Jovin, Thomas M.

[["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","656"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Journal of Cell Science"],["dc.bibliographiccitation.lastpage","666"],["dc.bibliographiccitation.volume","122"],["dc.contributor.author","Papusheva, Ekaterina"],["dc.contributor.author","de Queiroz, Fernanda Mello"],["dc.contributor.author","Dalous, Jeremie"],["dc.contributor.author","Han, Yunyun"],["dc.contributor.author","Esposito, Alessandro"],["dc.contributor.author","Jares-Erijman, Elizabeth A."],["dc.contributor.author","Jovin, Thomas M."],["dc.contributor.author","Bunt, Gertrude"],["dc.date.accessioned","2018-11-07T08:32:14Z"],["dc.date.available","2018-11-07T08:32:14Z"],["dc.date.issued","2009"],["dc.description.abstract","Focal adhesion kinase (FAK) controls cellular adhesion and motility processes by its tight link to integrin- and extracellular-matrix-mediated signaling. To explore the dynamics of the regulation of FAK, we constructed a FRET-based probe that visualizes conformational rearrangements of the FERM domain of FAK in living cells. The sensor reports on an integrin-mediated conformational change in FAK following cellular adhesion. The perturbation is kinase-independent and involves the polybasic KAKTLR sequence in the FERM domain. It is manifested by an increased FRET signal and is expressed primarily in focal adhesions, and to a lesser extent in the cytoplasm. The conformational change in the FERM domain of FAK is observed in two consecutive phases during spreading - early and late - and is enriched in fully adhered motile cells at growing and sliding peripheral focal-adhesion sites, but not in stable or retracting focal adhesions. Inhibition of the actomyosin system indicates the involvement of tension signaling induced by Rho-associated kinase, rather than by myosin light-chain kinase, in the modulation of the FERM response. We conclude that the heterogeneous conformation of the FERM domain in focal adhesions of migrating cells reflects a complex regulatory mechanism for FAK that appears to be under the influence of cellular traction forces."],["dc.identifier.doi","10.1242/jcs.028738"],["dc.identifier.isi","000263516400009"],["dc.identifier.pmid","19208768"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/17290"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Company Of Biologists Ltd"],["dc.relation.issn","0021-9533"],["dc.title","Dynamic conformational changes in the FERM domain of FAK are involved in focal-adhesion behavior during cell spreading and motility"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","e7541"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","PLoS One"],["dc.bibliographiccitation.volume","4"],["dc.contributor.author","Galli, Soledad"],["dc.contributor.author","Jahn, Olaf"],["dc.contributor.author","Hitt, Reiner"],["dc.contributor.author","Hesse, Doerte"],["dc.contributor.author","Opitz, Lennart"],["dc.contributor.author","Plessmann, Uwe"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Poderoso, Juan Jose"],["dc.contributor.author","Jares-Erijman, Elizabeth A."],["dc.contributor.author","Jovin, Thomas M."],["dc.date.accessioned","2019-07-09T11:52:42Z"],["dc.date.available","2019-07-09T11:52:42Z"],["dc.date.issued","2009"],["dc.description.abstract","Extracellular signal-regulated protein kinase 1 and 2 (ERK1/2) are members of the MAPK family and participate in the transduction of stimuli in cellular responses. Their long-term actions are accomplished by promoting the expression of specific genes whereas faster responses are achieved by direct phosphorylation of downstream effectors located throughout the cell. In this study we determined that hERK1 translocates to the mitochondria of HeLa cells upon a proliferative stimulus. In the mitochondrial environment, hERK1 physically associates with (i) at least 5 mitochondrial proteins with functions related to transport (i.e. VDAC1), signalling, and metabolism; (ii) histones H2A and H4; and (iii) other cytosolic proteins. This work indicates for the first time the presence of diverse ERK-complexes in mitochondria and thus provides a new perspective for assessing the functions of ERK1 in the regulation of cellular signalling and trafficking in HeLa cells."],["dc.format.extent","18"],["dc.identifier.doi","10.1371/journal.pone.0007541"],["dc.identifier.fs","569017"],["dc.identifier.pmid","19847302"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/5824"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/60253"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.publisher","Public