Ramljak, Sanja

[["dc.bibliographiccitation.firstpage","5370"],["dc.bibliographiccitation.issue","12"],["dc.bibliographiccitation.journal","Journal of Proteome Research"],["dc.bibliographiccitation.lastpage","5382"],["dc.bibliographiccitation.volume","12"],["dc.contributor.author","Schumacher, Julia"],["dc.contributor.author","Ramljak, Sanja"],["dc.contributor.author","Asif, Abdul R."],["dc.contributor.author","Schaffrath, Michael"],["dc.contributor.author","Zischler, Hans"],["dc.contributor.author","Herlyn, Holger"],["dc.date.accessioned","2018-11-07T09:17:03Z"],["dc.date.available","2018-11-07T09:17:03Z"],["dc.date.issued","2013"],["dc.description.abstract","We investigated possible associations between sequence evolution of mammalian sperm proteins and their phosphorylation status in humans. As a reference, spermatozoa from three normozoospermic men were analyzed combining two-dimensional gel electrophoresis, immuno-blotting, and mass spectrometry. We identified 99 sperm proteins (thereof 42 newly described) and determined the phosphorylation status for most of them. Sequence evolution was studied across six mammalian species using nonsynonymous/synonymous rate ratios (dN/dS) and amino acid distances. Site-specific purifying selection was assessed employing average ratios of evolutionary rates at phosphorylated versus nonphosphorylated amino acids (a). According to our data, mammalian sperm proteins do not show statistically significant sequence conservation difference, no matter if the human ortholog is a phosphoprotein with or without tyrosine (Y) phosphorylation. In contrast, overall phosphorylation of human sperm proteins, i.e., phosphorylation at serine (S), threonine (T), and/or Y residues, associates with above-average conservation of sequences. Complementary investigations suggest that numerous protein-protein interactants constrain sequence evolution of sperm phosphoproteins. Although our findings reject a special relevance of Y phosphorylation for sperm functioning, they still indicate that overall phosphorylation substantially contributes to proper functioning of sperm proteins. Hence, phosphorylated sperm proteins might be considered as prime candidates for diagnosis and treatment of reduced male fertility."],["dc.identifier.doi","10.1021/pr400228c"],["dc.identifier.isi","000328231300003"],["dc.identifier.pmid","23919900"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/28074"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Chemical Soc"],["dc.relation.issn","1535-3907"],["dc.relation.issn","1535-3893"],["dc.title","Evolutionary Conservation of Mammalian Sperm Proteins Associates with Overall, not Tyrosine, Phosphorylation in Human Spermatozoa"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","292"],["dc.bibliographiccitation.journal","Frontiers in Cellular Neuroscience"],["dc.bibliographiccitation.volume","10"],["dc.contributor.author","Ramljak, Sanja"],["dc.contributor.author","Herlyn, Holger"],["dc.contributor.author","Zerr, Inga"],["dc.date.accessioned","2018-11-07T10:04:26Z"],["dc.date.available","2018-11-07T10:04:26Z"],["dc.date.issued","2016"],["dc.description.abstract","The cellular prion protein (PrPc) and hypoxia appear to be tightly intertwined. Beneficial effects of PrPc on neuronal survival under hypoxic conditions such as focal cerebral ischemia are strongly supported. Conversely, increasing evidence indicates detrimental effects of increased PrPc expression on cancer progression, another condition accompanied by low oxygen tensions. A switch between anaerobic and aerobic metabolism characterizes both conditions. A cellular process that might unite both is glycolysis. Putative role of PrPc in stimulation of glycolysis in times of need is indeed thought provoking. A significance of astrocytic PrPc expression for neuronal survival under hypoxic conditions and possible association of PrPc with the astrocyte-neuron lactate shuttle is considered. We posit PrPc-induced lactate production via transactivation of lactate dehydrogenase A by hypoxia inducible factor 1 alpha as an important factor for survival of both neurons and tumor cells in hypoxic microenvironment. Concomitantly, we discuss a cross-talk between Wnt/beta-catenin and PI3K/Akt signaling pathways in executing PrPc-induced activation of glycolysis. Finally, we would like to emphasize that we see a great potential in joining expertise from both fields, neuroscience and cancer research in revealing the mechanisms underlying hypoxia-related pathologies. PrPc may prove focal point for future research."],["dc.description.sponsorship","Open-Access-Publikationsfonds 