Rizzoli, Silvio O.

[["dc.bibliographiccitation.firstpage","11440"],["dc.bibliographiccitation.issue","31"],["dc.bibliographiccitation.journal","Proceedings of the National Academy of Sciences of the United States of America"],["dc.bibliographiccitation.lastpage","11445"],["dc.bibliographiccitation.volume","103"],["dc.contributor.author","Donnert, Gerald"],["dc.contributor.author","Keller, Jan"],["dc.contributor.author","Medda, Rebecca"],["dc.contributor.author","Andrei, M. Alexandra"],["dc.contributor.author","Rizzoli, Silvio"],["dc.contributor.author","Lührmann, Reinhard"],["dc.contributor.author","Jahn, Reinhard"],["dc.contributor.author","Eggeling, Christian"],["dc.contributor.author","Hell, Stefan"],["dc.date.accessioned","2017-09-07T11:52:39Z"],["dc.date.available","2017-09-07T11:52:39Z"],["dc.date.issued","2006"],["dc.description.abstract","We demonstrate far-field fluorescence microscopy with a focal-plane resolution of 15-20 nm in biological samples. The 10- to 12-fold multilateral increase in resolution below the diffraction barrier has been enabled by the elimination of molecular triplet state excitation as a major source of photobleaching of a number of dyes in stimulated emission depletion microscopy. Allowing for relaxation of the triplet state between subsequent excitation-depletion cycles yields an up to 30-fold increase in total fluorescence signal as compared with reported stimulated emission depletion illumination schemes. Moreover, it enables the reduction of the effective focal spot area by up to approximate to 140-fold below that given by diffraction. Triplet-state relaxation can be realized either by reducing the repetition rate of pulsed lasers or by increasing the scanning speed such that the build-up of the triplet state is effectively prevented. This resolution in immunofluorescence imaging is evidenced by revealing nanoscale protein patterns on endosomes, the punctuated structures of intermediate filaments in neurons, and nuclear protein speckles in mammalian cells with conventional optics. The reported performance of diffraction-unlimited fluorescence microscopy opens up a pathway for addressing fundamental problems in the life sciences."],["dc.identifier.doi","10.1073/pnas.0604965103"],["dc.identifier.gro","3143651"],["dc.identifier.isi","000239616400005"],["dc.identifier.pmid","16864773"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1188"],["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","0027-8424"],["dc.title","Macromolecular-scale resolution in biological fluorescence microscopy"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","26349"],["dc.bibliographiccitation.issue","46"],["dc.bibliographiccitation.journal","Physical Chemistry Chemical Physics"],["dc.bibliographiccitation.lastpage","26355"],["dc.bibliographiccitation.volume","23"],["dc.contributor.author","Saul, Philip"],["dc.contributor.author","Yang, Shengjun"],["dc.contributor.author","Mamone, Salvatore"],["dc.contributor.author","Opazo, Felipe"],["dc.contributor.author","Meyer, Andreas"],["dc.contributor.author","Rizzoli, Silvio O."],["dc.contributor.author","Glöggler, Stefan"],["dc.date.accessioned","2021-12-01T09:20:55Z"],["dc.date.available","2021-12-01T09:20:55Z"],["dc.date.issued","2021"],["dc.description.abstract","Dendrimers display an exotic spin state behavior that we propose to tune for ion sensing."],["dc.description.abstract","Dendrimers are a class of branched, highly symmetric macromolecules that have been shown to be useful for a vast number of different applications. Potential uses as fluorescence sensors, in catalysis and perhaps most importantly in medical applications as drug delivery systems or cytotoxica have been proposed. Herein we report on an exotic behaviour of the nuclear spins in a dendritic macromolecule in the presence of different paramagnetic ions. We show that the stability of the long lived nuclear singlet state, is affected by the presence of Cu( ii ), whereas other ions did not have any influence at all. This effect could not be observed in the case of a simple tripeptide, in which the nuclear singlet stability was influenced by all investigated paramagnetic ions, a potentially useful effect in the development of Cu( ii ) selective probes. By adding a fluorescent marker to our molecule we could show that the nuclear singlet multimer (NUSIMER) is taken up by living cells. Furthermore we were able to show that nuclear singlet state NMR can be used to investigate the NUSIMER in the presence of living cells, showing that an application in in vivo NMR can be feasible."],["dc.description.abstract","Dendrimers display an exotic spin state behavior that we propose to tune for ion sensing."],["dc.description.abstract","Dendrimers are a class of branched, highly symmetric macromolecules that have been shown to