Anti-MRPL11 Antibody (ARG41863)

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Product datasheet [email protected] ARG41863 Package: 100 μl anti-MRPL11 antibody Store at: -20°C Summary Product Description Rabbit Polyclonal antibody recognizes MRPL11 Tested Reactivity Hu, Ms, Rat Tested Application IHC-P, WB Host Rabbit Clonality Polyclonal Isotype IgG Target Name MRPL11 Antigen Species Human Immunogen Recombinant fusion protein corresponding to aa. 1-192 of Human MRPL11. (NP_057134.1) Conjugation Un-conjugated Alternate Names MRP-L11; 39S ribosomal protein L11, mitochondrial; L11MT; L11mt; CGI-113 Application Instructions Application table Application Dilution IHC-P 1:50 - 1:100 WB 1:500 - 1:2000 Application Note * The dilutions indicate recommended starting dilutions and the optimal dilutions or concentrations should be determined by the scientist. Positive Control A549 Calculated Mw 21 kDa Observed Size ~ 19 kDa Properties Form Liquid Purification Affinity purified. Buffer PBS (pH 7.3), 0.02% Sodium azide and 50% Glycerol. Preservative 0.02% Sodium azide Stabilizer 50% Glycerol Storage instruction For continuous use, store undiluted antibody at 2-8°C for up to a week. For long-term storage, aliquot and store at -20°C. Storage in frost free freezers is not recommended. Avoid repeated freeze/thaw cycles. Suggest spin the vial prior to opening. The antibody solution should be gently mixed before use. www.arigobio.com 1/2 Note For laboratory research only, not for drug, diagnostic or other use. Bioinformation Gene Symbol MRPL11 Gene Full Name mitochondrial ribosomal protein L11 Background This nuclear gene encodes a 39S subunit component of the mitochondial ribosome. Alternative splicing results in multiple transcript variants. Pseudogenes for this gene are found on chromosomes 5 and 12. [provided by RefSeq, May 2014] Cellular Localization Mitochondrion. [UniProt] Images ARG41863 anti-MRPL11 antibody IHC-P image Immunohistochemistry: Paraffin-embedded Human stomach tissue stained with ARG41863 anti-MRPL11 antibody 1:100 dilution. ARG41863 anti-MRPL11 antibody WB image Western blot: 25 µg of A549 cell lysate stained with ARG41863 anti- MRPL11 antibody at 1:1000 dilution. www.arigobio.com 2/2 Powered by TCPDF (www.tcpdf.org).

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MRPL11 Antibody A
Revision 1 C 0 2 - t MRPL11 Antibody a e r o t S Orders: 877-616-CELL (2355) [email protected] Support: 877-678-TECH (8324) 9 9 Web: [email protected] 1 www.cellsignal.com 2 # 3 Trask Lane Danvers Massachusetts 01923 USA For Research Use Only. Not For Use In Diagnostic Procedures. Applications: Reactivity: Sensitivity: MW (kDa): Source: UniProt ID: Entrez-Gene Id: WB, IP H Mk Endogenous 21 Rabbit Q9Y3B7 65003 Product Usage Information Application Dilution Western Blotting 1:1000 Immunoprecipitation 1:50 Storage Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA and 50% glycerol. Store at –20°C. Do not aliquot the antibody. Specificity / Sensitivity MRPL11 Antibody detects endogenous levels of total MRPL11 protein. Species Reactivity: Human, Monkey Source / Purification Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to the sequence of human MRPL11. Antibodies are purified by peptide affinity chromatography. Background A subset of mitochondrial proteins are synthesized on the ribosomes within mitochondria (1). The 55S mammalian mitochondrial ribosomes are composed of a 28S small subunit and a 39S large subunit (1). Over 40 protein components have been identified from the large subunit of the human mitochondrial ribosome (1). The mitochondrial ribosomal protein L11 (MRPL11) is one such component (1). In animals, plants and fungi, this protein is translated from a gene in the nuclear genome (2). 1. Koc, E.C. et al. (2001) J Biol Chem 276, 43958-69. 2. Handa, H. et al. (2001) Mol Genet Genomics 265, 569-75.
