Dihazi, Hassan

[["dc.bibliographiccitation.firstpage","5858"],["dc.bibliographiccitation.issue","11"],["dc.bibliographiccitation.journal","International Journal of Molecular Sciences"],["dc.bibliographiccitation.volume","22"],["dc.contributor.affiliation","Serin, Nazli; \t\t \r\n\t\t Clinic for Nephrology and Rheumatology, University Medical Center Göttingen, Robert-Koch-Strasse 40, 37075 Göttingen, Germany, nazli.serin@med.uni-goettingen.de\t\t \r\n\t\t Department of Hematology and Oncology, University of Medical Center Göttingen, Robert-Koch-Strasse 40, 37075 Göttingen, Germany, nazli.serin@med.uni-goettingen.de"],["dc.contributor.affiliation","Dihazi, Gry H.; \t\t \r\n\t\t Institute of Clinical Chemistry/UMG-Laboratories, University Medical Center Göttingen, Robert-Koch-Strasse 40, 37075 Göttingen, Germany, gryhelene.dihazi@med.uni-goettingen.de"],["dc.contributor.affiliation","Tayyeb, Asima; \t\t \r\n\t\t School of Biological Sciences, University of the Punjab, Lahore 54590, Pakistan, asima.sbs@pu.edu.pk"],["dc.contributor.affiliation","Lenz, Christof; \t\t \r\n\t\t Institute of Clinical Chemistry/UMG-Laboratories, University Medical Center Göttingen, Robert-Koch-Strasse 40, 37075 Göttingen, Germany, christof.lenz@med.uni-goettingen.de\t\t \r\n\t\t Bioanalytical Mass Spectrometry, Max Planck Institute for Biophysical Chemistry, 37077 Göttingen, Germany, christof.lenz@med.uni-goettingen.de"],["dc.contributor.affiliation","Müller, Gerhard A.; \t\t \r\n\t\t Clinic for Nephrology and Rheumatology, University Medical Center Göttingen, Robert-Koch-Strasse 40, 37075 Göttingen, Germany, gmueller@med.uni-goettingen.de"],["dc.contributor.affiliation","Zeisberg, Michael; \t\t \r\n\t\t Clinic for Nephrology and Rheumatology, University Medical Center Göttingen, Robert-Koch-Strasse 40, 37075 Göttingen, Germany, michael.zeisberg@med.uni-goettingen.de"],["dc.contributor.affiliation","Dihazi, Hassan; \t\t \r\n\t\t Clinic for Nephrology and Rheumatology, University Medical Center Göttingen, Robert-Koch-Strasse 40, 37075 Göttingen, Germany, dihazi@med.uni-goettingen.de\t\t \r\n\t\t Center for Biostructural Imaging of Neurodegeneration (BIN), University Medical Center Göttingen, 37075 Göttingen, Germany, dihazi@med.uni-goettingen.de"],["dc.contributor.author","Serin, Nazli"],["dc.contributor.author","Dihazi, Gry H."],["dc.contributor.author","Tayyeb, Asima"],["dc.contributor.author","Lenz, Christof"],["dc.contributor.author","Müller, Gerhard A."],["dc.contributor.author","Zeisberg, Michael"],["dc.contributor.author","Dihazi, Hassan"],["dc.date.accessioned","2021-07-05T15:00:46Z"],["dc.date.available","2021-07-05T15:00:46Z"],["dc.date.issued","2021"],["dc.date.updated","2022-09-06T07:10:18Z"],["dc.description.abstract","Nephrogenesis is driven by complex signaling pathways that control cell growth and differentiation. The endoplasmic reticulum chaperone calreticulin (Calr) is well known for its function in calcium storage and in the folding of glycoproteins. Its role in kidney development is still not understood. We provide evidence for a pivotal role of Calr in nephrogenesis in this investigation. We show that Calr deficiency results in the disrupted formation of an intact nephrogenic zone and in retardation of nephrogenesis, as evidenced by the disturbance in the formation of comma-shaped and s-shaped bodies. Using proteomics and transcriptomics approaches, we demonstrated that in addition to an alteration in Wnt-signaling key proteins, embryonic kidneys from Calr−/− showed an overall impairment in expression of ribosomal proteins which reveals disturbances in protein synthesis and nephrogenesis. CRISPR/cas9 mediated knockout confirmed that Calr deficiency is associated with a deficiency of several ribosomal proteins and key proteins in ribosome biogenesis. Our data highlights a direct link between Calr expression and the ribosome biogenesis."],["dc.description.abstract","Nephrogenesis is driven by complex signaling pathways that control cell growth and differentiation. The endoplasmic reticulum chaperone calreticulin (Calr) is well known for its function in calcium storage and in the folding of