Results 31 to 40 of about 6,595 (270)

CRISPRi-mediated suppression of E. coli Nissle 1917 virulence factors: A strategy for creating an engineered probiotic using csgD gene suppression

open access: yesFrontiers in Nutrition, 2022
BackgroundBiofilm formation is a complex phenomenon, and it is the causative agent of several human infections. Bacterial amyloids are involved in biofilm formation leading to infection persistence.
Mohd W. Azam, Asad U. Khan
doaj   +1 more source

Amyloid prions in fungi [PDF]

open access: yes, 2016
Prions are infectious protein polymers that have been found to cause fatal diseases in mammals. Prions have also been identified in fungi (yeast and filamentous fungi), where they behave as cytoplasmic non-Mendelian genetic elements.
Aguzzi   +122 more
core   +2 more sources

Bacterial mimetics of endocrine secretory granules as immobilized in vivo depots for functional protein drugs [PDF]

open access: yes, 2016
Altres ajuts: MARATOTV3/2013/3930In the human endocrine system many protein hormones including urotensin, glucagon, obestatin, bombesin and secretin, among others, are supplied from amyloidal secretory granules.
Abasolo, Ibane   +15 more
core   +2 more sources

Self-assembling dipeptide antibacterial nanostructures with membrane disrupting activity. [PDF]

open access: yes, 2017
Peptide-based supramolecular assemblies are a promising class of nanomaterials with important biomedical applications, specifically in drug delivery and tissue regeneration.
Adler-Abramovich, Lihi   +10 more
core   +3 more sources

Blessings in disguise: biological benefits of prion-like mechanisms [PDF]

open access: yes, 2013
Prions and amyloids are often associated with disease, but related mechanisms provide beneficial functions in nature. Prion-like mechanisms (PriLiMs) are found from bacteria to humans, where they alter the biological and physical properties of prion-like
Lindquist, Susan, Newby, Gregory Arthur
core   +1 more source

The Poly-Histidine Tag H6 Mediates Structural and Functional Properties of Disintegrating, Protein-Releasing Inclusion Bodies

open access: yesPharmaceutics, 2022
The coordination between histidine-rich peptides and divalent cations supports the formation of nano- and micro-scale protein biomaterials, including toxic and non-toxic functional amyloids, which can be adapted as drug delivery systems.
Julieta María Sánchez   +10 more
doaj   +1 more source

Bacterial curli protein promotes the conversion of PAP248-286 into the amyloid SEVI: cross-seeding of dissimilar amyloid sequences [PDF]

open access: yes, 2013
Fragments of prostatic acid phosphatase (PAP248-286) in human semen dramatically increase HIV infection efficiency by increasing virus adhesion to target cells.
Apostol   +67 more
core   +1 more source

Bacterial inclusion bodies are industrially exploitable amyloids [PDF]

open access: yesFEMS Microbiology Reviews, 2018
Understanding the structure, functionalities and biology of functional amyloids is an issue of emerging interest. Inclusion bodies, namely protein clusters formed in recombinant bacteria during protein production processes, have emerged as unanticipated, highly tunable models for the scrutiny of the physiology and architecture of functional amyloids ...
Ario de Marco   +9 more
openaire   +2 more sources

In vivo synthesis of bacterial amyloid curli contributes to joint inflammation during S. Typhimurium infection.

open access: yesPLoS Pathogens, 2020
Reactive arthritis, an autoimmune disorder, occurs following gastrointestinal infection with invasive enteric pathogens, such as Salmonella enterica.
Amanda L Miller   +16 more
doaj   +1 more source

Staphylococcus aureus functional amyloids catalyze degradation of β-lactam antibiotics

open access: yesNature Communications, 2023
Antibiotic resistance of bacteria is considered one of the most alarming developments in modern medicine. While varied pathways for bacteria acquiring antibiotic resistance have been identified, there still are open questions concerning the mechanisms ...
Elad Arad   +9 more
doaj   +1 more source

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