Jahn, Olaf

[["dc.bibliographiccitation.firstpage","6564"],["dc.bibliographiccitation.issue","18"],["dc.bibliographiccitation.journal","International Journal of Molecular Sciences"],["dc.bibliographiccitation.volume","21"],["dc.contributor.affiliation","Klafki, Hans W.; \t\t \r\n\t\t Department of Psychiatry and Psychotherapy, University Medical Center (UMG), Georg-August-University, D37075 Göttingen, Germany, hans.klafki@med.uni-goettingen.de"],["dc.contributor.affiliation","Rieper, Petra; \t\t \r\n\t\t Department of Psychiatry and Psychotherapy, University Medical Center (UMG), Georg-August-University, D37075 Göttingen, Germany, petra.rieper@med.uni-goettingen.de"],["dc.contributor.affiliation","Matzen, Anja; \t\t \r\n\t\t IBL International GmbH, Tecan Group Company, D-22335 Hamburg, Germany, Anja.Matzen@tecan.com"],["dc.contributor.affiliation","Zampar, Silvia; \t\t \r\n\t\t Department of Psychiatry and Psychotherapy, University Medical Center (UMG), Georg-August-University, D37075 Göttingen, Germany, silvia.zampar@med.uni-goettingen.de"],["dc.contributor.affiliation","Wirths, Oliver; \t\t \r\n\t\t Department of Psychiatry and Psychotherapy, University Medical Center (UMG), Georg-August-University, D37075 Göttingen, Germany, oliver.wirths@medizin.uni-goettingen.de"],["dc.contributor.affiliation","Vogelgsang, Jonathan; \t\t \r\n\t\t Department of Psychiatry and Psychotherapy, University Medical Center (UMG), Georg-August-University, D37075 Göttingen, Germany, jonathan.vogelgsang@med.uni-goettingen.de"],["dc.contributor.affiliation","Osterloh, Dirk; \t\t \r\n\t\t Roboscreen GmbH, D-04129 Leipzig, Germany, dirk.osterloh@roboscreen.com"],["dc.contributor.affiliation","Rohdenburg, Lara; \t\t \r\n\t\t Department of Psychiatry and Psychotherapy, University Medical Center (UMG), Georg-August-University, D37075 Göttingen, Germany, lara.rohdenburg@stud.uni-goettingen.de"],["dc.contributor.affiliation","Oberstein, Timo J.; \t\t \r\n\t\t Department of Psychiatry and Psychotherapy, Friedrich-Alexander-University of Erlangen-Nuremberg, D-91054 Erlangen, Germany, Timo.Oberstein@uk-erlangen.de"],["dc.contributor.affiliation","Jahn, Olaf; \t\t \r\n\t\t Max-Planck-Institute of Experimental Medicine, Proteomics Group, D-37075 Göttingen, Germany, jahn@em.mpg.de"],["dc.contributor.affiliation","Beyer, Isaak; \t\t \r\n\t\t Faculty of Chemistry, Technische Universität Dresden, D-01069 Dresden, Germany, isaak.beyer@web.de"],["dc.contributor.affiliation","Lachmann, Ingolf; \t\t \r\n\t\t Roboscreen GmbH, D-04129 Leipzig, Germany, ingolf.lachmann@roboscreen.com"],["dc.contributor.affiliation","Knölker, Hans-Joachim; \t\t \r\n\t\t Faculty of Chemistry, Technische Universität Dresden, D-01069 Dresden, Germany, hans-joachim.knoelker@tu-dresden.de"],["dc.contributor.affiliation","Wiltfang, Jens; \t\t \r\n\t\t Department of Psychiatry and Psychotherapy, University Medical Center (UMG), Georg-August-University, D37075 Göttingen, Germany, Jens.Wiltfang@med.uni-goettingen.de\t\t \r\n\t\t German Center for Neurodegenerative Diseases (DZNE), D-37075 Göttingen, Germany, Jens.Wiltfang@med.uni-goettingen.de\t\t \r\n\t\t Neurosciences and Signaling Group, Institute of Biomedicine (iBiMED), Department of Medical Sciences, University of Aveiro, 3810-193 Aveiro, Portugal, Jens.Wiltfang@med.uni-goettingen.de"],["dc.contributor.author","Klafki, Hans W."],["dc.contributor.author","Rieper, Petra"],["dc.contributor.author","Matzen, Anja"],["dc.contributor.author","Zampar, Silvia"],["dc.contributor.author","Wirths, Oliver"],["dc.contributor.author","Vogelgsang, Jonathan"],["dc.contributor.author","Osterloh, Dirk"],["dc.contributor.author","Rohdenburg, Lara"],["dc.contributor.author","Oberstein, Timo J."],["dc.contributor.author","Jahn, Olaf"],["dc.contributor.author","Beyer, Isaak"],["dc.contributor.author","Lachmann, Ingolf"],["dc.contributor.author","Knölker, Hans-Joachim"],["dc.contributor.author","Wiltfang, Jens"],["dc.date.accessioned","2021-04-14T08:32:33Z"],["dc.date.available","2021-04-14T08:32:33Z"],["dc.date.issued","2020"],["dc.date.updated","2022-09-06T16:24:24Z"],["dc.identifier.doi","10.3390/ijms21186564"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/17555"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/83948"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.notes.intern","Merged