SIAH2 Antibody

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Efficient Professional Protein and Antibody Platforms SIAH2 Antibody Basic information: Catalog No.: UPA61750 Source: Rabbit Size: 50ul/100ul Clonality: polyclonal Concentration: 1mg/ml Isotype: Rabbit IgG Purification: affinity purified by Protein A Useful Information: Applications: WB:1:500-2000 Reactivity: Human, Mouse, Rat, Chicken, Dog, Pig, Cow, Horse, Rabbit Specificity: This antibody recognizes SIAH2 protein. Immunogen: KLH conjugated synthetic peptide derived from human SIAH2 201-300/324 E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioe- ster and then directly transfers the ubiquitin to targeted substrates. Medi- ates E3 ubiquitin ligase activity either through direct binding to substrates or by functioning as the essential RING domain subunit of larger E3 com- plexes. Triggers the ubiquitin-mediated degradation of many substrates, in- Description: cluding proteins involved in transcription regulation (POU2AF1, PML, NCOR1), a cell surface receptor (DCC), an antiapoptotic protein (BAG1), and a protein involved in synaptic vesicle function in neurons (SYP). Mediates ubiquitination and proteasomal degradation of DYRK2 in response to hy- poxia. It is thereby involved in apoptosis, tumor suppression, cell cycle, transcription and signaling processes. Has some overlapping function with SIAH1. Triggers the ubiquitin-mediated degradation of TRAF2, whereas SI- AH1 can not. Promotes monoubiquitination of SNCA. Uniprot: O43255 Human BiowMW: 35 KDa Buffer: 0.01M TBS(pH7.4) with 1% BSA, 0.03% Proclin300 and 50% Glycerol. Storage: Store at 4°C short term and -20°C long term. Avoid freeze-thaw cycles. Note: For research use only, not for use in diagnostic procedure. Data: Gene Universal Technology Co. Ltd www.universalbiol.com Tel: 0550-3121009 E-mail: [email protected] Efficient Professional Protein and Antibody Platforms Sample: K562(Human) Cell Lysate at 30 ug Pri- mary: Anti- SIAH2 at 1/1000 dilution Secondary: IRDye800CW Goat Anti-Rabbit IgG at 1/20000 dilution Predicted band size: 35 kD Observed band size: 36 kD Gene Universal Technology Co. Ltd www.universalbiol.com Tel: 0550-3121009 E-mail: [email protected] .

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Critical Function of Siah2 in Tumorigenesis
AIMS Molecular Science, 4(4): 415-423 DOI: 10.3934/molsci.2017.4.415 Received 31 July 2017, Accepted 21 September 2017, Published 11 October 2017 http://www.aimspress.com/journal/Molecular Review Critical function of Siah2 in tumorigenesis Kazunobu Baba, Tadaaki Miyazaki* Department of Probiotics Immunology, Institute for Genetic Medicine, Hokkaido University, North 15 West 7, Kita-ku, Sapporo City, Hokkaido, Japan * Correspondence: Email: [email protected]; Tel: 81-011-706-8095. Abstract: The seven in absentia homolog (Siah) family proteins are components of E3 RING zinc finger ubiquitin ligase complexes that catalyze the ubiquitination of proteins. Siah proteins target their substrates for proteasomal degradation. Evidence is growing that Siah proteins are implicated in the progression of various cancer cells and play a critical role in angiogenesis and tumorigenesis, particularly through Ras, p53, estrogen, and hypoxia inducible factor (HIF)-mediated signaling pathways in response to DNA damage or hypoxia. Keywords: Siah2; Nrf2; ROS metabolism; Hypoxia 1. Introduction The seven in absentia (Sina) gene was initially identified to be critical for photoreceptor cell development in Drosophila [1]. As its mammalian orthologs, murine and human homologs of the Sina gene have also been identified. In Xenopus and mice, Sina homologs (Siahs) were isolated as three Siah proteins, Siah1a, Siah1b, and Siah2, which are encoded by different genes [2]. In contrast, the human Siah proteins consist of two homologs, Siah1 and Siah2, which are encoded by the SIAH1 and SIAH2 genes, respectively [3]. Siah1 and Siah2 have the high sequence similarity of their N-terminal RING finger domain, central cysteine-rich domain, and C-terminal substrate binding domain (SBD); however, Siah1 and Siah2 apparently have distinct but overlapping functions as proteins of a tumor suppressor gene and a proto-oncogene, respectively (Figure 1) [4].
