Liepold, Thomas

[["dc.bibliographiccitation.firstpage","849"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Journal of Alzheimer's Disease"],["dc.bibliographiccitation.lastpage","858"],["dc.bibliographiccitation.volume","67"],["dc.contributor.author","Hornung, Karen"],["dc.contributor.author","Zampar, Silvia"],["dc.contributor.author","Engel, Nadine"],["dc.contributor.author","Klafki, Hans"],["dc.contributor.author","Liepold, Thomas"],["dc.contributor.author","Bayer, Thomas A."],["dc.contributor.author","Wiltfang, Jens"],["dc.contributor.author","Jahn, Olaf"],["dc.contributor.author","Wirths, Oliver"],["dc.date.accessioned","2020-12-10T18:44:12Z"],["dc.date.available","2020-12-10T18:44:12Z"],["dc.date.issued","2019"],["dc.identifier.doi","10.3233/JAD-181134"],["dc.identifier.eissn","1875-8908"],["dc.identifier.issn","1387-2877"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/78365"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","N-Terminal Truncated Aβ4-42 Is a Substrate for Neprilysin Degradation in vitro and in vivo"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","5908"],["dc.bibliographiccitation.issue","25"],["dc.bibliographiccitation.journal","Biochemistry"],["dc.bibliographiccitation.lastpage","5921"],["dc.bibliographiccitation.volume","48"],["dc.contributor.author","Dimova, Kalina"],["dc.contributor.author","Kalkhof, Stefan"],["dc.contributor.author","Pottratz, Ines"],["dc.contributor.author","Ihling, Christian"],["dc.contributor.author","Rodriguez-Castaneda, Fernando"],["dc.contributor.author","Liepold, Thomas"],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.author","Brose, Nils"],["dc.contributor.author","Sinz, Andrea"],["dc.contributor.author","Jahn, Olaf"],["dc.date.accessioned","2017-09-07T11:47:26Z"],["dc.date.available","2017-09-07T11:47:26Z"],["dc.date.issued","2009"],["dc.description.abstract","Munc13 proteins are essential regulators of synaptic vesicle priming and play a key role in adaptive synaptic plasticity phenomena. We recently identified and characterized the Ca(2+)-dependent interaction of Munc13 and calmodulin (CaM) as the molecular mechanism linking changes in residual Ca(2+) concentrations to presynaptic vesicle priming and short-term plasticity. Here, we used peptidic photoprobes covering the established CaM-binding motif of Munc 13 for photoaffinity labeling (PAL) of CaM, followed by structural characterization of the covalent photoadducts. Our innovative analytical workflow based on isotopically labeled CaM and mass spectrometry revealed that, in the bound state, the hydrophobic anchor residue of the CaM-binding motif in Munc13s contacts two distinct methionine residues in the C-terminal domain of CaM. To address the orientation of the peptide during binding, we obtained additional distance constraints from the mass spectrometric analysis of chemically cross-linked CaM-Munc13 peptide adducts. The constraints from both complementary cross-linking approaches were integrated into low-resolution three-dimensional structure models of the CaM-Munc13 peptide complexes. Our experimental data are best compatible with the structure of the complex formed by CaM and a CaM-binding peptide derived from neuronal NO synthase and show that Munc13-1 and ubMunc13-2 bind to CaM in an antiparallel orientation through a 1-5-8 motif. The structural information about the CaM-Munc13 peptide complexes will facilitate the design of Munc13 variants with altered CaM affinity and thereby advance the detailed functional analysis of the role of Munc13 proteins in synaptic transmission and plasticity."],["dc.identifier.doi","10.1021/bi900300r"],["dc.identifier.gro","3143097"],["dc.identifier.isi","000267326500016"],["dc.identifier.pmid","19492809"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/574"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Amer Chemical Soc"],["dc.relation.issn","0006-2960"],["dc.title","Structural Insights into the Calmodulin-Munc13 Interaction Obtained by Cross-Linking and Mass Spectrometry"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Glia"],["dc.bibliographiccitation.volume","65"],["dc.contributor.author","Kusch, Kathrin"],["dc.contributor.author","Uecker, Martin"],["dc.contributor.author","Liepold, Thomas"],["dc.contributor.author","Möbius, Wiebke"],["dc.contributor.author","Werner, Hauke