from goescholar"],["dc.relation.eissn","1422-0067"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Development and Technical Validation of an Immunoassay for the Detection of APP669–711 (Aβ−3–40) in Biological Samples"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","8685"],["dc.bibliographiccitation.issue","25"],["dc.bibliographiccitation.journal","Chemistry - A European Journal"],["dc.bibliographiccitation.lastpage","8693"],["dc.bibliographiccitation.volume","22"],["dc.contributor.author","Beyer, Isaak"],["dc.contributor.author","Rezaei-Ghaleh, Nasrollah"],["dc.contributor.author","Klafki, Hans-Wolfgang"],["dc.contributor.author","Jahn, Olaf"],["dc.contributor.author","Haußmann, Ute"],["dc.contributor.author","Wiltfang, Jens"],["dc.contributor.author","Zweckstetter, Markus"],["dc.contributor.author","Knölker, Hans-Joachim"],["dc.date.accessioned","2017-09-07T11:44:41Z"],["dc.date.available","2017-09-07T11:44:41Z"],["dc.date.issued","2016"],["dc.description.abstract","In addition to the prototypic amyloid-β (Aβ) peptides Aβ1–40 and Aβ1–42, several Aβ variants differing in their amino and carboxy termini have been described. Synthetic availability of an Aβ variant is often the key to study its role under physiological or pathological conditions. Herein, we report a protocol for the efficient solid-phase peptide synthesis of the N-terminally elongated Aβ-peptides Aβ−3–38, Aβ−3–40, and Aβ−3–42. Biophysical characterization by NMR spectroscopy, CD spectroscopy, an aggregation assay, and electron microscopy revealed that all three peptides were prone to aggregation into amyloid fibrils. Immunoprecipitation, followed by mass spectrometry, indicated that Aβ−3–38 and Aβ−3–40 are generated by transfected cells even in the presence of a tripartite β-site amyloid precursor protein cleaving enzyme 1 (BACE1) inhibitor. The elongated Aβ peptides starting at Val(−3) can be separated from N-terminally-truncated Aβ forms by high-resolution isoelectric-focusing techniques, despite virtually identical isoelectric points. The synthetic Aβ variants and the methods presented here are providing tools to advance our understanding of the potential roles of N-terminally elongated Aβ variants in Alzheimer's disease."],["dc.identifier.doi","10.1002/chem.201600892"],["dc.identifier.gro","3151723"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/14030"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/8544"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","public"],["dc.notes.submitter","chake"],["dc.relation.issn","0947-6539"],["dc.rights","CC BY-NC-ND 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by-nc-nd/4.0"],["dc.title","Solid-Phase Synthesis and Characterization of N-Terminally Elongated Aβ−3-x-Peptides"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.peerReviewed","no"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","643"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","The Journal of Cell Biology"],["dc.bibliographiccitation.lastpage","656"],["dc.bibliographiccitation.volume","195"],["dc.contributor.author","Schulz, Christian"],["dc.contributor.author","Lytovchenko, Oleksandr"],["dc.contributor.author","Melin, Jonathan"],["dc.contributor.author","Chacinska, Agnieszka"],["dc.contributor.author","Guiard, Bernard"],["dc.contributor.author","Neumann, Piotr"],["dc.contributor.author","Ficner, Ralf"],["dc.contributor.author","Jahn, Olaf"],["dc.contributor.author","Schmidt, Bernhard"],["dc.contributor.author","Rehling, Peter"],["dc.date.accessioned","2017-09-07T11:43:19Z"],["dc.date.available","2017-09-07T11:43:19Z"],["dc.date.issued","2011"],["dc.description.abstract","N-terminal targeting signals (presequences) direct proteins across the TOM complex in the outer mitochondrial membrane and the TIM23 complex in the inner mitochondrial membrane. Presequences provide directionality to the transport process and regulate