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Supplementary Materials
Supplementary materials Supplementary Table S1: MGNC compound library Ingredien Molecule Caco- Mol ID MW AlogP OB (%) BBB DL FASA- HL t Name Name 2 shengdi MOL012254 campesterol 400.8 7.63 37.58 1.34 0.98 0.7 0.21 20.2 shengdi MOL000519 coniferin 314.4 3.16 31.11 0.42 -0.2 0.3 0.27 74.6 beta- shengdi MOL000359 414.8 8.08 36.91 1.32 0.99 0.8 0.23 20.2 sitosterol pachymic shengdi MOL000289 528.9 6.54 33.63 0.1 -0.6 0.8 0 9.27 acid Poricoic acid shengdi MOL000291 484.7 5.64 30.52 -0.08 -0.9 0.8 0 8.67 B Chrysanthem shengdi MOL004492 585 8.24 38.72 0.51 -1 0.6 0.3 17.5 axanthin 20- shengdi MOL011455 Hexadecano 418.6 1.91 32.7 -0.24 -0.4 0.7 0.29 104 ylingenol huanglian MOL001454 berberine 336.4 3.45 36.86 1.24 0.57 0.8 0.19 6.57 huanglian MOL013352 Obacunone 454.6 2.68 43.29 0.01 -0.4 0.8 0.31 -13 huanglian MOL002894 berberrubine 322.4 3.2 35.74 1.07 0.17 0.7 0.24 6.46 huanglian MOL002897 epiberberine 336.4 3.45 43.09 1.17 0.4 0.8 0.19 6.1 huanglian MOL002903 (R)-Canadine 339.4 3.4 55.37 1.04 0.57 0.8 0.2 6.41 huanglian MOL002904 Berlambine 351.4 2.49 36.68 0.97 0.17 0.8 0.28 7.33 Corchorosid huanglian MOL002907 404.6 1.34 105 -0.91 -1.3 0.8 0.29 6.68 e A_qt Magnogrand huanglian MOL000622 266.4 1.18 63.71 0.02 -0.2 0.2 0.3 3.17 iolide huanglian MOL000762 Palmidin A 510.5 4.52 35.36 -0.38 -1.5 0.7 0.39 33.2 huanglian MOL000785 palmatine 352.4 3.65 64.6 1.33 0.37 0.7 0.13 2.25 huanglian MOL000098 quercetin 302.3 1.5 46.43 0.05 -0.8 0.3 0.38 14.4 huanglian MOL001458 coptisine 320.3 3.25 30.67 1.21 0.32 0.9 0.26 9.33 huanglian MOL002668 Worenine
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Siah - a Promising Anti-Cancer Target
Author Manuscript Published OnlineFirst on March 1, 2013; DOI: 10.1158/0008-5472.CAN-12-4348 Author manuscripts have been peer reviewed and accepted for publication but have not yet been edited. Siah - a promising anti-cancer target Christina SF Wong1 and Andreas Möller1 1 Tumour Microenvironment Laboratory, Queensland Institute of Medical Research, 300 Herston Road, Herston, Queensland 4006, Australia. Corresponding Author: Andreas Möller ([email protected]) Running title: Siah and Cancer Keywords: Siah1, Siah2, E3 Ubiquitin ligases, Cancer Potential conflict of interest: The authors declare no conflict of interest. Word count: Abstract: 100 words; Text: 2590 words; Number of Figures: 1; Number of Tables: 1 1 Downloaded from cancerres.aacrjournals.org on September 29, 2021. © 2013 American Association for Cancer Research. Author Manuscript Published OnlineFirst on March 1, 2013; DOI: 10.1158/0008-5472.CAN-12-4348 Author manuscripts have been peer reviewed and accepted for publication but have not yet been edited. Abstract: Siah ubiquitin ligases play important roles in a number of signaling pathways involved in the progression and spread of cancer in cell-based models but their role in tumor progression remains controversial. Siah proteins have been described to be both oncogenic as well as tumor-suppressive in a variety of patient cohort studies and animal cancer models. This review collates the current knowledge of Siah in cancer progression and identifies potential methods of translation of these findings into the clinic. Furthermore, key experiments needed to close the gaps in our understanding of the role Siah proteins play in tumor progression are suggested. 2 Downloaded from cancerres.aacrjournals.org on September 29, 2021.
