Jovin, Thomas M.

[["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Biophysical Journal"],["dc.bibliographiccitation.volume","108"],["dc.contributor.author","Valley, Christopher C."],["dc.contributor.author","Arndt-Jovin, Donna J."],["dc.contributor.author","Jovin, Thomas M."],["dc.contributor.author","Steinkamp, Mara P."],["dc.contributor.author","Chizhik, Alexey I."],["dc.contributor.author","Karedla, Narain V. R."],["dc.contributor.author","Hlavacek, William S."],["dc.contributor.author","Wilson, Bridget S."],["dc.contributor.author","Lidke, Keith A."],["dc.contributor.author","Lidke, Diane S."],["dc.date.accessioned","2018-11-07T10:01:57Z"],["dc.date.available","2018-11-07T10:01:57Z"],["dc.date.issued","2015"],["dc.format.extent","351A"],["dc.identifier.isi","000362849400177"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/38135"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Cell Press"],["dc.publisher.place","Cambridge"],["dc.relation.conference","59th Annual Meeting of the Biophysical-Society"],["dc.relation.eventlocation","Baltimore, MD"],["dc.relation.issn","1542-0086"],["dc.relation.issn","0006-3495"],["dc.title","Inside-Out Signaling of Oncogenic EGFR Mutants Promotes Ligand-Independent Dimerization"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","041014"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Physical Review X"],["dc.bibliographiccitation.volume","6"],["dc.contributor.author","Abbott, B. P."],["dc.contributor.author","Abbott, R."],["dc.contributor.author","Abbott, T. D."],["dc.contributor.author","Abernathy, M. R."],["dc.contributor.author","Acernese, F."],["dc.contributor.author","Ackley, K."],["dc.contributor.author","Adams, C."],["dc.contributor.author","Adams, T."],["dc.contributor.author","Addesso, P."],["dc.contributor.author","Adhikari, R. X."],["dc.contributor.author","Chao, S."],["dc.contributor.author","Chen, Y."],["dc.contributor.author","Chung, S."],["dc.contributor.author","Dent, T."],["dc.contributor.author","Ghosh, S."],["dc.contributor.author","Gras, S."],["dc.contributor.author","Huang, S."],["dc.contributor.author","Karki, S."],["dc.contributor.author","Khan, S."],["dc.contributor.author","Munch, J."],["dc.contributor.author","Nguyen, T. T."],["dc.contributor.author","Oliver, M."],["dc.contributor.author","Qin, J."],["dc.contributor.author","Schmidt, J."],["dc.contributor.author","Singh, A."],["dc.contributor.author","Thomas, M."],["dc.contributor.author","Thomas, P."],["dc.contributor.author","Wang, H."],["dc.contributor.author","Wang, Y."],["dc.contributor.author","Westphal, T."],["dc.contributor.author","Zhang, M."],["dc.contributor.author","Zhang, Y."],["dc.contributor.author","Röver, C."],["dc.contributor.author","De, S."],["dc.date.accessioned","2016-11-04T09:18:28Z"],["dc.date.accessioned","2021-10-27T13:20:48Z"],["dc.date.available","2016-11-04T09:18:28Z"],["dc.date.available","2021-10-27T13:20:48Z"],["dc.date.issued","2016"],["dc.identifier.doi","10.1103/PhysRevX.6.041014"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/13828"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/91981"],["dc.language.iso","en"],["dc.notes.intern","Migrated from goescholar"],["dc.relation.issn","2160-3308"],["dc.relation.orgunit","Universitätsmedizin Göttingen"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Improved analysis of GW150914 using a fully spin-precessing waveform model"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","407"],["dc.bibliographiccitation.journal","ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY"],["dc.bibliographiccitation.lastpage","415"],["dc.bibliographiccitation.volume","61"],["dc.contributor.author","Alexopoulos, E."],["dc.contributor.author","Jares-Erijman, Elizabeth A."],["dc.contributor.author","Jovin, Thomas M."],["dc.contributor.author","Klement, R."],["dc.contributor.author","Machinek, R."],["dc.contributor.author","Sheldrick, George M."],["dc.contributor.author","Uson, I."],["dc.date.accessioned","2018-11-07T11:08:51Z"],["dc.date.available","2018-11-07T11:08:51Z"],["dc.date.issued","2005"],["dc.description.abstract","The formation of the complex of 7-amino-actinomycin D with potentially