Results 161 to 170 of about 288,605 (343)

A Computational Study of Amyloid Fibrils and their Structural Properties [PDF]

open access: yes, 2017
The term amyloid describes misfolded protein aggregates in which a highly ordered cross β-sheet pattern is adopted. While there exist functional amyloids, the majority of known amyloids are associated with diseases in multicellular organisms.
Alred, Erik
core  

Recent Advances (2023–2025) of Capillary Electrophoresis‐Mass Spectrometry (CE‐MS) for Top‐Down Proteomics

open access: yesMass Spectrometry Reviews, EarlyView.
ABSTRACT Top‐down proteomics (TDP) characterizes proteoforms in cells, tissues, and biofluids, in discovery mode and on a global scale, requiring analytical tools with high peak capacity for proteoform separation and high sensitivity for proteoform detection, given the extremely high proteoform complexity and wide proteoform concentration dynamic range.
Guijie Zhu   +5 more
wiley   +1 more source

Tracking Genetic Parkinson's Disease with Molecular Imaging: A Systematic Review

open access: yesMovement Disorders Clinical Practice, EarlyView.
Abstract Background Parkinson's disease (PD) is a worldwide, complex neurodegenerative disorder influenced by both genetic and environmental factors. Around 15–20% of PD cases are linked to genetic mutations, providing insights into the disease's pathogenesis.
Chiara Meneghini   +5 more
wiley   +1 more source

Co‐ and Multi‐Pathologies in Parkinson's Disease: An International Parkinson and Movement Disorder Society Scientific Issues Committee Review

open access: yesMovement Disorders, EarlyView.
Abstract Parkinson's disease (PD) has been historically defined as a disease of striatal dopamine deficiency secondary to degeneration of dopaminergic neurons in the substantia nigra pars compacta, related to the presence of Lewy bodies and Lewy neurites.
Michele Matarazzo   +10 more
wiley   +1 more source

Cytochrome Display on Amyloid Fibrils

open access: yes, 2016
Protein amyloid fibrils can be functionalized by coating the core protofilament with high concentrations of proteins and enzymes. This can be done elegantly by appending a functional domain to an amyloidogenic protein monomer, then assembling the ...
John Christodoulou (450398)   +5 more
core   +1 more source

Seeing Invisible Oligomers: Rethinking α‐Synuclein Pathology Through Proximity Ligation Assay

open access: yesMovement Disorders, EarlyView.
Abstract Parkinson's disease (PD) and multiple system atrophy are defined by α‐synuclein (αSYN)‐positive inclusions – Lewy bodies (LBs) and glial cytoplasmic inclusions – yet mounting evidence indicates that these inclusions represent only a fraction of disease‐relevant pathology.
Hiroaki Sekiya   +3 more
wiley   +1 more source

Structural and dynamical properties of central nervous system proteins with pharmaceutical and biotechnological potential.

open access: yes, 2010
Neurodegenerative diseases are widespread pathologies of large social impact that include: prion, Alzheimer and Parkinson disease, Huntington chorea and amyotrophic lateral sclerosis.
Stanzione, Francesca
core  

Heterogenous Neuropathology in a Pedigree with RAB39B‐Related Parkinson's Disease

open access: yesMovement Disorders, EarlyView.
Abstract Background In 2015, we reported a family with Parkinson's disease resulting from the RAB39B p.G192R (c.574G>A) variant. Since then, two affected brothers from the family have undergone autopsy. Objectives To characterize neuropathological findings, assess intracellular distribution of RAB39B protein, and examine the effect of p.G192R on α ...
Caitlin Latimer   +15 more
wiley   +1 more source

Interactions of Amyloid Fibrils with Functional Proteins: Modulating Effect of Polyphenols

open access: yesEast European Journal of Physics
The elucidation of interactions between functional proteins and amyloid fibrils is crucial for understanding the molecular basis of amyloid diseases, which are characterized by protein misfolding and aggregation.
Valeriya Trusova   +2 more
doaj   +1 more source

Protein mis-folding and human disease

open access: yes, 2010
Serum Amyloid P Component (SAP), a putative molecular chaperone, is a homopentamericplasma protein of 25kDa subunits. It binds to the amyloid fibrils ofmisfolded proteins, which cause amyloidosis in humans. SAP not only stabilizesamyloid fibrils but also
Pal, Mohinder
core  

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