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SIAH2-Mediated and Organ-Specific Restriction of HO-1 Expression by A
www.nature.com/scientificreports OPEN SIAH2-mediated and organ-specifc restriction of HO-1 expression by a dual mechanism Shashipavan Chillappagari1*, Ratnal Belapurkar1, Andreas Möller2, Nicole Molenda3, Michael Kracht4, Susanne Rohrbach3 & M. Lienhard Schmitz1* The intracellular levels of the cytoprotective enzyme heme oxygenase-1 (HO-1) are tightly controlled. Here, we reveal a novel mechanism preventing the exaggerated expression of HO-1. The analysis of mice with a knock-out in the ubiquitin E3 ligase seven in absentia homolog 2 (SIAH2) showed elevated HO-1 protein levels in specifc organs such as heart, kidney and skeletal muscle. Increased HO-1 protein amounts were also seen in human cells deleted for the SIAH2 gene. The higher HO-1 levels are not only due to an increased protein stability but also to elevated expression of the HO-1 encoding HMOX1 gene, which depends on the transcription factor nuclear factor E2-related factor 2 (NRF2), a known SIAH2 target. Dependent on its RING (really interesting new gene) domain, expression of SIAH2 mediates proteasome-dependent degradation of its interaction partner HO-1. Additionally SIAH2-defcient cells are also characterized by reduced expression levels of glutathione peroxidase 4 (GPX4), rendering the knock-out cells more sensitive to ferroptosis. Ubiquitin E3 ligases regulate the activity and turnover of many target proteins, thus controlling key features such as metabolism, stress signaling and cell cycle progression1. Te RING family of ubiquitin E3 ligases comprises the SIAH family. Te human genome encodes SIAH1 and the homologous SIAH2 protein as well as SIAH3, which lacks a functional RING domain and is only expressed in a limited subset of cancer cell lines2.
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Expression and Purification of the Predicted PEG10 Aspartyl Protease
Expression and purification of the predicted PEG10 aspartyl protease domain Caillan Crowe-McAuliffe A thesis submitted for the degree of Master of Science Department of Biochemistry University of Otago, Dunedin, New Zealand. April 2013 Abstract Paternally Expressed Gene 10 (PEG10) is an imprinted, retrotransposon-derived gene found in mammals. Although many of the retrotransposon domains have become de- generated in PEG10, a predicted retroviral-type aspartyl protease (AP) domain has been highly conserved. Retroviral-type APs play a crucial role in the replication of some retroviruses such as the Human Immunodeficiency Virus (HIV) and are there- fore important drug targets. Consequently, extensive biochemical and structural data are available for this class of proteins, although the vast majority of this has been gath- ered from only a small number of retroviral enzymes. Preliminary evidence indicates that the PEG10 AP is an active protease, although proteolysis by this enzyme has yet to be observed in vitro (Clark et al., 2007). This study aimed to express, purify, and characterise the predicted PEG10 AP. A number of PEG10 AP clones, each with different termini and across more than one recombinant expression system, were expressed to produce the PEG10 AP domain in E. coli. The majority of expressed proteins were largely insoluble and unsuitable for further characterisation. One clone, however, produced soluble PEG10 AP in sufficient quantities for purification and further analysis. Several lines of evidence indicated that the purified protein was dimeric in solution, consistent with the quaternary structure of other retroviral-type APs. The results presented in this thesis support the hypothesis that the PEG10 AP is active and has retained characteristics from the ancestral retrotransposon enzyme.