the transport machineries during translocation. However, surprisingly little is known about how presequence receptors interact with the signals and what role these interactions play during preprotein transport. Here, we identify signal-binding sites of presequence receptors through photo-affinity labeling. Using engineered presequence probes, photo cross-linking sites on mitochondrial proteins were mapped mass spectrometrically, thereby defining a presequence-binding domain of Tim50, a core subunit of the TIM23 complex that is essential for mitochondrial protein import. Our results establish Tim50 as the primary presequence receptor at the inner membrane and show that targeting signals and Tim50 regulate the Tim23 channel in an antagonistic manner."],["dc.identifier.doi","10.1083/jcb.201105098"],["dc.identifier.gro","3142630"],["dc.identifier.isi","000297206400012"],["dc.identifier.pmid","22065641"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/8033"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/55"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Rockefeller Univ Press"],["dc.relation.issn","0021-9525"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Tim50's presequence receptor domain is essential for signal driven transport across the TIM23 complex"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","e10079"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","PLoS One"],["dc.bibliographiccitation.volume","5"],["dc.contributor.author","Jesse, Sarah"],["dc.contributor.author","Steinacker, Petra"],["dc.contributor.author","Lehnert, Stefan"],["dc.contributor.author","Sdzuj, Martin"],["dc.contributor.author","Cepek, Lukas"],["dc.contributor.author","Tumani, Hayrettin"],["dc.contributor.author","Jahn, Olaf"],["dc.contributor.author","Schmidt, Holger"],["dc.contributor.author","Otto, Markus"],["dc.date.accessioned","2018-11-07T08:44:10Z"],["dc.date.available","2018-11-07T08:44:10Z"],["dc.date.issued","2010"],["dc.description.abstract","Background: The discrimination of bacterial meningitis (BM) versus viral meningitis (VM) shapes up as a problem, when laboratory data are not equivocal, in particular, when Gram stain is negative. Methodology/Principal Findings: With the aim to determine reliable marker for bacterial or viral meningitis, we subjected cerebrospinal fluid (CSF) to a quantitative proteomic screening. By using a recently established 2D-DIGE protocol which was adapted to the individual CSF flow, we compared a small set of patients with proven BM and VM. Thereby, we identified six potential biomarkers out of which Prostaglandin-H2 D-isomerase was already described in BM, showing proof of concept. In the subsequent validation phase on a more comprehensive collective of 80 patients, we could validate that in BM high levels of glial fibrillary acidic protein (GFAP) and low levels of soluble amyloid precursor protein alpha/beta (sAPP alpha/beta) are present as possible binding partner of Fibulin-1. Conclusions/Significance: We conclude that our CSF flow-adapted 2D-DIGE protocol is valid especially in comparing samples with high differences in total protein and suppose that GFAP and sAPP alpha/beta have a high potential as additional diagnostic markers for differentiation of BM from VM. In the clinical setting, this might lead to an improved early diagnosis and to an individual therapy."],["dc.identifier.doi","10.1371/journal.pone.0010079"],["dc.identifier.isi","000276482000014"],["dc.identifier.pmid","20386697"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/6922"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/20140"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Public Library Science"],["dc.relation.issn","1932-6203"],["dc.rights","CC BY 2.5"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","A Proteomic Approach for the Diagnosis of Bacterial Meningitis"],["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","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.artnumber","2530.e5"],["dc.bibliographiccitation.firstpage","2521"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","Cell