Results 91 to 100 of about 160,241 (252)

Probing the Energy Landscape of α‐Synuclein Amyloid Fibril Formation by Systematic K‐to‐Q Mutagenesis

Advanced Science, EarlyView.
We use lysine‐to‐glutamine mutations to study the effect of electrostatics on the kinetics and thermodynamics of alpha‐synuclein amyloid fibril formation. We find that mutational effects map on their structural context within fibrils and identify residues that modulate the energy landscape of alpha‐synuclein self‐assembly. Our work outlines a scalable,
Antonin Kunka, Azad Farzadfard, Jacob Aunstrup Larsen, Rasmus Krogh Norrild, Federica Saraceno, Celia Fricke, Hossein Mohammad‐Beigi, Ahmed Sadek, Jonas Folke, Susana Aznar, Alexander K. Buell   +10 more
wiley   +1 more source

Molecular Details of RNA Interactions With FUS Condensates Altering Assembly, Dynamics, and Aggregation

Angewandte Chemie, EarlyView.
Using NMR and molecular simulations, we map how RNA engages FUS LC‐RGG1 within condensates through electrostatic, π‐stacking, and polar contacts. These multivalent RNA contacts help stabilize RNA within FUS condensates while also reshaping condensate composition and dynamics.
Tongyin Zheng, Kandarp A. Sojitra, Samara Cummings, Qizan Chen, Priyesh Mohanty, Jeetain Mittal, Nicolas L. Fawzi   +6 more
wiley   +2 more sources

Toxic species in amyloid disorders: Oligomers or mature fibrils

Annals of Indian Academy of Neurology, 2015
Protein aggregation is the hallmark of several neurodegenerative disorders. These protein aggregation (fibrillization) disorders are also known as amyloid disorders. The mechanism of protein aggregation involves conformation switch of the native protein,
Meenakshi Verma, Abhishek Vats, Vibha Taneja   +2 more
doaj   +1 more source

Temporal Trajectories of the Tau Aggregate Interactome Reveal Stage‐Specific Vulnerabilities in Alzheimer's Disease

Advanced Science, EarlyView.
Tau populations with different aggregation states associate with distinct sets of proteins in the Alzheimer's disease brain. Proteomic discovery combined with single‐molecule analysis in neurons reveals dynamic associations involving proteostasis, metabolism and RNA biology.
Dorothea Böken, Paula Beltran Lobo, Yunzhao Wu, Lyla A. Rowe, Emre Fertan, Cara L. Croft, Maria Jimenez‐Sanchez, Dezerae Cox, David Klenerman   +8 more
wiley   +1 more source

Supramolecular Assembly of an Antimicrobial Peptide Into a Pore

Angewandte Chemie, EarlyView.
Supramolecular assembly of an AMP is linked to transport across the Staphylococcus aureus membrane. ABSTRACT Antimicrobial peptides (AMPs) have long been ascribed the ability to form pores. These structures, some observed, others inferred, vary in their mechanisms of action, though most are associated with lysis.
Kathyana Deeyagahage, Poonam Dhindwal, Michal T. Boniecki, Antonio Ruzzini   +3 more
wiley   +2 more sources

AL amyloidosis with non-amyloid forming monoclonal immunoglobulin deposition; a case mimicking AHL amyloidosis

BMC Nephrology, 2018
Background Immunoglobulin heavy-and-light-chain amyloidosis (AHL amyloidosis) is a newly established disease entity where both the immunoglobulin heavy-chain and light-chain compose amyloid fibrils. The immunoglobulins responsible for the amyloid fibrils
Shun Manabe, Chihiro Iwasaki, Michiyasu Hatano, Fuyuki Kametani, Masahide Yazaki, Kosaku Nitta, Michio Nagata   +6 more
doaj   +1 more source

On the reversibility of amyloid fibril formation

Biophysics Reviews
Amyloids are elongated supramolecular protein self-assemblies. Their formation is a non-covalent assembly process and as such is fully reversible. Amyloid formation is associated with several neurodegenerative diseases, and the reversibility is key to maintaining the healthy state.
Tinna Pálmadóttir, Josef Getachew, Lei Ortigosa-Pascual, Emil Axell, Jiapeng Wei, Ulf Olsson, Tuomas P. J. Knowles, Sara Linse   +7 more
openaire   +2 more sources

Zinc Fingers as Programmable Metalloprotein Scaffolds for Altering Pathogenic Biomolecular Phase Transitions

Advanced Science, EarlyView.
Modular zinc finger (ZF) metalloproteins function as programmable biomolecular scaffolds that modulate pathogenic amyloid assembly. Through direct protein–protein interactions, ZF arrays alter amyloid phase behavior and redirect β‐sheet fibrillization toward nontoxic aggregates.
Seongmin Park, Yunha Hwang, Jimin Kwak, Yuxi Lin, Hye‐Yeon Park, Eunju Nam, Jiyeon Han, Soyeon Park, Hyunyong Kim, Ju‐Eun Kim, Hyun Goo Kang, Jiyong Park, Young‐Ho Lee, Kyoung‐Shim Kim, Chul‐Ho Lee, Seung Jae Lee, Mi Hee Lim   +16 more
wiley   +1 more source

Preserving Proton Resolution Under Cryogenic Dynamic Nuclear Polarization for Biomolecular Solid‐State NMR

Angewandte Chemie, EarlyView.
High‐resolution proton detection is preserved under cryogenic dynamic nuclear polarization (DNP) by combining fast MAS, extensive deuteration and selective methyl protonation. This strategy enables proton‐detected structural studies of biomolecular solids with enhanced sensitivity under DNP conditions.
James Tolchard, Tanguy Le Marchand, Nadia El Mammeri, Kshama Sharma, Ajit Kumar Bishoyi, Mélanie Berbon, Kristaps Jaudzems, Dorothea Wisser, Asen Daskalov, Sven J. Saupe, Jan Stanek, Zhiyu Sun, Olivier Ouari, Birgit Habenstein, Anne Lesage, Guido Pintacuda, Antoine Loquet   +16 more
wiley   +2 more sources

Serum amyloid P colocalizes with apolipoproteins in human atheroma: functional implicationss⃞

Journal of Lipid Research, 2007
Serum amyloid P (SAP) is a common component of human amyloid deposits and has been identified in atherosclerotic lesions. We investigated the extent of the colocalization of SAP with apolipoprotein A-I (apoA-I), apoB, apoC-II, and apoE in human coronary ...
Cameron R. Stewart, Antonio Haw, III, Roland Lopez, Thomas O. McDonald, Judy M. Callaghan, Malcolm J. McConville, Kathryn J. Moore, Geoffrey J. Howlett, Kevin D. O'Brien   +8 more
doaj   +1 more source