• Lung adenocarcinoma
• MRPL21
• Pan-cancer analysis
• Prognosis
• Tumor microenvironment

• FSHD
• biosynthetic labelling
• deuterium oxide
• fractional synthesis rate
• heavy water
• mitochondria
• mitochondrial ribosome
• protein turnover
• proteome dynamics
• skeletal muscle

• Humans
• Muscular Dystrophy, Facioscapulohumeral/genetics
• Muscular Dystrophy, Facioscapulohumeral/metabolism
• Muscular Dystrophy, Facioscapulohumeral/pathology
• Proteome/metabolism
• Proteomics
• Homeodomain Proteins/metabolism
• Myoblasts/metabolism
• Muscle, Skeletal/metabolism

• R21 AR080887 NIAMS NIH HHS

Gastric carcinoma (GC) is a digestive system disease with high morbidity and mortality. However, early clinical detection is difficult, and the therapeutic effect for advanced disease is not satisfactory. Thus, finding new tumor markers and therapeutic targets conducive to the treatment of GC is imperative. MRPL35 is a member of the large subunit family of mitochondrial ribosomal protein. MRPL35 shows the characteristic of oncogene in colorectal cancer and esophageal cancer, which promotes the exploration of the correlation between MRPL35 and GC. We proposed that the expression of MRPL35 might be critical in GC.

To study the effect of MRPL35 knockdown on GC cell proliferation.

The expression of MRPL35 in GC was evaluated based on data from the public tumor database UALCAN (http://www.ualcan.path.uab.edu). The effect of the expression of MRPL35 on the prognosis was evaluated with KMplot (http://www.kmplot.com). The expression of MRPL35 was assessed on the tissue microarray by immunohistochemistry and the level of MRPL35 mRNA in 25 pairs of clinical GC tissues and matched adjacent tissues was detected by quantitative reverse transcription-polymerase chain reaction. Celigo cell count assay, colony formation assay, and flow cytometry were used to assess the role of MRPL35 in GC cell proliferation and apoptosis in vitro. Additionally, tumor formation experiment in BALB/c nude mice was utilized to determine the effect of MRPL35 on GC cell proliferation. After knockdown of MRPL35, related proteins were identified by isobaric tags for relative and absolute quantification analysis, and the expression of related proteins was detected by Western blot.

The expression of MRPL35 was up-regulated in GC (P = 1.77 × 10^-4). The Kaplan-Meier plots of the overall survival indicated that high expression of MRPL35 was associated with a poor survival in GC. Compared with adjacent tissues, the expression of MRPL35 in GC tissues was increased, which was related to age (P = 0.03), lymph node metastasis (P = 0.007), and pathological tumor-node-metastasis stage (P = 0.024). Knockdown of MRPL35 inhibited GC cell proliferation and colony formation and induced apoptosis. Animal experiment results showed that knockdown of MRPL35 inhibited tumor formation in BALB/c nude mice. Western blotting analysis showed that after knockdown of MRPL35, the expression of PICK1 and BCL-XL proteins decreased, and that of AGR2 protein increased.

Collectively, our findings demonstrate that knockdown of MRPL35 inhibits GC cell proliferation through related proteins including PICK1, BCL-XL, and AGR2.

• Gastric carcinoma
• MRPL35
• Apoptosis
• Proliferation
• Tissue microarray
• Isobaric tags for relative and absolute quantification

• Animals
• Apoptosis
• Cell Line, Tumor
• Cell Proliferation
• Gene Expression Regulation, Neoplastic
• Mice
• Mice, Inbred BALB C
• Mice, Nude
• Prognosis
• Stomach Neoplasms/genetics

• Parkinson's disease
• gut dysbiosis
• microbiome
• mitochondrial function
• mitoribosomes

To study the expression of MRPL13 in breast cancer tissues using TCGA database, analyze the correlation between the expression and clinicopathological characteristics of patients, and explore the role of MRPL13 in the development of breast cancer (BC).

The BC mRNA data and clinical information were downloaded from TCGA database. The correlation between MRPL13 expression and clinicopathological parameters was analyzed. Cox regression multivariate analysis was used to explore the factors affecting the prognosis of BC patients. The UALCAN database was used to analyze the expression level of MRPL13 in BC and its relationship with clinical pathological factors. The GSEA method was used to predict the possible regulatory pathways of MRPL13. Immune responses of MRPL13 expression were analyzed using TISIDB and CIBERSORT. Additionally, GEPIA, K-M survival analysis and data from the HPA were used to validate the outcomes.