Reports"],["dc.bibliographiccitation.volume","26"],["dc.contributor.author","López-Murcia, Francisco José"],["dc.contributor.author","Reim, Kerstin"],["dc.contributor.author","Jahn, Olaf"],["dc.contributor.author","Taschenberger, Holger"],["dc.contributor.author","Brose, Nils"],["dc.date.accessioned","2019-07-09T11:50:32Z"],["dc.date.available","2019-07-09T11:50:32Z"],["dc.date.issued","2019"],["dc.description.abstract","SNARE-mediated synaptic vesicle (SV) fusion is controlled by multiple regulatory proteins that determine neurotransmitter release efficiency. Complexins are essential SNARE regulators whose mode of action is unclear, as available evidence indicates positive SV fusion facilitation and negative \"fusion clamp\"-like activities, with the latter occurring only in certain contexts. Because these contradictory findings likely originate in part from different experimental perturbation strategies, we attempted to resolve them by examining a conditional complexin-knockout mouse line as the most stringent genetic perturbation model available. We found that acute complexin loss after synaptogenesis in autaptic and mass-cultured hippocampal neurons reduces SV fusion probability and thus abates the rates of spontaneous, synchronous, asynchronous, and delayed transmitter release but does not affect SV priming or cause \"unclamping\" of spontaneous SV fusion. Thus, complexins act as facilitators of SV fusion but are dispensable for \"fusion clamping\" in mammalian forebrain neurons."],["dc.identifier.doi","10.1016/j.celrep.2019.02.030"],["dc.identifier.pmid","30840877"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/15955"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/59788"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.relation","info:eu-repo/grantAgreement/EC/H2020/670283/EU//SYNPRIME"],["dc.relation.issn","2211-1247"],["dc.rights","CC BY-NC-ND 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by-nc-nd/4.0"],["dc.subject.ddc","573"],["dc.subject.ddc","612"],["dc.title","Acute Complexin Knockout Abates Spontaneous and Evoked Transmitter Release"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","PII S0370-2693(02)03008-3"],["dc.bibliographiccitation.firstpage","49"],["dc.bibliographiccitation.issue","1-2"],["dc.bibliographiccitation.journal","Physics Letters B"],["dc.bibliographiccitation.lastpage","55"],["dc.bibliographiccitation.volume","551"],["dc.contributor.author","Ahrens, J."],["dc.contributor.author","Altieri, S."],["dc.contributor.author","Annand, JRM"],["dc.contributor.author","Anton, G."],["dc.contributor.author","Arends, H. J."],["dc.contributor.author","Aulenbacher, K."],["dc.contributor.author","Beck, R."],["dc.contributor.author","Bradtke, C."],["dc.contributor.author","Braghieri, A."],["dc.contributor.author","Degrande, N."],["dc.contributor.author","D'Hose, N."],["dc.contributor.author","Dutz, H."],["dc.contributor.author","Goertz, S."],["dc.contributor.author","Grabmayr, P."],["dc.contributor.author","Hansen, K."],["dc.contributor.author","Harmsen, J."],["dc.contributor.author","von Harrach, D."],["dc.contributor.author","Hasegawa, S."],["dc.contributor.author","Hasegawa, T."],["dc.contributor.author","Heid, E."],["dc.contributor.author","Helbing, Krister"],["dc.contributor.author","Holvoet, H."],["dc.contributor.author","van Hoorebeke, L."],["dc.contributor.author","Horikawa, N."],["dc.contributor.author","Iwata, T."],["dc.contributor.author","Jahn, Olaf"],["dc.contributor.author","Jennewein, P."],["dc.contributor.author","Kageya, T."],["dc.contributor.author","Kiel, B."],["dc.contributor.author","Klein, F."],["dc.contributor.author","Kondratiev, R."],["dc.contributor.author","Kossert, K."],["dc.contributor.author","Krimmer, J."],["dc.contributor.author","Lang, M."],["dc.contributor.author","Lannoy, B."],["dc.contributor.author","Leukel, R."],["dc.contributor.author","Lisin, V."],["dc.contributor.author","Matsuda, T."],["dc.contributor.author","McGeorge, J. C."],["dc.contributor.author","Meier, A."],["dc.contributor.author","Menze, D."],["dc.contributor.author","Meyer, Werner"],["dc.contributor.author","Michel, Tanja