Russo, Luigi

[["dc.bibliographiccitation.firstpage","138"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Medizinische Klinik - Intensivmedizin und Notfallmedizin"],["dc.bibliographiccitation.lastpage","145"],["dc.bibliographiccitation.volume","116"],["dc.contributor.author","La Rosée, P."],["dc.contributor.author","Bremer, H.-C."],["dc.contributor.author","La Rosée, F."],["dc.contributor.author","Mohm, P."],["dc.contributor.author","Hochhaus, A."],["dc.contributor.author","Gehrke, I."],["dc.contributor.author","Kumle, B."],["dc.contributor.author","Benzing, A."],["dc.contributor.author","Russo, S."],["dc.date.accessioned","2021-04-14T08:32:16Z"],["dc.date.available","2021-04-14T08:32:16Z"],["dc.date.issued","2020"],["dc.identifier.doi","10.1007/s00063-020-00750-8"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/83865"],["dc.language.iso","de"],["dc.notes.intern","DOI Import GROB-399"],["dc.relation.eissn","2193-6226"],["dc.relation.haserratum","/handle/2/83401"],["dc.relation.issn","2193-6218"],["dc.title","Interdisziplinäres COVID-Board bei SARS-CoV-2-getriggerter hyperferritinämischer Inflammation"],["dc.title.translated","Interdisciplinary COVID board for patients with SARS-CoV-2-triggered hyperferritinemic Inflammation"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","17111"],["dc.bibliographiccitation.issue","45"],["dc.bibliographiccitation.journal","Journal of the American Chemical Society"],["dc.bibliographiccitation.lastpage","17120"],["dc.bibliographiccitation.volume","135"],["dc.contributor.author","Russo, Luigi"],["dc.contributor.author","Maestre-Martinez, Mitcheell"],["dc.contributor.author","Wolff, Sebastian"],["dc.contributor.author","Becker, Stefan"],["dc.contributor.author","Griesinger, Christian"],["dc.date.accessioned","2017-09-07T11:47:02Z"],["dc.date.available","2017-09-07T11:47:02Z"],["dc.date.issued","2013"],["dc.description.abstract","An ensemble-based approach is presented to explore the conformational space sampled by a multidomain protein showing moderate interdomain dynamics in terms of translational and rotational motions. The strategy was applied on a complex of calmodulin (CalvI) with the IQ:recognition motif from the voltage-gated calcium channel Ca(v)1.2 (IQ), which adopts three different interdomain orientations in the crystal. The N60D mutant of calmodulin was used to collect pseudocontact shifts and paramagnetically induced residual dipolar couplings for six different lanthanide ions. Then, starting from the crystal structure, pools of conformations were generated by free MD. We found the three crystal conformations in solution, but four additional MD-derived conformations had to be included into the ensemble to fulfill all the paramagnetic data and cross-validate optimally against unused paramagnetic data. Alternative approaches led to similar ensembles. Our \"ensemble\" approach is a simple and efficient tool to probe and describe the interdomain dynamics and represents a general method that can be used to provide a proper ensemble description of multidomain proteins."],["dc.identifier.doi","10.1021/ja408143f"],["dc.identifier.gro","3142250"],["dc.identifier.isi","000327103600053"],["dc.identifier.pmid","24111622"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/6198"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: Max Planck Society; BioNMR [EU 261863]"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Amer Chemical Soc"],["dc.relation.issn","0002-7863"],["dc.title","Interdornain Dynamics Explored by Paramagnetic NMR"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","145"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Medizinische Klinik - Intensivmedizin und Notfallmedizin"],["dc.bibliographiccitation.lastpage","145"],["dc.bibliographiccitation.volume","116"],["dc.contributor.author","La Rosée, P."],["dc.contributor.author","Bremer, H.-C."],["dc.contributor.author","La Rosée, F."],["dc.contributor.author","Mohm, P."],["dc.contributor.author","Hochhaus, A."],["dc.contributor.author","Gehrke, I."],["dc.contributor.author","Kumle, B."],["dc.contributor.author","Benzing, A."],["dc.contributor.author","Russo, S."],["dc.date.accessioned","2021-04-14T08:30:53Z"],["dc.date.available","2021-04-14T08:30:53Z"],["dc.date.issued","2020"],["dc.identifier.doi","10.1007/s00063-020-00763-3"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/83401"],["dc.language.iso","de"],["dc.notes.intern","DOI Import GROB-399"],["dc.relation.eissn","2193-6226"],["dc.relation.iserratumof","/handle/2/83865"],["dc.relation.issn","2193-6218"],["dc.title","Erratum zu: Interdisziplinäres COVID-Board bei SARS-CoV-2-getriggerter Hyperferritinämischer Inflammation"],["dc.title.translated","Erratum to: Interdisciplinary COVID board for patients with triggered hyperferritinemic Inflammation"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","erratum_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","16845"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Scientific Reports"],["dc.bibliographiccitation.volume","7"],["dc.contributor.author","Russo, Luigi"],["dc.contributor.author","Giller, Karin"],["dc.contributor.author","Pfitzner, Edith"],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.author","Becker, Stefan"],["dc.date.accessioned","2018-01-17T11:27:59Z"],["dc.date.available","2018-01-17T11:27:59Z"],["dc.date.issued","2017"],["dc.description.abstract","Crucial for immune and anti-inflammatory cellular responses, signal transducer and activator of transcription 6 (STAT6) regulates transcriptional activation in response to interleukin-4 and -13 -induced tyrosine phosphorylation by direct interaction with coactivators. The interaction of STAT6 with nuclear coactivator 1 (NCoA1) is mediated by a short region of the STAT6 transactivation domain that includes the motif LXXLL and interacts with the PAS-B domain of NCoA1. Despite the availability of an X-ray structure of the PAS-B domain/ Leu794-Gly814-STAT6 complex, the mechanistic details of this interaction are still