glycoproteins. Its role in kidney development is still not understood. We provide evidence for a pivotal role of Calr in nephrogenesis in this investigation. We show that Calr deficiency results in the disrupted formation of an intact nephrogenic zone and in retardation of nephrogenesis, as evidenced by the disturbance in the formation of comma-shaped and s-shaped bodies. Using proteomics and transcriptomics approaches, we demonstrated that in addition to an alteration in Wnt-signaling key proteins, embryonic kidneys from Calr−/− showed an overall impairment in expression of ribosomal proteins which reveals disturbances in protein synthesis and nephrogenesis. CRISPR/cas9 mediated knockout confirmed that Calr deficiency is associated with a deficiency of several ribosomal proteins and key proteins in ribosome biogenesis. Our data highlights a direct link between Calr expression and the ribosome biogenesis."],["dc.description.sponsorship","Open-Access-Publikationsfonds 2021"],["dc.identifier.doi","10.3390/ijms22115858"],["dc.identifier.pii","ijms22115858"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/87900"],["dc.language.iso","en"],["dc.notes.intern","DOI Import DOI-Import GROB-441"],["dc.relation.eissn","1422-0067"],["dc.relation.orgunit","Klinik für Nephrologie und Rheumatologie"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0/"],["dc.title","Calreticulin Deficiency Disturbs Ribosome Biogenesis and Results in Retardation in Embryonic Kidney Development"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","45"],["dc.bibliographiccitation.journal","Arthritis Research & Therapy"],["dc.bibliographiccitation.volume","17"],["dc.contributor.author","Blaschke, Sabine"],["dc.contributor.author","Rinke, Kathinka"],["dc.contributor.author","Maring, Michael"],["dc.contributor.author","Flad, Thomas"],["dc.contributor.author","Patschan, Susann A."],["dc.contributor.author","Jahn, Olaf"],["dc.contributor.author","Mueller, Claudia A."],["dc.contributor.author","Mueller, Georg Anton"],["dc.contributor.author","Dihazi, Hassan"],["dc.date.accessioned","2018-11-07T09:59:46Z"],["dc.date.available","2018-11-07T09:59:46Z"],["dc.date.issued","2015"],["dc.description.abstract","Introduction: The introduction of tumor necrosis factor-alpha (TNF-alpha) antagonists has substantially improved patient's clinical outcome in rheumatoid arthritis (RA). However, nearly 20% to 40% of RA patients do not respond to anti-TNF-alpha treatment strategies. To identify valid predictors of TNF-alpha antagonist response in RA, serum proteome profiles from responders (R) and non-responders (NR) to etanercept, a soluble recombinant TNF-alpha receptor/IgG Fc fusion protein receptor, were compared in a prospective cohort study. Methods: In this clinical study 50 RA patients with inadequate response to conventional DMARDs were included and treated with etanercept. The primary efficacy endpoint was response according to the European League against Rheumatism (EULAR) improvement criteria. Serum samples collected prior to initiation and after six months of etanercept therapy were cleared of the most abundant major proteins by immunoaffinity chromatography. After separation by two-dimensional differential gel electrophoresis (2D-DIGE) and identification by mass spectrometry (MS) data were validated by Western blot analysis. Results: After six months of etanercept treatment 62% (n = 31) of RA patients achieved response. Haptoglobin-alpha 1 (Hp-alpha 1) and -alpha 2 (Hp-alpha 2) and vitamin D-binding protein (VDBP) were found to be significantly upregulated in responder sera (P <= 0.02) at study entry. In contrast, apolipoprotein C-III (ApoC-III) showed significantly higher levels in non-responders (P = 0.0162). At study end ApoA-II, Hp-alpha 1, Hp-alpha 2 and VDBP were identified to be expressed at significantly higher levels (P < 0.05) in responder sera. Conclusions: By application of clinical proteomics in immunodepleted sera we could identify and validate for the first time Hp-alpha 1, -alpha 2, VDBP and ApoC-III as potential biomarkers for prediction of etanercept drug response in RA."],["dc.description.sponsorship","Pfizer