Maria"],["dc.contributor.author","Naumann, J."],["dc.contributor.author","Panzeri, A."],["dc.contributor.author","Pedroni, P."],["dc.contributor.author","Pinelli, T."],["dc.contributor.author","Preobrajenski, I."],["dc.contributor.author","Radtke, E."],["dc.contributor.author","Reichert, E."],["dc.contributor.author","Reicherz, G."],["dc.contributor.author","Rohlof, C."],["dc.contributor.author","Rosner, G."],["dc.contributor.author","Rostomyan, T."],["dc.contributor.author","Rovelli, C."],["dc.contributor.author","Rychbosch, D."],["dc.contributor.author","Schoch, B."],["dc.contributor.author","Schumacher, M."],["dc.contributor.author","Seitz, Bjoern"],["dc.contributor.author","Speckner, T."],["dc.contributor.author","Takabayashi, N."],["dc.contributor.author","Tamas, Gabor"],["dc.contributor.author","Thomas, Andy"],["dc.contributor.author","van de Vyver, R."],["dc.contributor.author","Wakai, A."],["dc.contributor.author","Weihofen, W."],["dc.contributor.author","Wissmann, F."],["dc.contributor.author","Zapadtka, F."],["dc.contributor.author","Zeitler, G."],["dc.date.accessioned","2018-11-07T10:41:45Z"],["dc.date.available","2018-11-07T10:41:45Z"],["dc.date.issued","2003"],["dc.description.abstract","The helicity dependence of the total cross section for the (γ) over right arrow(p) over right arrownpi(+) pi(0) reaction has been measured for the first time at incident photon energies from 400 to 800 MeV The measurement was performed with the large acceptance detector DAPHNE at the tagged photon beam facility of the MAMI accelerator in Mainz. This channel is found to be excited predominantly when the photon and proton have a parallel spin orientation, due to the intermediate production of the D-13 resonance. (C) 2002 Elsevier Science B.V. All rights reserved."],["dc.identifier.doi","10.1016/S0370-2693(02)03008-3"],["dc.identifier.isi","000180278700006"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/11250"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/46616"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Elsevier Science Bv"],["dc.relation.issn","0370-2693"],["dc.relation.orgunit","Fakultät für Physik"],["dc.rights","CC BY 3.0"],["dc.title","Helicity dependence of the (gamma)over-right-arrow (p)over-right-arrow > n pi(+) pi(0) reaction in the second resonance region"],["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","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","38"],["dc.bibliographiccitation.journal","BMC Medicine"],["dc.bibliographiccitation.volume","6"],["dc.contributor.author","Uhrig, Markus"],["dc.contributor.author","Brechlin, Peter"],["dc.contributor.author","Jahn, Olaf"],["dc.contributor.author","Knyazev, Yuri"],["dc.contributor.author","Weninger, Annette"],["dc.contributor.author","Busia, Laura"],["dc.contributor.author","Honarnejad, Kamran"],["dc.contributor.author","Otto, Markus"],["dc.contributor.author","Hartmann, Tobias"],["dc.date.accessioned","2018-11-07T11:07:53Z"],["dc.date.available","2018-11-07T11:07:53Z"],["dc.date.issued","2008"],["dc.description.abstract","Background: Alzheimer's disease (AD) is characterized by neurodegeneration and changes in cellular processes, including neurogenesis. Proteolytic processing of the amyloid precursor protein (APP) plays a central role in AD. Owing to varying APP processing, several beta-amyloid peptides (A beta) are generated. In contrast to the form with 40 amino acids (A beta(40)), the variant with 42 amino acids (A beta(42)) is thought to be the pathogenic form triggering the pathological cascade in AD. While total-A beta effects have been studied extensively, little is known about specific genome-wide effects triggered by A beta(42) or A beta(40) derived from their direct precursor C99. Methods: A combined transcriptomics/proteomics analysis was performed to measure the effects of intracellularly generated A beta peptides in human neuroblastoma cells. Data was validated by real-time polymerase chain reaction (real-time PCR) and a functional validation was carried out using RNA interference. Results: Here we studied the transcriptomic and proteomic