infectious prion protein aggregates. Here we report a high-resolution cryo-EM structure of amyloid fibrils formed by human prion protein with Y145Stop mutation that is associated with a familial prion disease. This structural insight allows us not only to explain previous biochemical findings, but also provides direct support for the conformational adaptability model of prion transmissibility barriers.

scholarly journals Lysozyme Fibrils Alter the Mechanism of Insulin Amyloid Aggregation

2021 ◽  
Vol 22 (4) ◽  
pp. 1775
Author(s):  
Mantas Ziaunys ◽  
Andrius Sakalauskas ◽  
Tomas Sneideris ◽  
Vytautas Smirnovas
Keyword(s):  
Protein Aggregation ◽  
Amyloid Fibrils ◽  
Protein Aggregates ◽  
Amyloid Aggregation ◽  
Amyloid Aggregates ◽  
Affected Tissue ◽  
New Ideas

Protein aggregation into amyloid fibrils is linked to multiple disorders. The understanding of how natively non-harmful proteins convert to these highly cytotoxic amyloid aggregates is still not sufficient, with new ideas and hypotheses being presented each year. Recently it has been shown that more than one type of protein aggregates may co-exist in the affected tissue of patients suffering from amyloid-related disorders, sparking the idea that amyloid aggregates formed by one protein may induce another protein’s fibrillization. In this work, we examine the effect that lysozyme fibrils have on insulin amyloid aggregation. We show that not only do lysozyme fibrils affect insulin nucleation, but they also alter the mechanism of its aggregation.

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