B."],["dc.contributor.author","Valerius, Oliver"],["dc.contributor.author","Jahn, Olaf"],["dc.contributor.author","Nave, Klaus-Armin"],["dc.date.accessioned","2018-11-07T10:23:03Z"],["dc.date.available","2018-11-07T10:23:03Z"],["dc.date.issued","2017"],["dc.identifier.isi","000403071700600"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/42387"],["dc.language.iso","en"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Wiley"],["dc.publisher.place","Hoboken"],["dc.relation.conference","13th European Meeting on Glial Cells in Health and Disease"],["dc.relation.eventlocation","Edinburgh, Scotland"],["dc.title","SIRT2 as a genetic modifier of axonal degeneration in white matter tracts"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2308"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","Journal of Neurochemistry"],["dc.bibliographiccitation.lastpage","2316"],["dc.bibliographiccitation.volume","68"],["dc.contributor.author","Hauger, R. L."],["dc.contributor.author","Dautzenberg, F. M."],["dc.contributor.author","Flaccus, A."],["dc.contributor.author","Liepold, T."],["dc.contributor.author","Spiess, J."],["dc.date.accessioned","2021-12-08T12:27:37Z"],["dc.date.available","2021-12-08T12:27:37Z"],["dc.date.issued","2002"],["dc.identifier.doi","10.1046/j.1471-4159.1997.68062308.x"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/95399"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-476"],["dc.relation.eissn","1471-4159"],["dc.relation.issn","0022-3042"],["dc.rights.uri","http://doi.wiley.com/10.1002/tdm_license_1.1"],["dc.title","Regulation of Corticotropin-Releasing Factor Receptor Function in Human Y-79 Retinoblastoma Cells: Rapid and Reversible Homologous Desensitization but Prolonged Recovery"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","3"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Proteomes"],["dc.bibliographiccitation.volume","5"],["dc.contributor.author","Kusch, Kathrin"],["dc.contributor.author","Uecker, Marina"],["dc.contributor.author","Liepold, Thomas"],["dc.contributor.author","Möbius, Wiebke"],["dc.contributor.author","Hoffmann, Christian"],["dc.contributor.author","Neumann, Heinz"],["dc.contributor.author","Werner, Hauke"],["dc.contributor.author","Jahn, Olaf"],["dc.date.accessioned","2020-12-10T18:47:19Z"],["dc.date.available","2020-12-10T18:47:19Z"],["dc.date.issued","2017"],["dc.identifier.doi","10.3390/proteomes5010003"],["dc.identifier.eissn","2227-7382"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/78723"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.publisher","MDPI"],["dc.relation.eissn","2227-7382"],["dc.rights","https://creativecommons.org/licenses/by/4.0/"],["dc.title","Partial Immunoblotting of 2D-Gels: A Novel Method to Identify Post-Translationally Modified Proteins Exemplified for the Myelin Acetylome"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Frontiers in Molecular Neuroscience"],["dc.bibliographiccitation.volume","12"],["dc.contributor.author","Akula, Asha Kiran"],["dc.contributor.author","Zhang, Xin"],["dc.contributor.author","Viotti, Julio S."],["dc.contributor.author","Nestvogel, Dennis"],["dc.contributor.author","Rhee, Jeong-Seop"],["dc.contributor.author","Ebrecht, Rene"],["dc.contributor.author","Reim, Kerstin"],["dc.contributor.author","Wouters, Fred"],["dc.contributor.author","Liepold, Thomas"],["dc.contributor.author","Jahn, Olaf"],["dc.contributor.author","Bogeski, Ivan"],["dc.contributor.author","Dresbach, Thomas"],["dc.date.accessioned","2020-12-10T18:44:35Z"],["dc.date.available","2020-12-10T18:44:35Z"],["dc.date.issued","2019"],["dc.description.abstract","Neurotransmitter release is mediated by an evolutionarily conserved machinery. The synaptic vesicle (SV) associated protein Mover/TPRGL/SVAP30 does not occur in all species and all synapses. Little is known about its molecular properties and how it may interact with the conserved components of the presynaptic machinery. Here, we show by deletion analysis that regions required for homomeric interaction of Mover are distributed across the entire molecule, including N-terminal, central and C-terminal regions. The same regions are also required for the accumulation of Mover in presynaptic terminals of cultured neurons. Mutating two phosphorylation sites in N-terminal regions did not affect these properties. In contrast, a point mutation in the predicted Calmodulin (CaM) binding sequence of Mover abolished both homomeric interaction and