responses to increased or decreased A beta(42) and A beta(40) levels generated in human neuroblastoma cells. Genome-wide expression profiles (Affymetrix) and proteomic approaches were combined to analyze the cellular response to the changed A beta(42)- and A beta(40)-levels. The cells responded to this challenge with significant changes in their expression pattern. We identified several dysregulated genes and proteins, but only the cellular retinoic acid binding protein 1 (CRABP1) was up-regulated exclusively in cells expressing an increased A beta(42)/A beta(40) ratio. This consequently reduced all-trans retinoic acid (RA)-induced differentiation, validated by CRABP1 knock down, which led to recovery of the cellular response to RA treatment and cellular sprouting under physiological RA concentrations. Importantly, this effect was specific to the AD typical increase in the A beta(42)/A beta(40) ratio, whereas a decreased ratio did not result in up-regulation of CRABP1. Conclusion: We conclude that increasing the A beta(42)/A beta(40) ratio up-regulates CRABP1, which in turn reduces the differentiation potential of the human neuroblastoma cell line SH-SY5Y, but increases cell proliferation. This work might contribute to the better understanding of AD neurogenesis, currently a controversial topic."],["dc.identifier.doi","10.1186/1741-7015-6-38"],["dc.identifier.isi","000264195100001"],["dc.identifier.pmid","19087254"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/11197"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/52680"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Biomed Central Ltd"],["dc.relation.issn","1741-7015"],["dc.rights","CC BY 2.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/2.0"],["dc.title","Upregulation of CRABP1 in human neuroblastoma cells overproducing the Alzheimer-typical A beta(42) reduces their differentiation potential"],["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","36"],["dc.bibliographiccitation.journal","BMC Developmental Biology"],["dc.bibliographiccitation.volume","13"],["dc.contributor.author","Nieber, Frank"],["dc.contributor.author","Hedderich, Marie"],["dc.contributor.author","Jahn, Olaf"],["dc.contributor.author","Pieler, Tomas"],["dc.contributor.author","Henningfeld, Kristine A."],["dc.date.accessioned","2018-11-07T09:18:40Z"],["dc.date.available","2018-11-07T09:18:40Z"],["dc.date.issued","2013"],["dc.description.abstract","Background: Members of the vertebrate Numb family of cell fate determinants serve multiple functions throughout early embryogenesis, including an essential role in the development of the nervous system. The Numb proteins interact with various partner proteins and correspondingly participate in multiple cellular activities, including inhibition of the Notch pathway. Results: Here, we describe the expression characteristics of Numb and Numblike (NumbL) during Xenopus development and characterize the function of NumbL during primary neurogenesis. NumbL, in contrast to Numb, is expressed in the territories of primary neurogenesis and is positively regulated by the Neurogenin family of proneural transcription factors. Knockdown of NumbL afforded a complete loss of primary neurons and did not lead to an increase in Notch signaling in the open neural plate. Furthermore, we provide evidence that interaction of NumbL with the AP-2 complex is required for NumbL function during primary neurogenesis. Conclusion: We demonstrate an essential role of NumbL during Xenopus primary neurogenesis and provide evidence for a Notch-independent function of NumbL in this context."],["dc.identifier.doi","10.1186/1471-213X-13-36"],["dc.identifier.isi","000325803700001"],["dc.identifier.pmid","24125469"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/10415"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/28454"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Biomed Central Ltd"],["dc.relation.issn","1471-213X"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","NumbL is essential for Xenopus primary neurogenesis"],["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"]]