Results 61 to 70 of about 3,689,678 (299)
European Journal of Medicinal Chemistry Reports, 2023 The accumulation, processing and toxicity of Aβ can be affected by interacting with transthyretin (TTR). We obtained 31 compounds with different structures by virtual screening based on protein structure.
Fantao Sun +5 more
doaj +1 more source
A Designed Protein Interface That Blocks Fibril Formation [PDF]
Journal of the American Chemical Society, 2004 Protein fibril formation is implicated in many diseases, and therefore much effort has been focused toward the development of inhibitors of this process. In a previous project, a monomeric protein was computationally engineered to bind itself and form a heterodimer complex following interfacial redesign.
Shukla, Ushma J. +4 more
openaire +3 more sources
Chiral separation of chloroalkanes with the chromatographic column onboard Martian rovers
FEBS Letters, EarlyView.Computer image of the Rosalind Franklin Rover of ESA's ExoMars mission. ExoMars is scheduled to land on planet Mars in Oxia Planum in 2029. This area represents an interesting spot to look for biosignatures. Investigations of ExoMars include measurement on molecular chirality. We show that chiral chloroalkanes, that have been identified on Mars, can be
Asma Merzougui +4 more
wiley +1 more source
Lysyl oxidase (LOX)‐mediated remodeling of the extracellular matrix
FEBS Letters, EarlyView.The lysyl oxidase (LOX) family of enzymes drives extracellular matrix remodeling by oxidizing collagen, elastin, and fibronectin, promoting covalent cross‐link formation. This activity regulates tissue architecture and mechanical properties, while its dysregulation contributes to fibrosis, cardiovascular disease, glaucoma, connective tissue disorders ...
Fernando Rodríguez‐Pascual +3 more
wiley +1 more source
Cryo-EM structure and polymorphism of Aβ amyloid fibrils purified from Alzheimer’s brain tissue
Nature Communications, 2019 Alzheimer’s disease is characterised by the deposition of Aβ amyloid fibrils and tau protein neurofibrillary tangles. Here the authors use cryo-EM to structurally characterise brain derived Aβ amyloid fibrils and find that they are polymorphic and right ...
Marius Kollmer +9 more
doaj +1 more source
Nanomaterials, 2021 The coupling of proteins that can assemble, recognise or mineralise specific inorganic species is a promising strategy for the synthesis of nanoscale materials with a controllable morphology and functionality.
Rocío Jurado, Natividad Gálvez
doaj +1 more source
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
Fracture of Protein Fibrils As Induced by Elongational Flow
, 2010 The length distribution of whey protein fibrils is important for application purposes. However, it is hard to influence the length distribution of whey protein fibrils during production.
Kroes-Nijboer, A. +3 more
core +1 more source
Fibronectin: Molecular Structure, Fibrillar Structure and Mechanochemical Signaling
Cells, 2021 The extracellular matrix (ECM) plays a key role as both structural scaffold and regulator of cell signal transduction in tissues. In times of ECM assembly and turnover, cells upregulate assembly of the ECM protein, fibronectin (FN).
Caleb J. Dalton, Christopher A. Lemmon
doaj +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