The expression of MRPL13 in BC tissues was significantly higher than normal counterparts, patients with low MRPL13 expression had a better survival prognosis, also indicated an independent prognostic factor. GSEA analysis showed that the regulation of cell migration, positive regulation of endothelial cell migration, and Notch signaling pathway were enriched in tissues with low expression of MRPL13. Additionally, depleting MRPL13 expression inhibited invasion in MCF-10A and MCF-7 cells. Furthermore, PCR showed that MRPL13 affected VEGFA and MMP gene expression. CIBERSORT analysis revealed that the amount of NK cells decreased when MRPL13 expression was high.

The expression of MRPL13 mRNA is upregulated in BC tissues, and the expression level of MRPL13 is significantly related to the clinicopathological factors of patients. High MRPL13 expression is a poor prognostic factor for BC, and it can be used as a molecular marker for prognosis judgment and as a potential therapeutic target.

• MRPL13
• breast cancer
• cancer genome map
• clinical significance

Mammalian mitochondrial ribosomes translate 13 proteins encoded by mitochondrial genes, all of which play roles in the mitochondrial respiratory chain. After a long period of reconstruction, mitochondrial ribosomes are the most protein-rich ribosomes. Mitochondrial ribosomal proteins (MRPs) are encoded by nuclear genes, synthesized in the cytoplasm and then, transported to the mitochondria to be assembled into mitochondrial ribosomes. MRPs not only play a role in mitochondrial oxidative phosphorylation (OXPHOS). Moreover, they participate in the regulation of cell state as apoptosis inducing factors. Abnormal expressions of MRPs will lead to mitochondrial metabolism disorder, cell dysfunction, etc. Many researches have demonstrated the abnormal expression of MRPs in various tumors. This paper reviews the basic structure of mitochondrial ribosome, focuses on the structure and function of MRPs, and their relationships with cell apoptosis and diseases. It provides a reference for the study of the function of MRPs and the disease diagnosis and treatment.

• apoptosis
• biomarker
• cancer
• mitochondrial disease
• mitochondrial ribosomal proteins
• mitochondrial ribosome

• Aneuploidy
• Chemoresistance
• Colon cancer
• Hydroxyurea
• p53

• MRPL42
• apoptosis
• cell cycle
• glioma
• proliferation

Metastasis is a lethal step in the progression of breast cancer. None of the metastasis-associated biomarkers identified up to now has a definite prognostic value in breast cancer patients. This study was designed to identify biomarkers for breast cancer metastasis and predictors of the prognosis of breast cancer patients. The differentially expressed proteins between 23 paired primary breast tumor and metastatic lymph nodes were identified by quantitative iTRAQ proteomic analysis. Immunohistochemistry was applied to locate and assess the expression of NUCB2 in paired primary breast tumor and metastatic lymph node tissues (n = 106). The relationship between NUCB2 expression and the clinicopathological characteristics of breast cancer patients (n = 189) were analyzed by χ² test. Kaplan-Meier analysis and Cox hazard regression analysis were utilized to investigate the relationship between its expression and prognosis of breast cancer patients. The iTRAQ proteomic results showed that 4,837 confidential proteins were identified, 643 of which were differentially expressed in the primary breast cancer tissues and the paired metastatic lymph nodes. NUCB2 protein was found decreased in paired metastatic lymph nodes (P = 0.000), with the positive expression rate being 82% in primary breast cancer tissues and 47% in paired metastatic lymph nodes, respectively. According to Kaplan-Meier analysis, the overall survival time of patients with positive expression of NUCB2 protein were shorter than those with negative NUCB2 expression (P = 0.004). Cox regression model suggested that NUCB2 was a risk factor of breast cancer patients (P = 0.045, RR = 1.854). We conclude that NUCB2 can be used as a potential biomarker for breast cancer metastasis and a prognostic predictor of breast cancer patients.