Research Initiative"],["dc.identifier.doi","10.1186/s13075-015-0553-1"],["dc.identifier.isi","000352187400001"],["dc.identifier.pmid","25884688"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/13467"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/37661"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Biomed Central Ltd"],["dc.relation.issn","1478-6362"],["dc.relation.issn","1478-6354"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Haptoglobin-alpha 1, -alpha 2, vitamin D-binding protein and apolipoprotein C-III as predictors of etanercept drug response in rheumatoid arthritis"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1277"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Molecular BioSystems"],["dc.bibliographiccitation.lastpage","1288"],["dc.bibliographiccitation.volume","7"],["dc.contributor.author","Eltoweissy, Marwa"],["dc.contributor.author","Mueller, Georg Anton"],["dc.contributor.author","Bibi, Asima"],["dc.contributor.author","Phuc Van Nguye, Phuc Van Nguye"],["dc.contributor.author","Dihazi, Gry Helene"],["dc.contributor.author","Mueller, Claudia A."],["dc.contributor.author","Dihazi, Hassan"],["dc.date.accessioned","2018-11-07T09:01:42Z"],["dc.date.available","2018-11-07T09:01:42Z"],["dc.date.issued","2011"],["dc.description.abstract","Renal fibrosis is a process that is characterized by declining excretory renal function. The molecular mechanisms of fibrosis are not fully understood. Oxidative stress pathways were reported to be involved in renal tissue deterioration and fibrosis progression. In order to identify new molecular targets associated with oxidative stress and renal fibrosis, differential proteomics analysis was performed with established renal cell lines (TK173 and HK-2). The cells were treated with oxidative stress triggering factor H(2)O(2) and the proteome alterations were investigated. Two dimensional protein maps were generated and differentially expressed proteins were processed and identified using mass spectrometry analysis combined with data base search. Interestingly the increase of ROS in the renal cell lines upon H(2)O(2) treatment was accompanied by alteration of a large number of proteins, which could be classified in three categories: the first category grouped the proteins that have been described to be involved in fibrogenesis (e.g. ACTA2, VIN, VIM, DES, KRT, COL1A1, COL4A1), the second category, which was more interesting involved proteins of the oxidative stress pathway (PRDX1, PRDX2, PRDX6, SOD, PARK7, HYOU1), which were highly up-regulated under oxidative stress, and the third category represented proteins, which are involved in different other metabolic pathways. Among the oxidative stress proteins the up-regulation of PARK7 was accompanied by a shift in the pI as a result of oxidation. Knockdown of PARK7 using siRNA led to significant reduction in renal cell viability under oxidative stress. Under H(2)O(2) treatment the PARK7 knockdown cells showed up to 80% decrease in cell viability and an increase in apoptosis compared to the controls. These results highlight for the first time the important role of PARK7 in oxidative stress resistance in renal cells."],["dc.identifier.doi","10.1039/c0mb00116c"],["dc.identifier.isi","000288329300036"],["dc.identifier.pmid","21308111"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/8349"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/24498"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Royal Soc Chemistry"],["dc.relation.issn","1742-206X"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Proteomics analysis identifies PARK7 as an important player for renal cell resistance and survival under oxidative stress"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","e204"],["dc.bibliographiccitation.firstpage","e204"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Neurology: Neuroimmunology & Neuroinflammation"],["dc.bibliographiccitation.volume","3"],["dc.contributor.author","Metz, Imke"],["dc.contributor.author","Beißbarth, Tim"],["dc.contributor.author","Ellenberger, David"],["dc.contributor.author","Pache, Florence"],["dc.contributor.author","Stork, Lidia"],["dc.contributor.author","Ringelstein, Marius"],["dc.contributor.author","Aktas, Orhan"],["dc.contributor.author","Jarius, Sven"],["dc.contributor.author","Wildemann, Brigitte"],["dc.contributor.author","Dihazi, Hassan"],["dc.contributor.author","Friede, Tim"],["dc.contributor.author","Brück, Wolfgang"],["dc.contributor.author","Ruprecht, Klemens"],["dc.contributor.author","Paul, Friedemann"],["dc.date.accessioned","2020-12-10T18:41:40Z"],["dc.date.available","2020-12-10T18:41:40Z"],["dc.date.issued","2016"],["dc.description.abstract","To assess in an observational study whether serum peptide antibody reactivities may distinguish aquaporin-4 (AQP4) antibody (Ab)-positive and -negative neuromyelitis optica spectrum disorders (NMOSD) and relapsing-remitting multiple sclerosis (RRMS)."],["dc.identifier.doi","10.1212/NXI.0000000000000204"],["dc.identifier.eissn","2332-7812"],["dc.identifier.pmid","26894206"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/12922"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/77646"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.notes.intern","Merged from goescholar"],["dc.relation.issn","2332-7812"],["dc.rights","CC BY-NC-ND 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by-nc-nd/4.0"],["dc.title","Serum peptide reactivities may distinguish neuromyelitis optica subgroups and multiple sclerosis"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","3051"],["dc.bibliographiccitation.issue","9"],["dc.bibliographiccitation.journal","Journal of Clinical Medicine"],["dc.bibliographiccitation.volume","9"],["dc.contributor.author","Lipphardt, Mark"],["dc.contributor.author","Dihazi, Hassan"],["dc.contributor.author","Maas, Jens-Holger"],["dc.contributor.author","Schäfer, Ann-Kathrin"],["dc.contributor.author","Amlaz, Saskia I."],["dc.contributor.author","Ratliff, Brian B."],["dc.contributor.author","Koziolek, Michael J."],["dc.contributor.author","Wallbach, Manuel"],["dc.date.accessioned","2021-04-14T08:32:33Z"],["dc.date.available","2021-04-14T08:32:33Z"],["dc.date.issued","2020"],["dc.identifier.doi","10.3390/jcm9093051"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/17590"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/83944"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.notes.intern","Merged from goescholar"],["dc.publisher","MDPI"],["dc.relation.eissn","2077-0383"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Syndecan-4 as a Marker of Endothelial Dysfunction in Patients with Resistant Hypertension"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1192"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","Cells"],["dc.bibliographiccitation.volume","8"],["dc.contributor.author","Beißbarth, Tim"],["dc.contributor.author","Bohrer, Rainer"],["dc.contributor.author","Feussner, Kirstin"],["dc.contributor.author","Jahn, Olaf"],["dc.contributor.author","Schmitt, Kerstin"],["dc.contributor.author","Valerius, Oliver"],["dc.contributor.author","Asif, Abdul R."],["dc.contributor.author","Dihazi, Hassan"],["dc.contributor.author","Majcherczyk, Andrzej"],["dc.contributor.author","Schmidt, Bernhard"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Lenz, Christof"],["dc.date.accessioned","2020-04-02T10:32:12Z"],["dc.date.available","2020-04-02T10:32:12Z"],["dc.date.issued","2019"],["dc.description.abstract","Mass spectrometry-based proteomics methods are finding increasing use in structural biology research. Beyond simple interaction networks, information about stable protein-protein complexes or spatially proximal proteins helps to elucidate the biological functions of proteins in a wider cellular context. To shed light on new developments in this field, the Göttingen Proteomics Forum organized a one-day symposium focused on complexome profiling and proximity labeling, two emerging technologies that are gaining significant attention in biomolecular research. The symposium was held in Göttingen, Germany on 23 May, 2019, as part of a series of regular symposia organized by the Göttingen Proteomics