Risselada, Herre Jelger

[["dc.bibliographiccitation.firstpage","552"],["dc.bibliographiccitation.issue","7374"],["dc.bibliographiccitation.journal","Nature"],["dc.bibliographiccitation.lastpage","555"],["dc.bibliographiccitation.volume","479"],["dc.contributor.author","van den Bogaart, Geert"],["dc.contributor.author","Meyenberg, Karsten"],["dc.contributor.author","Risselada, H. Jelger"],["dc.contributor.author","Amin, Hayder"],["dc.contributor.author","Willig, Katrin I."],["dc.contributor.author","Hubrich, Barbara E."],["dc.contributor.author","Dier, Markus"],["dc.contributor.author","Hell, Stefan"],["dc.contributor.author","Grubmüller, Helmut"],["dc.contributor.author","Diederichsen, Ulf"],["dc.contributor.author","Jahn, Reinhard"],["dc.date.accessioned","2017-09-07T11:43:16Z"],["dc.date.available","2017-09-07T11:43:16Z"],["dc.date.issued","2011"],["dc.description.abstract","Neuronal exocytosis is catalysed by the SNAP receptor protein syntaxin-1A(1), which is clustered in the plasma membrane at sites where synaptic vesicles undergo exocytosis(2,3). However, how syntaxin-1A is sequestered is unknown. Here we show that syntaxin clustering is mediated by electrostatic interactions with the strongly anionic lipid phosphatidylinositol-4,5-bisphosphate (PIP2). Using super-resolution stimulated-emission depletion microscopy on the plasma membranes of PC12 cells, we found that PIP2 is the dominant inner-leaflet lipid in microdomains about 73 nanometres in size. This high accumulation of PIP2 was required for syntaxin-1A sequestering, as destruction of PIP2 by the phosphatase synaptojanin-1 reduced syntaxin-1A clustering. Furthermore, coreconstitution of PIP2 and the carboxy-terminal part of syntaxin-1A in artificial giant unilamellar vesicles resulted in segregation of PIP2 and syntaxin-1A into distinct domains even when cholesterol was absent. Our results demonstrate that electrostatic protein-lipid interactions can result in the formation of microdomains independently of cholesterol or lipid phases."],["dc.identifier.doi","10.1038/nature10545"],["dc.identifier.gro","3142626"],["dc.identifier.isi","000297285600056"],["dc.identifier.pmid","22020284"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/51"],["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","0028-0836"],["dc.title","Membrane protein sequestering by ionic protein-lipid interactions"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","805"],["dc.bibliographiccitation.issue","7"],["dc.bibliographiccitation.journal","Nature Structural & Molecular Biology"],["dc.bibliographiccitation.lastpage","U82"],["dc.bibliographiccitation.volume","18"],["dc.contributor.author","van den Bogaart, Geert"],["dc.contributor.author","Thutupalli, Shashi"],["dc.contributor.author","Risselada, J. H."],["dc.contributor.author","Meyenberg, Karsten"],["dc.contributor.author","Holt, Matthew"],["dc.contributor.author","Riedel, Dietmar"],["dc.contributor.author","Diederichsen, Ulf"],["dc.contributor.author","Herminghaus, Stephan"],["dc.contributor.author","Grubmüller, Helmut"],["dc.contributor.author","Jahn, Reinhard"],["dc.date.accessioned","2017-09-07T11:44:10Z"],["dc.date.available","2017-09-07T11:44:10Z"],["dc.date.issued","2011"],["dc.description.abstract","Synaptotagmin-1 triggers Ca2+-sensitive, rapid neurotransmitter release by promoting interactions between SNARE proteins on synaptic vesicles and the plasma membrane. How synaptotagmin-1 promotes this interaction is unclear, and the massive increase in membrane fusion efficiency of Ca2+-bound synaptotagmin-1 has not been reproduced in vitro. However, previous experiments have been performed at relatively high salt concentrations, screening potentially important electrostatic interactions. Using functional reconstitution in liposomes, we show here that at low ionic strength SNARE-mediated membrane fusion becomes strictly dependent on both Ca2+ and synaptotagmin-1. Under these conditions, synaptotagmin-1 functions as a distance regulator that tethers the liposomes too far from the plasma membrane for SNARE nucleation in the absence of Ca2+, but while bringing the liposomes close enough for membrane fusion in the presence of Ca2+. These results may explain how the relatively weak electrostatic interactions between synaptotagmin-1 and membranes substantially accelerate