• Breast cancer
• Metastasis
• Nucleobindin-2.
• Prognosis
• iTRAQ

Mitochondrial ribosomal protein S23 (MRPS23) has been shown to be involved in breast cancer cell proliferation and metastatic phenotypes of cervical cancer. Here we investigated its biological features in breast cancer for the first time. It demonstrated that knockdown of MRPS23 reduced breast cancer cell proliferation and induced apoptosis in vitro. Besides, shRNA targeting MRPS23 (shMRPS23) inhibited tumour proliferation and metastasis by blocking tumor angiogenesis in breast cancer xenograft rat model. Small animal positron emission tomography/computed tomography (PET/CT) with 2′-deoxy-2′-[¹⁸F] fluoro-D-glucose (FDG) was performed at four weeks after tumour cell injection. We found that FDG maximum standardized uptake value (SUVmax) significantly decreased by 31 ± 3% in the shMRPS23-treated group. But this change was not independent of metabolic tumour size. In addition, we also found that shMRPS23 could significantly suppress breast cancer metastasis through inhibiting epithelial mesenchymal transition (EMT) phenotype. The epithelial marker E-cadherin was increased, whereas the metastasis associated gene vimentin was decreased. Mechanistically, shMRPS23-treated tumours failed to progress through p53 and p21^WAF1/CIP1 activation, but not cytochrome c-mediated pathway. These findings suggest that MRPS23 is a potential therapeutic target for interference of breast cancer proliferation, angiogenesis and metastasis.

• MRPS23
• breast cancer
• metastasis
• p21 WAF1/CIP1
• p53

• Apoptosis
• Cancer
• Mitochondrial ribosomes
• Therapy

• Bioinformatics analysis
• Differentially expressed genes
• Differentially expressed miRNA
• Oral lichen planus

Ribosomal protein S7 (RPS7) acts as a tumor suppressor in primary tumorigenesis but its role in cancer metabolism remains unclear. In this study, we demonstrate that RPS7 inhibits the colorectal cancer (CRC) cell glycolysis by suppressing the expression of hypoxia-inducible transcription factor-1α (HIF-1α) and the metabolic promoting proteins glucose transporter 4 (GLUT4) and lactate dehydrogenase B (LDHB). Further study found that the enhanced expression of HIF-1α abrogates the overexpression effects of RPS7 on CRC. In vivo assays also demonstrate that RPS7 suppresses colorectal cancer tumorigenesis and glycolysis. Clinically, the tissue microarray (TMA) analysis discloses the negative regulatory association between RPS7 and HIF-1α in colorectal cancer. Meanwhile, overexpression of RPS7 in colorectal cancer tissues predicts good overall survival and progression-free survival, but high expression level of HIF-1α indicates poor overall survival and progression-free survival. Overall, we reveal that RPS7 inhibits colorectal cancer glycolysis through HIF-1α-associated signaling and may be a promising biomarker for prognosis prediction and a potential target for therapeutic treatment.

• CRC
• HIF-1α
• RPS7
• glycolysis
• proliferation

• Cell cycle
• Epidermal growth factor
• Epithelial to mesenchymal transition
• Ovarian cancer

• Carcinogenesis/genetics
• Gene Expression Regulation, Neoplastic
• Humans
• Models, Genetic
• Neoplasm Metastasis
• Neoplasms/genetics
• Neoplasms/metabolism
• Neoplasms/pathology
• Neoplasms/therapy
• Ribosomal Proteins/genetics
• Ribosomal Proteins/metabolism
• Ribosomes/genetics
• Ribosomes/metabolism
• Signal Transduction/genetics
• Tumor Suppressor Proteins/genetics
• Tumor Suppressor Proteins/metabolism

During cell stress, the transcription and translation of immediate early genes are prioritized, while most other messenger RNAs (mRNAs) are stored away in stress granules or degraded in processing bodies (P-bodies). TIA-1 is an mRNA-binding protein that needs to translocate from the nucleus to seed the formation of stress granules in the cytoplasm. Because other stress granule components such as TDP-43, FUS, ATXN2, SMN, MAPT, HNRNPA2B1, and HNRNPA1 are crucial for the motor neuron diseases amyotrophic lateral sclerosis (ALS)/spinal muscular atrophy (SMA) and for the frontotemporal dementia (FTD), here we studied mouse nervous tissue to identify mRNAs with selective dependence on Tia1 deletion. Transcriptome profiling with oligonucleotide microarrays in comparison of spinal cord and cerebellum, together with independent validation in quantitative reverse transcriptase PCR and immunoblots demonstrated several strong and consistent dysregulations. In agreement with previously reported TIA1 knock down effects, cell cycle and apoptosis regulators were affected markedly with expression changes up to +2-fold, exhibiting increased levels for Cdkn1a, Ccnf, and Tprkb vs. decreased levels for Bid and Inca1 transcripts. Novel and surprisingly strong expression alterations were detected for fat storage and membrane trafficking factors, with prominent +3-fold upregulations of Plin4, Wdfy1, Tbc1d24, and Pnpla2 vs. a −2.4-fold downregulation of Cntn4 transcript, encoding an axonal membrane adhesion factor with established haploinsufficiency. In comparison, subtle effects on the RNA processing machinery included up to 1.2-fold upregulations of Dcp1b and Tial1. The effect on lipid dynamics factors is noteworthy, since also the gene deletion of Tardbp (encoding TDP-43) and Atxn2 led to fat metabolism phenotypes in mouse. In conclusion, genetic ablation of the stress granule nucleator TIA-1 has a novel major effect on mRNAs encoding lipid homeostasis factors in the brain, similar to the fasting effect.