single-stranded DNA has been studied by X-ray crystallography in the solid state, by NMR in solution and by molecular modelling. The crystal structures of the complex with 5'-TTAG[(BrU)-U-5]T-3' provide interesting examples of MAD phasing in which the dispersive component of the MAD signal was almost certainly enhanced by radiation damage. The trigonal and orthorhombic crystal modifications both contain antibiotic molecules and DNA strands in the form of a 2:4 complex: in the orthorhombic form there is one such complex in the asymmetric unit, while in the trigonal structure there are four. In both structures the phenoxazone ring of the first drug intercalates between a BrU-G (analogous to T-G) wobble pair and a G-T pair where the T is part of a symmetry-related molecule. The chromophore of the second actinomycin intercalates between the BrU-G and G-BrU wobble pairs of the partially paired third and fourth strands. The base stacking also involves (A T) T triplets and Watson-Crick A-T pairs and leads to similar complex three-dimensional networks in both structures, with looping-out of unpaired bases. Although the available NOE constraints of a solution containing the antibiotic and d(TTTAGTTT) strands in the ratio 1:1 are insufficient to determine the structure of the complex from the NMR data alone, they are consistent with the intercalation geometry observed in the crystal structure. Molecular-dynamics (MD) trajectories starting from the 1:2 complexes observed in the crystal showed that although the thymines flanking the d(AGT) core are rather flexible and the G-T pairing is not permanently preserved, both strands remain bound to the actinomycin by strong interactions between it and the guanines between which it is sandwiched. Similar strong binding (hemi-intercalation) of the actinomycin to a single guanine was observed in the MD trajectories of a 1:1 complex. The dominant interaction is between the antibiotic and guanine, but the complexes are stabilized further by promiscuous base-pairing."],["dc.description.sponsorship","ICREA"],["dc.identifier.doi","10.1107/S090744490500082X"],["dc.identifier.isi","000227867600007"],["dc.identifier.pmid","15805595"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/52882"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Blackwell Munksgaard"],["dc.relation.issn","0907-4449"],["dc.title","Crystal and solution structures of 7-amino-actinomycin D complexes with d(TTAGBrUT), d(TTAGTT) and d(TTTAGTTT)"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","591"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Molecules"],["dc.bibliographiccitation.lastpage","593"],["dc.bibliographiccitation.volume","5"],["dc.contributor.author","Giordano, L."],["dc.contributor.author","Macareno, J."],["dc.contributor.author","Song, L."],["dc.contributor.author","Jovin, T. M."],["dc.contributor.author","Irie, M."],["dc.contributor.author","Jares-Erijman, E. A."],["dc.date.accessioned","2019-07-09T11:53:56Z"],["dc.date.available","2019-07-09T11:53:56Z"],["dc.date.issued","2000"],["dc.description.abstract","We describe the preparation and photophysical characterization of two model compounds designed to test a new approach for the quantitative determination of Fluorescence Resonance Energy Transfer (FRET) in biological systems. The method enables modulation of FRET by exploiting the unique reversible spectral properties of photochromic diarylethenes and spiropyrans to create switchable energy acceptors."],["dc.identifier.doi","10.3390/50300591"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/60532"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Fluorescence Resonance Energy Transfer Using Spiropyran and Diarylethene Photochromic Acceptors"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","e1811"],["dc.bibliographiccitation.journal","Cell Death and