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Monoclonal Anti-Siah2 Antibody Produced in Mouse
Monoclonal Anti-Siah2 Clone Siah2-369 Purified Mouse Immunoglobulin Product Number S 7945 Product Description functions. Siah2 was implicated in the regulation of key Monoclonal Anti-Siah2 (mouse IgG1 isotype) is derived proteins in the immune system such as TRAF, Vav1, from the hybridoma Siah2-369 produced by the fusion of and OBF-1. Knockout mice of Siah1a exhibit severe mouse myeloma cells (NS1 cell) and splenocytes from growth retardation, early lethality and exhibit a block in BALB/c mice immunized with a synthetic peptide meiotic cell division during meiosis I of spermato- corresponding to amino acids 2-17 of human Siah2, genesis. However, knockout mice of Siah2 are largely conjugated to KLH. The isotype is determined using a phenotypically normal.4 Siah1a and Siah2 are important double diffusion immunoassay using Mouse Monoclonal for the regulation of the PHD enzymes (prolylhydrox- Antibody Isotyping Reagents (Sigma ISO-2). ylases) that are responsible for the prolyhydroxylation of HIF a protein under hypoxia conditions.5 Monoclonal Anti-Siah2 recognizes human, monkey, bovine, canine, hamster, and mouse Siah2 (~37 kDa). Reagent The antibody can be used in ELISA, immunocyto- The antibody is supplied as a solution in 0.01 M phos- chemistry, and immunoblotting. phate buffered saline, pH 7.4, containing 15 mM sodium azide. Ubiquitination of proteins is an important process in the pathway leading to their degradation through the Antibody Concentration: ~2 mg/mL proteasome. The Siah (Seven in absentia homologue) protein family belongs to the E3 ubiquitin ligase protein Precautions and Disclaimer family. These proteins can mediate E3 ubiquitin ligase Due to the sodium azide content, a material safety data activity either by direct binding to protein targets or by sheet (MSDS) for this product has been sent to the functioning as the essential RING domain subunit of attention of the safety officer of your institution.
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Pw1 Peg3 Is a Potential Cell Death Mediator and Cooperates With
Pw1͞Peg3 is a potential cell death mediator and cooperates with Siah1a in p53-mediated apoptosis Fre´ de´ ric Relaix*†, Xiao-jun Wei‡, Wei Li‡, Jianjing Pan‡, Yahong Lin‡§, David D. Bowtell¶, David A. Sassoon*, and Xiangwei Wu‡§ʈ ‡The Derald H. Ruttenberg Cancer Center and *The Brookdale Center for Molecular and Developmental Biology, The Mount Sinai Medical Center, New York, NY 10029; and ¶Trescowthick Research Laboratories, Peter MacCallum Cancer Institute, Melbourne, Victoria, Australia Edited by George F. Vande Woude, Van Andel Research Institute, Grand Rapids, MI, and approved December 17, 1999 (received for review September 3, 1999) Induction of wild-type p53 in mouse ﬁbroblasts causes cell cycle members of the Siah family as Pw1͞Peg3 interacting proteins, arrest at the G1 phase, whereas coexpression of p53 and the including Siah1a. This finding is striking because Siah1a also has protooncogene c-myc induces apoptosis. Although p53 transcrip- been implicated in the p53-mediated cell death pathway. The tional activity generally is required for both pathways, the molec- murine Siah1 gene was identified, via differential cDNA analysis, ular components mediating p53-dependent apoptosis are not well as a p53-induced gene in a leukemia cell line that conditionally understood. To identify factors that could mediate p53-induced cell undergoes growth arrest and apoptosis (6, 7). It also has been death, we used a comparative RNA differential display procedure. observed that overexpression of human Siah1a results in apo- We have identiﬁed Pw1͞Peg3 as a gene product induced during ptosis in U937 cell but only induces cellular growth arrest in two p53͞c-myc-mediated apoptosis.
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Downloaded Per Proteome Cohort Via the Web- Site Links of Table 1, Also Providing Information on the Deposited Spectral Datasets
www.nature.com/scientificreports OPEN Assessment of a complete and classifed platelet proteome from genome‑wide transcripts of human platelets and megakaryocytes covering platelet functions Jingnan Huang1,2*, Frauke Swieringa1,2,9, Fiorella A. Solari2,9, Isabella Provenzale1, Luigi Grassi3, Ilaria De Simone1, Constance C. F. M. J. Baaten1,4, Rachel Cavill5, Albert Sickmann2,6,7,9, Mattia Frontini3,8,9 & Johan W. M. Heemskerk1,9* Novel platelet and megakaryocyte transcriptome analysis allows prediction of the full or theoretical proteome of a representative human platelet. Here, we integrated the established platelet proteomes from six cohorts of healthy subjects, encompassing 5.2 k proteins, with two novel genome‑wide transcriptomes (57.8 k mRNAs). For 14.8 k protein‑coding transcripts, we assigned the proteins to 21 UniProt‑based classes, based on their preferential intracellular localization and presumed function. This classifed transcriptome‑proteome profle of platelets revealed: (i) Absence of 37.2 k genome‑ wide transcripts. (ii) High quantitative similarity of platelet and megakaryocyte transcriptomes (R = 0.75) for 14.8 k protein‑coding genes, but not for 3.8 k RNA genes or 1.9 k pseudogenes (R = 0.43–0.54), suggesting redistribution of mRNAs upon platelet shedding from megakaryocytes. (iii) Copy numbers of 3.5 k proteins that were restricted in size by the corresponding transcript levels (iv) Near complete coverage of identifed proteins in the relevant transcriptome (log2fpkm > 0.20) except for plasma‑derived secretory proteins, pointing to adhesion and uptake of such proteins. (v) Underrepresentation in the identifed proteome of nuclear‑related, membrane and signaling proteins, as well proteins with low‑level transcripts.
