Results 61 to 70 of about 91,213 (314)

Sequence determinants of RNA G‐quadruplex unfolding by Arg‐rich regions

FEBS Letters, EarlyView.
We show that Arg‐rich peptides selectively unfold RNA G‐quadruplexes, but not RNA stem‐loops or DNA/RNA duplexes. This length‐dependent activity is inhibited by acidic residues and is conserved among SR and SR‐related proteins (SRSF1, SRSF3, SRSF9, U1‐70K, and U2AF1).
Naiduwadura Ivon Upekala De Silva, Puspa Kunwar, Md Ibnul Rifat Rahman, Joanna Koryo Kwao, Nathan Lehman, Zihan Zhang, Trenton Paul, Claire Cheng, Nicholas Truex, Hui‐Ting Lee, Jun Zhang   +10 more
wiley   +1 more source

Revisiting protein aggregation as pathogenic in sporadic Parkinson and Alzheimer diseases. [PDF]

, 2019
The gold standard for a definitive diagnosis of Parkinson disease (PD) is the pathologic finding of aggregated α-synuclein into Lewy bodies and for Alzheimer disease (AD) aggregated amyloid into plaques and hyperphosphorylated tau into tangles.
Brundin, P, Cambi, F, Espay, AJ, Fasano, A, Fernandez, HH, Gan-Or, Z, Greenamyre, JT, Josephs, KA, Kauffman, MA, Lang, AE, Leverenz, JB, Litvan, I, Marsili, L, Mata, IF, Merola, A, Morgante, F, Perry, G, Sardi, SP, Savica, R, Schwarzschild, MA, Sherer, T, Simon, DK, Standaert, DG, Tanner, CM, Vizcarra, JA, Yamasaki, TR, Zabetian, CP   +26 more
core   +3 more sources

MOESM1 of α-Synuclein conformational strains spread, seed and target neuronal cells differentially after injection into the olfactory bulb

, 2019
Additional file 1. Quality control of the assemblies.
Rey, Nolwen, Bousset, Luc, George, Sonia, Madaj, Zachary, Meyerdirk, Lindsay, Schulz, Emily, Steiner, Jennifer, Melki, Ronald, Brundin, Patrik   +8 more
openaire   +1 more source

Interplay between RNA‐protein interactions and RNA structures in gene regulation

FEBS Open Bio, EarlyView.
Methodological advances in mapping transcriptome‐wide RNA‐protein interactions and RNA structures have started to uncover the potential of RNP conformations in gene regulation. Competing RNA–RNA, RNA‐protein and protein–protein interactions shape the compaction and function of RNPs throughout their lifetime and may provide novel therapeutic targets in ...
Jenni Rapakko, Mauro Scaravilli, Minna‐Liisa Änkö   +2 more
wiley   +1 more source

Differential microglial responses to structurally distinct alpha-synuclein polymorphs

Molecular Brain
Synucleinopathies are age-related neurological disorders which include dementia with Lewy bodies (DLB), Parkinson’s disease (PD), and multiple system atrophy (MSA).
Katherine Chang, Jina Kim, Michiyo Iba, Jae-Hyeon Park, Alexandria Beilina, Zulfeqhar A. Syed, Valentina Baena, Liam Horan-Portelance, Mark R. Cookson, Sungyong You, Changyoun Kim   +10 more
doaj   +1 more source

α-Synuclein pathology from the body to the brain: so many seeds so close to the central soil

Neural Regeneration Research
α-Synuclein is a protein that mainly exists in the presynaptic terminals. Abnormal folding and accumulation of α-synuclein are found in several neurodegenerative diseases, including Parkinson’s disease.
Yunying Yang, Zhentao Zhang
doaj   +1 more source

Assembly of α-synuclein and neurodegeneration in the central nervous system of heterozygous M83 mice following the peripheral administration of α-synuclein seeds

Acta Neuropathologica Communications, 2021
Peripheral administration (oral, intranasal, intraperitoneal, intravenous) of assembled A53T α-synuclein induced synucleinopathy in heterozygous mice transgenic for human mutant A53T α-synuclein (line M83).
Jennifer A. Macdonald, John L. Chen, Masami Masuda-Suzukake, Manuel Schweighauser, Zane Jaunmuktane, Thomas Warner, Janice L. Holton, Annabelle Grossman, Richard Berks, Isabelle Lavenir, Michel Goedert   +10 more
doaj   +1 more source

GM1 Ganglioside Modifies α-Synuclein Toxicity and is Neuroprotective in a Rat α-Synuclein Model of Parkinson\u27s Disease. [PDF]

, 2019
While GM1 may interact with α-synuclein in vitro to inhibit aggregation, the ability of GM1 to protect against α-synuclein toxicity in vivo has not been investigated.
Aras, Radha, Brotchie, Jonathan M., Koprich, James B., Schneider, Jay S., Singh, Vikrant, Williams, Courtney K.   +5 more
core   +1 more source

Accumulation of oligomer-prone α-synuclein exacerbates synaptic and neuronal degeneration in vivo [PDF]

, 2016
The toxicity of α-synuclein invivo is not well understood. Rockenstein etal. describe an α-synuclein transgenic model expressing the E57K mutant that forms stable oligomers. They show that oligomers accumulate at synapses and that the mutation interferes
Adame, Anthony, Campioni, Silvia, Gage, Fred H., Gerez, Juan, Jensen, Poul H., Mante, Michael, Masliah, Eliezer, Nuber, Silke, Overk, Cassia R., Patrick, Christina, Picotti, Paola, Riek, Roland, Rockenstein, Edward, Trejo-Morales, Margarita, Ubhi, Kiren, Winkler, Jürgen, Winner, Beate   +16 more
core   +2 more sources

The role of lipid metabolism in neuronal senescence

FEBS Open Bio, EarlyView.
Disrupted lipid metabolism, through alterations in lipid species or lipid droplet accumulation, can drive neuronal senescence. However, lipid dyshomeostasis can also occur alongside neuronal senescence, further amplifying tissue damage. Delineating how lipid‐induced senescence emerges in neurons and glial cells, and how it contributes to ageing and ...
Dikaia Tsagkari, Eleftheria Panagiotidou, Nektarios Tavernarakis   +2 more
wiley   +1 more source