Disease"],["dc.bibliographiccitation.volume","6"],["dc.contributor.author","Koch, J. C."],["dc.contributor.author","Bitow, F."],["dc.contributor.author","Haack, J."],["dc.contributor.author","D'Hedouville, Z."],["dc.contributor.author","Zhang, J-N"],["dc.contributor.author","Tönges, L."],["dc.contributor.author","Michel, U."],["dc.contributor.author","Oliveira, L. M. A."],["dc.contributor.author","Jovin, T. M."],["dc.contributor.author","Liman, Jan"],["dc.contributor.author","Tatenhorst, L."],["dc.contributor.author","Bähr, M."],["dc.contributor.author","Lingor, P."],["dc.date.accessioned","2017-09-07T11:43:42Z"],["dc.date.available","2017-09-07T11:43:42Z"],["dc.date.issued","2015"],["dc.description.abstract","Many neuropathological and experimental studies suggest that the degeneration of dopaminergic terminals and axons precedes the demise of dopaminergic neurons in the substantia nigra, which finally results in the clinical symptoms of Parkinson disease (PD). The mechanisms underlying this early axonal degeneration are, however, still poorly understood. Here, we examined the effects of overexpression of human wildtype alpha-synuclein (alpha Syn-WT), a protein associated with PD, and its mutant variants alpha Syn-A30P and -A53T on neurite morphology and functional parameters in rat primary midbrain neurons (PMN). Moreover, axonal degeneration after overexpression of alpha Syn-WT and -A30P was analyzed by live imaging in the rat optic nerve in vivo. We found that overexpression of alpha Syn-WT and of its mutants A30P and A53T impaired neurite outgrowth of PMN and affected neurite branching assessed by Sholl analysis in a variant-dependent manner. Surprisingly, the number of primary neurites per neuron was increased in neurons transfected with alpha Syn. Axonal vesicle transport was examined by live imaging of PMN co-transfected with EGFP-labeled synaptophysin. Overexpression of all alpha Syn variants significantly decreased the number of motile vesicles and decelerated vesicle transport compared with control. Macroautophagic flux in PMN was enhanced by alpha Syn-WT and -A53T but not by alpha Syn-A30P. Correspondingly, colocalization of alpha Syn and the autophagy marker LC3 was reduced for alpha Syn-A30P compared with the other alpha Syn variants. The number of mitochondria colocalizing with LC3 as a marker for mitophagy did not differ among the groups. In the rat optic nerve, both alpha Syn-WT and -A30P accelerated kinetics of acute axonal degeneration following crush lesion as analyzed by in vivo live imaging. We conclude that alpha Syn overexpression impairs neurite outgrowth and augments axonal degeneration, whereas axonal vesicle transport and autophagy are severely altered."],["dc.description.sponsorship","Open-Access Publikationsfonds 2015"],["dc.identifier.doi","10.1038/cddis.2015.169"],["dc.identifier.gro","3141868"],["dc.identifier.isi","000358788800011"],["dc.identifier.pmid","26158517"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/12015"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1967"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","2041-4889"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.subject","Central nervous system; Molecular neuroscience; Parkinson's disease"],["dc.title","Alpha-Synuclein affects neurite morphology, autophagy, vesicle transport and axonal degeneration in CNS neurons"],["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.firstpage","131"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","FEBS Letters"],["dc.bibliographiccitation.lastpage","135"],["dc.bibliographiccitation.volume","479"],["dc.contributor.author","Jakobs, Stefan"],["dc.contributor.author","Subramaniam, Vinod"],["dc.contributor.author","Schönle, Andreas"],["dc.contributor.author","Jovin, Thomas M."],["dc.contributor.author","Hell, Stefan W."],["dc.date.accessioned","2017-09-07T11:46:46Z"],["dc.date.available","2017-09-07T11:46:46Z"],["dc.date.issued","2000"],["dc.description.abstract","The green fluorescent protein (GFP) has become an invaluable marker for monitoring protein localization and gene expression in vivo. Recently a new red fluorescent protein (drFP583 or DsRed), isolated from tropical corals, has been described [Matz, M.V. et al, (1999) Nature Biotech, 17, 969-973]. With emission maxima at 509 and 583 nm respectively, EGFP and DsRed are suited for almost crossover free dual color labeling upon simultaneous excitation, We imaged mixed populations of Escherichia coli expressing either