fusion."],["dc.identifier.doi","10.1038/nsmb.2061"],["dc.identifier.gro","3142704"],["dc.identifier.isi","000292507500009"],["dc.identifier.pmid","21642968"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/138"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","1545-9993"],["dc.title","Synaptotagmin-1 may be a distance regulator acting upstream of SNARE nucleation"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1049"],["dc.bibliographiccitation.issue","7"],["dc.bibliographiccitation.journal","Chembiochem : a European journal of chemical biology"],["dc.bibliographiccitation.lastpage","1055"],["dc.bibliographiccitation.volume","12"],["dc.contributor.author","Risselada, Herre Jelger"],["dc.contributor.author","Kutzner, Carsten"],["dc.contributor.author","Grubmüller, Helmut"],["dc.date.accessioned","2018-02-13T10:05:22Z"],["dc.date.available","2018-02-13T10:05:22Z"],["dc.date.issued","2011-05-02"],["dc.description.abstract","Neurotransmitter release at the synapse requires fusion of synaptic vesicles with the presynaptic plasma membrane. SNAREs are the core constituents of the protein machinery responsible for this membrane fusion, but the actual fusion mechanism remains unclear. Here, we have simulated neuronal SNARE-mediated membrane fusion in molecular detail. In our simulations, membrane fusion progresses through an inverted micelle fusion intermediate before reaching the hemifused state. We show that at least one single SNARE complex is required for fusion, as has also been confirmed in a recent in vitro single-molecule fluoresence study. Further, the transmembrane regions of the SNAREs were found to play a vital role in the initiation of fusion by causing distortions of the lipid packing of the outer membrane leaflets, and the C termini of the transmembrane regions are associated with the formation of the fusion pores. The inherent mechanical stress in the linker region of the SNARE complex was found to drive both the subsequent formation and expansion of fusion pores. Our simulations also revealed that the presence of homodimerizations between the transmembrane regions leads to the formation of unstable fusion intermediates that are under high curvature stress. We show that multiple SNARE complexes mediate membrane fusion in a cooperative and synchronized process. Finally, we show that after fusion, the zipping of the SNAREs extends into the membrane region, in agreement with the recently resolved X-ray structure of the fully assembled state."],["dc.identifier.doi","10.1002/cbic.201100020"],["dc.identifier.pmid","21433241"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/12206"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.relation.eissn","1439-7633"],["dc.title","Caught in the act: visualization of SNARE-mediated fusion events in molecular detail"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","664a"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Biophysical Journal"],["dc.bibliographiccitation.volume","104"],["dc.contributor.author","Risselada, Herre Jelger"],["dc.contributor.author","Müller, Marcus"],["dc.contributor.author","Grubmüller, Karl Helmut"],["dc.date.accessioned","2018-11-07T09:29:00Z"],["dc.date.available","2018-11-07T09:29:00Z"],["dc.date.issued","2013"],["dc.identifier.doi","10.1016/j.bpj.2012.11.3664"],["dc.identifier.isi","000316074306354"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/30918"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-393"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Cell Press"],["dc.publisher.place","Cambridge"],["dc.relation.eventlocation","Philadelphia, PA"],["dc.relation.issn","0006-3495"],["dc.title","Fusion Proteins - Different Tools for Different Jobs?"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","743"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Molecular Microbiology"],["dc.bibliographiccitation.lastpage","759"],["dc.bibliographiccitation.volume","98"],["dc.contributor.author","Osadnik, Hendrik"],["dc.contributor.author","Schoepfel, Michael"],["dc.contributor.author","Heidrich, Eyleen"],["dc.contributor.author","Mehner, Denise"],["dc.contributor.author","Lilie, Hauke"],["dc.contributor.author","Parthier, Christoph"],["dc.contributor.author","Risselada, H. Jelger"],["dc.contributor.author","Grubmüller, Helmut"],["dc.contributor.author","Stubbs, Milton T."],["dc.contributor.author","Brueser, Thomas"],["dc.date.accessioned","2017-09-07T11:43:27Z"],["dc.date.available","2017-09-07T11:43:27Z"],["dc.date.issued","2015"],["dc.description.abstract","Phage