Schwappach-Pignataro, Blanche

[["dc.bibliographiccitation.artnumber","5715"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Nature Communications"],["dc.bibliographiccitation.volume","12"],["dc.contributor.author","Gomkale, Ridhima"],["dc.contributor.author","Linden, Andreas"],["dc.contributor.author","Neumann, Piotr"],["dc.contributor.author","Schendzielorz, Alexander Benjamin"],["dc.contributor.author","Stoldt, Stefan"],["dc.contributor.author","Dybkov, Olexandr"],["dc.contributor.author","Kilisch, Markus"],["dc.contributor.author","Schulz, Christian"],["dc.contributor.author","Cruz-Zaragoza, Luis Daniel"],["dc.contributor.author","Schwappach, Blanche"],["dc.contributor.author","Rehling, Peter"],["dc.date.accessioned","2021-10-01T09:57:33Z"],["dc.date.available","2021-10-01T09:57:33Z"],["dc.date.issued","2021"],["dc.description.abstract","Abstract Nuclear-encoded mitochondrial proteins destined for the matrix have to be transported across two membranes. The TOM and TIM23 complexes facilitate the transport of precursor proteins with N-terminal targeting signals into the matrix. During transport, precursors are recognized by the TIM23 complex in the inner membrane for handover from the TOM complex. However, we have little knowledge on the organization of the TOM-TIM23 transition zone and on how precursor transfer between the translocases occurs. Here, we have designed a precursor protein that is stalled during matrix transport in a TOM-TIM23-spanning manner and enables purification of the translocation intermediate. Combining chemical cross-linking with mass spectrometric analyses and structural modeling allows us to map the molecular environment of the intermembrane space interface of TOM and TIM23 as well as the import motor interactions with amino acid resolution. Our analyses provide a framework for understanding presequence handover and translocation during matrix protein transport."],["dc.description.sponsorship","Open-Access-Publikationsfonds 2021"],["dc.identifier.doi","10.1038/s41467-021-26016-1"],["dc.identifier.pii","26016"],["dc.identifier.pmid","34588454"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/89863"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/348"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/157"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-469"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation","SFB 1190: Transportmaschinen und Kontaktstellen zellulärer Kompartimente"],["dc.relation","SFB 1190 | P01: Untersuchung der Unterschiede in der Zusammensetzung, Funktion und Position von individuellen MICOS Komplexen in einzelnen Säugerzellen"],["dc.relation","SFB 1190 | P04: Der GET-Rezeptor als ein Eingangstor zum ER und sein Zusammenspiel mit GET bodies"],["dc.relation","SFB 1190 | P13: Protein Transport über den mitochondrialen Carrier Transportweg"],["dc.relation","SFB 1190 | Z02: Massenspektrometrie-basierte Proteomanalyse"],["dc.relation.eissn","2041-1723"],["dc.relation.workinggroup","RG Ficner (Molecular Structural Biology)"],["dc.relation.workinggroup","RG Jakobs (Structure and Dynamics of Mitochondria)"],["dc.relation.workinggroup","RG Rehling (Mitochondrial Protein Biogenesis)"],["dc.relation.workinggroup","RG Schwappach (Membrane Protein Biogenesis)"],["dc.relation.workinggroup","RG Urlaub (Bioanalytische Massenspektrometrie)"],["dc.rights","CC BY 4.0"],["dc.title","Mapping protein interactions in the active TOM-TIM23 supercomplex"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Matters"],["dc.contributor.author","Clancy, Anne"],["dc.contributor.author","Schrul, Bianca"],["dc.contributor.author","Schwappach, Blanche"],["dc.date.accessioned","2017-11-28T10:03:35Z"],["dc.date.available","2017-11-28T10:03:35Z"],["dc.date.issued","2016"],["dc.description.abstract","14-3-3 proteins are abundant modulators of cellular processes, in particular signal transduction. They function by binding to a broad spectrum of client proteins, thus affecting client protein localisation or function[1]Gardino 2011 [1]Morrison 2009 [2][2]. Animals and plants express 14-3-3 proteins encoded by several genes, which has made it difficult to study their unique rather than shared functions. The yeast Saccharomyces cerevisiae possesses only two highly homologous 14-3-3 genes, BMH1 and BMH2. Using this model system we now uncover novel aspects of functional specificity between the two yeast 14-3-3s. We show that bmh1 but not bmh2 cells display