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Identification of Novel Protein Interaction Partners of The
Zurich Open Repository and Archive University of Zurich Main Library Strickhofstrasse 39 CH-8057 Zurich www.zora.uzh.ch Year: 2007 Identification of novel protein interaction partners of the oxygen-sensing HIF prolyl-4-hydroxylase 1 (PHD1) and characterization of the interactor onconeural cerebellar degeneration-related protein 2 (Cdr2) Hofmann, Verena Simone Posted at the Zurich Open Repository and Archive, University of Zurich ZORA URL: https://doi.org/10.5167/uzh-163609 Dissertation Published Version Originally published at: Hofmann, Verena Simone. Identification of novel protein interaction partners of the oxygen-sensing HIF prolyl-4-hydroxylase 1 (PHD1) and characterization of the interactor onconeural cerebellar degeneration- related protein 2 (Cdr2). 2007, University of Zurich, Faculty of Science. Identification of Novel Protein Interaction Partners of the Oxygen-sensing HIF Prolyl-4-hydroxylase 1 (PHD1) and Characterization of the Interactor Onconeural Cerebellar Degeneration-related Protein 2 (Cdr2) Dissertation zur Erlangung der naturwissenschaftlichen Doktorwürde (Dr. sc. nat.) vorgelegt der Mathematisch-naturwissenschaftlichen Fakultät der Universität Zürich von Verena Simone Hofmann aus Deutschland Promotionskomitee Prof. Dr. Roland H. Wenger (Vorsitz) Dr. Gieri Camenisch (Leitung der Dissertation) PD Dr. Ingo Flamme Zürich, 2007 This work has been performed under the supervision of Dr. Gieri Camenisch and Prof. Dr. Roland H. Wenger at the Institute of Physiology and Zürich Center for Integrative Human Physiology (ZIHP),
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Vav1 Is Essential for HIF-1Α Activation Via a Lysosomal VEGFR1-Mediated Degradation Mechanism in Endothelial Cells
cancers Article Vav1 is Essential for HIF-1α Activation via a Lysosomal VEGFR1-Mediated Degradation Mechanism in Endothelial Cells , Jaewoo Hong * y , Yongfen Min y, Todd Wuest and P. Charles Lin * Center for Cancer Research, National Cancer Institute, National Institutes of Health, Frederick, MD 21704, USA; [email protected] (Y.M.); [email protected] (T.W.) * Correspondence: [email protected] (J.H.); [email protected] (P.C.L.) These authors contributed equally. y Received: 23 April 2020; Accepted: 25 May 2020; Published: 27 May 2020 Abstract: The vascular response to hypoxia and ischemia is essential for maintaining homeostasis during stressful conditions and is particularly critical for vital organs such as the heart. Hypoxia-inducible factor-1 (HIF-1) is a central regulator of the response to hypoxia by activating transcription of numerous target genes, including vascular endothelial growth factor (VEGF). Here we identify the guanine nucleotide exchange factor (GEF) Vav1, a regulator of the small Rho-GTPase and cell signaling in endothelial cells, as a key vascular regulator of hypoxia. We show that Vav1 is present in the vascular endothelium and is essential for HIF-1 activation under hypoxia. So, we hypothesized that Vav1 could be a key regulator of HIF-1 signaling. In our ﬁndings, Vav1 regulates HIF-1α stabilization through the p38/Siah2/PHD3 pathway. In normoxia, Vav1 binds to vascular endothelial growth factor receptor 1 (VEGFR1), which directs Vav1 to lysosomes for degradation. In contrast, hypoxia upregulates Vav1 protein levels by inhibiting lysosomal degradation, which is analogous to HIF-1α regulation by hypoxia: both proteins are constitutively produced and degraded in normoxia allowing for a rapid response when stress occurs.
