Inhibition of the formation of lysozyme fibrillar assemblies by the isoquinoline alkaloid coralyne

2022 ◽  
Author(s):  
Anirban Basu ◽  
Adil Mahammmad ◽  
Arindam Das
Keyword(s):  
Protein Aggregation ◽  
Type Ii Diabetes ◽  
Prion Diseases ◽  
Isoquinoline Alkaloid ◽  
Type Ii ◽  
Degenerative Diseases

Protein aggregation into oligomeric and fibrillar species are the hallmark of many degenerative diseases like Alzheimer’s and prion diseases, as well as type II diabetes. Compounds that can modulate protein...

scholarly journals The Potential Effect of Aberrant Testosterone Levels on Common Diseases: A Mendelian Randomization Study

Genes ◽  
2020 ◽  
Vol 11 (7) ◽  
pp. 721
Author(s):  
Ali Alamdar Shah Syed ◽  
Lin He ◽  
Yongyong Shi
Keyword(s):  
Type Ii Diabetes ◽  
Mendelian Randomization ◽  
Serum Testosterone ◽  
Potential Effect ◽  
Type Ii ◽  
Degenerative Diseases ◽  
Testosterone Levels ◽  
Unit Increase ◽  
Low Levels ◽  
Genetic Instruments

Testosterone has historically been linked to sexual dysfunction; however, it has recently been shown to affect other physical and mental attributes. We attempted to determine whether changes in serum testosterone could play a role in chronic or degenerative diseases. We used two separate genetic instruments comprising of variants from JMJD1C and SHBG regions and conducted a two-sample Mendelian randomization for type II diabetes (T2D), gout, rheumatoid arthritis (RA), schizophrenia, bipolar disorder, Alzheimer’s disease and depression. For the JMJD1C locus, one unit increase in log transformed testosterone was significantly associated with RA (OR = 1.69, p = 0.02), gout (OR = 0.469, p = 0.001) and T2D (OR = 0.769, p = 0.048). Similarly, one unit increase in log transformed testosterone using variants from the SHBG locus was associated with depression (OR = 1.02, p = 0.001), RA (OR = 1.32, p < 0.001) and T2D (OR = 0.88, p = 0.003). Our results show that low levels of serum testosterone levels may cause gout and T2D, while higher than normal levels of testosterone may result in RA and depression. Our findings suggest that fluctuations in testosterone levels may have severe consequences that warrant further investigation.

scholarly journals De Novo designed 13 mer hairpin-peptide arrests insulin and inhibits its aggregation: role of OH–π interactions between water and hydrophobic amino acids

RSC Advances ◽  
2020 ◽  
Vol 10 (25) ◽  
pp. 14991-14999
Author(s):  
Meghomukta Mukherjee ◽  
Nilanjan Banerjee ◽  
Subhrangsu Chatterjee
Keyword(s):  
Amino Acids ◽  
Neurodegenerative Diseases ◽  
Type Ii Diabetes ◽  
De Novo ◽  
Prion Diseases ◽  
Cellular Systems ◽  
Type Ii ◽  
P Protein ◽  
Hydrophobic Amino Acids

Protein aggregation in the cellular systems can be highly fatal causing a series of diseases including neurodegenerative diseases like ALS, Alzheimer, Prion Diseases, Parkinson's and other diseases like type II diabetes.

scholarly journals Proteome response at the edge of protein aggregation

Open Biology ◽  
2015 ◽  
Vol 5 (2) ◽  
pp. 140221 ◽  
Author(s):  
Natalia Sanchez de Groot ◽  
Ricardo A. Gomes ◽  
Anna Villar-Pique ◽  
M. Madan Babu ◽  
Ana Varela Coelho ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Protein Aggregation ◽  
Inclusion Body ◽  
Type Ii Diabetes ◽  
Amyloid Β ◽  
Amyloid Β Peptide ◽  
Type Ii ◽  
Cellular Functions ◽  
Human Disorders ◽  
Protein Recruitment

Proteins adopt defined structures and are crucial to most cellular functions. Their misfolding and aggregation is associated with numerous degenerative human disorders such as type II diabetes, Huntington's or Alzheimer's diseases. Here, we aim to understand why cells promote the formation of protein foci. Comparison of two amyloid-β-peptide variants, mostly insoluble but differently recruited by the cell (inclusion body versus diffused), reveals small differences in cell fitness and proteome response. We suggest that the levels of oxidative stress act as a sensor to trigger protein recruitment into foci. Our data support a common cytoplasmic response being able to discern and react to the specific properties of polypeptides.

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