Results 51 to 60 of about 3,255,404 (222)

Nanomaterials: amyloids reflect their brighter side

, 2011
Amyloid fibrils belong to the group of ordered nanostructures that are self-assembled from a wide range of polypeptides/proteins. Amyloids are highly rigid structures possessing a high mechanical strength.
Mankar, Shruti, Shruti Mankar, Sen, Shamik, Shamik Sen, Anoop, A., Samir K. Maji, Maji, Samir K., A. Anoop   +7 more
core   +1 more source

Biological Functions of Prokaryotic Amyloids in Interspecies Interactions: Facts and Assumptions

, 2020
Amyloids are fibrillar protein aggregates with an ordered spatial structure called “cross-β”. While some amyloids are associated with development of approximately 50 incurable diseases of humans and animals, the others perform various ...
Anton A. Nizhnikov, Kirill S. Antonets, Anastasiia O. Kosolapova, Mikhail V. Belousov   +3 more
core   +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

Structural Mimicry in Microbial and Antimicrobial Amyloids

, 2022
The remarkable variety of microbial species of human pathogens and microbiomes generates significant quantities of secreted amyloids, which are structured protein fibrils that serve diverse functions related to virulence and interactions with the host ...
Engelberg, Yizhaq, Landau, Meytal, Golan, Nimrod, Nimrod Golan, Yizhaq Engelberg, Meytal Landau   +5 more
core   +1 more source

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

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

Structural insights into Escherichia coli CsgA amyloid fibril assembly revisited

mBio
Curli are a widespread component of proteobacterial biofilms. They are functional amyloid fibers that aid in structuring the extracellular matrix that surrounds these multicellular communities. As a functional amyloid, they are the product of a dedicated
Mike Sleutel, Han Remaut
doaj   +1 more source

Fold modulating function: Bacterial toxins to functional amyloids

Frontiers in Microbiology, 2014
Many bacteria produce cytolytic toxins that target host cells or other competing microbes. It is well known that environmental factors control toxin expression, however recent work suggests that some bacteria manipulate the fold of these protein toxins ...
Adnan Khawaja Syed, Blaise R Boles
doaj   +1 more source

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

FEBS 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, Inho Kwon, Yong Hwan Kim, Ji‐Eun Bae, Joon Bum Kim, Seong Hyun Kim, Sungho Maeng, Doo Sin Jo, Dong‐Hyung Cho   +8 more
wiley   +1 more source

The Physiological and Pathological Implications of the Formation of Hydrogels, with a Specific Focus on Amyloid Polypeptides

Biomolecules, 2017
Hydrogels are water-swollen and viscoelastic three-dimensional cross-linked polymeric network originating from monomer polymerisation. Hydrogel-forming polypeptides are widely found in nature and, at a cellular and organismal level, they provide a wide ...
Létitia Jean, Alex C. Foley, David J. T. Vaux   +2 more
doaj   +1 more source

A gut bacterial amyloid promotes α-synuclein aggregation and motor impairment in mice

eLife, 2020
Amyloids are a class of protein with unique self-aggregation properties, and their aberrant accumulation can lead to cellular dysfunctions associated with neurodegenerative diseases. While genetic and environmental factors can influence amyloid formation,
Timothy R Sampson, Collin Challis, Neha Jain, Anastasiya Moiseyenko, Mark S Ladinsky, Gauri G Shastri, Taren Thron, Brittany D Needham, Istvan Horvath, Justine W Debelius, Stefan Janssen, Rob Knight, Pernilla Wittung-Stafshede, Viviana Gradinaru, Matthew Chapman, Sarkis K Mazmanian   +15 more
doaj   +1 more source