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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
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
ProteomicsLONP1 and mtHSP70 cooperate to promote mitochondrial protein folding
Because 99% of the mitochondrial proteome is encoded by the nucleus, most mitochondrial precursor polypeptides are imported from the cytosol into the mitochondrion, where they must efficiently fold into their functional state. Mitochondrial precursors are imported as unfolded polypeptides due to th...
ORGANISM(S): Homo sapiens (Human) 
2020-12-07 | PXD021939 | Pride
Aggregates Protein homeostasis Mitochondria Human 
ProteomicsLONP1 regulation of mitochondrial protein folding provides insight into beta cell failure in type 2 diabetes
Protein misfolding is a contributor to the development of type 2 diabetes (T2D), but it is unknown whether impaired proteostasis in T2D is generalized or has special features. Here, we report a robust accumulation of misfolded proteins within the mitochondria of human pancreatic islets from patients...
ORGANISM(S): Homo sapiens (Human) 
2025-06-05 | PXD060404 | Pride
Diabetes  apoptosis  mitochondrial protein folding  lonp1 
TranscriptomicsPervasive and dynamic protein binding sites of the mRNA transcriptome in Saccharomyces cerevisiae
Protein-RNA interactions are integral components of nearly every aspect of biology including regulation of gene expression, assembly of cellular architectures, and pathogenesis of human diseases. However, studies in the past few decades have only uncovered a small fraction of the vast landscape of t...
ORGANISM(S): Saccharomyces cerevisiae 
2013-01-29 | E-GEOD-43747 | biostudies-arrayexpress
UnknownLONP1 and mtHSP70 cooperate to promote mitochondrial protein folding.
Not available
S-EPMC7801493 | biostudies-literature
TranscriptomicsMitochondrial unfolded protein response controls matrix pre-RNA processing and translation
This SuperSeries is composed of the SubSeries listed below. Refer to individual Series
ORGANISM(S): Homo sapiens 
2016-06-28 | E-GEOD-75411 | biostudies-arrayexpress
TranscriptomicsLipid biosynthesis coordinates a Mitochondrial to Cytosolic Stress Response
Defects in mitochondrial metabolism have been increasingly linked with age-onset protein misfolding diseases such as Alzheimer’s, Parkinson’s, and Huntington’s. In response to protein folding stress, compartment-specific unfolded protein responses (UPRs) within the endoplasmic reticulum, mitoc...
ORGANISM(S): Caenorhabditis elegans 
2016-09-08 | E-GEOD-83722 | biostudies-arrayexpress
GenomicsNAC promotes co-translational protein folding at the ribosomal tunnel exit
NAC promotes co-translational protein folding at the ribosomal tunnel exit
PRJNA1230285 | ENA
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