Ivanović, Aleksandra

[["dc.bibliographiccitation.firstpage","735"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Journal of Cell Science"],["dc.bibliographiccitation.lastpage","744"],["dc.bibliographiccitation.volume","122"],["dc.contributor.author","Wozny, Christian"],["dc.contributor.author","Breustedt, Jörg"],["dc.contributor.author","Wolk, Friederike"],["dc.contributor.author","Varoqueaux, Frédérique"],["dc.contributor.author","Boretius, Susann"],["dc.contributor.author","Zivkovic, Aleksandar R."],["dc.contributor.author","Neeb, Antje"],["dc.contributor.author","Frahm, Jens"],["dc.contributor.author","Schmitz, Dietmar"],["dc.contributor.author","Brose, Nils"],["dc.contributor.author","Ivanovic, Aleksandra"],["dc.date.accessioned","2017-09-07T11:45:27Z"],["dc.date.available","2017-09-07T11:45:27Z"],["dc.date.issued","2009"],["dc.description.abstract","AMPA-type glutamate receptors mediate fast excitatory synaptic transmission in the vertebrate brain. Their surface expression at synapses between neurons is regulated in an activity-dependent and activity-independent manner. The protein machinery that regulates synaptic targeting, anchoring and turnover of AMPA receptors consists of several types of specialized scaffolding proteins. The FERM domain scaffolding proteins 4.1G and 4.1N were previously suggested to act jointly in binding and regulating synaptic trafficking of the AMPA receptor subunits GluR1 and GluR4. To determine the functions of 4.1G and 4.1N in vivo, we generated a mutant mouse line that lacks 4.1G entirely and expresses 4.1N at 22% of wild-type levels. These mice had combined 4.1G and 4.1N protein expression in the hippocampus at 12% of wild-type levels (equivalent to 8-10% of combined GluR1 and GluR4 expression levels). They show a moderate reduction in synaptosomal expression levels of the AMPA receptor subunit GluR1 at 3 weeks of age, but no change in basic glutamatergic synaptic transmission and long-term potentiation in the hippocampus. Our study indicates that 4.1G and 4.1N do not have a crucial role in glutamatergic synaptic transmission and the induction and maintenance of long-term plastic changes in synaptic efficacy."],["dc.identifier.doi","10.1242/jcs.037382"],["dc.identifier.gro","3150376"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/7134"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.relation.issn","0021-9533"],["dc.subject","Knockout; Mouse; Hippocampus; GluR1; GluR4; Synaptic plasticity"],["dc.title","The function of glutamatergic synapses is not perturbed by severe knockdown of 4.1N and 4.1G expression"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.peerReviewed","no"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","037207"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Physical Review Letters"],["dc.bibliographiccitation.volume","105"],["dc.contributor.author","Suchaneck, A."],["dc.contributor.author","Hinkov, V."],["dc.contributor.author","Haug, D."],["dc.contributor.author","Schulz, L."],["dc.contributor.author","Bernhard, C."],["dc.contributor.author","Ivanov, A."],["dc.contributor.author","Hradil, Klaudia"],["dc.contributor.author","Lin, C. T."],["dc.contributor.author","Bourges, Philippe"],["dc.contributor.author","Keimer, B."],["dc.contributor.author","Sidis, Y."],["dc.date.accessioned","2018-11-07T08:41:20Z"],["dc.date.available","2018-11-07T08:41:20Z"],["dc.date.issued","2010"],["dc.description.abstract","We report an inelastic-neutron-scattering and muon-spin-relaxation study of the effect of 2% spinless (Zn) impurities on the magnetic order and dynamics of YBa2Cu3O6.6, an underdoped high-temperature superconductor that exhibits a prominent spin pseudogap in its normal state. Zn substitution induces static magnetic order at low temperatures and triggers a large-scale spectral-weight redistribution from the magnetic resonant mode at 38 meV into uniaxial, incommensurate spin excitations with energies well below the spin pseudogap. These observations indicate a competition between incommensurate magnetic order and superconductivity close to a quantum critical point. Comparison to prior data on La2-xSrxCuO4 suggests that this behavior is universal for the layered copper oxides and analogous to impurity-induced magnetic order in one-dimensional quantum magnets."],["dc.description.sponsorship","DFG [FOR538]"],["dc.identifier.doi","10.1103/PhysRevLett.105.037207"],["dc.identifier.isi","000280008900019"],["dc.identifier.pmid","20867803"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/19444"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Physical Soc"],["dc.relation.issn","0031-9007"],["dc.title","Incommensurate Magnetic Order and Dynamics Induced by Spinless Impurities in YBa2Cu3O6.6"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","337"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","The Journal of Cell