Walla, Peter Jomo

[["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Biophysical Journal"],["dc.bibliographiccitation.volume","106"],["dc.contributor.author","Walla, Peter Jomo"],["dc.contributor.author","Hafi, Nour"],["dc.contributor.author","Grunwald, Matthias"],["dc.contributor.author","van den Heuvel, Laura"],["dc.contributor.author","Timo, Aspelmeier"],["dc.contributor.author","Zagrebelsky, Marta"],["dc.contributor.author","Korte, Martin"],["dc.contributor.author","Munk, Axel"],["dc.date.accessioned","2018-11-07T09:44:56Z"],["dc.date.available","2018-11-07T09:44:56Z"],["dc.date.issued","2014"],["dc.identifier.isi","000337000400120"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/34507"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Cell Press"],["dc.publisher.place","Cambridge"],["dc.relation.eventlocation","San Francisco, CA"],["dc.title","Nanoscopy by Fluorescence Demodulation and Polarization Angle Narrowing"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","5859"],["dc.bibliographiccitation.journal","Nature Communications"],["dc.bibliographiccitation.volume","5"],["dc.contributor.author","Lin, Chao-Chen"],["dc.contributor.author","Seikowski, Jan"],["dc.contributor.author","Perez-Lara, Angel"],["dc.contributor.author","Jahn, Reinhard"],["dc.contributor.author","Höbartner, Claudia"],["dc.contributor.author","Walla, Peter Jomo"],["dc.date.accessioned","2018-11-07T09:31:47Z"],["dc.date.available","2018-11-07T09:31:47Z"],["dc.date.issued","2014"],["dc.description.abstract","Fast synchronous neurotransmitter release is triggered by calcium that activates synaptotagmin-1 (syt-1), resulting in fusion of synaptic vesicles with the presynaptic membrane. Syt-1 possesses two Ca2+-binding C2 domains that tether membranes via interactions with anionic phospholipids. It is capable of crosslinking membranes and has recently been speculated to trigger fusion by decreasing the gap between them. As quantitative information on membrane gaps is key to understanding general cellular mechanisms, including the role of syt-1, we developed a fluorescence-lifetime based inter-membrane distance ruler using membrane-anchored DNAs of various lengths as calibration standards. Wild-type and mutant data provide evidence that full-length syt-1 indeed regulates membrane gaps: without Ca2+, syt-1 maintains membranes at distances of similar to 7-8 nm. Activation with 100 mu M Ca2+ decreases the distance to similar to 5 nm by binding the C2 domains to opposing membranes, respectively. These values reveal that activated syt-1 adjusts membrane distances to the level that promotes SNARE complex assembly."],["dc.identifier.doi","10.1038/ncomms6859"],["dc.identifier.isi","000347683100001"],["dc.identifier.pmid","25500905"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/31610"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.relation.issn","2041-1723"],["dc.title","Control of membrane gaps by synaptotagmin-Ca2+ measured with a novel membrane distance ruler"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","666"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Nature Communications"],["dc.bibliographiccitation.volume","9"],["dc.contributor.author","Pieper, Alexander"],["dc.contributor.author","Hohgardt, Manuel"],["dc.contributor.author","Willich, Maximilian"],["dc.contributor.author","Gacek, Daniel Alexander"],["dc.contributor.author","Hafi, Nour"],["dc.contributor.author","Pfennig, Dominik"],["dc.contributor.author","Albrecht, Andreas"],["dc.contributor.author","Walla, Peter Jomo"],["dc.date.accessioned","2019-12-03T15:20:48Z"],["dc.date.available","2019-12-03T15:20:48Z"],["dc.date.issued","2018"],["dc.description.abstract","Efficient sunlight harvesting and re-directioning onto small areas has great potential for more widespread use of precious high-performance photovoltaics but so far intrinsic solar concentrator loss mechanisms outweighed the benefits. Here we present an antenna concept allowing high light absorption without high reabsorption or escape-cone losses. An excess of randomly oriented pigments collects light from any direction and funnels the energy to individual acceptors all having identical orientations and emitting ~90% of photons into angles suitable for total internal reflection waveguiding to desired energy converters (funneling diffuse-light re-directioning, FunDiLight). This is achieved using distinct molecules that align efficiently within stretched polymers together with others staying randomly orientated. Emission quantum efficiencies can be >80% and single-foil reabsorption <0.5%. Efficient donor-pool energy funneling, dipole