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Supplementary Figures 1-14 and Supplementary References
SUPPORTING INFORMATION Spatial Cross-Talk Between Oxidative Stress and DNA Replication in Human Fibroblasts Marko Radulovic,1,2 Noor O Baqader,1 Kai Stoeber,3† and Jasminka Godovac-Zimmermann1* 1Division of Medicine, University College London, Center for Nephrology, Royal Free Campus, Rowland Hill Street, London, NW3 2PF, UK. 2Insitute of Oncology and Radiology, Pasterova 14, 11000 Belgrade, Serbia 3Research Department of Pathology and UCL Cancer Institute, Rockefeller Building, University College London, University Street, London WC1E 6JJ, UK †Present Address: Shionogi Europe, 33 Kingsway, Holborn, London WC2B 6UF, UK TABLE OF CONTENTS 1. Supplementary Figures 1-14 and Supplementary References. Figure S-1. Network and joint spatial razor plot for 18 enzymes of glycolysis and the pentose phosphate shunt. Figure S-2. Correlation of SILAC ratios between OXS and OAC for proteins assigned to the SAME class. Figure S-3. Overlap matrix (r = 1) for groups of CORUM complexes containing 19 proteins of the 49-set. Figure S-4. Joint spatial razor plots for the Nop56p complex and FIB-associated complex involved in ribosome biogenesis. Figure S-5. Analysis of the response of emerin nuclear envelope complexes to OXS and OAC. Figure S-6. Joint spatial razor plots for the CCT protein folding complex, ATP synthase and V-Type ATPase. Figure S-7. Joint spatial razor plots showing changes in subcellular abundance and compartmental distribution for proteins annotated by GO to nucleocytoplasmic transport (GO:0006913). Figure S-8. Joint spatial razor plots showing changes in subcellular abundance and compartmental distribution for proteins annotated to endocytosis (GO:0006897). Figure S-9. Joint spatial razor plots for 401-set proteins annotated by GO to small GTPase mediated signal transduction (GO:0007264) and/or GTPase activity (GO:0003924).
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MPV17L2 Is Required for Ribosome Assembly in Mitochondria Ilaria Dalla Rosa1,†, Romina Durigon1,†, Sarah F
8500–8515 Nucleic Acids Research, 2014, Vol. 42, No. 13 Published online 19 June 2014 doi: 10.1093/nar/gku513 MPV17L2 is required for ribosome assembly in mitochondria Ilaria Dalla Rosa1,†, Romina Durigon1,†, Sarah F. Pearce2,†, Joanna Rorbach2, Elizabeth M.A. Hirst1, Sara Vidoni2, Aurelio Reyes2, Gloria Brea-Calvo2, Michal Minczuk2, Michael W. Woellhaf3, Johannes M. Herrmann3, Martijn A. Huynen4,IanJ.Holt1 and Antonella Spinazzola1,* 1MRC National Institute for Medical Research, Mill Hill, London NW7 1AA, UK, 2MRC Mitochondrial Biology Unit, Wellcome Trust-MRC Building, Hills Road, Cambridge CB2 0XY, UK, 3Cell Biology, University of Kaiserslautern, 67663 Kaiserslautern, Germany and 4Centre for Molecular and Biomolecular Informatics, Radboud University Medical Centre, Geert Grooteplein Zuid 26–28, 6525 GA Nijmegen, Netherlands Received January 15, 2014; Revised May 7, 2014; Accepted May 23, 2014 ABSTRACT INTRODUCTION MPV17 is a mitochondrial protein of unknown func- The mammalian mitochondrial proteome comprises 1500 tion, and mutations in MPV17 are associated with or more gene products. The deoxyribonucleic acid (DNA) mitochondrial deoxyribonucleic acid (DNA) mainte- inside mitochondria DNA (mtDNA) contributes only 13 ∼ nance disorders. Here we investigated its most sim- of these proteins, and they make up 20% of the subunits ilar relative, MPV17L2, which is also annotated as of the oxidative phosphorylation (OXPHOS) system, which produces much of the cells energy. All the other proteins a mitochondrial protein. Mitochondrial fractionation
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C6orf203 Controls OXPHOS Function Through Modulation of Mitochondrial Protein Biosynthesis