Forum."],["dc.identifier.doi","10.3390/cells8101192"],["dc.identifier.pmid","31581721"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/16914"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/63512"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/95"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.publisher","MDPI"],["dc.relation","SFB 1190: Transportmaschinen und Kontaktstellen zellulärer Kompartimente"],["dc.relation","SFB 1190 | Z02: Massenspektrometrie-basierte Proteomanalyse"],["dc.relation.conference","Seventh Symposium of the Göttingen Proteomics Forum"],["dc.relation.eissn","2073-4409"],["dc.relation.eventlocation","Göttingen"],["dc.relation.eventstart","2019-05-23"],["dc.relation.issn","2073-4409"],["dc.relation.orgunit","Gesellschaft für wissenschaftliche Datenverarbeitung"],["dc.relation.workinggroup","RG Urlaub (Bioanalytische Massenspektrometrie)"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Mapping Cellular Microenvironments: Proximity Labeling and Complexome Profiling"],["dc.type","conference_paper"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","10"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Proteome Science"],["dc.bibliographiccitation.volume","16"],["dc.contributor.author","Dihazi, Gry H."],["dc.contributor.author","Mueller, Gerhard A."],["dc.contributor.author","Asif, Abdul R."],["dc.contributor.author","Eltoweissy, Marwa"],["dc.contributor.author","Wessels, Johannes T."],["dc.contributor.author","Dihazi, Hassan"],["dc.date.accessioned","2019-07-09T11:45:30Z"],["dc.date.available","2019-07-09T11:45:30Z"],["dc.date.issued","2018"],["dc.description.abstract","Upon publication of the original article [1], Marwa Eltoweissy noticed that her affiliation: “3. Department of Zoology, Faculty of Science, Alexandria University, Alexandria, Egypt” was missing. This affiliation has now been added in this correction article."],["dc.identifier.doi","10.1186/s12953-018-0138-4"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/15230"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/59243"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.relation.iserratumof","/handle/2/37930"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Correction to: Proteomic characterization of adrenal gland embryonic development reveals early initiation of steroid metabolism and reduction of the retinoic acid pathway"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","erratum_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","9"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","World Journal of Stem Cells"],["dc.bibliographiccitation.lastpage","25"],["dc.bibliographiccitation.volume","5"],["dc.contributor.author","Dihazi, Gry H."],["dc.contributor.author","Bibi, Asima"],["dc.contributor.author","Jahn, Olaf"],["dc.contributor.author","Nolte, Jessica"],["dc.contributor.author","Mueller, Gerhard A."],["dc.contributor.author","Engel, Wolfgang"],["dc.contributor.author","Dihazi, Hassan"],["dc.date.accessioned","2019-07-09T11:40:20Z"],["dc.date.available","2019-07-09T11:40:20Z"],["dc.date.issued","2013-01-26"],["dc.description.abstract","AIM: To investigate the proteome changes of stem cells due to ciclopirox olamine (CPX) treatment compared to control and retinoic acid treated cells. METHODS: Stem cells (SCs) are cells, which have the ability to continuously divide and differentiate into various other kinds of cells. Murine embryonic stem cells (ESCs) and multipotent adult germline stem cells (maGSCs) were treated with CPX, which has been shown to have an antiproliferative effect on stem cells, and compared to stem cells treated with retinoic acid (RA), which is known to have a differentiating effect on stem cells. Classical proteomic techniques like 2-D gel electrophoresis and differential in-gel electrophoresis (DIGE) were used to generate 2D protein maps from stem cells treated with RA or CPX as well as from non-treated stem cells. The resulting 2D gels were scanned and the digitalized images were collated with the help of Delta 2D software. The differentially expressed proteins were analyzed by a MALDI-TOF-TOF mass spectrometer, and the identified proteins were investigated and categorized using bioinformatics. RESULTS: Treatment of stem cells