Results 1 to 10 of about 754,932 (265)
Contractile protein biochemistry in the Pollard Lab in Baltimore [PDF]
Biophysical Reviews, 2018 John Cooper, , Kiehart Daniel P
exaly +2 more sources
AA amyloid fibrils from diseased tissue are structurally different from in vitro formed SAA fibrils
Nature Communications, 2021 Systemic AA amyloidosis is a protein misfolding disease caused by the formation of amyloid fibrils from serum amyloid A (SAA) protein. Here, the authors present the cryo-EM structures of AA amyloid fibrils isolated from mouse tissue and in vitro formed ...
Akanksha Bansal +8 more
doaj +1 more source
Cryo-EM structure of a catalytic amyloid fibril
Scientific Reports, 2023 Catalytic amyloid fibrils are novel types of bioinspired, functional materials that combine the chemical and mechanical robustness of amyloids with the ability to catalyze a certain chemical reaction.
Thomas Heerde +3 more
doaj +1 more source
Cryo-EM demonstrates the in vitro proliferation of an ex vivo amyloid fibril morphology by seeding
Nature Communications, 2022 Here, the authors present the cryo-EM structure of in vitro amyloid fibrils from recombinant SAA1.1 protein that were formed by seeding with fibrils purified from systemic AA amyloidosis tissue.
Thomas Heerde +12 more
doaj +1 more source
Nature Communications, 2021 Despite recent success in computational design of structured cyclic peptides, de novo design of cyclic peptides that bind to any protein functional site remains difficult.
Parisa Hosseinzadeh +17 more
doaj +1 more source
Exchange catalysis by tapasin exploits conserved and allele-specific features of MHC-I molecules
Nature Communications, 2021 Tapasin is part of the peptide loading complex necessary for presenting antigenic peptides on MHC-I for the induction of adaptive immunity. Here the authors show that tapasin interacts with MHC-I in both conserved and allele-specific regions to promote ...
Huan Lan +9 more
doaj +1 more source
Cryo-EM reveals structural breaks in a patient-derived amyloid fibril from systemic AL amyloidosis
Nature Communications, 2021 Systemic AL amyloidosis is a protein misfolding disease caused by the aggregation and fibrillation of immunoglobulin light chains (LCs). Here, the authors present the cryo-EM structures of λ3 LC-derived amyloid fibrils that were isolated from patient ...
Lynn Radamaker +8 more
doaj +1 more source
Peptide targeting of lysophosphatidylinositol-sensing GPR55 for osteoclastogenesis tuning
Cell Communication and Signaling, 2021 Background The G-protein-coupled receptor GPR55 has been implicated in multiple biological activities, which has fuelled interest in its functional targeting.
Maria Giovanna Mosca +4 more
doaj +1 more source
Improved protein structure refinement guided by deep learning based accuracy estimation
Nature Communications, 2021 Here the authors present DeepAccNet, a deep learning framework that estimates per-residue accuracy and residue-residue distance signed error in protein models, which are used to guide Rosetta protein structure refinement.
Naozumi Hiranuma +5 more
doaj +1 more source