bioRxiv preprint doi: https://doi.org/10.1101/704403; this version posted July 17, 2019. The copyright holder for this preprint (which was not certified by peer review) is the author/funder. All rights reserved. No reuse allowed without permission. C6orf203 controls OXPHOS function through modulation of mitochondrial protein biosynthesis number of characters excluding Materials and Methods: 40,651 Sara Palacios-Zambrano1,2, Luis Vázquez-Fonseca1,2, Cristina González-Páramos1,2, Laura Mamblona1,2, Laura Sánchez-Caballero3, Leo Nijtmans3, Rafael Garesse1,2 and Miguel Angel Fernández-Moreno1,2,* 1 Departamento de Bioquímica, Instituto de Investigaciones Biomédicas “Alberto Sols” UAM CSIC and Centro de Investigación Biomédica en Red en Enfermedades Raras (CIBERER). Facultad de Medicina, Universidad Autónoma de Madrid. Madrid 28029, Spain. 2 Instituto de Investigación Sanitaria Hospital 12 de Octubre (imas12), Madrid 28041, Spain. 3 Department of Pediatrics, Radboud Center for Mitochondrial Medicine, Radboud University Medical Center, Nijmegen, The Netherlands. * To whom correspondence should be addressed. Tel:+34 91 497 31 29; Email: [email protected] Running title “C6orf203 controls mt-proteins synthesis” bioRxiv preprint doi: https://doi.org/10.1101/704403; this version posted July 17, 2019. The copyright holder for this preprint (which was not certified by peer review) is the author/funder. All rights reserved. No reuse allowed without permission. ABSTRACT Mitochondria are essential organelles present in the vast majority of eukaryotic cells. Their central function is to produce cellular energy through the OXPHOS system, and functional alterations provoke so-called mitochondrial OXPHOS diseases. It is estimated that several hundred mitochondrial proteins have unknown functions. Very recently, C6orf203 was described to participate in mitochondrial transcription under induced mitochondrial DNA depletion stress conditions.
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MRPL11 Antibody (N-Term) Affinity Purified Rabbit Polyclonal Antibody (Pab) Catalog # Ap19151a
10320 Camino Santa Fe, Suite G San Diego, CA 92121 Tel: 858.875.1900 Fax: 858.622.0609 MRPL11 Antibody (N-term) Affinity Purified Rabbit Polyclonal Antibody (Pab) Catalog # AP19151a Specification MRPL11 Antibody (N-term) - Product Information Application WB,E Primary Accession Q9Y3B7 Other Accession NP_057134.1 Reactivity Human Host Rabbit Clonality Polyclonal Isotype Rabbit Ig Calculated MW 20683 Antigen Region 36-62 MRPL11 Antibody (N-term) - Additional Information MRPL11 Antibody (N-term) (Cat. #AP19151a) Gene ID 65003 western blot analysis in A549 cell line lysates (35ug/lane).This demonstrates the MRPL11 Other Names 39S ribosomal protein L11, mitochondrial, antibody detected the MRPL11 protein L11mt, MRP-L11, MRPL11 (arrow). Target/Specificity This MRPL11 antibody is generated from MRPL11 Antibody (N-term) - Background rabbits immunized with a KLH conjugated synthetic peptide between 36-62 amino Mammalian mitochondrial ribosomal proteins acids from the N-terminal region of human are encoded by MRPL11. nuclear genes and help in protein synthesis within the Dilution mitochondrion. Mitochondrial ribosomes WB~~1:1000 (mitoribosomes) consist of a small 28S subunit and a large 39S subunit. Format They have an estimated Purified polyclonal antibody supplied in PBS 75% protein to rRNA composition compared to with 0.09% (W/V) sodium azide. This prokaryotic ribosomes, antibody is purified through a protein A where this ratio is reversed. Another difference column, followed by peptide affinity between mammalian purification. mitoribosomes and prokaryotic ribosomes is that the latter contain Storage a 5S rRNA. Among different species, the Maintain refrigerated at 2-8°C for up to 2 proteins comprising the weeks. For long term storage store at -20°C mitoribosome differ greatly in sequence, and in small aliquots to prevent freeze-thaw sometimes in cycles.
