Results 51 to 60 of about 160,241 (252)
mBio, 2023 Staphylococcus aureus secretes phenol-soluble modulins (PSMs), a family of small, amphipathic, secreted peptides with multiple biologic activities. Community-acquired S.
Xiaogang Wang +5 more
doaj +1 more source
Site-specific perturbations of alpha-synuclein fibril structure by the Parkinson's disease associated mutations A53T and E46K. [PDF]
, 2013 PMCID: PMC3591419This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited ...
Chad M Rienstra +33 more
core +2 more sources
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
Nanomechanical properties of single amyloid fibrils [PDF]
, 2012 Amyloid fibrils are traditionally associated with neurodegenerative diseases like Alzheimer's disease, Parkinson's disease or Creutzfeldt-Jakob disease. However, the ability to form amyloid fibrils appears to be a more generic property of proteins. While
Bennink, Martin L. +5 more
core +1 more source
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
Zinc–dysprosium functionalized amyloid fibrils [PDF]
Dalton Transactions, 2019 The heterometallic Zn 2 Dy 2 entity bearing partially saturated metal centres covalently decorates a highly ordered amyloid fibril core and the functionalised assembly exhibits catalytic Lewis acid behaviour.
Stavroula I. Sampani +4 more
openaire +3 more sources
The VHL tumor suppressor at the crossroad of protein folding, aggregation, and cancer
Molecular Oncology, EarlyView.Mutations, environmental stress, and chaperone dysfunction can destabilize pVHL, promoting its conversion from the native folded state into amyloid‐like assemblies. This transition may contribute to protein storage, cell dormancy, survival, and drug resistance.
Lara Abad +2 more
wiley +1 more source
Mechanisms and rates of nucleation of amyloid fibrils [PDF]
The Journal of Chemical Physics, 2017 The classical nucleation theory finds the rate of nucleation proportional to the monomer concentration raised to the power, which is the “critical nucleus size,” nc. The implicit assumption, that amyloids nucleate in the same way, has been recently challenged by an alternative two-step mechanism, when the soluble monomers first form a metastable ...
Cheng-Tai Lee, Eugene M. Terentjev
openaire +3 more sources
FEBS Open Bio, EarlyView.Repair of neuronal DNA damage in Alzheimer's disease by KCL‐286. (A) Amyloid‐β oligomers and plaques impair neuronal DNA repair pathways, leading to DNA double‐strand breaks and glial activation. (B) KCL‐286 activates RARβ/RXR signalling via retinoic acid response elements (RAREs), associated with increased BRCA1 expression, enhanced DNA repair and ...
Natasha Hill +6 more
wiley +1 more source
Cytochrome Display on Amyloid Fibrils
Journal of the American Chemical Society, 2006 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 monomers into a fibril. To display an array of biologically functional porphyrins on the surface of protein
Baldwin, A +5 more
openaire +3 more sources