EGFP or DsRed by one-photon confocal and by two-photon microscopy, Both excitation modes proved to be suitable for imaging cells expressing either of the fluorescent proteins. DsRed had an extended maturation time and E, coli expressing this fluorescent protein were significantly smaller than those expressing EGFP, In aging bacterial cultures DsRed appeared to aggregate within the cells, accompanied by a strong reduction in its fluorescence lifetime as determined by fluorescence lifetime imaging microscopy, (C) 2000 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved."],["dc.identifier.doi","10.1016/S0014-5793(00)01896-2"],["dc.identifier.gro","3144363"],["dc.identifier.isi","000088963900011"],["dc.identifier.pmid","10981721"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1979"],["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","0014-5793"],["dc.title","EGFP and DsRed expressing cultures of Escherichia coli imaged by confocal, two-photon and fluorescence lifetime microscopy"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1399"],["dc.bibliographiccitation.journal","Brain"],["dc.bibliographiccitation.lastpage","1419"],["dc.bibliographiccitation.volume","140"],["dc.contributor.author","Miranda, Hugo Vicente"],["dc.contributor.author","Szego, Eva M."],["dc.contributor.author","Oliveira, Luis M. A."],["dc.contributor.author","Breda, Carlo"],["dc.contributor.author","Darendelioglu, Ekrem"],["dc.contributor.author","de Oliveira, Rita Machado"],["dc.contributor.author","Ferreira, Diana G."],["dc.contributor.author","Gomes, Marcos Antonio"],["dc.contributor.author","Rott, Ruth"],["dc.contributor.author","Oliveira, Marcia"],["dc.contributor.author","Munari, Francesca"],["dc.contributor.author","Enguita, Francisco Javier"],["dc.contributor.author","Simoes, Tania"],["dc.contributor.author","Rodrigues, Eva F."],["dc.contributor.author","Heinrich, Michael"],["dc.contributor.author","Martins, Ivo C."],["dc.contributor.author","Zamolo, Irina"],["dc.contributor.author","Riess, Olaf"],["dc.contributor.author","Cordeiro, Carlos"],["dc.contributor.author","Ponces-Freire, Ana"],["dc.contributor.author","Lashuel, Hilal Ahmed"],["dc.contributor.author","Santos, Nuno C."],["dc.contributor.author","Lopes, Luisa Vaqueiro"],["dc.contributor.author","Xiang, Wei"],["dc.contributor.author","Jovin, Thomas M."],["dc.contributor.author","Penque, Deborah"],["dc.contributor.author","Engelender, Simone"],["dc.contributor.author","Zweckstetter, Markus"],["dc.contributor.author","Klucken, Jochen"],["dc.contributor.author","Giorgini, Flaviano"],["dc.contributor.author","Quintas, Alexandre"],["dc.contributor.author","Outeiro, Tiago Fleming"],["dc.date.accessioned","2018-11-07T10:24:40Z"],["dc.date.available","2018-11-07T10:24:40Z"],["dc.date.issued","2017"],["dc.description.abstract","alpha-Synuclein misfolding and aggregation is a hallmark in Parkinson's disease and in several other neurodegenerative diseases known as synucleinopathies. The toxic properties of alpha-synuclein are conserved from yeast to man, but the precise underpinnings of the cellular pathologies associated are still elusive, complicating the development of effective therapeutic strategies. Combining molecular genetics with target-based approaches, we established that glycation, an unavoidable age-associated post-translational modification, enhanced alpha-synuclein toxicity in vitro and in vivo, in Drosophila and in mice. Glycation affected primarily the N-terminal region of alpha-synuclein, reducing membrane binding, impaired the clearance of alpha-synuclein, and promoted the accumulation of toxic oligomers that impaired neuronal synaptic transmission. Strikingly, using glycation inhibitors, we demonstrated that normal clearance of alpha-synuclein was re-established, aggregation was reduced, and motor phenotypes in Drosophila were alleviated. Altogether, our study demonstrates glycation constitutes a novel drug target that can be explored in synucleinopathies as well as in other neurodegenerative conditions."],["dc.identifier.doi","10.1093/brain/awx056"],["dc.identifier.isi","000400069900026"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/42703"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Oxford