an altered morphology of the endomembrane system and specific trafficking defects under glucose starvation. This but not a second phenotype specific to the bmh1 strain, that is, the accumulation of glycogen, was rescued by overexpression of the nucleotide exchange factor Gea1, suggesting a role for Bmh1 in Gea1’s function or regulation."],["dc.identifier.doi","10.19185/matters.201609000004"],["dc.identifier.fs","626945"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/10613"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/61"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.relation","SFB 1190: Transportmaschinen und Kontaktstellen zellulärer Kompartimente"],["dc.relation","SFB 1190 | Z03: Synthetische genetische Analyse, automatisierte Mikroskopie und Bildanalyse"],["dc.relation.issn","2297-8240"],["dc.relation.workinggroup","RG Schwappach (Membrane Protein Biogenesis)"],["dc.title","The guanine nucleotide exchange factor Gea1 rescues an isoform-specific 14-3-3 phenotype"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.peerReviewed","unknown"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1055"],["dc.bibliographiccitation.issue","7"],["dc.bibliographiccitation.journal","FEMS Yeast Research"],["dc.bibliographiccitation.lastpage","1067"],["dc.bibliographiccitation.volume","14"],["dc.contributor.author","Elbaz-Alon, Yael"],["dc.contributor.author","Morgan, Bruce"],["dc.contributor.author","Clancy, Anne"],["dc.contributor.author","Amoako, Theresa N. E."],["dc.contributor.author","Zalckvar, Einat"],["dc.contributor.author","Dick, Tobias P."],["dc.contributor.author","Schwappach, Blanche"],["dc.contributor.author","Schuldiner, Maya"],["dc.date.accessioned","2017-09-07T11:45:25Z"],["dc.date.available","2017-09-07T11:45:25Z"],["dc.date.issued","2014"],["dc.description.abstract","Glutathione, the most abundant small-molecule thiol in eukaryotic cells, is synthesized de novo solely in the cytosol and must subsequently be transported to other cellular compartments. The mechanisms of glutathione transport into and out of organelles remain largely unclear. We show that budding yeast Opt2, a close homolog of the plasma membrane glutathione transporter Opt1, localizes to peroxisomes. We demonstrate that deletion of OPT2 leads to major defects in maintaining peroxisomal, mitochondrial, and cytosolic glutathione redox homeostasis. Furthermore, opt2 strains display synthetic lethality with deletions of genes central to iron homeostasis that require mitochondrial glutathione redox homeostasis. Our results shed new light on the importance of peroxisomes in cellular glutathione homeostasis."],["dc.identifier.doi","10.1111/1567-1364.12196"],["dc.identifier.gro","3142025"],["dc.identifier.isi","000344918500007"],["dc.identifier.pmid","25130273"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/3712"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Wiley-blackwell"],["dc.relation.eissn","1567-1364"],["dc.relation.issn","1567-1356"],["dc.title","The yeast oligopeptide transporter Opt2 is localized to peroxisomes and affects glutathione redox homeostasis"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","887"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","Journal of Molecular and Cellular Cardiology"],["dc.bibliographiccitation.lastpage","894"],["dc.bibliographiccitation.volume","38"],["dc.contributor.author","Neagoe, Ioana"],["dc.contributor.author","Schwappach, Blanche"],["dc.date.accessioned","2017-09-07T11:54:18Z"],["dc.date.available","2017-09-07T11:54:18Z"],["dc.date.issued","2005"],["dc.identifier.doi","10.1016/j.yjmcc.2004.11.023"],["dc.identifier.gro","3145138"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/2841"],["dc.language.iso","en"],["dc.notes.intern","Crossref Import"],["dc.notes.status","final"],["dc.relation.issn","0022-2828"],["dc.title","Pas de deux in groups of four—the biogenesis of K channels"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.peerReviewed","no"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","4353"],["dc.bibliographiccitation.issue","20"],["dc.bibliographiccitation.journal","Journal of Cell Science"],["dc.bibliographiccitation.lastpage","4363"],["dc.bibliographiccitation.volume","119"],["dc.contributor.author","Heusser, Katja"],["dc.contributor.author","Yuan, Hebao"],["dc.contributor.author","Neagoe, Ioana"],["dc.contributor.author","Tarasov, Andrei I."],["dc.contributor.author","Ashcroft, Frances