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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
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 
ProteomicsGroEL interaction and folding of MetF studied by hydrogen/deuterium exchange – mass spectrometry
The cylindrical chaperonin GroEL and its cofactor GroES mediate ATP-dependent protein folding in E. coli by transiently encapsulating non-native substrate in a nano-cage formed by the GroEL ring cavity and the lid-shaped GroES. We analyzed the spontaneous and chaperonin-assisted folding of the essen...
ORGANISM(S): Escherichia coli 
2020-03-05 | PXD016666 | Pride
Groel Chaperone Folding Metf Hydrogen/deuterium exchange Chaperonin 
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) 
TranscriptomicsGenome-wide probing of RNA structure reveals active unfolding of mRNA structures in vivo
We present an approach for globally monitoring RNA structure in native conditions in vivo with single nucleotide precision. This method is based on in vivo modification with dimethyl sulfate (DMS), which reacts with unpaired adenine and cytosine residues9, followed by deep sequencing to monitor modi...
ORGANISM(S): Homo sapiens 
2013-12-15 | E-GEOD-45803 | biostudies-arrayexpress
GenomicsGene regulatory landscape of cerebral cortex folding
Gene regulatory landscape of cerebral cortex folding
PRJNA722759 | ENA
ProteomicsNovel calcium-binding sites in the acylated segment control the folding and membrane penetration of RTX toxins
The Repeats in ToXin (RTX) domain of RTX cytolysins harbors numerous hexacoordinated Ca2+-binding sites that facilitate cooperative and vectorial folding of the RTX β-rolls. Recent study identified Ca2+-binding sites in the acylated N-terminal extension of the RTX domain of Bordetella pertussis aden...
ORGANISM(S): Bordetella pertussis 
2026-04-22 | PXD058094 | Pride
Membrane penetration H/d exchange Rtx toxin Folding Calcium binding site Acylated segment 
GenomicsStress promotes RNA G-quadruplex folding in human cells
Stress promotes RNA G-quadruplex folding in human cells
PRJNA826109 | ENA
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