Univ Press"],["dc.relation.haserratum","/handle/2/103764"],["dc.relation.issn","1460-2156"],["dc.relation.issn","0006-8950"],["dc.title","Glycation potentiates alpha-synuclein-associated neurodegeneration in synucleinopathies"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","e1994"],["dc.bibliographiccitation.journal","Cell Death and Disease"],["dc.bibliographiccitation.volume","6"],["dc.contributor.author","Oliveira, Luis M. A."],["dc.contributor.author","Falomir-Lockhart, Lisandro J."],["dc.contributor.author","Botelho, Michelle Gralle"],["dc.contributor.author","Lin, K-H"],["dc.contributor.author","Wales, Pauline"],["dc.contributor.author","Koch, Jan Christoph"],["dc.contributor.author","Gerhardt, Ellen"],["dc.contributor.author","Taschenberger, Holger"],["dc.contributor.author","Outeiro, Tiago Fleming"],["dc.contributor.author","Lingor, Paul"],["dc.contributor.author","Schuele, B."],["dc.contributor.author","Arndt-Jovin, Donna J."],["dc.contributor.author","Jovin, Thomas M."],["dc.date.accessioned","2018-11-07T09:49:15Z"],["dc.date.available","2018-11-07T09:49:15Z"],["dc.date.issued","2015"],["dc.description.abstract","We have assessed the impact of alpha-synuclein overexpression on the differentiation potential and phenotypic signatures of two neural-committed induced pluripotent stem cell lines derived from a Parkinson's disease patient with a triplication of the human SNCA genomic locus. In parallel, comparative studies were performed on two control lines derived from healthy individuals and lines generated from the patient iPS-derived neuroprogenitor lines infected with a lentivirus incorporating a small hairpin RNA to knock down the SNCA mRNA. The SNCA triplication lines exhibited a reduced capacity to differentiate into dopaminergic or GABAergic neurons and decreased neurite outgrowth and lower neuronal activity compared with control cultures. This delayed maturation phenotype was confirmed by gene expression profiling, which revealed a significant reduction in mRNA for genes implicated in neuronal differentiation such as delta-like homolog 1 (DLK1), gamma-aminobutyric acid type B receptor subunit 2 (GABABR2), nuclear receptor related 1 protein (NURR1), G-protein-regulated inward-rectifier potassium channel 2 (GIRK-2) and tyrosine hydroxylase (TH). The differentiated patient cells also demonstrated increased autophagic flux when stressed with chloroquine. We conclude that a two-fold overexpression of alpha-synuclein caused by a triplication of the SNCA gene is sufficient to impair the differentiation of neuronal progenitor cells, a finding with implications for adult neurogenesis and Parkinson's disease progression, particularly in the context of bioenergetic dysfunction."],["dc.identifier.doi","10.1038/cddis.2015.318"],["dc.identifier.isi","000367155300027"],["dc.identifier.pmid","26610207"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/12755"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/35470"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Nature Publishing Group"],["dc.relation.issn","2041-4889"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Elevated alpha-synuclein caused by SNCA gene triplication impairs neuronal differentiation and maturation in Parkinson's patient-derived induced pluripotent stem cells"],["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","1430"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Proceedings of the National Academy of Sciences"],["dc.bibliographiccitation.lastpage","1435"],["dc.bibliographiccitation.volume","102"],["dc.contributor.author","Bertoncini, Carlos W."],["dc.contributor.author","Jung, Y. S."],["dc.contributor.author","Fernandez, Claudio O."],["dc.contributor.author","Hoyer, W."],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.author","Jovin, Thomas M."],["dc.contributor.author","Zweckstetter, Markus"],["dc.date.accessioned","2017-09-07T11:43:01Z"],["dc.date.available","2017-09-07T11:43:01Z"],["dc.date.issued","2005"],["dc.description.abstract","In idiopathic Parkinson's disease, intracytoplasmic neuronal inclusions (Lewy bodies) containing aggregates