2016"],["dc.identifier.doi","10.3389/fncel.2016.00292"],["dc.identifier.isi","000390160200001"],["dc.identifier.pmid","28066187"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/14019"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/38694"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Frontiers Media Sa"],["dc.relation.issn","1662-5102"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Cellular Prion Protein (PrPc) and Hypoxia: True to Each Other in Good Times and in Bad, in Sickness, and in Health"],["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","1203"],["dc.bibliographiccitation.issue","11"],["dc.bibliographiccitation.journal","ELECTROPHORESIS"],["dc.bibliographiccitation.lastpage","1214"],["dc.bibliographiccitation.volume","43"],["dc.contributor.affiliation","Kwiatkowski, Marcel; 1\r\nDepartment of Biochemistry and Center for Molecular Biosciences Innsbruck\r\nUniversity of Innsbruck\r\nInnsbruck Austria"],["dc.contributor.affiliation","Hotze, Madlen; 1\r\nDepartment of Biochemistry and Center for Molecular Biosciences Innsbruck\r\nUniversity of Innsbruck\r\nInnsbruck Austria"],["dc.contributor.affiliation","Schumacher, Julia; 2\r\nAbbott GmbH\r\nCore Diagnostics\r\nWiesbaden Germany"],["dc.contributor.affiliation","Asif, Abdul R.; 3\r\nDepartment of Clinical Chemistry/UMG‐Laboratories\r\nUniversity Medical Center\r\nGöttingen Germany"],["dc.contributor.affiliation","Pittol, Jose Miguel Ramos; 1\r\nDepartment of Biochemistry and Center for Molecular Biosciences Innsbruck\r\nUniversity of Innsbruck\r\nInnsbruck Austria"],["dc.contributor.affiliation","Brenig, Bertram; 4\r\nDepartment of Molecular Biology of Livestock\r\nInstitute of Veterinary Medicine\r\nUniversity of Göttingen\r\nGöttingen Germany"],["dc.contributor.affiliation","Ramljak, Sanja; 5\r\nDigital Diagnostics AG\r\nMainz Germany"],["dc.contributor.affiliation","Zischler, Hans; 6\r\nInstitute of Organismic and Molecular Evolution, Anthropology\r\nUniversity of Mainz\r\nMainz Germany"],["dc.contributor.author","Kwiatkowski, Marcel"],["dc.contributor.author","Hotze, Madlen"],["dc.contributor.author","Schumacher, Julia"],["dc.contributor.author","Asif, Abdul R."],["dc.contributor.author","Pittol, Jose Miguel Ramos"],["dc.contributor.author","Brenig, Bertram"],["dc.contributor.author","Ramljak, Sanja"],["dc.contributor.author","Zischler, Hans"],["dc.contributor.author","Herlyn, Holger"],["dc.date.accessioned","2022-04-01T10:01:29Z"],["dc.date.available","2022-04-01T10:01:29Z"],["dc.date.issued","2022"],["dc.date.updated","2022-06-14T22:04:26Z"],["dc.description.abstract","Abstract Multiple spotting due to protein speciation might increase a protein's chance of being captured in a random selection of 2‐DE spots. We tested this expectation in new (PXD015649) and previously published 2‐DE/MS data of porcine and human tissues. For comparison, we included bottom‐up proteomics studies (BU‐LC/MS) of corresponding biological materials. Analyses of altogether ten datasets proposed that amino acid modification fosters multispotting in 2‐DE. Thus, the number of 2‐DE spots containing a particular protein more tightly associated with a peptide diversity measure accounting for amino acid modification than with an alternative one disregarding it. Furthermore, every 11th amino acid was a post‐translational modification candidate site in 2‐DE/MS proteins, whereas in BU‐LC/MS proteins this was merely the case in every 21st amino acid. Alternative splicing might contribute to multispotting, since genes encoding 2‐DE/MS proteins were found to have on average about 0.3 more transcript variants than their counterparts from BU‐LC/MS studies. Correspondingly, resolution completeness as estimated from the representation of transcript variant‐rich genes was higher in 2‐DE/MS than BU‐LC/MS datasets. These findings suggest that the ability to resolve proteomes down to protein species can lead to enrichment of multispotting proteins in 2‐DE/MS. Low sensitivity of stains and MS instruments appears to enhance this effect."],["dc.description.sponsorship","University of Mainz"],["dc.identifier.doi","10.1002/elps.202000393"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/105675"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-530"],["dc.relation.eissn","1522-2683"],["dc.relation.issn","0173-0835"],["dc.rights","This is an open access article under the terms of the Creative Commons Attribution‐NonCommercial License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited and is not used for commercial purposes."],["dc.rights.uri","http://onlinelibrary.wiley.com/termsAndConditions#vor"],["dc.title","Protein speciation is likely to increase the chance of proteins to be determined in 2‐DE/MS"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]