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Transcriptomic and Proteomic Landscape of Mitochondrial
TOOLS AND RESOURCES Transcriptomic and proteomic landscape of mitochondrial dysfunction reveals secondary coenzyme Q deficiency in mammals Inge Ku¨ hl1,2†*, Maria Miranda1†, Ilian Atanassov3, Irina Kuznetsova4,5, Yvonne Hinze3, Arnaud Mourier6, Aleksandra Filipovska4,5, Nils-Go¨ ran Larsson1,7* 1Department of Mitochondrial Biology, Max Planck Institute for Biology of Ageing, Cologne, Germany; 2Department of Cell Biology, Institute of Integrative Biology of the Cell (I2BC) UMR9198, CEA, CNRS, Univ. Paris-Sud, Universite´ Paris-Saclay, Gif- sur-Yvette, France; 3Proteomics Core Facility, Max Planck Institute for Biology of Ageing, Cologne, Germany; 4Harry Perkins Institute of Medical Research, The University of Western Australia, Nedlands, Australia; 5School of Molecular Sciences, The University of Western Australia, Crawley, Australia; 6The Centre National de la Recherche Scientifique, Institut de Biochimie et Ge´ne´tique Cellulaires, Universite´ de Bordeaux, Bordeaux, France; 7Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden Abstract Dysfunction of the oxidative phosphorylation (OXPHOS) system is a major cause of human disease and the cellular consequences are highly complex. Here, we present comparative *For correspondence: analyses of mitochondrial proteomes, cellular transcriptomes and targeted metabolomics of five [email protected] knockout mouse strains deficient in essential factors required for mitochondrial DNA gene (IKu¨ ); expression, leading to OXPHOS dysfunction. Moreover,
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LETM1 Couples Mitochondrial DNA Metabolism and Nutrient Preference
Research Article LETM1 couples mitochondrial DNA metabolism and nutrient preference Romina Durigon1, Alice L Mitchell1,†, Aleck WE Jones1,†, Andreea Manole2,3, Mara Mennuni1, Elizabeth MA Hirst4, Henry Houlden2,3, Giuseppe Maragni5, Serena Lattante5, Paolo Niccolo’ Doronzio5, Ilaria Dalla Rosa1, Marcella Zollino5, Ian J Holt1,6,7 & Antonella Spinazzola1,2,* Abstract transcribed from mitochondrial DNA (mtDNA) and synthesized by the mitochondrial ribosomes (mitoribosomes), via a highly special- The diverse clinical phenotypes of Wolf–Hirschhorn syndrome ized system that is tightly coupled to the inner mitochondrial (WHS) are the result of haploinsufficiency of several genes, one of membrane (IMM; Liu & Spremulli, 2000). In yeasts, the proposed which, LETM1, encodes a protein of the mitochondrial inner machinery of co-translational membrane insertion includes Oxa1, membrane of uncertain function. Here, we show that LETM1 is mba1, and mdm38 (Ott & Herrmann, 2010). Mdm38 is an integral associated with mitochondrial ribosomes, is required for mitochon- inner membrane protein conserved among eukaryotes, and it is drial DNA distribution and expression, and regulates the activity of suggested to play a role in multiple facets of mitochondrial metabo- an ancillary metabolic enzyme, pyruvate dehydrogenase. LETM1 lism, the precise nature of which remains unclear. Under certain deficiency in WHS alters mitochondrial morphology and DNA orga- conditions, it co-fractionates with the mitoribosome, on buoyant nization, as does substituting ketone bodies for glucose in control density gradients (Frazier et al, 2006; Kehrein et al, 2015), and it is cells. While this change in nutrient availability leads to the death proposed to regulate mitochondrial translation (Bauerschmitt et al, of fibroblasts with normal amounts of LETM1, WHS-derived fibrob- 2010).
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International Journal of Biochemistry and Cell Biology 116 (2019) 105616
International Journal of Biochemistry and Cell Biology 116 (2019) 105616 Contents lists available at ScienceDirect International Journal of Biochemistry and Cell Biology journal homepage: www.elsevier.com/locate/biocel Mitochondrial oxidative phosphorylation is impaired in TALLYHO mice, a new obesity and type 2 diabetes animal model T Caroline A. Hunter, Funda Kartal, Zeynep C. Koc, Tamara Murphy, Jung Han Kim, James Denvir, ⁎ Emine C. Koc Department of Biomedical Sciences, Joan C. Edwards School of Medicine, Marshall University, Huntington, WV, 25755, United States ARTICLE INFO ABSTRACT Keywords: Type 2 diabetes has become an epidemic disease largely explained by the dramatic increase in obesity in recent TALLYHO/Jng mice years. Mitochondrial dysfunction is suggested as an underlying factor in obesity and type 2 diabetes. In this Mitochondrial biogenesis study, we evaluated changes in oxidative phosphorylation and mitochondrial biogenesis in a new human obesity Oxidative phosphorylation and type 2 diabetes model, TALLYHO/Jng mice. We hypothesized that the sequence variants identified in the Mitochondrial ribosomal proteins whole genome analysis of TALLYHO/Jng mice would affect oxidative phosphorylation and contribute to obesity Type 2 diabetes and insulin resistant phenotypes. To test this hypothesis, we investigated differences in the expression and activity of oxidative phosphorylation complexes, including the transcription and translation of nuclear- and mitochondrial-encoded subunits and enzymatic activities, in the liver and kidney of TALLYHO/Jng and C57BL/ 6 J mice. A significant decrease was observed in the expression of nuclear- and mitochondrial-encoded subunits of complex I and IV, respectively, in TALLYHO/Jng mice, which coincided with significant reductions in their enzymatic activities.
