Song, Chen

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[["dc.bibliographiccitation.firstpage","539a"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Biophysical Journal"],["dc.bibliographiccitation.volume","106"],["dc.contributor.author","Kopfer, David A."],["dc.contributor.author","Song, Chen"],["dc.contributor.author","Zachariae, Ulrich"],["dc.contributor.author","de Groot, Bert L."],["dc.date.accessioned","2021-03-05T08:57:57Z"],["dc.date.available","2021-03-05T08:57:57Z"],["dc.date.issued","2014"],["dc.identifier.doi","10.1016/j.bpj.2013.11.3005"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/79945"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-393"],["dc.relation.issn","0006-3495"],["dc.title","Ion Permeation Efficiency through Potassium Channels"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","4586"],["dc.bibliographiccitation.issue","12"],["dc.bibliographiccitation.journal","Proceedings of the National Academy of Sciences"],["dc.bibliographiccitation.lastpage","4591"],["dc.bibliographiccitation.volume","110"],["dc.contributor.author","Song, Chen"],["dc.contributor.author","Weichbrodt, Conrad"],["dc.contributor.author","Salnikov, Evgeniy S."],["dc.contributor.author","Dynowski, Marek"],["dc.contributor.author","Forsberg, Björn O."],["dc.contributor.author","Bechinger, Burkhard"],["dc.contributor.author","Steinem, Claudia"],["dc.contributor.author","Groot, Bert L. de"],["dc.contributor.author","Zachariae, Ulrich"],["dc.contributor.author","Zeth, Kornelius"],["dc.date.accessioned","2017-09-07T11:47:46Z"],["dc.date.available","2017-09-07T11:47:46Z"],["dc.date.issued","2013"],["dc.description.abstract","Multicellular organisms fight bacterial and fungal infections by producing peptide-derived broad-spectrum antibiotics. These host-defense peptides compromise the integrity of microbial cell membranes and thus evade pathways by which bacteria develop rapid antibiotic resistance. Although more than 1,700 host-defense peptides have been identified, the structural and mechanistic basis of their action remains speculative. This impedes the desired rational development of these agents into next-generation antibiotics. We present the X-ray crystal structure as well as solid-state NMR spectroscopy, electrophysiology, and MD simulations of human dermcidin in membranes that reveal the antibiotic mechanism of this major human antimicrobial, found to suppress Staphylococcus aureus growth on the epidermal surface. Dermcidin forms an architecture of high-conductance transmembrane channels, composed of zinc-connected trimers of antiparallel helix pairs. Molecular dynamics simulations elucidate the unusual membrane permeation pathway for ions and show adjustment of the pore to various membranes. Our study unravels the comprehensive mechanism for the membrane-disruptive action of this mammalian host-defense peptide at atomistic level. The results may form a foundation for the structure-based design of peptide antibiotics."],["dc.identifier.doi","10.1073/pnas.1214739110"],["dc.identifier.gro","3142374"],["dc.identifier.isi","000317521600044"],["dc.identifier.pmid","23426625"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/7575"],["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","0027-8424"],["dc.title","Crystal structure and functional mechanism of a human antimicrobial membrane channel"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

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[["dc.bibliographiccitation.firstpage","129a"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Biophysical Journal"],["dc.bibliographiccitation.volume","108"],["dc.contributor.author","Song, Chen"],["dc.contributor.author","Gruene, Tim"],["dc.contributor.author","Sheldrick, George M."],["dc.contributor.author","Sansom, Mark S. P."],["dc.contributor.author","Zachariae, Ulrich"],["dc.contributor.author","de Groot, Bert L."],["dc.contributor.author","Köpfer, David A."],["dc.date.accessioned","2018-11-07T10:01:56Z"],["dc.date.available","2018-11-07T10:01:56Z"],["dc.date.issued","2015"],["dc.format.extent","129A"],["dc.identifier.doi","10.1016/j.bpj.2014.11.721"],["dc.identifier.isi","000359471700647"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/38131"],["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.issn","1542-0086"],["dc.relation.issn","0006-3495"],["dc.title","Direct Contacts of K+ Ions in the Selectivity Filter Enable the High Conductance of K+ Channels"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","352"],["dc.bibliographiccitation.issue","6207"],["dc.bibliographiccitation.journal","Science"],["dc.bibliographiccitation.lastpage","355"],["dc.bibliographiccitation.volume","346"],["dc.contributor.author","Koepfer, David A."],["dc.contributor.author","Song, Chen"],["dc.contributor.author","Gruene, Tim"],["dc.contributor.author","Sheldrick, George M."],["dc.contributor.author","Zachariae, Ulrich"],["dc.contributor.author","de Groot, Bert L."],["dc.date.accessioned","2018-11-07T09:33:31Z"],["dc.date.available","2018-11-07T09:33:31Z"],["dc.date.issued","2014"],["dc.description.abstract","Potassium channels selectively conduct K+ ions across cellular membranes with extraordinary efficiency. Their selectivity filter exhibits four binding sites with approximately equal electron density in crystal structures with high K+ concentrations, previously thought to reflect a superposition of alternating ion-and water-occupied states. Consequently, cotranslocation of ions with water has become a widely accepted ion conduction mechanism for potassium channels. By analyzing more than 1300 permeation events from molecular dynamics simulations at physiological voltages, we observed instead that permeation occurs via ion-ion contacts between neighboring K+ ions. Coulomb repulsion between adjacent ions is found to be the key to high-efficiency K+ conduction. Crystallographic data are consistent with directly neighboring K+ ions in the selectivity filter, and our model offers an intuitive explanation for the high throughput rates of K+ channels."],["dc.identifier.doi","10.1126/science.1254840"],["dc.identifier.isi","000343041100045"],["dc.identifier.pmid","25324389"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/31983"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Assoc Advancement Science"],["dc.relation.issn","1095-9203"],["dc.relation.issn","0036-8075"],["dc.title","Ion permeation in K+ channels occurs by direct Coulomb knock-on"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","241a"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Biophysical Journal"],["dc.bibliographiccitation.volume","104"],["dc.contributor.author","Song, Chen"],["dc.contributor.author","Weichbrodt, Conrad"],["dc.contributor.author","Dynowski, Marek"],["dc.contributor.author","Steinem, Claudia"],["dc.contributor.author","Zachariae, Ulrich"],["dc.contributor.author","Zeth, Kornelius"],["dc.contributor.author","de Groot, Bert L."],["dc.contributor.author","Forsberg, Björn O."],["dc.date.accessioned","2018-11-07T09:28:59Z"],["dc.date.available","2018-11-07T09:28:59Z"],["dc.date.issued","2013"],["dc.format.extent","241A"],["dc.identifier.doi","10.1016/j.bpj.2012.11.1359"],["dc.identifier.isi","000316074302239"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/30915"],["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","Channel Crystal Structure and Antimicrobial Mechanism of Dermcidin from Human Skin"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]