be useful for a vast number of different applications. Potential uses as fluorescence sensors, in catalysis and perhaps most importantly in medical applications as drug delivery systems or cytotoxica have been proposed. Herein we report on an exotic behaviour of the nuclear spins in a dendritic macromolecule in the presence of different paramagnetic ions. We show that the stability of the long lived nuclear singlet state, is affected by the presence of Cu( ii ), whereas other ions did not have any influence at all. This effect could not be observed in the case of a simple tripeptide, in which the nuclear singlet stability was influenced by all investigated paramagnetic ions, a potentially useful effect in the development of Cu( ii ) selective probes. By adding a fluorescent marker to our molecule we could show that the nuclear singlet multimer (NUSIMER) is taken up by living cells. Furthermore we were able to show that nuclear singlet state NMR can be used to investigate the NUSIMER in the presence of living cells, showing that an application in in vivo NMR can be feasible."],["dc.identifier.doi","10.1039/D1CP04483D"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/94301"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-478"],["dc.relation.eissn","1463-9084"],["dc.relation.issn","1463-9076"],["dc.rights.uri","http://creativecommons.org/licenses/by/3.0/"],["dc.title","Exotic nuclear spin behavior in dendritic macromolecules"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","3333"],["dc.bibliographiccitation.issue","12"],["dc.bibliographiccitation.journal","Nature Protocols"],["dc.bibliographiccitation.lastpage","3365"],["dc.bibliographiccitation.volume","14"],["dc.contributor.author","Alevra, Mihai"],["dc.contributor.author","Mandad, Sunit"],["dc.contributor.author","Ischebeck, Till"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Rizzoli, Silvio O."],["dc.contributor.author","Fornasiero, Eugenio F."],["dc.date.accessioned","2020-12-10T18:10:05Z"],["dc.date.available","2020-12-10T18:10:05Z"],["dc.date.issued","2019"],["dc.identifier.doi","10.1038/s41596-019-0222-y"],["dc.identifier.pmid","31685960"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/73844"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/110"],["dc.identifier.url","https://sfb1286.uni-goettingen.de/literature/publications/80"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation","SFB 1286: Quantitative Synaptologie"],["dc.relation","SFB 1286 | A03: Dynamische Analyse der Remodellierung der extrazellulären Matrix (ECM) als Mechanismus der Synapsenorganisation und Plastizität"],["dc.relation.workinggroup","RG Rizzoli (Quantitative Synaptology in Space and Time)"],["dc.relation.workinggroup","RG Urlaub (Bioanalytische Massenspektrometrie)"],["dc.title","A mass spectrometry workflow for measuring protein turnover rates in vivo"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1069"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","Neurobiology of Disease"],["dc.bibliographiccitation.lastpage","1081"],["dc.bibliographiccitation.volume","8"],["dc.contributor.author","Basile, A. S."],["dc.contributor.author","Koustova, E."],["dc.contributor.author","Ioan, P"],["dc.contributor.author","Rizzoli, Silvio"],["dc.contributor.author","Rogawski, M. A."],["dc.contributor.author","Usherwood, P. N. R."],["dc.date.accessioned","2017-09-07T11:45:59Z"],["dc.date.available","2017-09-07T11:45:59Z"],["dc.date.issued","2001"],["dc.description.abstract","Biochemical and immunological studies have shown that mice infected with LP-BM5 virus develop antibodies to ionotropic glutamate receptors. Here, IgG isolated from brain of infected mice has been tested electrophysiologically on cultured rat cortical and hippocampal neurons. The IgG elicited glycine-independent currents that reversed at similar to0 mV. Equivalent concentrations of IgG from uninfected mice were inactive. The glycine-independent currents were less influenced by DNQX and GYKI-52466 than currents elicited by AMPA and KA. The IgG also elicited glycine-dependent currents that reversed at -10 mV and were blocked by dl-AP5, 5,7-DCKA, and polyamine amides. Glycine-dependent and -independent currents were unaffected by tetrodotoxin, strychnine, the transmembrane Cl- gradient or d-tubocurare. Although part of the glycine-independent current remains uncharacterized, these results confirm that a virus-induced immunopathology produces IgG clones that activate ionotropic glutamate receptors and that could, thereby, contribute to the excitotoxic neurological syndrome observed in LP-BM5-infected mice. (C) 2001 Elsevier Science."],["dc.identifier.doi","10.1006/nbdi.2001.0442"],["dc.identifier.gro","3144240"],["dc.identifier.isi","000172892100015"],["dc.identifier.pmid","11741402"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1842"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Academic