Results 71 to 80 of about 97,377 (307)

Turning Unpredictable Biomolecule Adsorption to Controlled Corona Formation: Focus on Carbon Nanomaterials

open access: yesAdvanced Materials, EarlyView.
Controlling the protein corona formation onto carbon nanomaterials (CNMs) enhances their functionalities as platforms for cancer theranostics. Here, we reviewed the effects of the intrinsic and acquired properties of CNMs on protein corona formation, the consequent biological and toxicological outcomes, and the strategies to reshape corona formation ...
Yajuan Zou   +5 more
wiley   +1 more source

A high-content neuron imaging assay demonstrates inhibition of prion disease-associated neurotoxicity by an anti-prion protein antibody

open access: yesScientific Reports, 2022
There is an urgent need to develop disease-modifying therapies to treat neurodegenerative diseases which pose increasing challenges to global healthcare systems.
Madeleine Reilly   +7 more
doaj   +1 more source

The Molecular Pathology of Prion Diseases [PDF]

open access: yes, 2004
Prion diseases, or transmissible spongiform encephalopathies (TSEs), are a group of invariably fatal neurodegenerative disorders. Uniquely, they may present as sporadic, inherited, or infectious forms, all of which involve conversion of the normal ...
Herms, Jochen   +2 more
core  

RNF213 Is an Interferon‐Stimulated Gene That Targets Influenza A Virus NP and Activates MDA5 to Restrict Infection

open access: yesAdvanced Science, EarlyView.
RNF213 is characterized as a dual‐functional antiviral effector. It directly mediates the degradation of the influenza A virus nucleoprotein (NP) while simultaneously activating the MDA5‐mediated innate immune signaling pathway. This coordinated response establishes a powerful host defense system against viral infection. ABSTRACT Influenza A virus (IAV)
Haoning Li   +5 more
wiley   +1 more source

Cytosolic Prion Protein Toxicity Is Independent of Cellular Prion Protein Expression and Prion Propagation [PDF]

open access: yesJournal of Virology, 2007
ABSTRACT Prion diseases are transmissible neurodegenerative diseases caused by a conformational isoform of the prion protein (PrP), a host-encoded cell surface sialoglycoprotein. Recent evidence suggests a cytosolic fraction of PrP (cyPrP) functions either as an initiating factor or toxic element of prion disease.
Eric M, Norstrom   +4 more
openaire   +2 more sources

Unique Properties of the Rabbit Prion Protein Oligomer. [PDF]

open access: yesPLoS ONE, 2016
Prion diseases, also known as transmissible spongiform encephalopathies (TSEs), are a group of fatal neurodegenerative disorders infecting both humans and animals.
Ziyao Yu   +6 more
doaj   +1 more source

Astrocyte in prion disease: a double-edged sword

open access: yesNeural Regeneration Research, 2022
Prion diseases are infectious protein misfolding disorders of the central nervous system that result from misfolding of the cellular prion protein (PrPC) into the pathologic isoform PrPSc.
Waqas Tahir   +2 more
doaj   +1 more source

A survey and a molecular dynamics study on the (central) hydrophobic region of prion proteins

open access: yes, 2014
Prion diseases are invariably fatal neurodegenerative diseases that affect humans and animals. Unlike most other amyloid forming neurodegenerative diseases, these can be highly infectious. Prion diseases occur in a variety of species.
Wang, Feng, Zhang, Jiapu
core   +1 more source

Role of Prion protein-EGFR multimolecular complex during neuronal differentiation of human dental pulp-derived stem cells [PDF]

open access: yes, 2018
Cellular prion protein (PrPC) is expressed in a wide variety of stem cells in which regulates their self-renewal as well as differentiation potential. In this study we investigated the presence of PrPCin human dental pulp-derived stem cells (hDPSCs) and ...
Manganelli, Valeria   +6 more
core   +1 more source

Ecological Adaptation Mechanisms Underlying Successful Plant Reproduction

open access: yesAdvanced Science, EarlyView.
During floral induction, various environmental and endogenous signals converge to regulate the florigen protein, which is transported from leaves to the SAM to initiate flowering. Within the SAM, a complex network of receptor kinases and small peptides orchestrates floral development with high spatiotemporal precision.
Hang Zhao   +8 more
wiley   +1 more source

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