Schatz, Michaela

[["dc.bibliographiccitation.journal","European Biophysics Journal"],["dc.bibliographiccitation.volume","42"],["dc.contributor.author","Schatz, M."],["dc.contributor.author","Soykan, T."],["dc.contributor.author","Brose, Nils"],["dc.contributor.author","Steinem, Claudia"],["dc.date.accessioned","2018-11-07T09:22:34Z"],["dc.date.available","2018-11-07T09:22:34Z"],["dc.date.issued","2013"],["dc.format.extent","S155"],["dc.identifier.isi","000330215300463"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/29375"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Springer"],["dc.publisher.place","New york"],["dc.relation.eventlocation","Lisbon, Portugal"],["dc.relation.issn","1432-1017"],["dc.relation.issn","0175-7571"],["dc.title","Lipid binding characteristics of collybistin"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","European Biophysics Journal"],["dc.bibliographiccitation.volume","40"],["dc.contributor.author","Schatz, Michaela"],["dc.contributor.author","Steinem, Claudia"],["dc.date.accessioned","2018-11-07T08:53:34Z"],["dc.date.available","2018-11-07T08:53:34Z"],["dc.date.issued","2011"],["dc.format.extent","59"],["dc.identifier.isi","000293637300079"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/22443"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Springer"],["dc.publisher.place","New York"],["dc.relation.eventlocation","Budapest, Hungary"],["dc.relation.issn","0175-7571"],["dc.title","Macromolecular transport across hyaluronic acid barriers"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","683"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Biomacromolecules"],["dc.bibliographiccitation.lastpage","687"],["dc.bibliographiccitation.volume","14"],["dc.contributor.author","Weiher, Felix"],["dc.contributor.author","Schatz, Michaela"],["dc.contributor.author","Steinem, Claudia"],["dc.contributor.author","Geyer, Armin"],["dc.date.accessioned","2017-09-07T11:47:47Z"],["dc.date.available","2017-09-07T11:47:47Z"],["dc.date.issued","2013"],["dc.description.abstract","Oligomeric Pro-Hyp-Gly- (POG-) peptides, wherein the collagenous triple helix is supported by C-terminal capping, exhibit silica precipitation properties (O, Hyp = (2S,4R)hydroxyproline). As quantified by a molybdate assay, the length of the covalently tethered triple helix (number, of POG units) determines the amount of amorphous silica obtained from silicic acid solution. Although lacking charged side chains, the synthetic collagens precipitate large quantities of silicic acid resulting in micrometer, sized spheres of varying surface morphologies as analyzed by scanning electron microscopy. Similar precipitation efficiencies on a fast time scale of less than 10 min were previously described only for biogenic diatom protein's and sponge collagen, respectively, which have a considerably higher structural complexity and limited accessibility. The rninicollagens described he provide an unexpected alternative to the widely used precipitation conditions, which generally depend on (poly-)amines in phosphate buffer. Collagen can form intimate connections with inorganic matter. Hence, silica-enclosed collagens have promising perspectives as composite materials."],["dc.identifier.doi","10.1021/bm301737m"],["dc.identifier.gro","3142381"],["dc.identifier.isi","000316044700012"],["dc.identifier.pmid","23363425"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/7652"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","1525-7797"],["dc.title","Silica Precipitation by Synthetic Minicollagens"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","532"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Biochemical and Biophysical Research Communications"],["dc.bibliographiccitation.lastpage","537"],["dc.bibliographiccitation.volume","437"],["dc.contributor.author","Morick, Daniela"],["dc.contributor.author","Schatz, Michaela"],["dc.contributor.author","Hubrich, Raphael"],["dc.contributor.author","Hoffmeister, Helen"],["dc.contributor.author","Krefft, Anya"],["dc.contributor.author","Witzgall, Ralph"],["dc.contributor.author","Steinem, Claudia"],["dc.date.accessioned","2017-09-07T11:47:38Z"],["dc.date.available","2017-09-07T11:47:38Z"],["dc.date.issued","2013"],["dc.description.abstract","Polycystin-2 (PC2) trafficking has been proposed to be a result of the interaction of PIGEA14 with PC2 as a function of the phosphorylation state of PC2. Here, we investigated the interaction of PIGEA14 with the C-terminal part of polycystin-2 wild type (cPC2wt) and the pseudophosphorylated mutant (cPC2S812D) to first, quantify the binding affinity between cPC2 and PIGEA14 and second, to elucidate the influence of PC2 phosphorylation on PIGEA14 binding. Solid supported membranes composed of octanethiol/1,2-dioleoyl-sn-glycero-3-phosphocholine doped with the receptor lipid DOGS-NTA-Ni were used to attach PIGEA14 to the membrane via its hexahistidine tag. By means of the quartz crystal microbalance technique, binding affinities as well as kinetic constants of the interaction were extracted in a label-free manner by applying the scaled particle theory. The results show that the dissociation constant of cPC2 to PIGEA14 is in the 10 nM regime providing strong evidence of a very specific interaction of cPC2 with PIGEA14. The interaction of cPC2wt is twofold larger than that of cPC2S812D. The moderate higher binding affinity of cPC2wt to PIGEA14 is discussed in light of PC2 trafficking to the plasma membrane. (C) 