Press Inc Elsevier Science"],["dc.relation.issn","0969-9961"],["dc.title","IgG isolated from LP-BM5 infected mouse brain activates ionotropic glutamate receptors"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","606"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","Microscopy research and technique"],["dc.bibliographiccitation.lastpage","617"],["dc.bibliographiccitation.volume","73"],["dc.contributor.author","Geumann, Ulf"],["dc.contributor.author","Schaefer, Christina"],["dc.contributor.author","Riedel, Dietmar"],["dc.contributor.author","Jahn, Reinhard"],["dc.contributor.author","Rizzoli, Silvio"],["dc.date.accessioned","2017-09-07T11:46:02Z"],["dc.date.available","2017-09-07T11:46:02Z"],["dc.date.issued","2010"],["dc.description.abstract","In the plasma membrane, membrane proteins are frequently organized in microdomains that are stabilized both by protein-protein and protein-lipid interactions, with the membrane lipid cholesterol being instrumental for microdomain stability. However, it is unclear whether such microdomains persist during endocytotic membrane trafficking. We used stimulated emission-depletion microscopy to investigate the domain structure of the endosomes. We developed a semiautomatic method for counting the individual domains, an approach that we have validated by immunoelectron microscopy. We found that in endosomes derived from neuroendocrine PC12 cells synaptophysin and several SNARE proteins are organized in microdomains. Cholesterol depletion by methyl-beta-cyclodextrin disintegrates most of the domains. Interestingly, no change in the frequency of microdomains was observed when endosomes were fused with protein-free liposomes of similar size (in what constitutes a novel approach in modifying acutely the lipid composition of organelles), regardless of whether the membrane lipid composition of the liposomes was similar or very different from that of the endosomes. Similarly, Rab depletion from the endosome membranes left the domain structure unaffected. Furthermore, labeled exogenous protein, introduced into endosomes by liposome fusion, equilibrated with the corresponding microdomains. We conclude that synaptic membrane proteins are organized in stable but dynamic clusters within endosomes, which are likely to persist during membrane recycling. Microsc. Res. Tech. 73:606-617, 2010. (C) 2009 Wiley-Liss, Inc."],["dc.identifier.doi","10.1002/jemt.20800"],["dc.identifier.gro","3142915"],["dc.identifier.isi","000278641200004"],["dc.identifier.pmid","19937745"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/372"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Wiley-liss"],["dc.relation.issn","1059-910X"],["dc.title","Synaptic Membrane Proteins Form Stable Microdomains in Early Endosomes"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2037"],["dc.bibliographiccitation.issue","5666"],["dc.bibliographiccitation.journal","Science"],["dc.bibliographiccitation.lastpage","2039"],["dc.bibliographiccitation.volume","303"],["dc.contributor.author","Rizzoli, Silvio"],["dc.contributor.author","Betz, William J."],["dc.date.accessioned","2017-09-07T11:43:59Z"],["dc.date.available","2017-09-07T11:43:59Z"],["dc.date.issued","2004"],["dc.description.abstract","The defining morphological feature of chemical synapses is the vesicle cluster in the presynaptic nerve terminal. It has generally been assumed that vesicles closest to release sites are recruited first during nerve activity. We tested this by selectively labeling the \"readily releasable\" pool, those vesicles released first during physiological stimulation. The readily releasable vesicles were not clustered close to the presynaptic membrane but instead were dispersed almost randomly throughout the vesicle cluster. Thus, vesicles are not recruited according to proximity to release sites but are mobilized differently, perhaps by being peeled from the surface of the cluster."],["dc.identifier.doi","10.1126/science.1094682"],["dc.identifier.gro","3144004"],["dc.identifier.isi","000220429800047"],["dc.identifier.pmid","15044806"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1581"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: NINDS NIH HHS [5 RO1 NS023466]"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Amer Assoc Advancement Science"],["dc.relation.issn","0036-8075"],["dc.title","The structural organization of the readily releasable pool of synaptic vesicles"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","13221"],["dc.bibliographiccitation.issue","67"],["dc.bibliographiccitation.journal","Chemical Communications"],["dc.bibliographiccitation.lastpage","13224"],["dc.bibliographiccitation.volume","51"],["dc.contributor.author","Kabatas, Selda"],["dc.contributor.author","Vreja, Ingrid