Calorimetry and FTIR reveal the ability of URG7 protein to modify the aggregation state of both cell lysate and amylogenic α-synuclein

Calorimetry and FTIR reveal the ability of URG7 protein to modify the aggregation state of both cell lysate and amylogenic α-synuclein

Differential scanning calorimetry and FITR analyses allowed to investigate the role of URG7 (up-regulated gene clone 7) protein involved in the development of hepatocellular carcinoma induced by hepatitis B virus infection, on the physical structure both of lysates of human hepatoblastoma cells (Hep...

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Bibliographic Details
Main Authors: Jany Dandurand, Angela Ostuni, Maria Francesca Armentano, Maria Antonietta Crudele, Vincenza Dolce, Federica Marra, Valérie Samouillan, Faustino Bisaccia
Format: Article
Language:English
Published: AIMS Press 2020-06-01
Series:AIMS Biophysics
Subjects:
urg7
differential scanning calorimetry
physical structure
interfacial water
protein aggregation
synuclein
Online Access:https://www.aimspress.com/article/10.3934/biophy.2020015/fulltext.html

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https://www.aimspress.com/article/10.3934/biophy.2020015/fulltext.html

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