shock protein A (PspA) belongs to the highy conserved PspA/IM30 family and is a key component of the stress inducible Psp system in Escherichia coli. One of its central roles is the regulatory interaction with the transcriptional activator of this system, the sigma(54) enhancer-binding protein PspF, a member of the AAA+ protein family. The PspA/F regulatory system has been intensively studied and serves as a paradigm for AAA+ enzyme regulation by trans-acting factors. However, the molecular mechanism of how exactly PspA controls the activity of PspF and hence sigma(54)-dependent expression of the psp genes is still unclear. To approach this question, we identified the minimal PspF-interacting domain of PspA, solved its structure, determined its affinity to PspF and the dissociation kinetics, identified residues that are potentially important for PspF regulation and analyzed effects of their mutation on PspFin vivo and in vitro. Our data indicate that several characteristics of AAA+ regulation in the PspAF complex resemble those of the AAA+ unfoldase ClpB, with both proteins being regulated by a structurally highly conserved coiled-coil domain. The convergent evolution of both regulatory domains points to a general mechanism to control AAA+ activity for divergent physiologic tasks via coiled-coil domains."],["dc.identifier.doi","10.1111/mmi.13154"],["dc.identifier.gro","3141798"],["dc.identifier.isi","000364534200011"],["dc.identifier.pmid","26235546"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1190"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: German Research Foundation (DFG) [BR2285/4-1]"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1365-2958"],["dc.relation.issn","0950-382X"],["dc.title","PspF‐binding domain PspA1–144 and the PspA·F complex: New insights into the coiled–coil‐dependent regulation of AAA+ proteins"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","679"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","Nature Structural & Molecular Biology"],["dc.bibliographiccitation.lastpage","686"],["dc.bibliographiccitation.volume","20"],["dc.contributor.author","Honigmann, Alf"],["dc.contributor.author","van den Bogaart, Geert"],["dc.contributor.author","Iraheta, Emilio"],["dc.contributor.author","Risselada, H. Jelger"],["dc.contributor.author","Milovanovic, Dragomir"],["dc.contributor.author","Mueller, Veronika"],["dc.contributor.author","Müllar, Stefan"],["dc.contributor.author","Diederichsen, Ulf"],["dc.contributor.author","Fasshauer, Dirk"],["dc.contributor.author","Grubmüller, Helmut"],["dc.contributor.author","Hell, Stefan"],["dc.contributor.author","Eggeling, Christian"],["dc.contributor.author","Kühnel, Karin"],["dc.contributor.author","Jahn, Reinhard"],["dc.date.accessioned","2017-09-07T11:47:41Z"],["dc.date.available","2017-09-07T11:47:41Z"],["dc.date.issued","2013"],["dc.description.abstract","Synaptic-vesicle exocytosis is mediated by the vesicular Ca2+ sensor synaptotagmin-1. Synaptotagmin-1 interacts with the SNARE protein syntaxin-1A and acidic phospholipids such as phosphatidylinositol 4,5-bisphosphate (PIP2). However, it is unclear how these interactions contribute to triggering membrane fusion. Using PC12 cells from Rattus norvegicus and artificial supported bilayers, we show that synaptotagmin-1 interacts with the polybasic linker region of syntaxin-1A independent of Ca2+ through PIP2. This interaction allows both Ca2+-binding sites of synaptotagmin-1 to bind to phosphatidylserine in the vesicle membrane upon Ca2+ triggering. We determined the crystal structure of the C2B domain of synaptotagmin-1 bound to phosphoserine, allowing development of a high-resolution model of synaptotagmin bridging two different membranes. Our results suggest that PIP2 clusters organized by syntaxin-1 act as molecular beacons for vesicle docking, with the subsequent Ca2+ influx bringing the vesicle membrane close enough for membrane fusion."],["dc.identifier.doi","10.1038/nsmb.2570"],["dc.identifier.gro","3142345"],["dc.identifier.isi","000319915900008"],["dc.identifier.pmid","23665582"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/7253"],["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","1545-9993"],["dc.title","Phosphatidylinositol 4,5-bisphosphate clusters act as molecular beacons for vesicle recruitment"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","188102"],["dc.bibliographiccitation.issue","18"],["dc.bibliographiccitation.journal","Physical