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ProteomicsFolding correctors can retore CFTR post-translational folding landscape by allosteric domain-domain coupling
Numerous missense mutations cause misfolding and premature degradation of ATP-binding cassette (ABC)-transporters-transporters, accounting for several human conformational diseases with poorly under-stood molecular mechanisms. Recent breakthroughs in small molecule combination therapy led transforma...
ORGANISM(S): Homo sapiens (Human) 
2024-01-26 | PXD042481 | Pride
Biogenesis Post-translational protein folding Cystic fibrosis mutation Protein dynamics Coupled domain folding Hydrogen-deuterium exchange and mass spectrometry (hdx-ms) Abc-transporter Folding corrector drugs Allostery Cystic fibrosis transmembrane conductance regulator (cftr) 
UnknownNascent chains can form co-translational folding intermediates that promote post-translational folding outcomes in a disease-causing protein.
Not available
S-EPMC8576036 | biostudies-literature
UnknownAccurate prediction of cellular co-translational folding indicates proteins can switch from post- to co-translational folding.
Not available
S-EPMC4759629 | biostudies-literature
ProteomicsReactive Metabolite-induced Protein Glutathionylation Mechanistically Accounts for Acetaminophen Hepatotoxicity
Although covalent protein binding is established as the pivotal event underpinning acetaminophen (APAP) toxicity, its mechanistic details remain unclear. In this study, we demonstrated that APAP induces widespread protein glutathionylation in a time-, dose- and bioactivation-dependent manner in Hepa...
ORGANISM(S): Homo Sapiens (human) 
2018-09-20 | PXD009986 | JPOST Repository
OtherAccurate prediction of cellular co-translational folding indicates proteins can switch from post- to co-translational folding
The rates at which domains fold and codons are translated are important factors in determining whether a nascent protein will co-translationally fold and function or misfold and malfunction. In this study, we develop a chemical kinetic model that calculates a protein domain’s co-translational foldin...
ORGANISM(S): Saccharomyces cerevisiae 
2016-01-30 | GSE75322 | GEO
UnknownA comprehensive resource for integrating and displaying protein post-translational modifications.
Not available
S-EPMC2713254 | biostudies-literature
ProteomicsS-Sulfenylation regulates non-enzymatic oxidative protein folding
The post-translational modification S-Sulfenylation functions as a key sensor of oxidative stress yet the dynamics of sulfenic acids in proteins is largely elusive due to it's fleeting nature. LC-MS/MS analysis has detected the evolution of this modification in oxidative and reducing states.
ORGANISM(S): Homo sapiens (Human) 
2016-12-23 | PXD004514 | Pride
Lc-ms/ms Post-translational modifications Human titin 
GenomicsSaccharomyces cerevisiae
Accurate prediction of cellular co-translational folding indicates proteins can switch from post- to co-translational folding
PRJNA303186 | ENA
UnknownDynamic Lipid-dependent Modulation of Protein Topology by Post-translational Phosphorylation.
Not available
S-EPMC5290939 | biostudies-literature
UnknownMolecular dynamics simulation of phosphorylated KID post-translational modification.
Not available
S-EPMC2717803 | biostudies-literature
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