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DERIVED HUMAN MESENCHYMAL STEM CELLS Patricia Janicki, Stephane Boeuf, Eric Steck, Marcus Egermann, Philip Kasten§ and Wiltrud Richter*
PEuropean Janicki et Cells al. and Materials Vol. 21 2011 (pages 488-507) DOI: 10.22203/eCM.v021a37 Prediction of bone formation ISSNof human 1473-2262 MSC PREDICTION OF IN VIVO BONE FORMING POTENCY OF BONE MARROW- DERIVED HUMAN MESENCHYMAL STEM CELLS Patricia Janicki, Stephane Boeuf, Eric Steck, Marcus Egermann, Philip Kasten§ and Wiltrud Richter* Research Centre for Experimental O rthopaedics, Orthopaedic University Hospital Heidelberg, Heidelberg, Germany §Current address: Department of Orthopaedic Surgery, University of Dresden, Dresden, Germany A bstract Introduction Human mesenchymal stem cells (MSC) have attracted Mesenchymal stem cells (MSC) support the homeostasis much attention for tissue regeneration including repair of of mesenchymal tissues and their trophic and mesengenic non-healing bone defects. Heterogeneity of MSC cultures activities bear a high therapeutic potential for tissue and considerable donor variability however, still preclude regeneration. Reﬂ ecting the complexity of the stromal standardised production of MSC and point on functional system in bone marrow, MSC populations expanded deﬁ cits for some human MSC populations. We aimed to from marrow aspirates are heterogeneous in nature with identify functional correlates of donor-dependency of bone the exact composition depending on the donor (Rickard formation in order to develop a potency assay predicting et al., 1996; Majors et al., 1997; Muschler et al., 2001), the therapeutic capacity of human MSC before clinical the individual aspirate (Lazarus et al., 1997; Muschler transplantation. MSC from 29 donors were characterised in et al., 1997; Phinney et al., 1999; Muschler et al., 2001; vitro and results were correlated to bone formation potency Hernigou et al., 2006), applied isolation methods and in a beta-tricalcium-phosphate (β-TCP)-scaffold after expansion conditions, the latter of which differ largely subcutaneous implantation into immunocompromised mice.
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Mitochondrial Proteostasis Requires Genes Encoded in a Neurodevelopmental Syndrome Locus That Are Necessary for Synapse Function
bioRxiv preprint doi: https://doi.org/10.1101/2020.02.22.960971; this version posted February 25, 2020. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under aCC-BY 4.0 International license. Mitochondrial Proteostasis Requires Genes Encoded in a Neurodevelopmental Syndrome Locus that are Necessary for Synapse Function. Avanti Gokhale1*#, Chelsea E. Lee*1, Stephanie A. Zlatic1, Amanda A. H. Freeman1-2, Nicole Shearing1, Cortnie Hartwig1, Oluwaseun Ogunbona3, Julia L. Bassell1, Meghan E. Wynne1, Erica Werner1, Chongchong Xu4, Zhexing Wen1,4, Nicholas Seyfried5, Carrie E. Bearden6, Jill Glausier7, David A. Lewis7, Victor FaundeZ1#**. Departments of Cell Biology1, Center for the Study of Human Health2, Pathology3, and Psychiatry and Behavioral Sciences4, and Biochemistry5, Emory University, Atlanta, GA, USA, 30322. Semel Institute for Neuroscience and Human Behavior and Department of Psychology, UCLA, Los Angeles, CA, 900956. Departments of Psychiatry and Neuroscience, University of Pittsburgh, Pittsburgh, PA, 152137. #Address Correspondence to VF or AG [email protected] [email protected] * These authors contributed equally . bioRxiv preprint doi: https://doi.org/10.1101/2020.02.22.960971; this version posted February 25, 2020. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under aCC-BY 4.0 International license. 2 Abstract Eukaryotic cells maintain proteostasis through mechanisms that require cytoplasmic and mitochondrial translation.