re-orientation, and ~1.5-2 nm nearest donor-acceptor transfer occurs within hundreds to ~20 ps. Single-molecule 3D-polarization experiments confirm nearly parallel emitters. Stacked pigment selection may allow coverage of the entire solar spectrum."],["dc.identifier.doi","10.1038/s41467-018-03103-4"],["dc.identifier.pmid","29445168"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/62733"],["dc.language.iso","en"],["dc.relation.eissn","2041-1723"],["dc.relation.issn","2041-1723"],["dc.title","Biomimetic light-harvesting funnels for re-directioning of diffuse light"],["dc.type","journal_article"],["dc.type.internalPublication","no"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","815"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","Nature Structural & Molecular Biology"],["dc.bibliographiccitation.lastpage","823"],["dc.bibliographiccitation.volume","22"],["dc.contributor.author","Park, Yongsoo"],["dc.contributor.author","Seo, Jong Bae"],["dc.contributor.author","Fraind, Alicia"],["dc.contributor.author","Perez-Lara, Angel"],["dc.contributor.author","Yavuz, Halenur"],["dc.contributor.author","Han, Kyungreem"],["dc.contributor.author","Jung, Seung-Ryoung"],["dc.contributor.author","Kattan, Iman"],["dc.contributor.author","Walla, Peter Jomo"],["dc.contributor.author","Choi, MooYoung"],["dc.contributor.author","Cafiso, David S."],["dc.contributor.author","Koh, Duk-Su"],["dc.contributor.author","Jahn, Reinhard"],["dc.date.accessioned","2019-12-03T15:11:07Z"],["dc.date.available","2019-12-03T15:11:07Z"],["dc.date.issued","2015"],["dc.description.abstract","The Ca(2+) sensor synaptotagmin-1 is thought to trigger membrane fusion by binding to acidic membrane lipids and SNARE proteins. Previous work has shown that binding is mediated by electrostatic interactions that are sensitive to the ionic environment. However, the influence of divalent or polyvalent ions, at physiological concentrations, on synaptotagmin's binding to membranes or SNAREs has not been explored. Here we show that binding of rat synaptotagmin-1 to membranes containing phosphatidylinositol 4,5-bisphosphate (PIP2) is regulated by charge shielding caused by the presence of divalent cations. Surprisingly, polyvalent ions such as ATP and Mg(2+) completely abrogate synaptotagmin-1 binding to SNAREs regardless of the presence of Ca(2+). Altogether, our data indicate that at physiological ion concentrations Ca(2+)-dependent synaptotagmin-1 binding is confined to PIP2-containing membrane patches in the plasma membrane, suggesting that membrane interaction of synaptotagmin-1 rather than SNARE binding triggers exocytosis of vesicles."],["dc.identifier.doi","10.1038/nsmb.3097"],["dc.identifier.pmid","26389740"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/62732"],["dc.language.iso","en"],["dc.relation.eissn","1545-9985"],["dc.relation.issn","1545-9993"],["dc.relation.issn","1545-9985"],["dc.title","Synaptotagmin-1 binds to PIP(2)-containing membrane but not to SNAREs at physiological ionic strength"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","7a"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Biophysical Journal"],["dc.bibliographiccitation.lastpage","8a"],["dc.bibliographiccitation.volume","108"],["dc.contributor.author","Walla, Peter J."],["dc.contributor.author","Hafi, Nour"],["dc.contributor.author","Matthias, Grunwald"],["dc.contributor.author","Jess, Laura S."],["dc.contributor.author","Aspelmeier, Timo"],["dc.contributor.author","Martha, Zagrebelski"],["dc.contributor.author","Pfennig, Dominik"],["dc.contributor.author","Korte, Martin"],["dc.contributor.author","Munk, Axel"],["dc.date.accessioned","2022-06-08T07:57:47Z"],["dc.date.available","2022-06-08T07:57:47Z"],["dc.date.issued","2015"],["dc.identifier.doi","10.1016/j.bpj.2014.11.063"],["dc.identifier.pii","S0006349514012727"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/110212"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-575"],["dc.relation.issn","0006-3495"],["dc.title","Fluorescence Nanoscopy by Polarization Modulation (SPoD) and Polarization Angle Narrowing (ExPAN)"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","579"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Nature Methods"],["dc.bibliographiccitation.lastpage","584"],["dc.bibliographiccitation.volume","11"],["dc.contributor.author","Hafi, Nour"],["dc.contributor.author","Grunwald, Matthias"],["dc.contributor.author","van den Heuvel, Laura S."],["dc.contributor.author","Aspelmeier, Timo"],["dc.contributor.author","Chen, Jian-Hua"],["dc.contributor.author","Zagrebelsky, Marta"],["dc.contributor.author","Schütte, Ole