presynaptic targeting. We show that this sequence indeed binds Calmodulin, and that recombinant Mover increases Calmodulin signaling upon heterologous expression. Our data suggest that presynaptic accumulation of Mover requires homomeric interaction mediated by regions distributed across large areas of the protein, and corroborate the hypothesis that Mover functionally interacts with Calmodulin signaling."],["dc.identifier.doi","10.3389/fnmol.2019.00249"],["dc.identifier.eissn","1662-5099"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/16645"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/78512"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.notes.intern","Merged from goescholar"],["dc.publisher","Frontiers Media S.A."],["dc.relation.eissn","1662-5099"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","The Calmodulin Binding Region of the Synaptic Vesicle Protein Mover Is Required for Homomeric Interaction and Presynaptic Targeting"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1850"],["dc.bibliographiccitation.issue","8"],["dc.bibliographiccitation.journal","Biochimica et Biophysica Acta (BBA) - Molecular Cell Research"],["dc.bibliographiccitation.lastpage","1859"],["dc.bibliographiccitation.volume","1853"],["dc.contributor.author","Melin, Jonathan"],["dc.contributor.author","Kilisch, Markus"],["dc.contributor.author","Neumann, Piotr"],["dc.contributor.author","Lytovchenko, Oleksandr"],["dc.contributor.author","Gomkale, Ridhima"],["dc.contributor.author","Schendzielorz, Alexander Benjamin"],["dc.contributor.author","Schmidt, Bernhard"],["dc.contributor.author","Liepold, Thomas"],["dc.contributor.author","Ficner, Ralf"],["dc.contributor.author","Jahn, Olaf"],["dc.contributor.author","Rehling, Peter"],["dc.contributor.author","Schulz, Christian"],["dc.date.accessioned","2017-09-07T11:43:40Z"],["dc.date.available","2017-09-07T11:43:40Z"],["dc.date.issued","2015"],["dc.description.abstract","The translocase of the outer mitochondrial membrane (TOM complex) is the general entry gate into mitochondria for almost all imported proteins. A variety of specific receptors allow the TOM complex to recognize targeting signals of various precursor proteins that are transported along different import pathways. Aside from the well-characterized presequence receptors Tom20 and Tom22 a third TOM receptor, Tom70, binds proteins of the carrier family containing multiple transmembrane segments. Here we demonstrate that Tom70 directly binds to presequence peptides using a dedicated groove. A single point mutation in the cavity of this pocket (M551R) reduces the presequence binding affinity of Tom70 ten-fold and selectively impairs import of the presequence-containing precursor Mdl1 but not the ADP/ATP carrier (MC). Hence Tom70 contributes to the presequence import pathway by recognition of the targeting signal of the Mdl1 precursor. (C) 2015 Elsevier B.V. All rights reserved."],["dc.identifier.doi","10.1016/j.bbamcr.2015.04.021"],["dc.identifier.gro","3141858"],["dc.identifier.isi","000356209600009"],["dc.identifier.pmid","25958336"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1856"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","0006-3002"],["dc.relation.issn","0167-4889"],["dc.title","A presequence-binding groove in Tom70 supports import of Mdl1 into mitochondria"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","578"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Journal of Neurochemistry"],["dc.bibliographiccitation.lastpage","589"],["dc.bibliographiccitation.volume","160"],["dc.contributor.affiliation","Wirths, Oliver; 1\r\nDepartment of Psychiatry and Psychotherapy\r\nUniversity Medical Center Goettingen (UMG)\r\nGeorg‐August‐University\r\nGoettingen Germany"],["dc.contributor.affiliation","Mollenhauer, Brit; 2\r\nDepartment of Neurology\r\nUniversity Medical Center Goettingen (UMG)\r\nGeorg‐August‐University\r\nGoettingen Germany"],["dc.contributor.affiliation","Liepold, Thomas; 4\r\nMax Planck Institute of Experimental Medicine\r\nProteomics Group\r\nGoettingen Germany"],["dc.contributor.affiliation","Rieper, Petra; 1\r\nDepartment of Psychiatry and Psychotherapy\r\nUniversity Medical Center Goettingen (UMG)\r\nGeorg‐August‐University\r\nGoettingen Germany"],["dc.contributor.affiliation","Esselmann, Hermann; 1\r\nDepartment of Psychiatry and Psychotherapy\r\nUniversity Medical Center