Review Letters"],["dc.bibliographiccitation.volume","117"],["dc.contributor.author","Bubnis, Gregory"],["dc.contributor.author","Risselada, Herre Jelger"],["dc.contributor.author","Grubmüller, Helmut"],["dc.date.accessioned","2018-02-09T07:42:37Z"],["dc.date.available","2018-02-09T07:42:37Z"],["dc.date.issued","2016"],["dc.description.abstract","A complete physical description of membrane remodeling processes, such as fusion or fission, requires knowledge of the underlying free energy landscapes, particularly in barrier regions involving collective shape changes, topological transitions, and high curvature, where Canham-Helfrich (CH) continuum descriptions may fail. To calculate these free energies using atomistic simulations, one must address not only the sampling problem due to high free energy barriers, but also an orthogonal sampling problem of combinatorial complexity stemming from the permutation symmetry of identical lipids. Here, we solve the combinatorial problem with a permutation reduction scheme to map a structural ensemble into a compact, nondegenerate subregion of configuration space, thereby permitting straightforward free energy calculations via umbrella sampling. We applied this approach, using a coarse-grained lipid model, to test the CH description of bending and found sharp increases in the bending modulus for curvature radii below 10 nm. These deviations suggest that an anharmonic bending term may be required for CH models to give quantitative energetics of highly curved states."],["dc.identifier.doi","10.1103/PhysRevLett.117.188102"],["dc.identifier.eissn","1079-7114"],["dc.identifier.issn","0031-9007"],["dc.identifier.pmid","27834997"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/12076"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.notes.status","final"],["dc.relation.eissn","1079-7114"],["dc.title","Exploiting Lipid Permutation Symmetry to Compute Membrane Remodeling Free Energies"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","11043"],["dc.bibliographiccitation.issue","30"],["dc.bibliographiccitation.journal","Proceedings of the National Academy of Sciences"],["dc.bibliographiccitation.lastpage","11048"],["dc.bibliographiccitation.volume","111"],["dc.contributor.author","Risselada, Herre Jelger"],["dc.contributor.author","Bubnis, Gregory"],["dc.contributor.author","Grubmüller, Helmut"],["dc.date.accessioned","2017-09-07T11:45:42Z"],["dc.date.available","2017-09-07T11:45:42Z"],["dc.date.issued","2014"],["dc.description.abstract","Over the past 20 years, it has been widely accepted that membrane fusion proceeds via a hemifusion step before opening of the productive fusion pore. An initial hourglass-shaped lipid structure, the fusion stalk, is formed between the adjacent membrane leaflets (cis leaflets). It remains controversial if and how fusion proteins drive the subsequent transition (expansion) of the stalk into a fusion pore. Here, we propose a comprehensive and consistent thermodynamic understanding in terms of the underlying free-energy landscape of stalk expansion. We illustrate how the underlying free energy landscape of stalk expansion and the concomitant pathway is altered by subtle differences in membrane environment, such as leaflet composition, asymmetry, and flexibility. Nonleaky stalk expansion (stalk widening) requires the formation of a critical trans-leaflet contact. The fusion machinery can mechanically enforce trans-leaflet contact formation either by directly enforcing the trans-leaflets in close proximity, or by (electrostatically) condensing the area of the cis leaflets. The rate of these fast fusion reactions may not be primarily limited by the energetics but by the forces that the fusion proteins are able to exert."],["dc.identifier.doi","10.1073/pnas.1323221111"],["dc.identifier.gro","3142085"],["dc.identifier.isi","000339500200046"],["dc.identifier.pmid","25024174"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/4378"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: Deutsche Forschungsgemeinschaft [SFB 803]"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0027-8424"],["dc.title","Expansion of the fusion stalk and its implication for biological membrane fusion"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","187"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Current Opinion in Structural