with CPX, a synthetic antifungal clinically used to treat superficial mycoses, resulted in an antiproliferative effect in vitro, without impairment of pluripotency. To understand the mechanisms induced by CPX treatments which results in arrest of cell cycle without any marked effect on pluripotency, a comparative proteomics study was conducted. The obtained data revealed that the CPX impact on cell proliferation was accompanied with a significant alteration in stem cell proteome. By peptide mass fingerprinting and tandem mass spectrometry combined with searches of protein sequence databases, a set of 316 proteins was identified, corresponding to a library of 125 non-redundant proteins. With proteomic analysis of ESCs and maGSCs treated with CPX and RA, we could identify more than 90 single proteins, which were differently expressed in both cell lines. We could highlight, that CPX treatment of stem cells, with subsequent proliferation inhibition, resulted in an alteration of the expression of 56 proteins compared to non-treated cells, and 54 proteins compared to RA treated cells. Bioinformatics analysis of the regulated proteins demonstrated their involvement in various biological processes. To our interest, a number of proteins have potential roles in the regulation of cell proliferation either directly or indirectly. Furthermore the classification of the altered polypeptides according to their main known/postulated functions revealed that the majority of these proteins are involved in molecular functions like nucleotide binding and metal ion binding, and biological processes like nucleotide biosynthetic processes, gene expression, embryonic development, regulation of transcription, cell cycle processes, RNA and mRNA processing. Proteins, which are involved in nucleotide biosynthetic process and proteolysis, were downregulated in CPX treated cells compared to control, as well as in RA treated cells, which may explain the cell cycle arrest. Moreover, proteins which were involved in cell death, positive regulation of biosynthetic process, response to organic substance, glycolysis, anti-apoptosis, and phosphorylation were downregulated in RA treated cells compared to control and CPX treated cells. CONCLUSION: The CPX treatment of SCs results in downregulation of nucleotide binding proteins and leads to cell cycle stop without impairment of pluripotency."],["dc.identifier.doi","10.4252/wjsc.v5.i1.9"],["dc.identifier.fs","603239"],["dc.identifier.pmid","23362436"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/10937"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/58149"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.relation.issn","1948-0210"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Impact of the antiproliferative agent ciclopirox olamine treatment on stem cells proteome."],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1"],["dc.bibliographiccitation.journal","Journal of Pathogens"],["dc.bibliographiccitation.lastpage","9"],["dc.bibliographiccitation.volume","2011"],["dc.contributor.author","Dihazi, Abdelhi"],["dc.contributor.author","Serghini, Mohammed Amine"],["dc.contributor.author","Jaiti, Fatima"],["dc.contributor.author","Daayf, Fouad"],["dc.contributor.author","Driouich, Azeddine"],["dc.contributor.author","Dihazi, Hassan"],["dc.contributor.author","El Hadrami, Ismail"],["dc.date.accessioned","2019-07-09T11:53:35Z"],["dc.date.available","2019-07-09T11:53:35Z"],["dc.date.issued","2011"],["dc.description.abstract","Histochemical and ultrastructural analyses were carried out to assess structural and biochemical changes in date palm roots pretreated with salicylic acid (SA) then inoculated with Fusarium oxysporum f. sp. albedinis (Foa). Flavonoids, induced proteins, and peroxidase activity were revealed in root tissues of SA-treated plants after challenge by Foa. These reactions were closely associated with plant resistance to Foa. Host reactions induced after inoculation of SA-treated plants with Foa included the plugging of intercellular spaces, the deposition of electron-dense materials at the sites of pathogen penetration, and several damages to