Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

HEK293 cells overexpressing HNF4a2 wild type or mutant forms C106R or R154X

ABSTRACT: Identification of genes regulated by the transcription factor HNF4a2 Keywords: ordered

ORGANISM(S): Homo sapiens

PROVIDER: GSE8289 | GEO | 2008/06/20

SECONDARY ACCESSION(S): PRJNA101255

REPOSITORIES: GEO

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
		Other

Items per page:

1 - 1 of 1

Similar Datasets

HEK293 cells overexpressing wild type HNF4a2 or mutant forms HNF4a2 C106R or HNF4a2 R154X

Project description:Analysis of gene expression in human embryonic kidney cells HEK293 overexpressing the transcription factors HNF4a2 or mutant forms HNF4a2 C106R and HNF4a2 R154X, which were introduced by FRT/FLP recombination. The analysis was performed 24 hours following 1µg/ml tetracycline treatment to induce the expression of the genes. Results identify HNF4a regulated genes in kidney cells being several of these genes deregulated in renal cell carcinoma. Keywords = HEK293 embryonic kidney cells Keywords = HNF4a2 Keywords = tetracycline Keywords = FRT Keywords: ordered

2005-07-21 | GSE2700 | GEO

Transcription profiling of human HEK293 cells overexpressing HNF4a2 wild type or mutant forms C106R or R154X

Project description:Identification of genes regulated by the transcription factor HNF4a2 Experiment Overall Design: We used microarrays to identify genes regulated by the transcription factor HNF4a2. HEK293 cell lines containing doxycyclin-inducible wilt type or mutant forms of HNF4a2m which were introduced by FRT/FLP mediated recombination into FLP-In T-REx 293 cells (Invitrogen) were treated for 24 hours with 1 Âµg/ml doxycyclin. Gene expression profiles of induced and noninduced cells were compared to identify HNF4 regulated targets.

2008-10-18 | E-GEOD-8289 | biostudies-arrayexpress

Transcription profiling of human embryonic kidney cells HEK293 overexpressing the transcription factors HNF4a2 or mutant forms HNF4a2 C106R and HNF4a2 R154X to identify HNF4a regulated genes in kidney cells being several of these genes deregulated in renal cell carcinoma

Project description:Analysis of gene expression in human embryonic kidney cells HEK293 overexpressing the transcription factors HNF4a2 or mutant forms HNF4a2 C106R and HNF4a2 R154X, which were introduced by FRT/FLP recombination. The analysis was performed 24 hours following 1sg/ml tetracycline treatment to induce the expression of the genes. Results identify HNF4a regulated genes in kidney cells being several of these genes deregulated in renal cell carcinoma.<br><br>Note that files GSM52180.txt and GSM52184.txt as downloaded from GEO are identical.

2007-10-30 | E-GEOD-2700 | biostudies-arrayexpress

Porphyromonas gingivalis: Control (Wild-type W83) vs. its htrA mutant

Project description:Transcriptional profiling of the wild-type and its htrA mutant. Identification of genes that are affected by the htrA mutation in P. gingivalis Keywords: Genetic modification

2008-02-01 | GSE10027 | GEO

Analysis of spinal and muscle pathology in transgenic mice overexpressing wild-type and ALS-linked mutant MATR3.

Project description:Mutations in MATR3 have been associated with amyotrophic lateral sclerosis (ALS) as well as a form of distal myopathy termed vocal cord pharyngeal distal myopathy (VCPDM). To begin to understand how mutations in MATR3 may cause disease, here we provide initial characterization of transgenic (Tg) mice expressing human wild-type (WT) MATR3 (MATR3WT) and ALS-mutant F115C MATR3 (MATR3F115C) proteins under the control of the mouse prion promoter (MoPrP). For each construct, we established multiple independent lines of mice that stably transmitted the transgene. Unexpectedly, for all stably-transmitting lines examined, MATR3 transgenic mRNA expression was more robust in muscle, with minimal expression in spinal cord. The levels of transgenic mRNA in muscle did not differ between mice from our lead MATR3F115C line and lead MATR3WT line, but mice from the lead MATR3F115C line had significantly higher levels of MATR3 protein in muscle over the lead MATR3WT line. Mice from the three independent, established lines of MATR3F115C mice developed weakness in both fore- and hind-limbs as early as < 1 months of age; whereas, MATR3WT mice aged to > 20 months were not overtly distinguishable from non-transgenic (NT) littermates based on basic motor phenotype. Muscle of both MATR3WT and MATR3F115C mice showed vacuoles by 2 months of age which worsened by ~ 10 months, but vacuolation was noticeably more severe in MATR3F115C mice. Overall, our results indicate that increasing the levels of MATR3 in muscle can cause pathologic changes associated with myopathy, with MATR3F115C expression causing overt muscle atrophy and a profound motor phenotype. The findings suggest that analysis of muscle pathology in individuals harboring ALS-linked MATR3 mutations should be routinely considered.

