Perspectives on evolutionary and functional importance of intrinsically disordered proteins
Structural biology of proteins emphasises that proteins ought to have an ordered structure to
perform their biological role optimally. The over-reliance on the ordered structure of proteins …
perform their biological role optimally. The over-reliance on the ordered structure of proteins …
Advances in protein misfolding, amyloidosis and its correlation with human diseases
Protein aggregation, their mechanisms and trends in the field of neurodegenerative
diseases is still far from completely being decoded. It is mainly attributed to the complexity …
diseases is still far from completely being decoded. It is mainly attributed to the complexity …
Efficient production of 2-keto-L-gulonic acid from D-glucose in Gluconobacter oxydans ATCC9937 by mining key enzyme and transporter
G Li, D Li, W Zeng, Z Qin, J Chen, J Zhou - Bioresource Technology, 2023 - Elsevier
Direct production of 2-keto-L-gulonic acid (2-KLG, the precursor of vitamin C) from D-
glucose through 2, 5-diketo-D-gluconic acid (2, 5-DKG) is a promising alternative route. To …
glucose through 2, 5-diketo-D-gluconic acid (2, 5-DKG) is a promising alternative route. To …
Functionalisation of polyvinylpyrrolidone on gold nanoparticles enhances its anti-amyloidogenic propensity towards hen egg white lysozyme
Protein amyloids are characterized by aggregates that usually consist of fibres containing
misfolded proteins and having a cross β-sheet conformation. These aggregates can …
misfolded proteins and having a cross β-sheet conformation. These aggregates can …
Proline functionalized gold nanoparticles modulates lysozyme fibrillation
Amyloid fibrils are the hallmarks of neurodegenerative diseases like Alzheimer's,
Parkinson's and other proteopathies. Inhibition of fibrillation is a potential strategy to check …
Parkinson's and other proteopathies. Inhibition of fibrillation is a potential strategy to check …
Curcumin's pre-incubation temperature affects its inhibitory potency toward amyloid fibrillation and fibril-induced cytotoxicity of lysozyme
KN Liu, CM Lai, YT Lee, SN Wang, RPY Chen… - … et Biophysica Acta (BBA …, 2012 - Elsevier
BACKGROUND: More than twenty-seven human proteins can fold abnormally to form
amyloid deposits associated with a number of degenerative diseases. The research …
amyloid deposits associated with a number of degenerative diseases. The research …
Effect of sodium tetrathionate on amyloid fibril: Insight into the role of disulfide bond in amyloid progression
Tissue deposition of fibrillar protein aggregates called amyloid is the root cause of several
degenerative diseases. Thus identification of compounds which can prevent or reduce …
degenerative diseases. Thus identification of compounds which can prevent or reduce …
Rottlerin dissolves pre-formed protein amyloid: A study on hen egg white lysozyme
BACKGROUND: Deposition of protein fibrillar aggregates called amyloids in the tissue, is
the principal cause of several degenerative diseases. Here, we have shown the …
the principal cause of several degenerative diseases. Here, we have shown the …
Copper (II) directs formation of toxic amorphous aggregates resulting in inhibition of hen egg white lysozyme fibrillation under alkaline salt-mediated conditions
Hen egg white lysozyme (HEWL) adopts a molten globule-like state at high pH (~ 12.75) and
is found to form amyloid fibrils at alkaline pH. Here, we report that Cu (II) inhibits self …
is found to form amyloid fibrils at alkaline pH. Here, we report that Cu (II) inhibits self …
[HTML][HTML] Crowded milieu prevents fibrillation of hen egg white lysozyme with retention of enzymatic activity
Molten globule state plays a crucial role in the amyloidogenesis of several proteins. Hen egg
white lysozyme (HEWL) acquires a molten globule state at alkaline pH (12.75). Our study …
white lysozyme (HEWL) acquires a molten globule state at alkaline pH (12.75). Our study …