Milovanovic, Dragomir

[["dc.bibliographiccitation.artnumber","959570"],["dc.bibliographiccitation.journal","Frontiers in Physiology"],["dc.bibliographiccitation.volume","13"],["dc.contributor.author","Milovanovic, Dragomir"],["dc.contributor.author","Rizzoli, Silvio O."],["dc.date.accessioned","2022-09-01T09:51:08Z"],["dc.date.available","2022-09-01T09:51:08Z"],["dc.date.issued","2022"],["dc.identifier.doi","10.3389/fphys.2022.959570"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/113891"],["dc.notes.intern","DOI-Import GROB-597"],["dc.relation.eissn","1664-042X"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0/"],["dc.title","Editorial: Protein Phase Separation and Aggregation in (Patho)Physiology of Neurons"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","100011"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Biophysical Reports"],["dc.bibliographiccitation.volume","1"],["dc.contributor.author","Wang, Huan"],["dc.contributor.author","Kelley, Fleurie M."],["dc.contributor.author","Milovanovic, Dragomir"],["dc.contributor.author","Schuster, Benjamin S."],["dc.contributor.author","Shi, Zheng"],["dc.date.accessioned","2022-08-25T10:36:09Z"],["dc.date.available","2022-08-25T10:36:09Z"],["dc.date.issued","2021"],["dc.description.abstract","The material properties of biomolecular condensates have been suggested to play important biological and pathological roles. Despite the rapid increase in the number of biomolecules identified that undergo liquid-liquid phase separation, quantitative studies and direct measurements of the material properties of the resulting condensates have been severely lagging behind. Here, we develop a micropipette-based technique that uniquely, to our knowledge, allows quantifications of both the surface tension and viscosity of biomolecular condensates, independent of labeling and surface-wetting effects. We demonstrate the accuracy and versatility of this technique by measuring condensates of LAF-1 RGG domains and a polymer-based aqueous two-phase system. We further confirm our measurements using established condensate fusion and fluorescence recovery after photobleaching assays. We anticipate the micropipette-based technique will be widely applicable to biomolecular condensates and will resolve several limitations regarding current approaches."],["dc.identifier.doi","10.1016/j.bpr.2021.100011"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/113229"],["dc.identifier.url","https://sfb1286.uni-goettingen.de/literature/publications/129"],["dc.language.iso","en"],["dc.relation","SFB 1286: Quantitative Synaptologie"],["dc.relation.issn","2667-0747"],["dc.relation.workinggroup","RG Rizzoli (Quantitative Synaptology in Space and Time)"],["dc.rights","CC BY-NC-ND 4.0"],["dc.title","Surface tension and viscosity of protein condensates quantified by micropipette aspiration"],["dc.type","journal_article"],["dc.type.internalPublication","no"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","891508"],["dc.bibliographiccitation.journal","Frontiers in Molecular Biosciences"],["dc.bibliographiccitation.volume","9"],["dc.contributor.author","Brodin, Lennart"],["dc.contributor.author","Milovanovic, Dragomir"],["dc.contributor.author","Rizzoli, Silvio O."],["dc.contributor.author","Shupliakov, Oleg"],["dc.date.accessioned","2022-07-01T07:35:29Z"],["dc.date.available","2022-07-01T07:35:29Z"],["dc.date.issued","2022"],["dc.description.abstract","The protein α-synuclein, which is well-known for its links to Parkinson’s Disease, is associated with synaptic vesicles (SVs) in nerve terminals. Despite intensive studies, its precise physiological function remains elusive. Accumulating evidence indicates that liquid-liquid phase separation takes part in the assembly and/or maintenance of different synaptic compartments. The current review discusses recent data suggesting α-synuclein as a component of the SV liquid phase. We also consider possible implications of these data for disease."],["dc.description.sponsorship"," Vetenskapsrådet http://dx.doi.org/10.13039/501100004359"],["dc.description.sponsorship"," Hjärnfonden