Results 41 to 50 of about 928,578 (204)

Smaller is better: nanobodies meet NMR

FEBS Letters, EarlyView.
Nanobodies are single‐domain antigen‐binding fragments derived from camelid heavy chain antibodies. Their small size, high stability, and exceptional specificity make nanobodies uniquely useful probes for NMR studies of protein dynamics, transient conformational states, and protein–protein interactions.
Oleg Y. Dmitriev
wiley   +1 more source

The role of autophagy in synucleinopathy: clearance versus spread of α-synuclein

Autophagy Reports
Emerging evidence suggests that the propagation of α-synuclein pathology underlies the progression of Parkinson’s disease and supports the hypothesis that transmission of α-synuclein aggregates contributes to dopaminergic degeneration.
Emily Birnbaum, Zhenyu Yue
doaj   +1 more source

Data_Sheet_1_Activated Endolysosomal Cation Channel TRPML1 Facilitates Maturation of α-Synuclein-Containing Autophagosomes.pdf

, 2022
Background: Protein aggregates are degraded via the autophagy-lysosome pathway and alterations in the lysosomal system leading to the accumulation of pathogenic proteins, including aggregates of α-synuclein in Parkinson’s disease (PD).
Natalia Rodriguez-Muela (13003398), Maike R. Pollmanns (13003389), Björn H. Falkenburger (3335691), Judith Beer (13003392), Ines Rosignol (13003395), Elisabeth Dinter (13003401)   +5 more
core   +1 more source

Invisible but not inaccessible—Revealing transient oligomers formed by intrinsically disordered proteins with solution NMR and complementary methods

FEBS Letters, EarlyView.
Transient oligomers formed by intrinsically disordered proteins may be ‘invisible’ to direct detection yet remain accessible to solution NMR through equilibrium‐exchange measurements and pressure‐jump experiments. Complementary methods report on mass, stoichiometry, selected distance distributions, morphology, and internal packing.
Martin D. Gelenter, Ad Bax
wiley   +1 more source

Inhibition of copper transporter 1 prevents α-synuclein pathology and alleviates nigrostriatal degeneration in AAV-based mouse model of Parkinson's disease

Redox Biology, 2021
The formation of α-synuclein aggregates is a major pathological hallmark of Parkinson's disease. Copper promotes α-synuclein aggregation and toxicity in vitro.
De-Hai Gou, Ting-Ting Huang, Wen Li, Xin-Di Gao, Caroline Haikal, Xin-He Wang, Dong-Yan Song, Xin Liang, Lin Zhu, Yong Tang, Chen Ding, Jia-Yi Li   +11 more
doaj   +1 more source

Fibrillar form of α-synuclein-specific scFv antibody inhibits α-synuclein seeds induced aggregation and toxicity

, 2022
Synucleinopathies including Parkinson’s disease (PD), dementia with Lewy bodies (DLB), and multiple system atrophy (MSA) are characterized by pathological accumulation of α-synuclein (α-syn).
Issam Hmila (9239059), Mohamed M. Emara (9913215), Vijay Gupta (209146), Tamas Lukacsovich (23182), Nishant N. Vaikath (2901785), Simona S. Ghanem (12267227), Nour K. Majbour (8809316), Houari B. Abdesselem (14152827), Indulekha P. Sudhakaran (9611154), Sara A. Abdulla (13902015), Safa Salim (9186786), Omar M. A. El-Agnaf (8809331), Daniel Erskine (3471959)   +12 more
core   +1 more source

Adenosine triphosphate as a modulator of protein interactions and stability

FEBS Open Bio, EarlyView.
ATP is best known as the cell's energy currency, but it also shapes how proteins fold, interact, aggregate and form biomolecular condensates. This review explains the emerging physical principles behind these effects, including weak binding to charged protein regions, magnesium‐dependent behaviour and concentration‐dependent control of protein ...
Shuyuan Tan, Robin Curtis
wiley   +1 more source

Figure 2. DJ-1Pox inhibits nucleation of α-synuclein

, 2019
Time-dependent visualisation of α-synuclein aggregation inhibition in presence of DJ-1Pox. The first five .jpk files represents normal aggregation pattern followed by α-synuclein (200 μM) and next five .jpk files represents amorphous like species when α ...
Tushar Maiti (6991979)
core   +1 more source

The C‐terminal domain of yeast Arginyltransferase1 is essential for its catalytic activity

FEBS Open Bio, EarlyView.
Arginyltransferase 1 (Ate1), a eukaryotic enzyme, catalyses arginylation, transferring arginine from tRNA‐Arg to the amino terminus of the target protein. Overexpression of Ate1 in yeast is lethal and is dependent on arginylation. This study elucidates how mutations in the cofactor‐binding and active site of Ate1 and truncation of its structural ...
Vikas Kumar Yadav, Shweta Shweta, Manisha Malhotra, Vikash Maurya, Akhilesh Kumar   +4 more
wiley   +1 more source

β-synuclein regulates the phase transitions and amyloid conversion of α-synuclein

Nature Communications
Parkinson’s disease (PD) and Dementia with Lewy Bodies (DLB) are neurodegenerative disorders characterized by the accumulation of α-synuclein aggregates. α-synuclein forms droplets via liquid-liquid phase separation (LLPS), followed by liquid-solid phase
Xi Li, Linwei Yu, Xikai Liu, Tianyi Shi, Yu Zhang, Yushuo Xiao, Chen Wang, Liangliang Song, Ning Li, Xinran Liu, Yuchen Chen, Robert B. Petersen, Xiang Cheng, Weikang Xue, Yanxun V. Yu, Li Xu, Ling Zheng, Hong Chen, Kun Huang   +18 more
doaj   +1 more source