• Animals
• Apoptosis Regulatory Proteins/genetics
• Brain/metabolism
• Carrier Proteins/metabolism
• Cell Cycle Proteins/genetics
• Contactins/metabolism
• Cytoplasmic Granules/metabolism
• Gene Expression Profiling
• Homeostasis
• Lipid Metabolism/genetics
• Membrane Proteins/genetics
• Membrane Proteins/metabolism
• Mice
• Mice, Inbred C57BL
• Mice, Knockout
• Perilipin-4
• RNA, Messenger/metabolism
• RNA-Binding Proteins/genetics
• Spinal Cord/metabolism
• Stress, Physiological/genetics
• T-Cell Intracellular Antigen-1

• RP-MDM2-p53 pathway
• cancer
• drug discovery
• ribosomal protein
• ribosomopathy

Kaposi's sarcoma-associated herpesvirus (KSHV) is causally linked to several human cancers, including Kaposi's sarcoma, primary effusion lymphoma and multicentric Castleman's disease, malignancies commonly found in HIV-infected patients. While KSHV encodes diverse functional products, its mechanism of oncogenesis remains unknown. In this study, we determined the roles KSHV microRNAs (miRs) in cellular transformation and tumorigenesis using a recently developed KSHV-induced cellular transformation system of primary rat mesenchymal precursor cells. A mutant with a cluster of 10 precursor miRs (pre-miRs) deleted failed to transform primary cells, and instead, caused cell cycle arrest and apoptosis. Remarkably, the oncogenicity of the mutant virus was fully restored by genetic complementation with the miR cluster or several individual pre-miRs, which rescued cell cycle progression and inhibited apoptosis in part by redundantly targeting IκBα and the NF-κB pathway. Genomic analysis identified common targets of KSHV miRs in diverse pathways with several cancer-related pathways preferentially targeted. These works define for the first time an essential viral determinant for KSHV-induced oncogenesis and identify NF-κB as a critical pathway targeted by the viral miRs. Our results illustrate a common theme of shared functions with hierarchical order among the KSHV miRs.

Kaposi's sarcoma-associated herpesvirus (KSHV) is the causal agent of several human cancers. KSHV encodes over two dozen genes that regulate diverse cellular pathways. However, the molecular mechanism of KSHV-induced oncogenesis remains unknown. In this study, we determined the roles of KSHV microRNAs (miRs) in KSHV-induced oncogenesis using a recently developed KSHV cellular transformation system of primary rat mesenchymal precursor cells. A KSHV mutant with a cluster of 10 precursor miRs (pre-miRs) deleted failed to transform primary cells, and instead, caused cell cycle arrest and apoptosis. Expression of the miR cluster or several pre-miRs was sufficient to restore the oncogenicity of the mutant virus. KSHV miRs regulated cell cycle progression and inhibited apoptosis in part by redundantly targeting IκBα and the NF-κB pathway. By integrating gene expression profiling and target prediction, we identified common targets of KSHV miRs in diverse pathways. Importantly, several cancer-related pathways were preferentially targeted by KSHV miRs. These works have demonstrated for the first time the important roles of KSHV miRs in oncogenesis and identified NF-κB as a critical pathway targeted by the miRs. Our results reveal that shared function is a common theme of KSHV miRs, which manifest functional hierarchical order.

