Mechanistic insight into the early stages of amyloid formation using an anuran peptide

2019 ◽  
Vol 111 (5) ◽  
Author(s):  
Sourav Ray ◽  
Stephanie Holden ◽  
Lisandra L. Martin ◽  
Ajay Singh Panwar
2013 ◽  
Vol 425 (10) ◽  
pp. 1765-1781 ◽  
Author(s):  
Jae Sun Jeong ◽  
Annalisa Ansaloni ◽  
Raffaele Mezzenga ◽  
Hilal A. Lashuel ◽  
Giovanni Dietler

2019 ◽  
Vol 24 (9) ◽  
pp. 1258-1267 ◽  
Author(s):  
Andreea Oliviana Diaconescu ◽  
Daniel Jonas Hauke ◽  
Stefan Borgwardt

Open Biology ◽  
2018 ◽  
Vol 8 (1) ◽  
pp. 170229 ◽  
Author(s):  
Dorin Sade ◽  
Shira Shaham-Niv ◽  
Zohar A. Arnon ◽  
Omid Tavassoly ◽  
Ehud Gazit

The accumulation of various metabolites appears to be associated with diverse human diseases. However, the aetiological link between metabolic alteration and the observed diseases is still elusive. This includes the correlation between the abnormally high levels of homocysteine and quinolinic acid in Alzheimer's disease, as well as the accumulation of oncometabolites in malignant processes. Here, we suggest and discuss a possible mechanistic insight into metabolite accumulation in conditions such as neurodegenerative diseases and cancer. Our hypothesis is based on the demonstrated ability of metabolites to form amyloid-like structures in inborn error of metabolism disorders and the potential of such metabolite amyloids to promote protein aggregation. This notion can provide a new paradigm for neurodegeneration and cancer, as both conditions were linked to loss of function due to protein aggregation. Similar to the well-established observation of amyloid formation in many degenerative disorders, the formation of amyloids by tumour-suppressor proteins, including p53, was demonstrated in malignant states. Moreover, this new paradigm could fill the gap in understanding the high occurrence of specific types of cancer among genetic error of metabolism patients. This hypothesis offers a fresh view on the aetiology of some of the most abundant human maladies and may redirect the efforts towards new therapeutic developments.


2010 ◽  
Vol 191 (4) ◽  
pp. 741-749 ◽  
Author(s):  
Mathew P. Estey ◽  
Caterina Di Ciano-Oliveira ◽  
Carol D. Froese ◽  
Margaret T. Bejide ◽  
William S. Trimble

Septins are a family of GTP-binding proteins implicated in mammalian cell division. Most studies examining the role of septins in this process have treated the family as a whole, thus neglecting the possibility that individual members may have diverse functions. To address this, we individually depleted each septin family member expressed in HeLa cells by siRNA and assayed for defects in cell division by immunofluorescence and time-lapse microscopy. Depletion of SEPT2, SEPT7, and SEPT11 causes defects in the early stages of cytokinesis, ultimately resulting in binucleation. In sharp contrast, SEPT9 is dispensable for the early stages of cell division, but is critical for the final separation of daughter cells. Rescue experiments indicate that SEPT9 isoforms containing the N-terminal region are sufficient to drive cytokinesis. We demonstrate that SEPT9 mediates the localization of the vesicle-tethering exocyst complex to the midbody, providing mechanistic insight into the role of SEPT9 during abscission.


RSC Advances ◽  
2021 ◽  
Vol 11 (34) ◽  
pp. 20961-20969
Author(s):  
Yunqing He ◽  
Wanli Nie ◽  
Ying Xue ◽  
Qishan Hu

Hydrosilylation or amination products? It depends on water amount and nucleophiles like excess water or produced/added amines.


2021 ◽  
Vol 154 (12) ◽  
pp. 124313
Author(s):  
L. M. Hunnisett ◽  
P. F. Kelly ◽  
S. Bleay ◽  
F. Plasser ◽  
R. King ◽  
...  

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