http://dx.doi.org/10.13039/501100003792"],["dc.description.sponsorship"," Parkinsonfonden http://dx.doi.org/10.13039/100008444"],["dc.description.sponsorship"," Russian Science Support Foundation http://dx.doi.org/10.13039/100009409"],["dc.description.sponsorship"," Deutsche Forschungsgemeinschaft http://dx.doi.org/10.13039/501100001659"],["dc.identifier.doi","10.3389/fmolb.2022.891508"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/112184"],["dc.notes.intern","DOI-Import GROB-581"],["dc.relation.eissn","2296-889X"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0/"],["dc.title","α-Synuclein in the Synaptic Vesicle Liquid Phase: Active Player or Passive Bystander?"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","679"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","Nature Structural & Molecular Biology"],["dc.bibliographiccitation.lastpage","686"],["dc.bibliographiccitation.volume","20"],["dc.contributor.author","Honigmann, Alf"],["dc.contributor.author","van den Bogaart, Geert"],["dc.contributor.author","Iraheta, Emilio"],["dc.contributor.author","Risselada, H. Jelger"],["dc.contributor.author","Milovanovic, Dragomir"],["dc.contributor.author","Mueller, Veronika"],["dc.contributor.author","Müllar, Stefan"],["dc.contributor.author","Diederichsen, Ulf"],["dc.contributor.author","Fasshauer, Dirk"],["dc.contributor.author","Grubmüller, Helmut"],["dc.contributor.author","Hell, Stefan"],["dc.contributor.author","Eggeling, Christian"],["dc.contributor.author","Kühnel, Karin"],["dc.contributor.author","Jahn, Reinhard"],["dc.date.accessioned","2017-09-07T11:47:41Z"],["dc.date.available","2017-09-07T11:47:41Z"],["dc.date.issued","2013"],["dc.description.abstract","Synaptic-vesicle exocytosis is mediated by the vesicular Ca2+ sensor synaptotagmin-1. Synaptotagmin-1 interacts with the SNARE protein syntaxin-1A and acidic phospholipids such as phosphatidylinositol 4,5-bisphosphate (PIP2). However, it is unclear how these interactions contribute to triggering membrane fusion. Using PC12 cells from Rattus norvegicus and artificial supported bilayers, we show that synaptotagmin-1 interacts with the polybasic linker region of syntaxin-1A independent of Ca2+ through PIP2. This interaction allows both Ca2+-binding sites of synaptotagmin-1 to bind to phosphatidylserine in the vesicle membrane upon Ca2+ triggering. We determined the crystal structure of the C2B domain of synaptotagmin-1 bound to phosphoserine, allowing development of a high-resolution model of synaptotagmin bridging two different membranes. Our results suggest that PIP2 clusters organized by syntaxin-1 act as molecular beacons for vesicle docking, with the subsequent Ca2+ influx bringing the vesicle membrane close enough for membrane fusion."],["dc.identifier.doi","10.1038/nsmb.2570"],["dc.identifier.gro","3142345"],["dc.identifier.isi","000319915900008"],["dc.identifier.pmid","23665582"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/7253"],["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","1545-9993"],["dc.title","Phosphatidylinositol 4,5-bisphosphate clusters act as molecular beacons for vesicle recruitment"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","10336"],["dc.bibliographiccitation.issue","27"],["dc.bibliographiccitation.journal","Journal of the American Chemical Society"],["dc.bibliographiccitation.lastpage","10339"],["dc.bibliographiccitation.volume","133"],["dc.contributor.author","Bryn Fenwick, R."],["dc.contributor.author","Esteban-Martin, Santi"],["dc.contributor.author","Richter, Barbara"],["dc.contributor.author","Lee, Donghan"],["dc.contributor.author","Walter, Korvin F. A."],["dc.contributor.author","Milovanovic, Dragomir"],["dc.contributor.author","Becker, Stefan"],["dc.contributor.author","Lakomek, Nils-Alexander"],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.author","Salvatella, Xavier"],["dc.date.accessioned","2017-09-07T11:44:07Z"],["dc.date.available","2017-09-07T11:44:07Z"],["dc.date.issued","2011"],["dc.description.abstract","Long-range correlated motions in proteins are candidate mechanisms for processes that require