• Animals
• Carcinogenesis/genetics
• Cell Proliferation
• Cell Survival/genetics
• Cell Transformation, Viral/genetics
• Cells, Cultured
• Gene Regulatory Networks
• Gene Targeting
• Herpesvirus 8, Human/genetics
• Humans
• MicroRNAs/physiology
• Microarray Analysis
• Rats
• Signal Transduction/genetics
• Transcriptome

• CA132637 NCI NIH HHS
• R01 CA096512 NCI NIH HHS
• R01 CA124332 NCI NIH HHS
• CA096512 NCI NIH HHS
• P01 CA180779 NCI NIH HHS
• R01 CA177377 NCI NIH HHS
• CA124332 NCI NIH HHS
• CA177377 NCI NIH HHS

• cyclin E
• flow cytometry
• human peripheral blood lymphocyte
• restriction point

Our previous works revealed that human ribosomal protein S13 (RPS13) was up-regulated in multidrug-resistant gastric cancer cells and overexpression of RPS13 could protect gastric cancer cells from drug-induced apoptosis. The present study was designed to explore the role of RPS13 in tumorigenesis and development of gastric cancer. The expression of RPS13 in gastric cancer tissues and normal gastric mucosa was evaluated by immunohistochemical staining and Western blot analysis. It was found RPS13 was expressed at a higher level in gastric cancer tissues than that in normal gastric mucosa. RPS13 was then genetically overexpressed in gastric cancer cells or knocked down by RNA interference. It was demonstrated that up-regulation of RPS13 accelerated the growth, enhanced in vitro colony forming and soft agar cologenic ability and promoted in vivo tumour formation potential of gastric cancer cells. Meanwhile, down-regulation of RPS13 in gastric cancer cells resulted in complete opposite effects. Moreover, overexpression of RPS13 could promote G1 to S phase transition whereas knocking down of RPS13 led to G1 arrest of gastric cancer cells. It was further demonstrated that RPS13 down-regulated p27^kip1 expression and CDK2 kinase activity but did not change the expression of cyclin D, cyclin E, CDK2, CDK4 and p16^INK4A. Taken together, these data indicate that RPS13 could promote the growth and cell cycle progression of gastric cancer cells at least through inhibiting p27^kip1 expression.

• Animals
• Apoptosis
• Base Sequence
• Blotting, Western
• DNA Primers
• Humans
• Mice
• Mitochondrial Proteins/genetics
• Mitochondrial Proteins/metabolism
• Mutation
• NIH 3T3 Cells
• Protein Binding
• Proto-Oncogene Proteins c-bcl-2/metabolism
• Ribosomal Proteins/genetics
• Ribosomal Proteins/metabolism
• Sequence Deletion
• Two-Hybrid System Techniques

• 1SC3GM083732 NIGMS NIH HHS
• S06 GM08127-28 NIGMS NIH HHS

• Adenosine Triphosphate/genetics
• Adenosine Triphosphate/metabolism
• DNA, Mitochondrial/metabolism
• Disease/genetics
• Gene Expression
• Genes, Mitochondrial
• Humans
• Mitochondria/genetics
• Mitochondria/metabolism
• Mitochondrial Diseases/genetics
• Mitochondrial Proteins/metabolism
• RNA/metabolism
• RNA, Mitochondrial
• Ribosomes/metabolism
• Transcription, Genetic

• R01 HL059655 NHLBI NIH HHS
• R01 NS056206 NINDS NIH HHS
• R01 NS056206-03 NINDS NIH HHS
• HL-059655 NHLBI NIH HHS

AIM: To investigate alternative or subordinate pathways involved in colorectal tumorigenesis and tumor growth, possibly determining at-risk populations and predicting responses to treatment.

METHODS: Using microarray gene-expression analysis, we analyzed patterns of gene expression relative to canonical molecular changes and clinicopathological features in 84 sporadic colorectal cancer patients, standardized by tumor location. Subsets of differentially expressed genes were confirmed by real-time reverse-transcript polymerase chain reaction (RT-PCR).

RESULTS: The largest number of genes identified as being differentially expressed was by tumor location, and the next largest number by lymphovascular or neural invasion of tumor cells and by mismatch repair (MMR) defects. Amongst biological processes, the immune response was significantly implicated in entire molecular changes observed during colorectal tumorigenesis (P < 0.001). Amongst 47 differentially expressed genes, seven (PISD, NIBP, BAI2, STOML1, MRPL21, MRPL16, and MKKS) were newly found to correlate with tumorigenesis and tumor growth. Most location-associated molecular changes had distinct effects on gene expression, but the effects of the latter were sometimes contradictory.