C."],["dc.contributor.author","Saka, Sinem K."],["dc.contributor.author","Hoeschen, Carmen"],["dc.contributor.author","Kroehnert, Katharina"],["dc.contributor.author","Opazo, Felipe"],["dc.contributor.author","Rizzoli, S. O."],["dc.contributor.author","Diederichsen, Ulf"],["dc.date.accessioned","2017-09-07T11:44:43Z"],["dc.date.available","2017-09-07T11:44:43Z"],["dc.date.issued","2015"],["dc.description.abstract","Imaging techniques should differentiate between specific signals, from the biomolecules of interest, and non-specific signals, from the background. We present a probe containing N-15 and N-14 isotopes in approximately equal proportion, for secondary ion mass spectrometry imaging. This probe designed for a precise biomolecule analysis is insensitive to background signals."],["dc.identifier.doi","10.1039/c5cc03895b"],["dc.identifier.gro","3141979"],["dc.identifier.isi","000359246500017"],["dc.identifier.pmid","26195041"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/3201"],["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","1364-548X"],["dc.relation.issn","1359-7345"],["dc.title","A contamination-insensitive probe for imaging specific biomolecules by secondary ion 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","Molecular Biology of the Cell"],["dc.bibliographiccitation.volume","25"],["dc.contributor.author","Saka, S. K."],["dc.contributor.author","Honigmann, A."],["dc.contributor.author","Eggeling, C."],["dc.contributor.author","Hell, Stefan W."],["dc.contributor.author","Lang, T."],["dc.contributor.author","Rizzoli, Silvio"],["dc.date.accessioned","2018-11-07T09:31:35Z"],["dc.date.available","2018-11-07T09:31:35Z"],["dc.date.issued","2014"],["dc.identifier.isi","000352094103168"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/31561"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Soc Cell Biology"],["dc.publisher.place","Bethesda"],["dc.relation.eventlocation","Philadelphia, PA"],["dc.relation.issn","1939-4586"],["dc.relation.issn","1059-1524"],["dc.title","Multi-protein assemblies underlie the mesoscale organization of the plasma membrane."],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","427"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Communicative & Integrative Biology"],["dc.bibliographiccitation.lastpage","429"],["dc.bibliographiccitation.volume","3"],["dc.contributor.author","Opazo, Felipe"],["dc.contributor.author","Rizzoli, S. O."],["dc.date.accessioned","2017-09-07T11:54:04Z"],["dc.date.available","2017-09-07T11:54:04Z"],["dc.date.issued","2010"],["dc.description.abstract","Neurotransmitter release relies on the fusion of synaptic vesicles with the plasma membrane of synaptic boutons, which is followed by the recycling of vesicle components and formation of new vesicles. It is not yet clear whether upon fusion the vesicles persist as multimolecular patches in the plasma membrane, or whether they segregate into individual components. Evidence supporting each of these two models has been suggested in recent years. Using diffraction-unlimited imaging (stimulated emission depletion, or STED) of native synaptic vesicle proteins, we have proposed that vesicle proteins remain in clusters on the neuronal surface. These clusters do not appear to intermix. We discuss here these findings in the context of previous studies on synaptic vesicle fusion, and we propose a recycling model which accounts for most of the recent findings on the post-fusion fate of synaptic vesicle components."],["dc.identifier.doi","10.4161/cib.3.5.12132"],["dc.identifier.gro","3145094"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/2793"],["dc.language.iso","en"],["dc.notes.intern","Crossref Import"],["dc.notes.status","final"],["dc.relation.issn","1942-0889"],["dc.title","The fate of synaptic vesicle components upon fusion"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.peerReviewed","no"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","591"],["dc.bibliographiccitation.issue","6940"],["dc.bibliographiccitation.journal","Nature"],["dc.bibliographiccitation.lastpage","592"],["dc.bibliographiccitation.volume","423"],["dc.contributor.author","Rizzoli, Silvio"],["dc.contributor.author","Betz, William J."],["dc.date.accessioned","2017-09-07T11:45:00Z"],["dc.date.available","2017-09-07T11:45:00Z"],["dc.date.issued","2003"],["dc.identifier.doi","10.1038/423591a"],["dc.identifier.gro","3144100"],["dc.identifier.isi","000183301200021"],["dc.identifier.pmid","12789318"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1687"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Nature Publishing Group"],["dc.relation.issn","0028-0836"],["dc.title","Neurobiology: All change at the synapse"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","letter_note"],["dspace.entity.type","Publication"]]