Biology"],["dc.bibliographiccitation.lastpage","344"],["dc.bibliographiccitation.volume","196"],["dc.contributor.author","Ivanovic, Aleksandra"],["dc.contributor.author","Horresh, Ida"],["dc.contributor.author","Golan, Neev"],["dc.contributor.author","Spiegel, Ivo"],["dc.contributor.author","Sabanay, Helena"],["dc.contributor.author","Frechter, Shahar"],["dc.contributor.author","Ohno, Shinichi"],["dc.contributor.author","Terada, Nobuo"],["dc.contributor.author","Möbius, Wiebke"],["dc.contributor.author","Rosenbluth, Jack"],["dc.contributor.author","Brose, Nils"],["dc.contributor.author","Peles, Elior"],["dc.date.accessioned","2017-09-07T11:48:59Z"],["dc.date.available","2017-09-07T11:48:59Z"],["dc.date.issued","2012"],["dc.description.abstract","Myelinating Schwann cells regulate the localization of ion channels on the surface of the axons they ensheath. This function depends on adhesion complexes that are positioned at specific membrane domains along the myelin unit. Here we show that the precise localization of internodal proteins depends on the expression of the cytoskeletal adapter protein 4.1G in Schwann cells. Deletion of 4.1G in mice resulted in aberrant distribution of both glial adhesion molecules and axonal proteins that were present along the internodes. In wild-type nerves, juxtaparanodal proteins (i.e., Kv1 channels, Caspr2, and TAG-1) were concentrated throughout the internodes in a double strand that flanked paranodal junction components (i.e., Caspr, contactin, and NF155), and apposes the inner mesaxon of the myelin sheath. In contrast, in 4.1G(-/-) mice, these proteins \"piled up\" at the juxtaparanodal region or aggregated along the internodes. These findings suggest that protein 4.1G contributes to the organization of the internodal axolemma by targeting and/or maintaining glial transmembrane proteins along the axoglial interface."],["dc.identifier.doi","10.1083/jcb.201111127"],["dc.identifier.gro","3142582"],["dc.identifier.isi","000300117300006"],["dc.identifier.pmid","22291039"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/8948"],["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","0021-9525"],["dc.title","The cytoskeletal adapter protein 4.1G organizes the internodes in peripheral myelinated nerves"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","214512"],["dc.bibliographiccitation.issue","21"],["dc.bibliographiccitation.journal","PHYSICAL REVIEW B"],["dc.bibliographiccitation.volume","76"],["dc.contributor.author","Fauque, B."],["dc.contributor.author","Sidis, Y."],["dc.contributor.author","Capogna, L."],["dc.contributor.author","Ivanov, A."],["dc.contributor.author","Hradil, Klaudia"],["dc.contributor.author","Ulrich, Cornelia M."],["dc.contributor.author","Rykov, A. I."],["dc.contributor.author","Keimer, B."],["dc.contributor.author","Bourges, Philippe"],["dc.date.accessioned","2018-11-07T10:50:18Z"],["dc.date.available","2018-11-07T10:50:18Z"],["dc.date.issued","2007"],["dc.description.abstract","We report a neutron scattering study of the spin excitation spectrum in the superconducting state of the slightly overdoped Bi2Sr2CaCu2O8+delta system (T-c= 87 K). We focus on the dispersion of the resonance peak in the superconducting state that is due to a S= 1 collective mode. The measured spin excitation spectrum bears a strong similarity to the spectrum of the YBa(2)Cu(3)On(6+x) system for a similar doping level (i.e., x similar to 0.95-1), which can be described as intersecting upward- and downward-dispersing branches. A close comparison of the threshold of the electron-hole spin flip continuum, known from angle resolved photoemission measurements in the same system, indicates that the magnetic response in the superconducting state is confined, in both energy and momentum, below the gapped Stoner continuum. In contrast to YBa2Cu3O6+x, the spin excitation spectrum is broader than the experimental resolution. In the framework of an itinerant-electron model, we quantitatively relate this intrinsic energy width to the superconducting gap distribution observed in scanning tunneling microscopy experiments. Our study further suggests a significant in-plane anisotropy of the magnetic response."],["dc.identifier.doi","10.1103/PhysRevB.76.214512"],["dc.identifier.isi","000251986100096"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/48624"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Physical Soc"],["dc.relation.issn","2469-9969"],["dc.relation.issn","2469-9950"],["dc.title","Dispersion of the odd magnetic resonant mode in near-optimally doped Bi2Sr2CaCu2O8+delta"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","E1717"],["dc.bibliographiccitation.issue","9"],["dc.bibliographiccitation.journal","Proceedings of the National Academy of Sciences of the United States of America"],["dc.bibliographiccitation.lastpage","E1726"],["dc.bibliographiccitation.volume","114"],["dc.contributor.author","Picher, Maria Magdalena"],["dc.contributor.author","Gehrt, Anna"],["dc.contributor.author","Meese, Sandra"],["dc.contributor.author","Ivanovic, Aleksandra"],["dc.contributor.author","Predoehl, Friederike"],["dc.contributor.author","Jung, SangYong"],["dc.contributor.author","Schrauwen, Isabelle"],["dc.contributor.author","Dragonetti, Alberto Giulio"],["dc.contributor.author","Colombo, Roberto"],["dc.contributor.author","Van Camp, Guy"],["dc.contributor.author","Strenzke, Nicola"],["dc.contributor.author","Moser, Tobias"],["dc.date.accessioned","2018-01-17T11:41:34Z"],["dc.date.available","2018-01-17T11:41:34Z"],["dc.date.issued","2017-02-28"],["dc.description.abstract","Ca2+-binding