fungal cells. On the other hand, untreated inoculated plants showed marked cell wall degradation and total cytoplasm disorganization, indicating the protective effects provided by salicylic acid in treated plants."],["dc.identifier.doi","10.4061/2011/280481"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/7727"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/60454"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Structural and Biochemical Changes in Salicylic-Acid-Treated Date Palm Roots Challenged with Fusarium oxysporum f. sp. albedinis"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","e2557"],["dc.bibliographiccitation.journal","Cell Death and Disease"],["dc.bibliographiccitation.volume","8"],["dc.contributor.author","Zafar, Saima"],["dc.contributor.author","Behrens, Christina"],["dc.contributor.author","Dihazi, Hassan"],["dc.contributor.author","Schmitz, Matthias"],["dc.contributor.author","Zerr, Inga"],["dc.contributor.author","Schulz-Schaeffer, Walter J."],["dc.contributor.author","Ramljak, Sanja"],["dc.contributor.author","Asif, Abdul R."],["dc.date.accessioned","2018-11-07T10:29:07Z"],["dc.date.available","2018-11-07T10:29:07Z"],["dc.date.issued","2017"],["dc.description.abstract","Anti-apoptotic properties of physiological and elevated levels of the cellular prion protein (PrPc) under stress conditions are well documented. Yet, detrimental effects of elevated PrPc levels under stress conditions, such as exposure to staurosporine (STS) have also been described. In the present study, we focused on discerning early apoptotic STS-induced proteome and phosphoproteome changes in SH-SY5Y human neuroblastoma cells stably transfected either with an empty or PRNP-containing vector, expressing physiological or supraphysiological levels of PrPc, respectively. PrPc-overexpression per se appears to stress the cells under STS-free conditions as indicated by diminished cell viability of PrPc-overexpressing versus control cells. However, PrPc-overexpression becomes advantageous following exposure to STS. Thus, only a short exposure (2 h) to 1 mu M STS results in lower survival rates and significantly higher caspase-3 activity in control versus PrPc-overexpressing cells. Hence, by exposing both experimental groups to the same apoptotic conditions we were able to induce apoptosis in control, but not in PrPc-overexpressing cells (as assessed by caspase-3 activity), which allowed for filtering out proteins possibly contributing to protection against STS-induced apoptosis in PrPc-overexpressing cells. Among other proteins regulated by different PrPc levels following exposure to STS, those involved in maintenance of cytoskeleton integrity caught our attention. In particular, the finding that elevated PrPc levels significantly reduce profilin-1 (PFN-1) expression. PFN-1 is known to facilitate STS-induced apoptosis. Silencing of PFN-1 expression by siRNA significantly increased viability of PrPc-overexpressing versus control cells, under STS treatment. In addition, PrPc-overexpressing cells depleted of PFN-1 exhibited increased viability versus PrPc-overexpressing cells with preserved PFN-1 expression, both subjected to STS. Concomitant increase in caspase-3 activity was observed in control versus PrPc-overexpressing cells after treatment with siRNA-PFN-1 and STS. We suggest that reduction of PFN-1 expression by elevated levels of PrPc may contribute to protective effects PrPc-overexpressing SH-SY5Y cells confer against STS-induced apoptosis."],["dc.description.sponsorship","Open-Access-Publikationsfonds 2016"],["dc.identifier.doi","10.1038/cddis.2016.384"],["dc.identifier.isi","000393679000006"],["dc.identifier.pmid","28102851"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/14209"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/43571"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Nature Publishing Group"],["dc.relation.issn","2041-4889"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Cellular prion protein mediates early apoptotic proteome alternation and phospho-modification in human neuroblastoma cells"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]