M."],["dc.contributor.author","Steinem, Claudia"],["dc.contributor.author","Korte, Martin"],["dc.contributor.author","Munk, Axel"],["dc.contributor.author","Walla, Peter J."],["dc.date.accessioned","2017-09-07T11:46:16Z"],["dc.date.available","2017-09-07T11:46:16Z"],["dc.date.issued","2014"],["dc.description.abstract","When excited with rotating linear polarized light, differently oriented fluorescent dyes emit periodic signals peaking at different times. We show that measurement of the average orientation of fluorescent dyes attached to rigid sample structures mapped to regularly defined (50 nm)(2) image nanoareas can provide subdiffraction resolution (super resolution by polarization demodulation, SPoD). Because the polarization angle range for effective excitation of an oriented molecule is rather broad and unspecific, we narrowed this range by simultaneous irradiation with a second, de-excitation, beam possessing a polarization perpendicular to the excitation beam (excitation polarization angle narrowing, ExPAN). This shortened the periodic emission flashes, allowing better discrimination between molecules or nanoareas. Our method requires neither the generation of nanometric interference structures nor the use of switchable or blinking fluorescent probes. We applied the method to standard wide-field microscopy with camera detection and to two-photon scanning microscopy, imaging the fine structural details of neuronal spines."],["dc.identifier.doi","10.1038/NMETH.2919"],["dc.identifier.gro","3142133"],["dc.identifier.isi","000335873400027"],["dc.identifier.pmid","24705472"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/4911"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1548-7105"],["dc.relation.haserratum","/handle/2/768"],["dc.relation.issn","1548-7091"],["dc.title","Fluorescence nanoscopy by polarization modulation and polarization angle narrowing"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","11310"],["dc.bibliographiccitation.journal","Nature Communications"],["dc.bibliographiccitation.volume","7"],["dc.contributor.author","Hiragami-Hamada, Kyoko"],["dc.contributor.author","Soeroes, Szabolcs"],["dc.contributor.author","Nikolov, Miroslav"],["dc.contributor.author","Wilkins, Bryan J."],["dc.contributor.author","Kreuz, Sarah"],["dc.contributor.author","Chen, Carol"],["dc.contributor.author","De La Rosa-Velazquez, Inti A."],["dc.contributor.author","Zenn, Hans Michael"],["dc.contributor.author","Kost, Nils"],["dc.contributor.author","Pohl, Wiebke"],["dc.contributor.author","Chernev, Aleksandar"],["dc.contributor.author","Schwarzer, Dirk"],["dc.contributor.author","Jenuwein, Thomas"],["dc.contributor.author","Lorincz, Matthew"],["dc.contributor.author","Zimmermann, Bastian"],["dc.contributor.author","Walla, Peter Jomo"],["dc.contributor.author","Neumann, Heinz"],["dc.contributor.author","Baubec, Tuncay"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Fischle, Wolfgang"],["dc.date.accessioned","2018-11-07T10:16:11Z"],["dc.date.available","2018-11-07T10:16:11Z"],["dc.date.issued","2016"],["dc.description.abstract","Histone H3 trimethylation of lysine 9 (H3K9me3) and proteins of the heterochromatin protein 1 (HP1) family are hallmarks of heterochromatin, a state of compacted DNA essential for genome stability and long-term transcriptional silencing. The mechanisms by which H3K9me3 and HP1 contribute to chromatin condensation have been speculative and controversial. Here we demonstrate that human HP1 beta is a prototypic HP1 protein exemplifying most basal chromatin binding and effects. These are caused by dimeric and dynamic interaction with highly enriched H3K9me3 and are modulated by various electrostatic interfaces. HP1 beta bridges condensed chromatin, which we postulate stabilizes the compacted state. In agreement, HP1 beta genome-wide localization follows H3K9me3-enrichment and artificial bridging of chromatin fibres is sufficient for maintaining cellular heterochromatic conformation. Overall, our findings define a fundamental mechanism for chromatin higher order structural changes caused by HP1 proteins, which might contribute to the plastic nature of condensed chromatin."],["dc.identifier.doi","10.1038/ncomms11310"],["dc.identifier.isi","000374291900001"],["dc.identifier.pmid","27090491"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/13282"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/40987"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.relation.issn","2041-1723"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Dynamic and flexible H3K9me3 bridging via HP1 beta dimerization establishes a plastic state of condensed