information transfer across protein structures, such as allostery and signal transduction. However, the observation of backbone correlations between distant residues has remained elusive, and only local correlations have been revealed using residual dipolar couplings measured by NMR spectroscopy. In this work, we experimentally identified and characterized collective motions spanning four beta-strands separated by up to 15 angstrom in ubiquitin. The observed correlations link molecular recognition sites and result from concerted conformational changes that are in part mediated by the hydrogen-bonding network."],["dc.identifier.doi","10.1021/ja200461n"],["dc.identifier.gro","3142698"],["dc.identifier.isi","000293149800004"],["dc.identifier.pmid","21634390"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/131"],["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","0002-7863"],["dc.title","Weak Long-Range Correlated Motions in a Surface Patch of Ubiquitin Involved in Molecular Recognition"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","16"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Signal Transduction and Targeted Therapy"],["dc.bibliographiccitation.volume","7"],["dc.contributor.author","Hoffmann, Christian"],["dc.contributor.author","Rankovic, Branislava"],["dc.contributor.author","Milovanovic, Dragomir"],["dc.date.accessioned","2022-08-25T11:45:57Z"],["dc.date.available","2022-08-25T11:45:57Z"],["dc.date.issued","2022"],["dc.identifier.doi","10.1038/s41392-022-00876-5"],["dc.identifier.pmid","35027537"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/113232"],["dc.identifier.url","https://sfb1286.uni-goettingen.de/literature/publications/149"],["dc.language.iso","en"],["dc.relation","SFB 1286: Quantitative Synaptologie"],["dc.relation","SFB 1286 | B10: Nanoskalige Dynamik und Regulation von Synapsin-Kondensaten"],["dc.relation.issn","2059-3635"],["dc.relation.workinggroup","RG Milovanovic (Molecular Neuroscience)"],["dc.rights","CC BY 4.0"],["dc.title","Signals from the interface: protein nanoclusters stabilize biomolecular condensates"],["dc.type","journal_article"],["dc.type.internalPublication","no"],["dc.type.subtype","overview_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","European Biophysics Journal"],["dc.bibliographiccitation.volume","42"],["dc.contributor.author","Schwenen, Lando L. G."],["dc.contributor.author","Hernandez, Jesus M."],["dc.contributor.author","Milovanovic, Dragomir"],["dc.contributor.author","Jahn, R."],["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","S162"],["dc.identifier.isi","000330215300487"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/29378"],["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","SNARE mediated membrane fusion on pore-spanning membranes"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","479"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","ChemBioChem"],["dc.bibliographiccitation.lastpage","485"],["dc.bibliographiccitation.volume","17"],["dc.contributor.author","Sadek, Muheeb"],["dc.contributor.author","Berndt, Daniel"],["dc.contributor.author","Milovanovic, Dragomir"],["dc.contributor.author","Jahn, Reinhard"],["dc.contributor.author","Diederichsen, Ulf"],["dc.date.accessioned","2018-11-07T10:16:48Z"],["dc.date.available","2018-11-07T10:16:48Z"],["dc.date.issued","2016"],["dc.description.abstract","Artificial SNARE analogues derived from SNARE proteins, which mediate synaptic membrane fusion, are of interest. They mimic the tetrameric -helix bundle of the SNARE motif with various bio-oligomer recognition units. Interaction between complementary oligomers linked to the respective membrane by lipid or peptide anchors leads to proximity of vesicles and to fusion of lipid bilayers. -Peptide nucleic acids were introduced as hybrid oligomers with the native SNARE protein transmembrane/linker sequence, in order to evaluate a fusion system that allows distance tuning of approaching membranes. Formation of a four-base pair -PNA double strand with 20 angstrom length is sufficient for vesicle membrane fusion. Elongation of the recognition -PNA duplex in the linker region yielded a 40 angstrom -peptide duplex and provided a vesicle-vesicle distance that only supported hemifusion of vesicle membranes."],["dc.description.sponsorship","Deutsche Forschungsgemeinschaft DFG [SFB 803]"],["dc.identifier.doi","10.1002/cbic.201500517"],["dc.identifier.isi","000373200900008"],["dc.identifier.pmid","26879104"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/41108"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.relation.issn","1439-7633"],["dc.relation.issn","1439-4227"],["dc.title","Distance Regulated Vesicle Fusion and Docking Mediated by -Peptide Nucleic Acid SNARE Protein Analogues"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","520a"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Biophysical Journal"],["dc.bibliographiccitation.volume","110"],["dc.contributor.author","Hubrich, Raphael"],["dc.contributor.author","Kuhlmann, Jan"],["dc.contributor.author","Schwenen, Lando L.G."],["dc.contributor.author","Milovanovic, Dragomir"],["dc.contributor.author","Jahn, Reinhard"],["dc.contributor.author","Geil, Burkhard"],["dc.contributor.author","Steinem, Claudia"],["dc.date.accessioned","2020-12-10T14:22:42Z"],["dc.date.available","2020-12-10T14:22:42Z"],["dc.date.issued","2016"],["dc.identifier.doi","10.1016/j.bpj.2015.11.2779"],["dc.identifier.isi","000375143000026"],["dc.identifier.issn","0006-3495"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/71699"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Cell Press"],["dc.publisher.place","Cambridge"],["dc.relation.eventlocation","Los Angeles, CA"],["dc.title","Planar Pore-Spanning Membranes: A Platform to Study Snare-Mediated Fusion Processes"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","7868"],["dc.bibliographiccitation.issue","15"],["dc.bibliographiccitation.journal","Journal of Biological Chemistry"],["dc.bibliographiccitation.lastpage","7876"],["dc.bibliographiccitation.volume","291"],["dc.contributor.author","Milovanovic, Dragomir"],["dc.contributor.author","Platen, Mitja"],["dc.contributor.author","Junius, Meike"],["dc.contributor.author","Diederichsen, Ulf"],["dc.contributor.author","Schaap, Iwan A. T."],["dc.contributor.author","Honigmann, Alf"],["dc.contributor.author","Jahn, Reinhard"],["dc.contributor.author","van den Bogaart, Geert"],["dc.date.accessioned","2020-12-10T18:12:56Z"],["dc.date.available","2020-12-10T18:12:56Z"],["dc.date.issued","2016"],["dc.description.abstract","Phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2) is a minor component of total plasma membrane lipids, but it has a substantial role in the regulation of many cellular functions, including exo- and endocytosis. Recently, it was shown that PI(4,5)P2and syntaxin 1, a SNARE protein that catalyzes regulated exocytosis, form domains in the plasma membrane that constitute recognition sites for vesicle docking. Also, calcium was shown to promote syntaxin 1 clustering in the plasma membrane, but the molecular mechanism was unknown. Here, using a combination of superresolution stimulated emission depletion microscopy, FRET, and atomic force microscopy, we show that Ca(2+)acts as a charge bridge that specifically and reversibly connects multiple syntaxin 1/PI(4,5)P2complexes into larger mesoscale domains. This transient reorganization of the plasma membrane by physiological Ca(2+)concentrations is likely to be important for Ca(2+)-regulated secretion."],["dc.identifier.doi","10.1074/jbc.M116.716225"],["dc.identifier.eissn","1083-351X"],["dc.identifier.issn","0021-9258"],["dc.identifier.pmid","26884341"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/13366"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/74536"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.notes.status","final"],["dc.relation.eissn","1083-351X"],["dc.relation.eissn","0021-9258"],["dc.rights","Goescholar"],["dc.rights.uri","https://goedoc.uni-goettingen.de/licenses"],["dc.title","Calcium Promotes the Formation of Syntaxin 1 Mesoscale Domains through Phosphatidylinositol 4,5-Bisphosphate"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]