2013 Elsevier Inc. All rights reserved."],["dc.identifier.doi","10.1016/j.bbrc.2013.06.105"],["dc.identifier.gro","3142309"],["dc.identifier.isi","000323584400007"],["dc.identifier.pmid","23838289"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/6853"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: Dorothea Schlozer Program of the University of Gottingen"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0006-291X"],["dc.title","Phosphorylation of C-terminal polycystin-2 influences the interaction with PIGEA14: A QCM study based on solid supported membranes"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","562"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Leukemia"],["dc.bibliographiccitation.lastpage","569"],["dc.bibliographiccitation.volume","30"],["dc.contributor.author","Gratwohl, Alois"],["dc.contributor.author","Pfirrmann, M."],["dc.contributor.author","Zander, A."],["dc.contributor.author","Kroger, Nikolaus"],["dc.contributor.author","Beelen, D."],["dc.contributor.author","Novotny, J."],["dc.contributor.author","Nerl, C."],["dc.contributor.author","Scheid, Christof"],["dc.contributor.author","Spiekermann, Karsten"],["dc.contributor.author","Mayer, J."],["dc.contributor.author","Sayer, Herbert G."],["dc.contributor.author","Falge, C."],["dc.contributor.author","Bunjes, Donald W."],["dc.contributor.author","Doehner, Hartmut"],["dc.contributor.author","Ganser, Arnold"],["dc.contributor.author","Schmidt-Wolf, Ingo G. H."],["dc.contributor.author","Schwerdtfeger, Rainer"],["dc.contributor.author","Baurmann, H."],["dc.contributor.author","Kuse, R."],["dc.contributor.author","Schmitz, Norbert"],["dc.contributor.author","Wehmeier, A."],["dc.contributor.author","Fischer, J. Th"],["dc.contributor.author","Ho, A. D."],["dc.contributor.author","Wilhelm, M."],["dc.contributor.author","Goebeler, M-E"],["dc.contributor.author","Lindemann, Hans Walter"],["dc.contributor.author","Bormann, M."],["dc.contributor.author","Hertenstein, Bernd"],["dc.contributor.author","Schlimok, G."],["dc.contributor.author","Baerlocher, Gabriela M."],["dc.contributor.author","Aul, Carlo"],["dc.contributor.author","Pfreundschuh, Michael"],["dc.contributor.author","Fabian, Merle"],["dc.contributor.author","Staib, Peter"],["dc.contributor.author","Edinger, M."],["dc.contributor.author","Schatz, M."],["dc.contributor.author","Fauser, A. A."],["dc.contributor.author","Arnold, R."],["dc.contributor.author","Kindler, Thomas"],["dc.contributor.author","Wulf, Gerald"],["dc.contributor.author","Rosselet, A."],["dc.contributor.author","Hellmann, A."],["dc.contributor.author","Schaefer, Edith"],["dc.contributor.author","Pruemmer, O."],["dc.contributor.author","Schenk, Marina"],["dc.contributor.author","Hasford, Joerg"],["dc.contributor.author","Heimpel, H."],["dc.contributor.author","Hossfeld, D. K."],["dc.contributor.author","Kolb, H-J"],["dc.contributor.author","Buesche, Guntram"],["dc.contributor.author","Haferlach, Claudia"],["dc.contributor.author","Schnittger, S."],["dc.contributor.author","Mueller, M. C."],["dc.contributor.author","Reiter, Alfred"],["dc.contributor.author","Berger, Uta"],["dc.contributor.author","Saussele, Susanne"],["dc.contributor.author","Hochhaus, Andreas"],["dc.contributor.author","Hehlmann, Ruediger"],["dc.date.accessioned","2018-11-07T10:17:45Z"],["dc.date.available","2018-11-07T10:17:45Z"],["dc.date.issued","2016"],["dc.description.abstract","Tyrosine kinase inhibitors represent today's treatment of choice in chronic myeloid leukemia (CML). Allogeneic hematopoietic stem cell transplantation (HSCT) is regarded as salvage therapy. This prospective randomized CML-study IIIA recruited 669 patients with newly diagnosed CML between July 1997 and January 2004 from 143 centers. Of these, 427 patients were considered eligible for HSCT and were randomized by availability of a matched family donor between primary HSCT (group A; N = 166 patients) and best available drug treatment (group B; N = 261). Primary end point was long-term survival. Survival probabilities were not different between groups A and B (10-year survival: 0.76 (95% confidence interval (CI): 0.69-0.82) vs 0.69 (95% CI: 0.61-0.76)), but influenced by disease and transplant risk. Patients with a low transplant risk showed superior survival compared with patients with high( P < 0.001) and non-high-risk disease (P = 0.047) in group B; after entering blast crisis, survival was not different with or without HSCT. Significantly more patients in group A were in molecular remission (56% vs 39%; P = 0.005) and free of drug treatment (56% vs 6%; P < 0.001). Differences in symptoms and Karnofsky score were not significant. In the era of tyrosine kinase inhibitors, HSCT remains a valid option when both disease and transplant risk are considered."],["dc.identifier.doi","10.1038/leu.2015.281"],["dc.identifier.isi","000371688500006"],["dc.identifier.pmid","26464170"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/14048"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/41288"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Nature Publishing Group"],["dc.relation.issn","1476-5551"],["dc.relation.issn","0887-6924"],["dc.rights","CC BY-NC-SA 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by-nc-sa/4.0"],["dc.title","Long-term outcome of patients with newly diagnosed chronic myeloid leukemia: a randomized comparison of stem cell transplantation with drug treatment"],["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"]]