chromatin"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","24a"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Biophysical Journal"],["dc.bibliographiccitation.volume","106"],["dc.contributor.author","Walla, Peter J."],["dc.contributor.author","Hafi, Nour"],["dc.contributor.author","Grunwald, Matthias"],["dc.contributor.author","Van den Heuvel, Laura"],["dc.contributor.author","Aspelmeier, Timo"],["dc.contributor.author","Zagrebelsky, Marta"],["dc.contributor.author","Korte, Martin"],["dc.contributor.author","Munk, Axel"],["dc.date.accessioned","2022-06-08T07:57:47Z"],["dc.date.available","2022-06-08T07:57:47Z"],["dc.date.issued","2014"],["dc.identifier.doi","10.1016/j.bpj.2013.11.186"],["dc.identifier.pii","S0006349513014215"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/110211"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-575"],["dc.relation.issn","0006-3495"],["dc.title","Nanoscopy by Fluorescence Demodulation and Polarization Angle Narrowing"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","8"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Nature Methods"],["dc.bibliographiccitation.lastpage","9"],["dc.bibliographiccitation.volume","13"],["dc.contributor.author","Hafi, Nour"],["dc.contributor.author","Grunwald, Matthias"],["dc.contributor.author","van den Heuvel, Laura S."],["dc.contributor.author","Aspelmeier, Timo"],["dc.contributor.author","Steinem, Claudia"],["dc.contributor.author","Korte, Martin"],["dc.contributor.author","Munk, Axel"],["dc.contributor.author","Walla, Peter J."],["dc.date.accessioned","2017-09-07T11:54:46Z"],["dc.date.available","2017-09-07T11:54:46Z"],["dc.date.issued","2016"],["dc.description.abstract","We are grateful to Keller et al. for the opportunity to clarify the role of the SPEED (sparsity penalty–enhanced estimation by demodulation) algorithm and the impact of the polarization information in SPoD (super-resolution by polarization demodulation). We concur with Keller et al. that for densely labeled and spatially sparse samples, the information gain from polarization is negligible in their reanalysis of our data, as they observed that nearly identical resolution can also be achieved by sparse deconvolution alone using the SPEED algorithm. However, this does not mean that no gain in resolution is possible with the modulation information alone."],["dc.identifier.doi","10.1038/nmeth.3721"],["dc.identifier.gro","3141759"],["dc.identifier.isi","000367463600005"],["dc.identifier.pmid","26716557"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/757"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1548-7105"],["dc.relation.issn","1548-7091"],["dc.title","Reply to \"Polarization modulation adds little additional information to super-resolution fluorescence microscopy\""],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","letter_note"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2797"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","Chemical Science"],["dc.bibliographiccitation.lastpage","2802"],["dc.bibliographiccitation.volume","9"],["dc.contributor.author","Becker, Yvonne"],["dc.contributor.author","Unger, Erik"],["dc.contributor.author","Fichte, Manuela A. H."],["dc.contributor.author","Gacek, Daniel A."],["dc.contributor.author","Dreuw, Andreas"],["dc.contributor.author","Wachtveitl, Josef"],["dc.contributor.author","Walla, Peter Jomo"],["dc.contributor.author","Heckel, Alexander"],["dc.date.accessioned","2019-12-03T15:26:20Z"],["dc.date.available","2019-12-03T15:26:20Z"],["dc.date.issued","2018"],["dc.description.abstract","Based on nitrodibenzofuran (NDBF) a new photocage with higher two-photon action cross section and red-shifted absorption was developed. Due to calculations, a dimethylamino functionality (DMA) was added at ring position 7. The uncaging of nucleobases after two-photon excitation (2PE) could be visualized via double-strand displacement in a hydrogel. With this assay we achieved three-dimensional photorelease of DMA-NDBF-protected DNA orthogonal to NDBF-protected strands. While being an excellent 2PE-cage, DMA-NDBF is surprisingly stable under visible-light one-photon excitation (1PE). This case of excitation-specific photochemistry enhances the scope of orthogonal photoregulation."],["dc.identifier.doi","10.1039/C7SC05182D"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/62735"],["dc.language.iso","en"],["dc.relation.issn","2041-6520"],["dc.relation.issn","2041-6539"],["dc.title","A red-shifted two-photon-only caging group for three-dimensional photorelease"],["dc.type","journal_article"],["dc.type.internalPublication","no"],["dspace.entity.type","Publication"]]