CONCLUSION: We show that several differentially expressed genes were associated with canonical molecular changes in sporadic colorectal cancers, possibly constituting alternative or subordinate pathways of tumorigenesis. As tumor location was the dominant factor influencing differential gene expression, location-specific analysis may identify location-associated pathways and enhance the accuracy of class prediction.

• Colorectal adenocarcinomas
• Sporadic
• Gene expression
• Profiling
• Tumorigenesis

• mitochondria
• ribosome
• ribosomal subunit
• respiratory chain complexes
• ribosomal proteins

• DNA, Mitochondrial/genetics
• DNA, Mitochondrial/metabolism
• Humans
• Mitochondria/genetics
• Mitochondria/physiology
• Mitochondrial Proteins/genetics
• Mitochondrial Proteins/physiology
• Models, Molecular
• Mutation
• RNA, Ribosomal/genetics
• RNA, Ribosomal, 16S/genetics
• Ribosomal Proteins/genetics
• Ribosomal Proteins/physiology
• Ribosome Subunits, Large/metabolism
• Ribosome Subunits, Small/metabolism

• R01 GM032734 NIGMS NIH HHS
• R01 GM032734-15 NIGMS NIH HHS

Ribosomal proteins are encoded by a gene family, members of which are overexpressed in human cancers. Many of them have been found, using oligonucleotide microarray hybridization, to be differentially expressed in the faeces of patients with various stages of col-orectal cancer (CRC). The gene encoding ribosomal protein L19 (RPL19), a prognostic marker for human prostate cancer, is differentially expressed in CRC patients. Measurement of faecal RPL19 mRNA might improve prognostic prediction for CRC patients. Using quantitative real-time reverse transcription PCR, levels of RPL19 mRNA were detected in samples of colonic tissues from 44 CRC patients, in the faeces of 54 CRC patients and 15 controls, and in 11 colonic cell lines. Seven of 24 patients with late-stage CRC (Dukes' stages C and D) expressed over 2-fold more RPL19 in colonic tumour tissues than in corresponding normal tissues (P= 0.038). The mean faecal RPL19 mRNA levels of late-staged patients were higher than those of controls (P= 0.003) and early-staged patients (P= 0.008). Patients with both high serum levels of carcinoembryonic antigen (CEA; >5 ng/mL) and high-faecal RPL19 mRNA (≥0.0069) had higher risk (odds ratio, 8.0; P= 0.015) and lower overall 48-month survival (33.8 ± 13.7%, P= 0.013). Oligonucleotide microarray hybridization analysis of faecal molecules identified gene transcripts differentially present in faeces. In conclusion, faecal RPL19 expression is associated with advanced tumour stages and addictive to serum CEA in predicting prognosis of CRC patients.

• Breeding
• DNA Primers
• Helianthus/genetics
• Linkage Disequilibrium
• Polymerase Chain Reaction
• Polymorphism, Single Nucleotide

• Breeding
• DNA Primers
• Helianthus/genetics
• Linkage Disequilibrium
• Polymerase Chain Reaction
• Polymorphism, Single Nucleotide

• Amino Acid Sequence
• Animals
• Base Sequence
• Blotting, Western
• Cell Cycle/genetics
• Cell Cycle/physiology
• Cell Proliferation
• Cell Survival/genetics
• Cell Survival/physiology
• Cyclin-Dependent Kinase Inhibitor p21/genetics
• Cyclin-Dependent Kinase Inhibitor p21/metabolism
• Gene Expression
• Immunohistochemistry
• Membrane Potential, Mitochondrial/physiology
• Mice
• Microscopy, Confocal
• Mitochondria/metabolism
• Mitochondria/physiology
• Mitochondrial Proteins/genetics
• Mitochondrial Proteins/metabolism
• Mitochondrial Proteins/physiology
• Molecular Sequence Data
• NIH 3T3 Cells
• Reactive Oxygen Species/metabolism
• Ribosomal Proteins/genetics
• Ribosomal Proteins/metabolism
• Ribosomal Proteins/physiology
• Sequence Alignment
• Tumor Suppressor Protein p53/genetics
• Tumor Suppressor Protein p53/metabolism

• Binding Sites
• Nuclear Proteins
• Recombinant Fusion Proteins
• Ribosomal Proteins/physiology
• Schizosaccharomyces/chemistry
• Schizosaccharomyces/genetics
• Schizosaccharomyces pombe Proteins/physiology
• Transcription Factors
• Transcriptional Activation