Results 51 to 60 of about 255,418 (267)
In situ molecular organization and heterogeneity of the Legionella Dot/Icm T4SS
FEBS Letters, EarlyView.We present a nearly complete in situ model of the Legionella Dot/Icm type IV secretion system, revealing its central secretion channel and identifying new components. Using cryo‐electron tomography with AI‐based modeling, our work highlights the structure, variability, and mechanism of this complex nanomachine, advancing understanding of bacterial ...
Przemysław Dutka +11 more
wiley +1 more source
Bioengineering & Translational MedicineSynucleinopathies, 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]
Annual 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
Sequence determinants of RNA G‐quadruplex unfolding by Arg‐rich regions
FEBS Letters, EarlyView.We show that Arg‐rich peptides selectively unfold RNA G‐quadruplexes, but not RNA stem‐loops or DNA/RNA duplexes. This length‐dependent activity is inhibited by acidic residues and is conserved among SR and SR‐related proteins (SRSF1, SRSF3, SRSF9, U1‐70K, and U2AF1).
Naiduwadura Ivon Upekala De Silva +10 more
wiley +1 more source
Study on the Influence of mRNA, the Genetic Language, on Protein Folding Rates
Frontiers in Genetics, 2021 Many works have reported that protein folding rates are influenced by the characteristics of amino acid sequences and protein structures. However, few reports on the problem of whether the corresponding mRNA sequences are related to the protein folding ...
Ruifang Li +4 more
doaj +1 more source
FEBS Letters, EarlyView.The Ile181Asn variant of human UDP‐xylose synthase (hUXS1), associated with a short‐stature genetic syndrome, has previously been reported as inactive. Our findings demonstrate that Ile181Asn‐hUXS1 retains catalytic activity similar to the wild‐type but exhibits reduced stability, a looser oligomeric state, and an increased tendency to precipitate ...
Tuo Li +2 more
wiley +1 more source
Scientific ReportsPrion diseases are fatal transmissible neurodegenerative diseases that affect many mammals, including humans, caused by the templated misfolding of the prion protein.
Hailey Pineau, Valerie L. Sim
doaj +1 more source
An ancient conserved role for prion protein in learning and memory
Biology Open, 2018 The misfolding of cellular prion protein (PrPC) to form PrP Scrapie (PrPSc) is an exemplar of toxic gain-of-function mechanisms inducing propagated protein misfolding and progressive devastating neurodegeneration. Despite this, PrPC function in the brain
Patricia L. A. Leighton +4 more
doaj +1 more source
Protein photo-folding and quantum folding theory [PDF]
Science China Life Sciences, 2012 17 pages, 1 ...
openaire +3 more sources
FEBS Letters, EarlyView.We reconstituted Synechocystis glycogen synthesis in vitro from purified enzymes and showed that two GlgA isoenzymes produce glycogen with different architectures: GlgA1 yields denser, highly branched glycogen, whereas GlgA2 synthesizes longer, less‐branched chains.
Kenric Lee +3 more
wiley +1 more source