M."],["dc.contributor.author","Schwappach, Blanche"],["dc.date.accessioned","2017-09-07T11:52:29Z"],["dc.date.available","2017-09-07T11:52:29Z"],["dc.date.issued","2006"],["dc.description.abstract","Arginine (Arg)-based endoplasmic reticulum (ER)-localization signals are involved in the quality control of different heteromultimeric membrane protein complexes. ATP-sensitive potassium (K-ATP) channels are unique because each subunit in the heterooctamer contains an Arg- based ER-localization signal. We have dissected the inactivation events that override the ER-localization activity of the eight peptide-sorting motifs. Employing a 14-3-3-scavenger construct to lower the availability of 14-3-3 proteins, we found that 14-3-3 proteins promote the cell-surface expression of heterologously expressed and native K-ATP channels. 14- 3- 3 proteins were detected in physical association with K-ATP channels in a pancreatic beta-cell line. Our results suggest that the Arg-based signal present in Kir6.2 is sterically masked by the SUR1 subunit. By contrast, 14-3-3 proteins functionally antagonized the Arg-based signal present in SUR1. The last ten amino acids were required for efficient 14-3-3 recruitment to multimeric forms of the Kir6.2 C-terminus. Channels containing a pore-forming subunit lacking these residues reached the cell surface inefficiently but were functionally indistinguishable from channels formed by the full-length subunits. In conclusion, 14-3-3 proteins promote the cell-surface transport of correctly assembled complexes but do not regulate the activity of K-ATP channels at the cell surface."],["dc.identifier.doi","10.1242/jcs.03196"],["dc.identifier.gro","3143613"],["dc.identifier.isi","000241217100023"],["dc.identifier.pmid","17038548"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1147"],["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","0021-9533"],["dc.title","Scavenging of 14-3-3 proteins reveals their involvement in the cell-surface transport of ATP-sensitive K+ channels"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","717"],["dc.bibliographiccitation.issue","8"],["dc.bibliographiccitation.journal","EMBO reports"],["dc.bibliographiccitation.lastpage","722"],["dc.bibliographiccitation.volume","6"],["dc.contributor.author","Michelsen, Kai"],["dc.contributor.author","Yuan, Hebao"],["dc.contributor.author","Schwappach, Blanche"],["dc.date.accessioned","2017-09-07T11:54:21Z"],["dc.date.available","2017-09-07T11:54:21Z"],["dc.date.issued","2005"],["dc.description.abstract","Arginine-based endoplasmic reticulum (ER)-localization signals are sorting motifs that are involved in the biosynthetic transport of multimeric membrane proteins. After their discovery in the invariant chain of the major histocompatibility complex class II, several hallmarks of these signals have emerged. They occur in polytopic membrane proteins that are subunits of membrane protein complexes; the presence of the signal maintains improperly assembled subunits in the ER by retention or retrieval until it is masked as a result of heteromultimeric assembly. A distinct consensus sequence and their position independence with respect to the distal termini of the protein distinguish them from other ER-sorting motifs. Recognition by the coatomer (COPI) vesicle coat explains ER retrieval. Often, di-leucine endocytic signals occur close to arginine-based signals. Recruitment of 14-3-3 family or PDZ-domain proteins can counteract ER-localization activity, as can phosphorylation. This, and the occurrence of arginine-based signals in alternatively spliced regions, implicates them in the regulated surface expression of multimeric membrane proteins in addition to their function in quality control."],["dc.identifier.doi","10.1038/sj.embor.7400480"],["dc.identifier.gro","3143818"],["dc.identifier.isi","000231249500009"],["dc.identifier.pmid","16065065"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1374"],["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","1469-221X"],["dc.title","Hide and run - Arginine-based endoplasmic-reticulum-sorting motifs in the assembly of heteromultimeric membrane proteins"],["dc.type","review"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","jcs209890"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Journal of Cell Science"],["dc.bibliographiccitation.volume","131"],["dc.contributor.author","Arakel, Eric