of the protein a-synuclein (alphaS) are deposited in the pigmented nuclei of the brainstem. The mechanisms underlying the structural transition of innocuous, presumably natively unfolded, aS to neurotoxic forms are largely unknown. Using paramagnetic relaxation enhancement and NMR dipolar couplings, we show that monomeric aS assumes conformations that are stabilized by long-range interactions and act to inhibit oligomerization and aggregation. The autoinhibitory conformations fluctuate in the range of nanoseconds to microseconds corresponding to the time scale of secondary structure formation during folding. Polyamine binding and/or temperature increase, conditions that induce aggregation in vitro, release this inherent tertiary structure, leading to a completely unfolded conformation that associates readily. Stabilization of the native, autoinhibitory structure of alphaS constitutes a potential strategy for reducing or inhibiting oligomerization and aggregation in Parkinson's disease."],["dc.identifier.doi","10.1073/pnas.0407146102"],["dc.identifier.gro","3143902"],["dc.identifier.isi","000226877300034"],["dc.identifier.pmid","15671169"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1467"],["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","Release of long-range tertiary interactions potentiates aggregation of natively unstructured alpha-synuclein"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","794"],["dc.bibliographiccitation.issue","9"],["dc.bibliographiccitation.journal","Cytometry Part A"],["dc.bibliographiccitation.lastpage","805"],["dc.bibliographiccitation.volume","83"],["dc.contributor.author","Ziomkiewicz, Iwona"],["dc.contributor.author","Loman, Anastasia"],["dc.contributor.author","Klement, Reinhard"],["dc.contributor.author","Fritsch, Cornelia"],["dc.contributor.author","Klymchenko, Andrey S."],["dc.contributor.author","Bunt, Gertrude"],["dc.contributor.author","Jovin, Thomas M."],["dc.contributor.author","Arndt-Jovin, Donna J."],["dc.date.accessioned","2018-11-07T09:20:45Z"],["dc.date.available","2018-11-07T09:20:45Z"],["dc.date.issued","2013"],["dc.description.abstract","We have revealed a reorientation of ectodomain I of the epidermal growth factor receptor (EGFR; ErbB1; Her1) in living CHO cells expressing the receptor, upon binding of the native ligand EGF. The state of the unliganded, nonactivated EGFR was compared to that exhibited after ligand addition in the presence of a kinase inhibitor that prevents endocytosis but does not interfere with binding or the ensuing conformational rearrangements. To perform these experiments, we constructed a transgene EGFR with an acyl carrier protein sequence between the signal peptide and the EGFR mature protein sequence. This protein, which behaves similarly to wild-type EGFR with respect to EGF binding, activation, and internalization, can be labeled at a specific serine in the acyl carrier tag with a fluorophore incorporated into a 4-phosphopantetheine (P-pant) conjugate transferred enzymatically from the corresponding CoA derivative. By measuring Forster resonance energy transfer between a molecule of Atto390 covalently attached to EGFR in this manner and a novel lipid probe NR12S distributed exclusively in the outer leaflet of the plasma membrane, we determined the apparent relative separation of ectodomain I from the membrane under nonactivating and activating conditions. The data indicate that the unliganded domain I of the EGFR receptor is situated much closer to the membrane before EGF addition, supporting the model of a self-inhibited configuration of the inactive receptor in quiescent cells. (c) 2013 International Society for Advancement of Cytometry"],["dc.identifier.doi","10.1002/cyto.a.22311"],["dc.identifier.isi","000323480200005"],["dc.identifier.pmid","23839800"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/28950"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.relation.issn","1552-4922"],["dc.title","Dynamic conformational transitions of the EGF receptor in living mammalian cells determined by FRET and fluorescence lifetime imaging microscopy"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]