Results 201 to 210 of about 4,734,550 (301)

Smaller is better: nanobodies meet NMR

open access: yesFEBS 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

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

open access: yesFEBS 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

Neutralization of the PTX3/CD44 axis suppresses TGF‐β1 signaling in kidney fibrosis

open access: yesFEBS Letters, EarlyView.
This study investigates how the PTX3/CD44 axis promotes kidney fibrosis by activating TGF‐β1 signaling. We demonstrate that the neutralizing antibody WHC‐001 effectively inhibits this pathway, suppressing myofibroblast activation and partial epithelial–mesenchymal transition (EMT).
Chao‐Chun Cheng   +8 more
wiley   +1 more source

Inhibition of dipeptidyl peptidase 7 impairs lysophagy in LLOMe‐treated HepG2 cells

open access: yesFEBS Letters, EarlyView.
DPP7 inhibition delays ubiquitin‐dependent lysophagy by attenuating ubiquitin accumulation and the recruitment of SQSTM1 and LC3 to damaged lysosomes, resulting in delayed clearance of damaged lysosomes and impaired restoration of lysosomal homeostasis. Created using FigureLabs (Certificate ID: FL‐PUB‐20260922‐Z99XNX).
Na Yeon Park   +8 more
wiley   +1 more source

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