Library of Science"],["dc.relation.issn","1932-6203"],["dc.rights","CC BY 2.5"],["dc.rights.uri","https://creativecommons.org/licenses/by/2.5"],["dc.subject.ddc","610"],["dc.subject.mesh","Amino Acid Sequence"],["dc.subject.mesh","Cell Proliferation"],["dc.subject.mesh","Gene Expression Profiling"],["dc.subject.mesh","Gene Expression Regulation, Enzymologic"],["dc.subject.mesh","Gene Expression Regulation, Neoplastic"],["dc.subject.mesh","Glutathione Transferase"],["dc.subject.mesh","Hela Cells"],["dc.subject.mesh","Humans"],["dc.subject.mesh","MAP Kinase Signaling System"],["dc.subject.mesh","Mitochondria"],["dc.subject.mesh","Mitogen-Activated Protein Kinase 3"],["dc.subject.mesh","Molecular Sequence Data"],["dc.subject.mesh","Proteomics"],["dc.subject.mesh","Sequence Homology, Amino Acid"],["dc.subject.mesh","Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization"],["dc.title","A new paradigm for MAPK: structural interactions of hERK1 with mitochondria in HeLa cells."],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1004"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Free Radical Biology and Medicine"],["dc.bibliographiccitation.lastpage","1015"],["dc.bibliographiccitation.volume","53"],["dc.contributor.author","Borsarelli, Claudio D."],["dc.contributor.author","Falomir-Lockhart, Lisandro J."],["dc.contributor.author","Ostatna, Veronika"],["dc.contributor.author","Fauerbach, Jonathan A."],["dc.contributor.author","Hsiao, He-Hsuan"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Palecek, Emil"],["dc.contributor.author","Jares-Erijman, Elizabeth A."],["dc.contributor.author","Jovin, Thomas M."],["dc.date.accessioned","2018-11-07T09:07:10Z"],["dc.date.available","2018-11-07T09:07:10Z"],["dc.date.issued","2012"],["dc.description.abstract","Alpha-synuclein (alpha S), a 140 amino acid presynaptic protein, is the major component of the fibrillar aggregates (Lewy bodies) observed in dopaminergic neurons of patients affected by Parkinson's disease. It is currently believed that noncovalent oligomeric forms of alpha S, arising as intermediates in its aggregation, may constitute the major neurotoxic species. However, attempts to isolate and characterize such oligomers in vitro, and even more so in living cells, have been hampered by their transient nature, low concentration, polymorphism, and inherent instability. In this work, we describe the preparation and characterization of low molecular weight covalently bound oligomeric species of alpha S obtained by crosslinking via tyrosyl radicals generated by blue-light photosensitization of the metal coordination complex ruthenium (II) tris-bipyridine in the presence of ammonium persulfate. Numerous analytical techniques were used to characterize the alpha S oligomers: biochemical (anion-exchange chromatography, SOS-PAGE, and Western blotting); spectroscopic (optical: UV/Vis absorption, steady state, dynamic fluorescence, and dynamic light scattering); mass spectrometry; and electrochemical. Light-controlled protein oligomerization was mediated by formation of Tyr-Tyr (dityrosine) dimers through -C-C- bonds acting as covalent bridges, with a predominant involvement of residue Y39. The diverse oligomeric species exhibited a direct effect on the in vitro aggregation behavior of wild-type monomeric alpha S, decreasing the total yield of amyloid fibrils in aggregation assays monitored by thioflavin T (ThioT) fluorescence and light scattering, and by atomic forte microscopy (AFM). Compared to the unmodified monomer, the photoinduced covalent oligomeric species demonstrated increased toxic effects on differentiated neuronal-like SH-SY5Y cells. The result's highlight the importance of protein modification induced by oxidative stress in the initial molecular events leading to Parkinson's disease. (C) 2012 Elsevier Inc. All rights reserved."],["dc.identifier.doi","10.1016/j.freeradbiomed.2012.06.035"],["dc.identifier.isi","000307920100035"],["dc.identifier.pmid","22771470"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/25731"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Elsevier Science Inc"],["dc.relation.issn","0891-5849"],["dc.title","Biophysical properties and cellular toxicity of covalent crosslinked oligomers of alpha-synuclein formed by photoinduced side-chain tyrosyl radicals"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]