Abstract from paper - Potti A, et al
A genomic strategy to refine prognosis in early-stage non-small-cell lung cancer.
No sample metadata fields
View SamplesSignatures of Oncogenic Pathway Deregulation in Human Cancers.
Oncogenic pathway signatures in human cancers as a guide to targeted therapies.
No sample metadata fields
View SamplesSignatures of Oncogenic Pathway Deregulation in Human Cancers.
Oncogenic pathway signatures in human cancers as a guide to targeted therapies.
No sample metadata fields
View SamplesSignatures of Oncogenic Pathway Deregulation in Human Cancers.
Oncogenic pathway signatures in human cancers as a guide to targeted therapies.
No sample metadata fields
View SamplesSignatures of Oncogenic Pathway Deregulation in Human Cancers
Oncogenic pathway signatures in human cancers as a guide to targeted therapies.
No sample metadata fields
View SamplesGene expression analysis on growing breast cancer cell lines.
Oncogenic pathway signatures in human cancers as a guide to targeted therapies.
No sample metadata fields
View SamplesThis SuperSeries is composed of the SubSeries listed below.
Multi-Institutional Prospective Validation of Prognostic mRNA Signatures in Early Stage Squamous Lung Cancer (Alliance).
Sex, Age, Specimen part, Disease
View SamplesPurpose: The primary objective of the current study was to validate biomarkers to identify the 10% to 27% of patients with stage I and 35% of patients with stage IIA squamous cell carcinoma of lung (SC) who are likely to recur following surgical resection, so that these patients may be offered enrollment in clinical trials evaluating directed ACT. A secondary objective was to identify patients with stage IIB SC who are unlikely to develop recurrences and might thereby be spared the potential significant toxicity and expense of ACT.
Multi-Institutional Prospective Validation of Prognostic mRNA Signatures in Early Stage Squamous Lung Cancer (Alliance).
Sex, Age, Specimen part, Disease
View SamplesPurpose: The primary objective of the current study was to validate biomarkers to identify the 10% to 27% of patients with stage I and 35% of patients with stage IIA squamous cell carcinoma of lung (SC) who are likely to recur following surgical resection, so that these patients may be offered enrollment in clinical trials evaluating directed ACT. A secondary objective was to identify patients with stage IIB SC who are unlikely to develop recurrences and might thereby be spared the potential significant toxicity and expense of ACT.
Multi-Institutional Prospective Validation of Prognostic mRNA Signatures in Early Stage Squamous Lung Cancer (Alliance).
Sex, Age, Specimen part, Disease
View SamplesThe 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, including mitochondrial chaperonins, to promote mitochondrial proteostasis. While misfolded mitochondrial matrix-localized ornithine trans-carbamylase (OTC) induces chaperonin expression, our understanding of mammalian UPRmt is rudimentary, reflecting a lack of acute triggers for UPRmt activation. This limitation has prevented analysis of the cellular responses to matrix protein misfolding and the effects of UPRmt on mitochondrial translation to control protein folding loads. Here, we combine pharmacological inhibitors of matrix-localized HSP90/TRAP1 or LON protease, which promote chaperonin expression, with global transcriptional and proteomic analysis to reveal an extensive and acute response of human cells to UPRmt. This response involved widespread induction of nuclear genes, including matrix-localized proteins involved in folding, pre-RNA processing and translation. Functional studies revealed rapid but reversible translation inhibition in mitochondria occurring concurrently with defects in pre-RNA processing due to transcriptional repression and LON-dependent turnover of the mitochondrial pre-RNA processing nuclease MRPP3. This study reveals that acute mitochondrial protein folding stress activates both increased chaperone availability within the matrix and reduced matrix-localized protein synthesis through translational inhibition, and provides a framework for further dissection of mammalian UPRmt. Overall design: triplicate experiment of 2 conditions (untreated, GTPP treatment)
Mitochondrial unfolded protein response controls matrix pre-RNA processing and translation.
No sample metadata fields
View Samples