Biology"],["dc.bibliographiccitation.lastpage","196"],["dc.bibliographiccitation.volume","22"],["dc.contributor.author","Risselada, Herre Jelger"],["dc.contributor.author","Grubmüller, Helmut"],["dc.date.accessioned","2017-09-07T11:48:55Z"],["dc.date.available","2017-09-07T11:48:55Z"],["dc.date.issued","2012"],["dc.description.abstract","SNARE molecules are the core constituents of the protein machinery that facilitate fusion of synaptic vesicles with the presynaptic plasma membrane, resulting in the release of neurotransmitter. On a molecular level, SNARE complexes seem to play a quite versatile and involved role during all stages of fusion. In addition to merely triggering fusion by forcing the opposing membranes into close proximity, SNARE complexes are now seen to also overcome subsequent fusion barriers and to actively guide the fusion reaction up to the expansion of the fusion pore. Here, we review recent advances in the understanding of SNARE-mediated membrane fusion by molecular simulations."],["dc.identifier.doi","10.1016/j.sbi.2012.01.007"],["dc.identifier.gro","3142554"],["dc.identifier.isi","000303368400009"],["dc.identifier.pmid","22365575"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/8918"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: DFG [SFB 803/B2]"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1879-033X"],["dc.relation.issn","0959-440X"],["dc.title","How SNARE molecules mediate membrane fusion: Recent insights from molecular simulations"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","e38302"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","PLoS ONE"],["dc.bibliographiccitation.volume","7"],["dc.contributor.author","Risselada, Herre Jelger"],["dc.contributor.author","Marelli, Giovanni"],["dc.contributor.author","Fuhrmans, Marc"],["dc.contributor.author","Smirnova, Yuliya G."],["dc.contributor.author","Grubmüller, Helmut"],["dc.contributor.author","Marrink, Siewert Jan"],["dc.contributor.author","Mueller, Marcus"],["dc.date.accessioned","2017-09-07T11:48:51Z"],["dc.date.available","2017-09-07T11:48:51Z"],["dc.date.issued","2012"],["dc.description.abstract","Our molecular simulations reveal that wild-type influenza fusion peptides are able to stabilize a highly fusogenic pre-fusion structure, i.e. a peptide bundle formed by four or more trans-membrane arranged fusion peptides. We rationalize that the lipid rim around such bundle has a non-vanishing rim energy (line-tension), which is essential to (i) stabilize the initial contact point between the fusing bilayers, i. e. the stalk, and (ii) drive its subsequent evolution. Such line-tension controlled fusion event does not proceed along the hypothesized standard stalk-hemifusion pathway. In modeled influenza fusion, single point mutations in the influenza fusion peptide either completely inhibit fusion (mutants G1V and W14A) or, intriguingly, specifically arrest fusion at a hemifusion state (mutant G1S). Our simulations demonstrate that, within a line-tension controlled fusion mechanism, these known point mutations either completely inhibit fusion by impairing the peptide's ability to stabilize the required peptide bundle (G1V and W14A) or stabilize a persistent bundle that leads to a kinetically trapped hemifusion state (G1S). In addition, our results further suggest that the recently discovered leaky fusion mutant G13A, which is known to facilitate a pronounced leakage of the target membrane prior to lipid mixing, reduces the membrane integrity by forming a 'super' bundle. Our simulations offer a new interpretation for a number of experimentally observed features of the fusion reaction mediated by the prototypical fusion protein, influenza hemagglutinin, and might bring new insights into mechanisms of other viral fusion reactions."],["dc.identifier.doi","10.1371/journal.pone.0038302"],["dc.identifier.fs","587227"],["dc.identifier.gro","3142512"],["dc.identifier.isi","000305826400002"],["dc.identifier.pmid","22761674"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/7878"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/8871"],["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","1932-6203"],["dc.relation.orgunit","Fakultät für Physik"],["dc.rights","CC BY 2.5"],["dc.rights.uri","http://creativecommons.org/licenses/by/2.5/"],["dc.title","Line-Tension Controlled Mechanism for Influenza Fusion"],["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"]]