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Mitochondrial Ribosomal Proteins: Candidate Genes for Mitochondrial Disease James E
March/April 2004 ⅐ Vol. 6 ⅐ No. 2 review Mitochondrial ribosomal proteins: Candidate genes for mitochondrial disease James E. Sylvester, PhD1, Nathan Fischel-Ghodsian, MD2, Edward B. Mougey, PhD1, and Thomas W. O’Brien, PhD3 Most of the energy requirement for cell growth, differentiation, and development is met by the mitochondria in the form of ATP produced by the process of oxidative phosphorylation. Human mitochondrial DNA encodes a total of 13 proteins, all of which are essential for oxidative phosphorylation. The mRNAs for these proteins are translated on mitochondrial ribosomes. Recently, the genes for human mitochondrial ribosomal proteins (MRPs) have been identified. In this review, we summarize their refined chromosomal location. It is well known that mutations in the mitochondrial translation system, i.e., ribosomal RNA and transfer RNA cause various pathologies. In this review, we suggest possible associations between clinical conditions and MRPs based on coincidence of genetic map data and chromosomal location. These MRPs may be candidate genes for the clinical condition or may act as modifiers of existing known gene mutations (mt-tRNA, mt-rRNA, etc.). Genet Med 2004:6(2):73–80. Key Words: mitochondrial, ribosomal proteins, oxidative phosphorylation, candidate genes, translation Most of the energy requirements for cell growth, differenti- THE MITORIBOSOME ation, and development are met by the mitochondrial ATP Human cells contain two genomes and two protein synthe- produced by the process of oxidative phosphorylation. Mito- sizing (translation) systems. The first is the nuclear genome of chondrial DNA encodes 13 essential proteins of this oxidative 3 ϫ 109 bp that has 30,000 to 40,000 genes coding a much phosphorylation system.
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Supplementary Table 2: Contd... Between Retinoblastoma and Controls No
Supplementary Table 2: Differential pathway genes (DPGs) Supplementary Table 2: Contd... between retinoblastoma and controls No. Genes No. Genes No. Genes No. Genes No. Genes No. Genes No. Genes No. Genes 67 MRPS18A 254 LPAR3 441 LAMC3 628 NTRK1 1 NUDT9 188 YARS 375 HDDC3 562 PGF 68 TARSL2 255 POLR1B 442 PDE6C 629 TPM3 2 MRPS2 189 WNT16 376 RPL30 563 VEGFC 69 GSK3B 256 MRPL16 443 FN1 630 TPR 3 EARS2 190 HLA‑DOA 377 GNG2 564 TGFA 70 C2 257 LPAR4 444 PDE6D 631 TFG 4 DCC 191 ENTPD6 378 PRUNE 565 EGF 71 APRT 258 ZNRD1 445 ITGA2 632 RASSF1 5 FGG 192 RPS27 379 RPL31 566 EGFR 72 MRPS21 259 MRPL17 446 PDE6G 633 RASSF5 6 ADPRM 193 YARS2 380 GNG3 567 ERBB2 73 SARS2 260 LPAR5 447 ITGA2B 634 STK4 7 MRPS5 194 FZD1 381 RPL32 568 PDGFA 74 TCF7 261 TWISTNB 448 PDE6H 635 DAPK1 8 EPRS 195 HLA‑DOB 382 GNG4 569 PDGFB 75 C5 262 MRPL18 449 ITGA3 636 DAPK3 9 CASP3 196 NUDT16 383 RPL34 570 PDGFRA 76 NT5C2 263 LPAR6 450 PDE9A 637 DAPK2 10 C3 197 RPS27L 384 GNG5 571 PDGFRB 77 RPS2 264 POLR1E 451 ITGA6 638 PLCG1 11 NUDT5 198 WARS2 385 RPL35 572 IGF1 78 SARS 265 MRPL19 452 PDE10A 639 PLCG2 12 MRPS6 199 FZD7 386 GNG7 573 IGF1R 79 TCF7L1 266 AGTR1 453 ITGAV 640 RALGDS 13 QRSL1 200 HLA‑DPA1 387 RPL35A 574 KITLG 80 C3AR1 267 POLR2A 454 PDE11A 641 RALA 14 CASP9 201 ITPA 388 GNG8 575 KIT 81 NT5C1A 268 MRPL20 455 ITGB1 642 RALB 15 CFB 202 RPS27A 389 RPL36 576 FLT3LG 82 RPS3 269 GNA12 456 ADSSL1 643 RALBP1 16 PGM1 203 WARS 390 GNG11 577 FLT3 83 PSTK 270 POLR2B 457 PTK2 644 CDC42 17 MRPS7 204 FZD2 391 RPL37 578 HGF 84 TCF7L2 271 MRPL21 458 ADSS 645 RAC1 18 GATB 205 HLA‑DPB1
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