Sort   by:  
 Page size 
ProteomicsBacterial RF3 Senses Chaperone Function in Co-translational Folding
Molecular chaperones assist in protein folding by interacting with nascent polypeptide chains (NCs) during translation, but whether the ribosome can sense chaperone defects and abort translation of misfolding NCs has not been explored. Here we used quantitative proteomics in E. coli to investigate t...
ORGANISM(S): Escherichia coli 
2022-12-09 | PXD025219 | Pride
Molecular chaperones Co-translational folding 
GenomicsNAC promotes co-translational protein folding at the ribosomal tunnel exit
NAC promotes co-translational protein folding at the ribosomal tunnel exit
PRJNA1230285 | ENA
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
UnknownAccurate prediction of cellular co-translational folding indicates proteins can switch from post- to co-translational folding.
Not available
S-EPMC4759629 | biostudies-literature
Genomics
Co-translational protein folding by AP Profiling
PRJNA1212592 | ENA
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
OtherNAC promotes co-translational protein folding at the ribosomal tunnel exit
The nascent polypeptide-associated complex (NAC) is crucial for protein biogenesis, coordinating enzymatic modifications and membrane targeting of nascent chains at the ribosomal tunnel exit. However, its role in co-translational folding remains unclear. Here, we report the genome-wide profiling of ...
ORGANISM(S): Homo sapiens 
2026-03-23 | GSE290865 | GEO
UnknownStructure formation during translocon-unassisted co-translational membrane protein folding.
Not available
S-EPMC5556060 | biostudies-literature
GenomicsProteome-wide determinants of co-translational chaperone binding in bacteria
Proteome-wide determinants of co-translational chaperone binding in bacteria
PRJNA1238275 | ENA
UnknownModulating co-translational protein folding by rational design and ribosome engineering.
Not available
S-EPMC9307626 | biostudies-literature
Sort   by:  
 Page size