Results 61 to 70 of about 6,771,465 (361)

Cellular prion protein distribution in the vomeronasal organ, parotid, and scent glands of white-tailed deer and mule deer

open access: yesPrion, 2022
Chronic wasting disease (CWD) is a contagious and fatal transmissible spongiform encephalopathy affecting species of the cervidae family. CWD has an expanding geographic range and complex, poorly understood transmission mechanics.
Anthony Ness   +10 more
doaj   +1 more source

The role and implications of mammalian cellular circadian entrainment

open access: yesFEBS Letters, EarlyView.
At their most fundamental level, mammalian circadian rhythms occur inside every individual cell. To tell the correct time, cells must align (or ‘entrain’) their circadian rhythm to the external environment. In this review, we highlight how cells entrain to the major circadian cues of light, feeding and temperature, and the implications this has for our
Priya Crosby
wiley   +1 more source

Exposure Risk of Chronic Wasting Disease in Humans

open access: yesViruses, 2020
The majority of human prion diseases are sporadic, but acquired disease can occur, as seen with variant Creutzfeldt–Jakob disease (vCJD) following consumption of bovine spongiform encephalopathy (BSE).
Satish K. Nemani   +4 more
doaj   +1 more source

Molecular bases of circadian magnesium rhythms across eukaryotes

open access: yesFEBS Letters, EarlyView.
Circadian rhythms in intracellular [Mg2+] exist across eukaryotic kingdoms. Central roles for Mg2+ in metabolism suggest that Mg2+ rhythms could regulate daily cellular energy and metabolism. In this Perspective paper, we propose that ancestral prokaryotic transport proteins could be responsible for mediating Mg2+ rhythms and posit a feedback model ...
Helen K. Feord, Gerben van Ooijen
wiley   +1 more source

Propagation of PrPSc in mice reveals impact of aggregate composition on prion disease pathogenesis

open access: yesCommunications Biology, 2023
Infectious prions consist of PrPSc, a misfolded, aggregation-prone isoform of the host’s prion protein. PrPSc assemblies encode distinct biochemical and biological properties.
Sheng Chun Chang   +6 more
doaj   +1 more source

Learning inverse folding from millions of predicted structures

open access: yesbioRxiv, 2022
We consider the problem of predicting a protein sequence from its backbone atom coordinates. Machine learning approaches to this problem to date have been limited by the number of available experimentally determined protein structures.
Chloe Hsu   +7 more
semanticscholar   +1 more source

Crosstalk between the ribosome quality control‐associated E3 ubiquitin ligases LTN1 and RNF10

open access: yesFEBS Letters, EarlyView.
Loss of the E3 ligase LTN1, the ubiquitin‐like modifier UFM1, or the deubiquitinating enzyme UFSP2 disrupts endoplasmic reticulum–ribosome quality control (ER‐RQC), a pathway that removes stalled ribosomes and faulty proteins. This disruption may trigger a compensatory response to ER‐RQC defects, including increased expression of the E3 ligase RNF10 ...
Yuxi Huang   +8 more
wiley   +1 more source

Rational design of structure‐based vaccines targeting misfolded alpha‐synuclein conformers of Parkinson's disease and related disorders

open access: yesBioengineering & Translational Medicine
Synucleinopathies, including Parkinson's disease (PD), multiple system atrophy (MSA), and dementia with Lewy bodies (DLB), are neurodegenerative disorders caused by the accumulation of misfolded alpha‐synuclein protein.
Jose Miguel Flores‐Fernandez   +13 more
doaj   +1 more source

Using Protein Folding Rates to Test Protein Folding Theories [PDF]

open access: yesAnnual Review of Biochemistry, 2004
▪ Abstract  The fastest simple, kinetically two-state protein folds a million times more rapidly than the slowest. Here we review many recent theories of protein folding kinetics in terms of their ability to qualitatively rationalize, if not quantitatively predict, this fundamental experimental observation.
Blake, Gillespie, Kevin W, Plaxco
openaire   +2 more sources

Peptide‐based ligand antagonists block a Vibrio cholerae adhesin

open access: yesFEBS Letters, EarlyView.
The structure of a peptide‐binding domain of the Vibrio cholerae adhesin FrhA was solved by X‐ray crystallography, revealing how the inhibitory peptide AGYTD binds tightly at its Ca2+‐coordinated pocket. Structure‐guided design incorporating D‐amino acids enhanced binding affinity, providing a foundation for developing anti‐adhesion therapeutics ...
Mingyu Wang   +9 more
wiley   +1 more source

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