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SIAH Proteins: Critical Roles in Leukemogenesis
Leukemia (2013) 27, 792–802 & 2013 Macmillan Publishers Limited All rights reserved 0887-6924/13 www.nature.com/leu REVIEW SIAH proteins: critical roles in leukemogenesis OH Kra¨mer1, RH Stauber2, G Bug3, J Hartkamp4 and SK Knauer5 The delicate balance between the synthesis and the degradation of proteins ensures cellular homeostasis. Proteases act in an irreversible manner and therefore have to be strictly regulated. The ubiquitin–proteasome system (UPS) is a major pathway for the proteolytic degradation of cellular proteins. As dysregulation of the UPS is observed in most cancers including leukemia, the UPS is a valid target for therapeutic intervention strategies. Ubiquitin-ligases selectively bind substrates to target them for poly- ubiquitinylation and proteasomal degradation. Therefore, pharmacological modulation of these proteins could allow a speciﬁc level of control. Increasing evidence accumulates that ubiquitin-ligases termed mammalian seven in absentia homologs (SIAHs) are not only critical for the pathogenesis of solid tumors but also for leukemogenesis. However, the relevance and therapeutic potential of SIAH-dependent processes has not been fully elucidated. Here, we summarize functions of SIAH ubiquitin-ligases in leukemias, how they select leukemia-relevant substrates for proteasomal degradation, and how the expression and activity of SIAH1 and SIAH2 can be modulated in vivo. We also discuss that epigenetic drugs belonging to the group of histone deacetylase inhibitors induce SIAH- dependent proteasomal degradation to accelerate the turnover of leukemogenic proteins. In addition, our review highlights potential areas for future research on SIAH proteins. Leukemia (2013) 27, 792–802; doi:10.1038/leu.2012.284 Keywords: leukemia fusion protein; proteasomal degradation; SIAH1; SIAH2; UBCH8 INTRODUCTION functions are controlled by ubiquitinylation-dependent proteaso- 1,2 Homeostasis relies on a balance between de novo protein mal degradation.
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Transcriptome Profiling Reveals the Complexity of Pirfenidone Effects in IPF
ERJ Express. Published on August 30, 2018 as doi: 10.1183/13993003.00564-2018 Early View Original article Transcriptome profiling reveals the complexity of pirfenidone effects in IPF Grazyna Kwapiszewska, Anna Gungl, Jochen Wilhelm, Leigh M. Marsh, Helene Thekkekara Puthenparampil, Katharina Sinn, Miroslava Didiasova, Walter Klepetko, Djuro Kosanovic, Ralph T. Schermuly, Lukasz Wujak, Benjamin Weiss, Liliana Schaefer, Marc Schneider, Michael Kreuter, Andrea Olschewski, Werner Seeger, Horst Olschewski, Malgorzata Wygrecka Please cite this article as: Kwapiszewska G, Gungl A, Wilhelm J, et al. Transcriptome profiling reveals the complexity of pirfenidone effects in IPF. Eur Respir J 2018; in press (https://doi.org/10.1183/13993003.00564-2018). This manuscript has recently been accepted for publication in the European Respiratory Journal. It is published here in its accepted form prior to copyediting and typesetting by our production team. After these production processes are complete and the authors have approved the resulting proofs, the article will move to the latest issue of the ERJ online. Copyright ©ERS 2018 Copyright 2018 by the European Respiratory Society. Transcriptome profiling reveals the complexity of pirfenidone effects in IPF Grazyna Kwapiszewska1,2, Anna Gungl2, Jochen Wilhelm3†, Leigh M. Marsh1, Helene Thekkekara Puthenparampil1, Katharina Sinn4, Miroslava Didiasova5, Walter Klepetko4, Djuro Kosanovic3, Ralph T. Schermuly3†, Lukasz Wujak5, Benjamin Weiss6, Liliana Schaefer7, Marc Schneider8†, Michael Kreuter8†, Andrea Olschewski1,
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