C."],["dc.contributor.author","Schwappach, Blanche"],["dc.date.accessioned","2020-12-10T18:41:52Z"],["dc.date.available","2020-12-10T18:41:52Z"],["dc.date.issued","2018"],["dc.description.abstract","The coat protein complex I (COPI) allows the precise sorting of lipids and proteins between Golgi cisternae and retrieval from the Golgi to the ER. This essential role maintains the identity of the early secretory pathway and impinges on key cellular processes, such as protein quality control. In this Cell Science at a Glance and accompanying poster, we illustrate the different stages of COPI-coated vesicle formation and revisit decades of research in the context of recent advances in the elucidation of COPI coat structure. By calling attention to an array of questions that have remained unresolved, this review attempts to refocus the perspectives of the field."],["dc.identifier.doi","10.1242/jcs.209890"],["dc.identifier.pmid","29535154"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/77706"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/25"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.relation","SFB 1190: Transportmaschinen und Kontaktstellen zellulärer Kompartimente"],["dc.relation","SFB 1190 | P04: Der GET-Rezeptor als ein Eingangstor zum ER und sein Zusammenspiel mit GET bodies"],["dc.relation.haserratum","/handle/2/102924"],["dc.relation.workinggroup","RG Schwappach (Membrane Protein Biogenesis)"],["dc.rights","CC BY 3.0"],["dc.title","Formation of COPI-coated vesicles at a glance"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","overview_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","134"],["dc.bibliographiccitation.issue","7631"],["dc.bibliographiccitation.journal","Nature"],["dc.bibliographiccitation.lastpage","138"],["dc.bibliographiccitation.volume","540"],["dc.contributor.author","Aviram, Naama"],["dc.contributor.author","Ast, Tslil"],["dc.contributor.author","Costa, Elizabeth A."],["dc.contributor.author","Arakel, Eric C."],["dc.contributor.author","Chuartzman, Silvia G."],["dc.contributor.author","Jan, Calvin H."],["dc.contributor.author","Haßdenteufel, Sarah"],["dc.contributor.author","Dudek, Johanna"],["dc.contributor.author","Jung, Martin"],["dc.contributor.author","Schorr, Stefan"],["dc.contributor.author","Zimmermann, Richard"],["dc.contributor.author","Schwappach, Blanche"],["dc.contributor.author","Weissman, Jonathan S."],["dc.contributor.author","Schuldiner, Maya"],["dc.date.accessioned","2018-04-23T11:49:05Z"],["dc.date.available","2018-04-23T11:49:05Z"],["dc.date.issued","2016"],["dc.description.abstract","In eukaryotes, up to one-third of cellular proteins are targeted to the endoplasmic reticulum, where they undergo folding, processing, sorting and trafficking to subsequent endomembrane compartments. Targeting to the endoplasmic reticulum has been shown to occur co-translationally by the signal recognition particle (SRP) pathway or post-translationally by the mammalian transmembrane recognition complex of 40 kDa (TRC40) and homologous yeast guided entry of tail-anchored proteins (GET) pathways. Despite the range of proteins that can be catered for by these two pathways, many proteins are still known to be independent of both SRP and GET, so there seems to be a critical need for an additional dedicated pathway for endoplasmic reticulum relay. We set out to uncover additional targeting proteins using unbiased high-content screening approaches. To this end, we performed a systematic visual screen using the yeast Saccharomyces cerevisiae and uncovered three uncharacterized proteins whose loss affected targeting. We suggest that these proteins work together and demonstrate that they function in parallel with SRP and GET to target a broad range of substrates to the endoplasmic reticulum. The three proteins, which we name Snd1, Snd2 and Snd3 (for SRP-independent targeting), can synthetically compensate for the loss of both the SRP and GET pathways, and act as a backup targeting system. This explains why it has previously been difficult to demonstrate complete loss of targeting for some substrates. Our discovery thus puts in place an essential piece of the endoplasmic reticulum targeting puzzle, highlighting how the targeting apparatus of the eukaryotic cell is robust, interlinked and flexible."],["dc.identifier.doi","10.1038/nature20169"],["dc.identifier.gro","3142487"],["dc.identifier.pmid","27905431"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/13639"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/3"],["dc.language.iso","en"],["dc.notes.intern","lifescience