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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) 
UnknownFolding correctors can restore CFTR posttranslational folding landscape by allosteric domain-domain coupling.
Not available
S-EPMC10611759 | biostudies-literature
UnknownMolecular Details of a Coupled Binding and Folding Reaction between the Amyloid Precursor Protein and a Folded Domain.
Not available
S-EPMC8291497 | biostudies-literature
UnknownSlow, reversible, coupled folding and binding of the spectrin tetramerization domain.
Not available
S-EPMC3512043 | biostudies-literature
ProteomicsDomain-selective folding of the tandem β-propeller protein Coronin 7 by the chaperonin CCT/TRiC
The Chaperonin containing tailless complex polypeptide 1 (CCT) or TCP-1 ring complex (TRiC) plays a central role in maintaining cellular homeostasis by supporting protein folding and damping protein aggregation. Besides the abundant cytoskeletal proteins, actin and tubulin, CCT/TRiC is emerging as a...
ORGANISM(S): Homo sapiens (Human) 
2026-02-20 | PXD073687 | Pride
Cct/tric Protein folding Chaperone-mediated folding Coronin 7 Bioid 
UnknownFormation of the folding nucleus of an SH3 domain investigated by loosely coupled molecular dynamics simulations.
Not available
S-EPMC1304005 | biostudies-literature
UnknownThe transition state structure for coupled binding and folding of disordered protein domains.
Not available
S-EPMC3691887 | biostudies-literature
UnknownWW domain folding complexity revealed by infrared spectroscopy.
Not available
S-EPMC4151701 | biostudies-literature
UnknownA structurally heterogeneous transition state underlies coupled binding and folding of disordered proteins.
Not available
S-EPMC6349112 | biostudies-literature
GenomicsThe ribosome synchronizes folding and assembly to promote oligomeric protein biogenesis
The ribosome synchronizes folding and assembly to promote oligomeric protein biogenesis
PRJNA1235181 | ENA
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