Results 61 to 70 of about 3,632,451 (277)

Structure-Function Analysis of the Curli Accessory Protein CsgE Defines Surfaces Essential for Coordinating Amyloid Fiber Formation

open access: yesmBio, 2018
Curli amyloid fibers are produced as part of the extracellular biofilm matrix and are composed primarily of the major structural subunit CsgA. The CsgE chaperone facilitates the secretion of CsgA through CsgG by forming a cap at the base of the nonameric
Roger D. Klein   +13 more
doaj   +1 more source

Engineering peptides into antibodies—opportunities and strategies for therapeutic innovation

open access: yesFEBS Letters, EarlyView.
Peptides and antibodies occupy complementary therapeutic niches. Peptides recognize difficult targets in a compact format, while antibodies add specificity, long half‐life, and effector functions. This review examines strategies that merge both modalities—peptide grafting into loops, terminal and Fc fusions, and bioconjugation—highlighting how ...
Jinling Wang   +2 more
wiley   +1 more source

Molecular Modulators of Bacterial Functional Amyloid Assembly. [PDF]

open access: yes, 2015
Amyloid formation is historically associated with protein misfolding and is the hallmark of many neurodegenerative conditions. A new class of “functional amyloids” has recently emerged that has transformed that amyloid field.
Evans, Margery Lee
core   +6 more sources

The Evolution of Functional Amyloids and Their Impact on Host–Microbe Interactions

open access: yesAdvanced Science
Amyloids are highly ordered β‐sheet‐rich structures that are well conserved across the domains of life. Amyloids have a unique repetitive structure that enables autocatalytic self‐replication.
Divya Kolli   +3 more
doaj   +1 more source

β-microglobulin amyloid fibril-induced membrane disruption is enhanced by endosomal lipids and acidic pH [PDF]

open access: yes, 2014
Although the molecular mechanisms underlying the pathology of amyloidoses are not well understood, the interaction between amyloid proteins and cell membranes is thought to play a role in several amyloid diseases. Amyloid fibrils of β-microglobulin (βm),
Eric W. Hewitt   +49 more
core   +1 more source

Autophagy and mitophagy in pancreatic β‐cell homeostasis and their involvement in diabetes pathophysiology

open access: yesFEBS Letters, EarlyView.
This review focuses on the role of autophagy and mitophagy in maintaining pancreatic β‐cell function and homeostasis. We discuss how genetic defects affecting these pathways contribute to the development of type 1, type 2, monogenic, and gestational diabetes. We further explore their potential as therapeutic targets. Created in BioRender.
Yunkyeong Lee   +2 more
wiley   +1 more source

Leucine‐rich glioma inactivated 1 (LGI1) is a ganglioside‐binding protein

open access: yesFEBS Letters, EarlyView.
Neuronal hyperexcitability associated with a decrease/absence of the extracellular protein LGI1 has been suggested to be primarily due to the downregulation of Kv1 channel expression. The molecular mechanisms underlying this decrease have not yet been elucidated.
Kévin Debreux   +7 more
wiley   +1 more source

Does the Hfq Protein Contribute to RNA Cargo Translocation into Bacterial Outer Membrane Vesicles?

open access: yesPathogens
Gram-negative bacteria release outer membrane vesicles (OMVs) that deliver various molecules, including virulence factors, to interact with their host.
Marisela Velez, Véronique Arluison
doaj   +1 more source

A Computational Study of Amyloid Fibrils and their Structural Properties [PDF]

open access: yes, 2017
The term amyloid describes misfolded protein aggregates in which a highly ordered cross β-sheet pattern is adopted. While there exist functional amyloids, the majority of known amyloids are associated with diseases in multicellular organisms.
Alred, Erik
core  

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

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