Results 101 to 110 of about 3,403,581 (279)
Disulfide Bonding in Neurodegenerative Misfolding Diseases
International Journal of Cell Biology, 2013 In recent years an increasing number of neurodegenerative diseases has been linked to the misfolding of a specific protein and its subsequent accumulation into aggregated species, often toxic to the cell.
Maria Francesca Mossuto
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Reporters of amyloid structural polymorphism
, 2014 Misfolding of proteins induced by environmental conditions or by the presence of destabilizing mutations often triggers squestration (aggresome formation) or cellular removal (unfolded protein response (UPR), autophagy) intracellular responses ...
Nilsson, Peter, +2 more
core
A Portal‐Preorganized Cucurbit[7]uril‐Ruthenium Conjugate Enables Motif‐Selective Protein Sensing
Angewandte Chemie International Edition, EarlyView.Reprogramming cucurbit[7]uril (CB7) recognition through portal engineering transforms an optically silent host into a motif‐selective photoluminescent receptor. The portal‐preorganized CB7‐Rubpy conjugate directly reports changes in aromatic motif accessibility, enabling optical sensing of protein misfolding and refolding.
Patrick Gruhs +10 more
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Applied SciencesProtein misfolding and aggregation represent key pathological mechanisms in neurodegenerative and systemic amyloid disorders, yet disease-modifying therapeutic strategies remain limited.
Corina Dalia Toderescu +5 more
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Disulfide Bond–Modified Proteomics Reveals the Effects of Riboflavin on Protein Folding Dynamics
Animal Research and One Health, EarlyView.Riboflavin deficiency impairs oxidative protein folding, causing ER misfolded protein accumulation, CHOP activation, and apoptosis, revealing a role of riboflavin in proteostasis. ABSTRACT Riboflavin is a crucial micronutrient essential for maintaining cellular homeostasis, acting as an important precursor for flavoproteins that utilize flavin ...
Bo Zhang, Shuisheng Hou, Jing Tang
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Biochemistry and Molecular Biology Education, Volume 53, Issue 2, Page 209-217, March/April 2025.Abstract We created a novel laboratory experience where undergraduate students explore the techniques used to study protein misfolding, unfolding, and aggregation. Despite the importance of protein misfolding and aggregation diseases, protein unfolding is not typically explored in undergraduate biochemistry laboratory classes.
Alison Bates +2 more
wiley +1 more source
Bridging the translational gap in clinical nanomedicine: From rational design to clinical reality
BMEMat, EarlyView.Nanotechnology offers a multi‐faceted approach to modern healthcare, encompassing high‐sensitivity diagnostic imaging, innovative vaccine delivery, and targeted therapeutics. This review explores how these nanomedicine applications address critical challenges in cancer recurrence and the treatment of neurologic and respiratory diseases to combat rising
Ahmed H. Ghonaim +9 more
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Biochemistry and Biophysics ReportsSignal peptides are a sequence of peptides located at the N-terminus of proteins and determine the protein secretion pathway and their destinations. The N-region is positively charged and influences the orientation of translocation.
Natalie G. Horgan +3 more
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Nanoimaging for protein misfolding diseases
, 2010 Misfolding and aggregation of proteins are widespread phenomena leading to the development of numerous neurodegenerative disorders such as Parkinson\u27s, Alzheimer\u27s, and Huntington\u27s diseases.
Junping Yu +7 more
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Chemistry – A European Journal, EarlyView.Balancing Act: Se─M bond serving as the fulcrum of the balance scale to compare the different weight of toxicity and therapeutic effects in biological environment. ABSTRACT The synthesis and characterization of organo‐selenium compounds have attracted considerable interest for decades, driven by the search for efficient catalysts and bioinspired ...
Matteo Filippi +6 more
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