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MetabolomicsThe patatin-like protein PlpD forms novel structurally dynamic homodimers in the Pseudomonas aeruginosa outer membrane

Members of the Omp85 superfamily of outer membrane proteins (OMPs) found in Gram-negative bacteria, mitochondria and chloroplasts are characterized by a distinctive 16-stranded β-barrel transmembrane domain and at least one periplasmic POTRA domain. All previously studied Omp85 proteins promote c...

2025-12-08 | MTBLS9803 | MetaboLights
ProteomicsGlobal Analysis of Protein Folding Thermodynamics for Disease State Characterization, MCF7 vs MDAMB231
Protein biomarkers can be used to characterize and diagnose disease states such as cancer. They can also serve as therapeutic targets. Current methods for protein biomarker discovery, which generally rely on the large-scale analysis of gene and/or protein expression levels, fail to detect protein b...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2017-03-29 | MSV000080761 | MassIVE
ProteomicsGlobal Analysis of Protein Folding Thermodynamics for Disease State Characterization, MCF7 vs MCF10A
Protein biomarkers can be used to characterize and diagnose disease states such as cancer. They can also serve as therapeutic targets. Current methods for protein biomarker discovery, which generally rely on the large-scale analysis of gene and/or protein expression levels, fail to detect protein b...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2017-03-29 | MSV000080760 | MassIVE
TranscriptomicsGenome-wide measurement of RNA folding energies
RNA structural transitions are important in the function and regulation of RNAs. Here, we reveal a layer of transcriptome organization in the form of RNA folding energies. By probing yeast RNA structures at different temperatures, we obtained relative melting temperatures (Tm) for RNA structures in ...
ORGANISM(S): Saccharomyces cerevisiae 
2012-09-09 | E-GEOD-39680 | biostudies-arrayexpress
TranscriptomicsTranslational profiling in the unfolded protein response
The unfolded protein response (UPR) couples cellular translation rates and gene expression to the protein folding status of the endoplasmic reticulum (ER). Upon activation, the UPR machinery elicits a general suppression of protein synthesis and activation of stress gene expression, which act coordi...
ORGANISM(S): Mus musculus 
2014-08-28 | E-GEOD-53743 | biostudies-arrayexpress
TranscriptomicsMitochondrial unfolded protein response controls matrix pre-RNA processing and translation
The mitochondrial matrix is unique in that it must integrate folding and assembly of proteins derived from nuclear and mitochondrial genomes. In C. elegans, the mitochondrial unfolded protein response (UPRmt) senses matrix protein misfolding and induces a program of nuclear gene expression, includin...
ORGANISM(S): Homo sapiens 
2016-06-28 | E-GEOD-75247 | biostudies-arrayexpress
TranscriptomicsMitochondrial unfolded protein response controls matrix pre-RNA processing and translation
The mitochondrial matrix is unique in that it must integrate folding and assembly of proteins derived from nuclear and mitochondrial genomes. In C. elegans, the mitochondrial unfolded protein response (UPRmt) senses matrix protein misfolding and induces a program of nuclear gene expression, includin...
ORGANISM(S): Homo sapiens 
2016-06-28 | E-GEOD-75410 | biostudies-arrayexpress
TranscriptomicsThe unfolded protein response in fission yeast modulates stability of select mRNAs to maintain protein homeostasis
Homeostatic control mechanisms are essentil to life. One such mechanism, the unfolded protein response (UPR) operates in all eukarytic cells to adjust protein folding capacity of the endoplasmic reticulum (ER) according to need. UPR induction in all eurkarytic cells to date involves Ire1 (kinase/end...
ORGANISM(S): Schizosaccharomyces pombe 
2012-11-21 | E-GEOD-40298 | biostudies-arrayexpress
GenomicsChaperone saturation mediates translation and protein folding efficiency
Chaperone saturation mediates translation and protein folding efficiency
PRJNA412310 | ENA
ProteomicsDnaK interaction and folding of firefly luciferase studied by hydrogen/deuterium exchange – mass spectrometry
The ATP-dependent chaperones of the Hsp70 class (DnaK in E. coli) function in protein folding in cooperation with J proteins and nucleotide exchange factors (DnaJ and GrpE in E. coli, respectively). Hsp70 prevents protein aggregation, increasing the folding yield, but whether it also enhances the ra...
ORGANISM(S): Escherichia coli 
2020-01-15 | PXD016509 | Pride
Deuterium exchange Chaperone Firefly luciferase Dnak Folding 
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