protein 2 (CaBP2) inhibits the inactivation of heterologously expressed voltage-gated Ca2+ channels of type 1.3 (CaV1.3) and is defective in human autosomal-recessive deafness 93 (DFNB93). Here, we report a newly identified mutation in CABP2 that causes a moderate hearing impairment likely via nonsense-mediated decay of CABP2-mRNA. To study the mechanism of hearing impairment resulting from CABP2 loss of function, we disrupted Cabp2 in mice (Cabp2LacZ/LacZ ). CaBP2 was expressed by cochlear hair cells, preferentially in inner hair cells (IHCs), and was lacking from the postsynaptic spiral ganglion neurons (SGNs). Cabp2LacZ/LacZ mice displayed intact cochlear amplification but impaired auditory brainstem responses. Patch-clamp recordings from Cabp2LacZ/LacZ IHCs revealed enhanced Ca2+-channel inactivation. The voltage dependence of activation and the number of Ca2+ channels appeared normal in Cabp2LacZ/LacZ mice, as were ribbon synapse counts. Recordings from single SGNs showed reduced spontaneous and sound-evoked firing rates. We propose that CaBP2 inhibits CaV1.3 Ca2+-channel inactivation, and thus sustains the availability of CaV1.3 Ca2+ channels for synaptic sound encoding. Therefore, we conclude that human deafness DFNB93 is an auditory synaptopathy."],["dc.identifier.doi","10.1073/pnas.1617533114"],["dc.identifier.pmid","28183797"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/11687"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.relation.eissn","1091-6490"],["dc.title","Ca2+-binding protein 2 inhibits Ca2+-channel inactivation in mouse inner hair cells"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","134503"],["dc.bibliographiccitation.issue","13"],["dc.bibliographiccitation.journal","PHYSICAL REVIEW B"],["dc.bibliographiccitation.volume","82"],["dc.contributor.author","Park, J. T."],["dc.contributor.author","Inosov, D. S."],["dc.contributor.author","Yaresko, A."],["dc.contributor.author","Graser, S."],["dc.contributor.author","Sun, D. L."],["dc.contributor.author","Bourges, Philippe"],["dc.contributor.author","Sidis, Y."],["dc.contributor.author","Li, Yuan"],["dc.contributor.author","Kim, J.-H."],["dc.contributor.author","Haug, D."],["dc.contributor.author","Ivanov, A."],["dc.contributor.author","Hradil, Klaudia"],["dc.contributor.author","Schneidewind, Astrid"],["dc.contributor.author","Link, P."],["dc.contributor.author","Faulhaber, Enrico"],["dc.contributor.author","Glavatskyy, I."],["dc.contributor.author","Lin, C. T."],["dc.contributor.author","Keimer, B."],["dc.contributor.author","Hinkov, V."],["dc.date.accessioned","2018-11-07T08:38:55Z"],["dc.date.available","2018-11-07T08:38:55Z"],["dc.date.issued","2010"],["dc.description.abstract","We study the symmetry of spin excitation spectra in 122-ferropnictide superconductors by comparing the results of first-principles calculations with inelastic neutron-scattering (INS) measurements on BaFe1.85Co0.15As2 and BaFe1.91Ni0.09As2 samples that exhibit neither static magnetic phases nor structural phase transitions. In both the normal and superconducting (SC) states, the spectrum lacks the three-dimensional 4(2)/m screw symmetry around the (1/2 1/2 L) axis that is implied by the I4/mmm space group. This is manifest both in the in-plane anisotropy of the normal- and SC-state spin dynamics and in the out-of-plane dispersion of the spin-resonance mode. We show that this effect originates from the higher symmetry of the magnetic Fe sublattice with respect to the crystal itself, hence the INS signal inherits the symmetry of the unfolded Brillouin zone (BZ) of the Fe sublattice. The in-plane anisotropy is temperature independent and can be qualitatively reproduced in normal-state density-functional-theory calculations without invoking a symmetry-broken (\"nematic\") ground state that was previously proposed as an explanation for this effect. Below the SC transition, the energy of the magnetic resonant mode omega(res), as well as its intensity and the SC spin gap inherit the normal-state intensity modulation along the out-of-plane direction L with a period twice larger than expected from the body-centered-tetragonal BZ symmetry. The amplitude of this modulation decreases at higher doping, providing an analogy to the splitting between even and odd resonant modes in bilayer cuprates. Combining our and previous data, we show that at odd L a universal linear relationship (h) over bar omega(res) approximate to 4.3 k(B)T(c) holds for all the studied Fe-based superconductors, independent of their carrier type. Its validity down to the lowest doping levels is consistent with weaker electron correlations in ferropnictides as compared to the underdoped cuprates."],["dc.description.sponsorship","DFG [1458, BO3537/1-1]"],["dc.identifier.doi","10.1103/PhysRevB.82.134503"],["dc.identifier.isi","000282358900007"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/18868"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Physical Soc"],["dc.relation.issn","1098-0121"],["dc.title","Symmetry of spin excitation spectra in the tetragonal paramagnetic and superconducting phases of 122-ferropnictides"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]