updates Crossref Import"],["dc.notes.status","final"],["dc.relation","SFB 1190: Transportmaschinen und Kontaktstellen zellulärer Kompartimente"],["dc.relation","SFB 1190 | P04: Der GET-Rezeptor als ein Eingangstor zum ER und sein Zusammenspiel mit GET bodies"],["dc.relation.issn","0028-0836"],["dc.relation.workinggroup","RG Schuldiner (Functional Genomics of Organelles)"],["dc.relation.workinggroup","RG Schwappach (Membrane Protein Biogenesis)"],["dc.title","The SND proteins constitute an alternative targeting route to the endoplasmic reticulum"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.peerReviewed","no"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","473"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Journal of Cell Science"],["dc.bibliographiccitation.lastpage","483"],["dc.bibliographiccitation.volume","126"],["dc.contributor.author","Powis, Katie"],["dc.contributor.author","Schrul, Bianca"],["dc.contributor.author","Tienson, Heather"],["dc.contributor.author","Gostimskaya, Irina"],["dc.contributor.author","Breker, Michal"],["dc.contributor.author","High, Stephen"],["dc.contributor.author","Schuldiner, Maya"],["dc.contributor.author","Jakob, Ursula"],["dc.contributor.author","Schwappach, Blanche"],["dc.date.accessioned","2017-09-07T11:48:18Z"],["dc.date.available","2017-09-07T11:48:18Z"],["dc.date.issued","2013"],["dc.description.abstract","The endomembrane system of yeast contains different tail-anchored proteins that are post-translationally targeted to membranes via their C-terminal transmembrane domain. This hydrophobic segment could be hazardous in the cytosol if membrane insertion fails, resulting in the need for energy-dependent chaperoning and the degradation of aggregated tail-anchored proteins. A cascade of GET proteins cooperates in a conserved pathway to accept newly synthesized tail-anchored proteins from ribosomes and guide them to a receptor at the endoplasmic reticulum, where membrane integration takes place. It is, however, unclear how the GET system reacts to conditions of energy depletion that might prevent membrane insertion and hence lead to the accumulation of hydrophobic proteins in the cytosol. Here we show that the ATPase Get3, which accommodates the hydrophobic tail anchor of clients, has a dual function: promoting tail-anchored protein insertion when glucose is abundant and serving as an ATP-independent holdase chaperone during energy depletion. Like the generic chaperones Hsp42, Ssa2, Sis1 and Hsp104, we found that Get3 moves reversibly to deposition sites for protein aggregates, hence supporting the sequestration of tail-anchored proteins under conditions that prevent tail-anchored protein insertion. Our findings support a ubiquitous role for the cytosolic GET complex as a triaging platform involved in cellular proteostasis."],["dc.identifier.doi","10.1242/jcs.112151"],["dc.identifier.gro","3142404"],["dc.identifier.isi","000316945600011"],["dc.identifier.pmid","23203805"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/10654"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/7908"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0021-9533"],["dc.rights","CC BY-NC-SA 3.0"],["dc.rights.uri","https://creativecommons.org/licenses/by-nc-sa/3.0"],["dc.title","Get3 is a holdase chaperone and moves to deposition sites for aggregated proteins when membrane targeting is blocked"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","400"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Kidney International"],["dc.bibliographiccitation.volume","60"],["dc.contributor.author","Zerangue, Noa"],["dc.contributor.author","Malan, Michael J."],["dc.contributor.author","Fried, Sharon R."],["dc.contributor.author","Dazin, Paul F."],["dc.contributor.author","Jan, Yuh Nung"],["dc.contributor.author","Jan, Lily Yeh"],["dc.contributor.author","Schwappach, Blanche"],["dc.date.accessioned","2022-03-01T11:46:17Z"],["dc.date.available","2022-03-01T11:46:17Z"],["dc.date.issued","2001"],["dc.identifier.doi","10.1046/j.1523-1755.2001.00821-6.x"],["dc.identifier.pii","S0085253815478718"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103615"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.issn","0085-2538"],["dc.title","Analysis of endoplasmic reticulum trafficking signals by combinatorial screening in mammalian cells"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]