Results 71 to 80 of about 1,155,621 (272)

The broad‐spectrum antibiofilm activity of amyloid‐forming hexapeptides

open access: yesMicrobial Biotechnology, 2021
Summary Evidence suggests that short amyloid‐forming peptides derived from bacterial proteomes have functional roles; however, the reported activities are diverse and the underlying mechanisms remain unclear.
Dongru Chen   +5 more
doaj   +1 more source

Multitasking of Hsp70 chaperone in the biogenesis of bacterial functional amyloids [PDF]

open access: yesCommunications Biology, 2018
AbstractBiofilms are intricate communities of microorganisms embedded in a self-produced matrix of extracellular polymer, which provides microbes survival advantages in stressful environments and can cause chronic infections in humans. Curli are functional amyloids that assemble on the extracellular surface of enteric bacteria such asEscherichia ...
Shinya Sugimoto   +5 more
openaire   +2 more sources

The C‐terminal domain of yeast Arginyltransferase1 is essential for its catalytic activity

open access: yesFEBS Open Bio, EarlyView.
Arginyltransferase 1 (Ate1), a eukaryotic enzyme, catalyses arginylation, transferring arginine from tRNA‐Arg to the amino terminus of the target protein. Overexpression of Ate1 in yeast is lethal and is dependent on arginylation. This study elucidates how mutations in the cofactor‐binding and active site of Ate1 and truncation of its structural ...
Vikas Kumar Yadav   +4 more
wiley   +1 more source

Magnetic Resonance Reveals Radical Stability in Native Biofilms and Its Role in Bacterial Resistance

open access: yesAngewandte Chemie, EarlyView.
The complex biofilm environment consists of planktonic bacterial cells and cells embedded in an extracellular matrix (ECM). Through an integrated magnetic resonance approach, we show that nitroxide radicals primarily interact with the polysaccharides and lipids in the ECM.
Alysia Mandato   +10 more
wiley   +2 more sources

Are Gastrointestinal Microorganisms Involved in the Onset and Development of Amyloid Neurodegenerative Diseases?

open access: yesMicrobiology Research, 2023
This review discusses a few examples of specific mechanisms mediating the contribution of the GIT microbiota to the development of amyloid neurodegenerative diseases caused by the pathologic transformation of prion protein, or alpha-synuclein. The effect
Vladimir I. Muronetz   +3 more
doaj   +1 more source

Chronobiology of Cancer: How Aging Fuels Oncogenesis at the Molecular Level

open access: yesAging and Cancer, EarlyView.
This graphical abstract illustrates the key biological pathways linking aging with cancer development and progression. In the upper left, cumulative exposure to ultraviolet radiation, toxins, and reactive oxygen species (ROS) causes DNA damage and genomic instability, whereas age‐related decline in repair mechanisms, such as ATM/ATR, BER, and NER ...
Anu Singh, Aroonima Misra, Sufian Zaheer
wiley   +1 more source

Anti-biofilm activity of anti-matrix molecules

open access: yesZdorovʹe Rebenka, 2020
The extracellular matrix of biofilms ensures the fixation of the biofilm on the biological surface and the protection of its bacteria from external adverse factors.
А.Е. Abaturov
doaj   +1 more source

A bacterial export system for generating extracellular amyloid aggregates [PDF]

open access: yesNature Protocols, 2013
Here we describe a protocol for the generation of amyloid aggregates of target amyloidogenic proteins using a bacteria-based system called curli-dependent amyloid generator (C-DAG). C-DAG relies on the natural ability of Escherichia coli cells to elaborate surface-associated amyloid fibers known as curli.
Viknesh, Sivanathan, Ann, Hochschild
openaire   +2 more sources

α‐Synuclein Forms Distinct Micelle‐Like Assemblies at Low Ionic Strengths

open access: yesAdvanced Science, EarlyView.
At high ionic strength, α‐synuclein forms diverse assemblies, including oligomers, fibrils, and condensates. Here, we show that at low ionic strength, α‐synuclein adopts a distinct, low‐abundance assembly state. These assemblies maintain a constant size above a critical concentration and do not coalesce, suggesting a micelle‐like organization ...
Sophie Hertel   +10 more
wiley   +1 more source

Beyond the expected: the structural and functional diversity of bacterial amyloids [PDF]

open access: yesCritical Reviews in Microbiology, 2018
Intense research has confirmed the formerly theoretical distribution of amyloids in nature, and studies on different systems have illustrated the role of these proteins in microbial adaptation and in interactions with the environment. Two lines of research are expanding our knowledge on functional amyloids: (i) structural studies providing insights ...
Cámara-Almirón, Jesús   +3 more
openaire   +2 more sources

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