| S-EPMC6299607 | biostudies-literature

Targets of HNF1b, HNF4a2 and HNF6 in INS-1 cells

Project description:A rat insulinoma cell line (INS-1) was generated that contains a FRT site for FLP recombinase mediated site specific integration of specific genes. In addition, the line contains the tetracycline repressor allowing tetracycline (tet) induction of the introduced gene. By comparing the gene expression profiles of uninduced and tet-induced cells, target genes of introduced transcription factors HNF1b, HNF4a2, and HNF6 (onecut1) were identified. Two different clones containing the same transcription factor were analyzed in the non-induced and tet-induced (24 h) state. Keywords: ordered

2004-11-05 | GSE1589 | GEO

Wild-type and mutant forms of the pyruvate dehydrogenase multienzyme complex from Bacillus subtilis.

Project description:A simple procedure is described for the purification of the pyruvate dehydrogenase complex and dihydrolipoamide dehydrogenase from Bacillus subtilis. The method is rapid and applicable to small quantities of bacterial cells. The purified pyruvate dehydrogenase complex (s0(20),w = 73S) comprises multiple copies of four different types of polypeptide chain, with apparent Mr values of 59 500, 55 000, 42 500 and 36 000: these were identified as the polypeptide chains of the lipoate acetyltransferase (E2), dihydrolipoamide dehydrogenase (E3) and the two types of subunit of the pyruvate decarboxylase (E1) components respectively. Pyruvate dehydrogenase complexes were also purified from two ace (acetate-requiring) mutants of B. subtilis. That from mutant 61142 was found to be inactive, owing to an inactive E1 component, which was bound less tightly than wild-type E1 and was gradually lost from the E2E3 subcomplex during purification. Subunit-exchange experiments demonstrated that the E2E3 subcomplex retained full enzymic activity, suggesting that the lesion was limited to the E1 component. Mutant 61141R elaborated a functional pyruvate dehydrogenase complex, but this also contained a defective E1 component, the Km for pyruvate being raised from 0.4 mM to 4.3 mM. The E1 component rapidly dissociated from the E2E3 subcomplex at low temperature (0-4 degrees C), leaving an E2E3 subcomplex which by subunit-exchange experiments was judged to retain full enzymic activity. These ace mutants provide interesting opportunities to analyse defects in the self-assembly and catalytic activity of the pyruvate dehydrogenase complex.

| S-EPMC1154380 | biostudies-other

Comparative Analysis of MMTV-neu tumors, preneoplastic MMTV-neu mammary gland, and Wild-type controls

Project description:To identify early events of erbB2-induced mammary tumorigenesis, we compared datasets from 14 genechip experiments including MMTV-neu tumors, preneoplastic neu mammary gland (adjacent neu), and age-matched, wild-type control mammary glands Keywords = transgenic mouse Keywords = MMTV-neu Keywords = erbB2 Keywords = HER2 Keywords = mammary tumor Keywords: ordered

2005-05-03 | GSE2528 | GEO

Kinetics and Thermodynamics of DNA Processing by Wild Type DNA-Glycosylase Endo III and Its Catalytically Inactive Mutant Forms.

Project description:Endonuclease III (Endo III or Nth) is one of the key enzymes responsible for initiating the base excision repair of oxidized or reduced pyrimidine bases in DNA. In this study, a thermodynamic analysis of structural rearrangements of the specific and nonspecific DNA-duplexes during their interaction with Endo III is performed based on stopped-flow kinetic data. 1,3-diaza-2-oxophenoxazine (tCO), a fluorescent analog of the natural nucleobase cytosine, is used to record multistep DNA binding and lesion recognition within a temperature range (5-37 °C). Standard Gibbs energy, enthalpy, and entropy of the specific steps are derived from kinetic data using Van't Hoff plots. The data suggest that enthalpy-driven exothermic 5,6-dihydrouracil (DHU) recognition and desolvation-accompanied entropy-driven adjustment of the enzyme-substrate complex into a catalytically active state play equally important parts in the overall process. The roles of catalytically significant amino acids Lys120 and Asp138 in the DNA lesion recognition and catalysis are identified. Lys120 participates not only in the catalytic steps but also in the processes of local duplex distortion, whereas substitution Asp138Ala leads to a complete loss of the ability of Endo III to distort a DNA double chain during enzyme-DNA complex formation.

| S-EPMC5924532 | biostudies-literature

Differentially expressed cellular genes in non-tumorigenic and tumorigenic HPV18 positive HeLa x fibroblast hybrid cells

Project description:Identification of genes differentially expressed in tumorigenic compared to non-tumorigenic, HPV18 positive cells Keywords: ordered

2013-11-27 | GSE14052 | GEO

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data