Goettingen (UMG)\r\nGeorg‐August‐University\r\nGoettingen Germany"],["dc.contributor.affiliation","Vogelgsang, Jonathan; 1\r\nDepartment of Psychiatry and Psychotherapy\r\nUniversity Medical Center Goettingen (UMG)\r\nGeorg‐August‐University\r\nGoettingen Germany"],["dc.contributor.affiliation","Wiltfang, Jens; 1\r\nDepartment of Psychiatry and Psychotherapy\r\nUniversity Medical Center Goettingen (UMG)\r\nGeorg‐August‐University\r\nGoettingen Germany"],["dc.contributor.author","Klafki, Hans‐Wolfgang"],["dc.contributor.author","Wirths, Oliver"],["dc.contributor.author","Mollenhauer, Brit"],["dc.contributor.author","Liepold, Thomas"],["dc.contributor.author","Rieper, Petra"],["dc.contributor.author","Esselmann, Hermann"],["dc.contributor.author","Vogelgsang, Jonathan"],["dc.contributor.author","Wiltfang, Jens"],["dc.contributor.author","Jahn, Olaf"],["dc.date.accessioned","2022-02-01T10:31:26Z"],["dc.date.available","2022-02-01T10:31:26Z"],["dc.date.issued","2022"],["dc.date.updated","2022-06-15T00:17:43Z"],["dc.description.abstract","Abstract Neurochemical biomarkers can support the diagnosis of Alzheimer’s disease and may facilitate clinical trials. In blood plasma, the ratio of the amyloid‐β (Aβ) peptides Aβ−3–40/Aβ1–42 can predict cerebral amyloid‐β pathology with high accuracy (Nakamura et al., 2018). Whether or not Aβ−3–40 (aka. amyloid precursor protein (APP) 669–711) is also present in cerebrospinal fluid (CSF) is not clear. Here, we investigated whether Aβ−3–40 can be detected in CSF and to what extent the CSF Aβ−3–40/Aβ42 ratio is able to differentiate between individuals with or without amyloid‐β positron emission tomography (PET) evidence of brain amyloid. The occurrence of Aβ−3–40 in human CSF was assessed by immunoprecipitation followed by mass spectrometry. For quantifying the CSF concentrations of Aβ−3–40 in 23 amyloid PET‐negative and 17 amyloid PET‐positive subjects, we applied a sandwich‐type immunoassay. Our findings provide clear evidence of the presence of Aβ−3–40 and Aβ−3–38 in human CSF. While there was no statistically significant difference in the CSF concentration of Aβ−3–40 between the two diagnostic groups, the CSF Aβ−3–40/Aβ42 ratio was increased in the amyloid PET‐positive individuals. We conclude that Aβ−3–40 appears to be a regular constituent of CSF and may potentially serve to accentuate the selective decrease in CSF Aβ42 in Alzheimer's disease. image"],["dc.description.abstract","Cerebral amyloid‐β pathology can be predicted by the Aβ−3–40/Aβ1–42 peptide ratio in blood plasma (Nakamura et al., 2018, Nature 554, 249). However, it is still unclear whether Aβ−3–x peptides occur in cerebrospinal fluid (CSF). By immunoprecipitation‐mass spectrometry (IP‐MS), we show that Aβ−3–40 and Aβ−3–38 are regular constituents of CSF. The CSF Aβ−3–40/Aβ42 ratio, measured with a sandwich immunoassay, was found to be increased in individuals with positron emission tomography (PET) evidence of brain amyloid. Thus, CSF Aβ−3–40 may serve to accentuate the selective decrease in CSF Aβ42 in Alzheimer's disease. image"],["dc.identifier.doi","10.1111/jnc.15571"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/98861"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-517"],["dc.relation.eissn","1471-4159"],["dc.relation.issn","0022-3042"],["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://creativecommons.org/licenses/by-nc/4.0/"],["dc.title","Detection and quantification of Aβ−3–40 (APP669‐711) in cerebrospinal fluid"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","507"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Neuropharmacology"],["dc.bibliographiccitation.lastpage","516"],["dc.bibliographiccitation.volume","41"],["dc.contributor.author","Brauns, Olaf"],["dc.contributor.author","Liepold, Thomas"],["dc.contributor.author","Radulovic, Jelena"],["dc.contributor.author","Spiess, Joachim"],["dc.date.accessioned","2021-06-01T10:50:06Z"],["dc.date.available","2021-06-01T10:50:06Z"],["dc.date.issued","2001"],["dc.identifier.doi","10.1016/S0028-3908(01)00094-6"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/86530"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-425"],["dc.relation.issn","0028-3908"],["dc.title","Pharmacological and chemical properties of astressin, antisauvagine-30 and α-helCRF: significance for behavioral experiments"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]