Results 31 to 40 of about 3,403,581 (279)

Effect of spermidine on misfolding and interactions of alpha-synuclein. [PDF]

open access: yesPLoS ONE, 2012
Alpha-synuclein (α-Syn) is a 140 aa presynaptic protein which belongs to a group of natively unfolded proteins that are unstructured in aqueous solutions.
Alexey V Krasnoslobodtsev   +5 more
doaj   +1 more source

Matrin3: Disorder and ALS Pathogenesis

open access: yesFrontiers in Molecular Biosciences, 2022
Amyotrophic lateral sclerosis (ALS) is a neurodegenerative disorder characterized by the degeneration of both upper and lower motor neurons in the brain and spinal cord.
Ahmed Salem   +7 more
doaj   +1 more source

Divergent effects of PERK and IRE1 signaling on cell viability.

open access: yesPLoS ONE, 2009
Protein misfolding in the endoplasmic reticulum (ER) activates a set of intracellular signaling pathways, collectively termed the Unfolded Protein Response (UPR). UPR signaling promotes cell survival by reducing misfolded protein levels.
Jonathan H Lin   +4 more
doaj   +1 more source

Prion protein self-peptides modulate prion interactions and conversion [PDF]

open access: yes, 2009
Background: Molecular mechanisms underlying prion agent replication, converting host-encoded cellular prion protein (PrPC) into the scrapie associated isoform (PrPSc), are poorly understood.
Bossers, A.   +12 more
core   +1 more source

Stress and viral insults do not trigger E200K PrP conversion in human cerebral organoids.

open access: yesPLoS ONE, 2022
Prion diseases are a group of rare, transmissible, and invariably fatal neurodegenerative diseases that affect both humans and animals. The cause of these diseases is misfolding of the prion protein into pathological isoforms called prions.
Anna Smith   +9 more
doaj   +1 more source

Bridging the gap: From protein misfolding to protein misfolding diseases

open access: yesFEBS Letters, 2009
Protein misfolding and aggregation are pathognomic for a number of the most common age‐related degenerative diseases. Great progress has been made in studying protein aggregation in the test tube and also in replicating protein aggregation in vertebrate animal models of these diseases.
Luheshi, Leila M.   +1 more
openaire   +2 more sources

CHAPTER 1.1. Disulfide Bonds in Protein Folding and Stability [PDF]

open access: yes, 2018
Disulfide bonds are unique among post-translational modifications, as they add covalent crosslinks to the polypeptide chain. Accordingly, they can exert pronounced effects on protein folding and stability. This is of particular importance for secreted or
Sub Cellular Protein Chemistry   +7 more
core   +1 more source

Protein folding on the ribosome studied using NMR spectroscopy [PDF]

open access: yes, 2013
NMR spectroscopy is a powerful tool for the investigation of protein folding and misfolding, providing a characterization of molecular structure, dynamics and exchange processes, across a very wide range of timescales and with near atomic resolution.
Christodoulou, J   +9 more
core   +1 more source

Protein misfolding and cellular stress in disease and ageing - Concepts and protocols

open access: yesEuropean Journal of Histochemistry, 2011
To those readers that already got the Protein misfolding and disease volume, this new title can sound as an update or a second edition of the previous volume: well, this is not the case.
Carlo Alberto Redi
doaj   +1 more source

RETRACTED ARTICLE: Neurotropic influenza A virus infection causes prion protein misfolding into infectious prions in neuroblastoma cells

open access: yesScientific Reports, 2021
Misfolding of the cellular prion protein, PrPC, into the amyloidogenic isoform, PrPSc, which forms infectious protein aggregates, the so-called prions, is a key pathogenic event in prion diseases.
Hideyuki Hara   +6 more
doaj   +1 more source

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