poorly understood. Here, we determine the structure of the NCoA1257-385/STAT6783-814 complex using Nuclear Magnetic Resonance (NMR) and X-ray crystallography. The STAT6783-814 peptide binds with additional N-terminal amino acids to NCoA1257-385, compared to the STAT6794-814 peptide, explaining its higher affinity. Secondary and tertiary structures existing in the free peptide are more highly populated in the complex, suggesting binding by conformational selection."],["dc.identifier.doi","10.1038/s41598-017-17088-5"],["dc.identifier.pmid","29203888"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/11676"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.relation.eissn","2045-2322"],["dc.title","Insight into the molecular recognition mechanism of the coactivator NCoA1 by STAT6"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2401"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","Biophysical Journal"],["dc.bibliographiccitation.lastpage","2410"],["dc.bibliographiccitation.volume","102"],["dc.contributor.author","Geiger, Anselm"],["dc.contributor.author","Russo, Luigi"],["dc.contributor.author","Gensch, Thomas"],["dc.contributor.author","Thestrup, Thomas"],["dc.contributor.author","Becker, Stefan"],["dc.contributor.author","Hopfner, Karl-Peter"],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.author","Witte, Gregor"],["dc.contributor.author","Griesbeck, Oliver"],["dc.date.accessioned","2017-09-07T11:48:52Z"],["dc.date.available","2017-09-07T11:48:52Z"],["dc.date.issued","2012"],["dc.description.abstract","Genetically encoded calcium indicators have become instrumental in imaging signaling in complex tissues and neuronal circuits in vivo. Despite their importance, structure-function relationships of these sensors often remain largely uncharacterized due to their artificial and multimodular composition. Here, we describe a combination of protein engineering and kinetic, spectroscopic, and biophysical analysis of the Forster resonance energy transfer (FRET)-based calcium biosensor TN-XXL. Using fluorescence spectroscopy of engineered tyrosines, we show that two of the four calcium binding EF-hands dominate the FRET output of TN-XXL and that local conformational changes of these hands match the kinetics of FRET change. Using small-angle x-ray scattering and NMR spectroscopy, we show that TN-XXL changes from a flexible elongated to a rigid globular shape upon binding calcium, thus resulting in FRET signal output. Furthermore, we compare calcium titrations using fluorescence lifetime spectroscopy with the ratiometric approach and investigate potential non-FRET effects that may affect the fluorophores. Thus, our data characterize the biophysics of TN-XXL in detail and may form a basis for further rational engineering of FRET-based biosensors."],["dc.identifier.doi","10.1016/j.bpj.2012.03.065"],["dc.identifier.gro","3142534"],["dc.identifier.isi","000304091100020"],["dc.identifier.pmid","22677394"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/8896"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Cell Press"],["dc.relation.eissn","1542-0086"],["dc.relation.issn","0006-3495"],["dc.title","Correlating Calcium Binding, Forster Resonance Energy Transfer, and Conformational Change in the Biosensor TN-XXL"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","175"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Nature Methods"],["dc.bibliographiccitation.lastpage","+"],["dc.bibliographiccitation.volume","11"],["dc.contributor.author","Thestrup, Thomas"],["dc.contributor.author","Litzlbauer, Julia"],["dc.contributor.author","Bartholomaeus, Ingo"],["dc.contributor.author","Mues, Marsilius"],["dc.contributor.author","Russo, Luigi"],["dc.contributor.author","Dana, Hod"],["dc.contributor.author","Kovalchuk, Yuri"],["dc.contributor.author","Liang, Yajie"],["dc.contributor.author","Kalamakis, Georgios"],["dc.contributor.author","Laukat, Yvonne"],["dc.contributor.author","Becker, Stefan"],["dc.contributor.author","Witte, Gregor"],["dc.contributor.author","Geiger, Anselm"],["dc.contributor.author","Allen, Taylor"],["dc.contributor.author","Rome, Lawrence C."],["dc.contributor.author","Chen, Tsai-Wen"],["dc.contributor.author","Kim, Douglas S."],["dc.contributor.author","Garaschuk, Olga"],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.author","Griesbeck, Oliver"],["dc.date.accessioned","2017-09-07T11:46:33Z"],["dc.date.available","2017-09-07T11:46:33Z"],["dc.date.issued","2014"],["dc.description.abstract","The quality of genetically encoded calcium indicators (GECIs) has improved dramatically in recent years, but high-performing ratiometric indicators are still rare. Here we describe a series of fluorescence resonance energy transfer (FRET)-based calcium biosensors with a reduced number of calcium binding sites per sensor. These 'Twitch' sensors are based on the C-terminal domain of Opsanus troponin C. Their FRET responses were optimized by a large-scale functional screen in bacterial colonies, refined by a secondary screen in rat hippocampal neuron cultures. We tested the in vivo performance of the most sensitive variants in the brain and lymph nodes of mice. The sensitivity of the Twitch sensors matched that of synthetic calcium dyes and allowed visualization of tonic action potential firing in neurons and high resolution functional tracking of T lymphocytes. Given their ratiometric readout, their brightness, large dynamic range and linear response properties, Twitch sensors represent versatile tools for neuroscience and immunology."],["dc.identifier.doi","10.1038/NMETH.2773"],["dc.identifier.gro","3142191"],["dc.identifier.isi","000331141600020"],["dc.identifier.pmid","24390440"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/5543"],["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.eissn","1548-7105"],["dc.relation.issn","1548-7091"],["dc.title","Optimized ratiometric calcium sensors for functional in vivo imaging of neurons and T lymphocytes"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]