Schmidt, Bernhard

[["dc.bibliographiccitation.firstpage","2343"],["dc.bibliographiccitation.issue","8"],["dc.bibliographiccitation.journal","The EMBO Journal"],["dc.bibliographiccitation.lastpage","2350"],["dc.bibliographiccitation.volume","7"],["dc.contributor.author","Pohlmann, Regina"],["dc.contributor.author","Krentler, Christiane"],["dc.contributor.author","Schmidt, Bernhard"],["dc.contributor.author","Schröder, Wolfgang"],["dc.contributor.author","Lorkowski, Gerhard"],["dc.contributor.author","Culley, Jan"],["dc.contributor.author","Mersmann, Guenther"],["dc.contributor.author","Geier, Carola"],["dc.contributor.author","Waheed, Abdul"],["dc.contributor.author","Gottschalk, Stephen"],["dc.contributor.author","Grzeschik, Karl-Heinz"],["dc.contributor.author","Hasilik, Andrej"],["dc.contributor.author","Figura, Kurt von"],["dc.date.accessioned","2019-07-10T08:12:44Z"],["dc.date.available","2019-07-10T08:12:44Z"],["dc.date.issued","1988"],["dc.description.abstract","A 2112-bp cDNA clone (λCT29) encoding the entire sequence of the human lysosomal acid phosphatase (EC 3.1.3.2) was isolated from a λgt11 human placenta cDNA library. The cDNA hybridized with a 2.3-kb mRNA from human liver and HL-60 promyelocytes. The gene for lysosomal acid phosphatase was localized to human chromosome 11. The cDNA includes a 12-bp 5' noncoding region, an open reading frame of 1269 bp and an 831-bp 3' non-coding region with a putative polyadenylation signal 25 bp upstream of a 3' poly(A) tract. The deduced amino acid sequence reveals a putative signal sequence of 30 amino acids followed by a sequence of 393 amino acids that contains eight potential glycosylation sites and a hydrophobic region, which could function as a transmembrane domain. A 60% homology between the known 23 N-terminal amino acid residues of human prostatic acid phosphatase and the N-terminal sequence of lysosomal acid phosphatase suggests an evolutionary link between these two phosphatases. Insertion of the cDNA into the expression vector pSVL yielded a construct that encoded enzymatically active acid phosphatase in transfected monkey COS cells."],["dc.format.mimetype","application/pdf"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?goescholar/3431"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/61020"],["dc.language.iso","en"],["dc.notes.intern","Migrated from goescholar"],["dc.publisher","Nature Publishing Group"],["dc.relation.issn","0261-4189"],["dc.rights","Goescholar"],["dc.rights.access","openAccess"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.subject","lysosomal acid hydrolyase; human chromosome 11"],["dc.subject.ddc","610"],["dc.title","Human lysosomal acid phosphatase: cloning, expression and chromosomal assignment"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","3497"],["dc.bibliographiccitation.issue","11"],["dc.bibliographiccitation.journal","The EMBO Journal"],["dc.bibliographiccitation.lastpage","3506"],["dc.bibliographiccitation.volume","9"],["dc.contributor.author","Peters, Christoph"],["dc.contributor.author","Braun, Martin"],["dc.contributor.author","Weber, Birgit"],["dc.contributor.author","Wendland, Martin"],["dc.contributor.author","Schmidt, Bernhard"],["dc.contributor.author","Pohlmann, Regina"],["dc.contributor.author","Waheed, Abdul"],["dc.contributor.author","Figura, Kurt von"],["dc.date.accessioned","2019-07-10T08:12:44Z"],["dc.date.available","2019-07-10T08:12:44Z"],["dc.date.issued","1990"],["dc.description.abstract","Lysosomal acid phosphatase (LAP) is synthesized as a transmembrane protein with a short carboxy-terminal cytoplasmic tail of 19 amino acids, and processed to a soluble protein after transport to lysosomes. Deletion of the membrane spanning domain and the cytoplasmic tail converts LAP to a secretory protein, while deletion of the cytoplasmic tail as well as substitution of tyrosine 413 within the cytoplasmic tail against phenylalanine causes accumulation at the cell surface. A chimeric polypeptide, in which the cytoplasmic tail of LAP was fused to the ectoplasmic and transmembrane domain of hemagglutinin is rapidly internalized and tyrosine 413 of the LAP tail is essential for internalization of the fusion protein. A chimeric polypeptide, in which the membrane spanning domain and cytoplasmic tail of LAP are fused to the ectoplasmic domain of the Mr 46 kd mannose 6-phosphate receptor, is rapidly transported to lysosomes, whereas wild type receptor is not transported to lysosomes. We conclude that a tyrosine containing endocytosis signal in the cytoplasmic tail of LAP is necessary and sufficient for targeting to lysosomes."],["dc.format.mimetype","application/pdf"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?goescholar/3435"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/61024"],["dc.language.iso","en"],["dc.notes.intern","Migrated from goescholar"],["dc.publisher","Nature Publishing Group"],["dc.relation.issn","0261-4189"],["dc.rights","Goescholar"],["dc.rights.access","openAccess"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.subject","endocytosis signal;intemalization; lysosomes; targeting"],["dc.subject.ddc","610"],["dc.title","Targeting of a lysosomal membrane protein: a tyrosine-containing endocytosis signal in the cytoplasmic tail of lysosomal acid phosphatase is necessary and sufficient for targeting to lysosomes"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2084"],["dc.bibliographiccitation.issue","8"],["dc.bibliographiccitation.journal","The EMBO Journal"],["dc.bibliographiccitation.lastpage","2091"],["dc.bibliographiccitation.volume","18"],["dc.contributor.author","Dierks, Thomas"],["dc.contributor.author","Lecca, M.Rita"],["dc.contributor.author","Schlotterhose, Petra"],["dc.contributor.author","Schmidt, Bernhard"],["dc.contributor.author","Figura, Kurt von"],["dc.date.accessioned","2019-07-10T08:12:46Z"],["dc.date.available","2019-07-10T08:12:46Z"],["dc.date.issued","1999"],["dc.description.abstract","Sulfatases carry at their catalytic site a unique posttranslational modification, an a-formylglycine residue that is essential for enzyme activity. Formylglycine is generated by oxidation of a conserved cysteine or, in some prokaryotic sulfatases, serine residue. In eukaryotes, this oxidation occurs in the endoplasmic reticulum during or shortly after import of the nascent sulfatase polypeptide. The modification of arylsulfatase A was studied in vitro and was found to be directed by a short linear sequence, CTPSR, starting with the cysteine to be modified. Mutational analyses showed that the cysteine, proline and arginine are the key residues within this motif, whereas formylglycine formation tolerated the individual, but not the simultaneous substitution of the threonine or serine. The CTPp. motif was transferred to a heterologous protein leading to low-efficient formylglycine formation. The efficiency reached control values when seven additional residues (AALLTGR) directly following the CTPSR motif in arylsulfatase A were present. Mutating up to four residues simultaneously within this heptamer sequence inhibited the modification only moderately. AALLTGR may, therefore, have an auxiliary function in presenting the core motif to the modifying enzyme. Within the two motifs, the key residues are fully, and other residues are highly conserved among all known members of the sulfatase family."],["dc.format.mimetype","application/pdf"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?goescholar/3445"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/61034"],["dc.language.iso","en"],["dc.notes.intern","Migrated from goescholar"],["dc.publisher","Nature Publishing Group"],["dc.relation.issn","0261-4189"],["dc.rights","Goescholar"],["dc.rights.access","openAccess"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.subject","cysteine; endoplasmic reticulum; multiple sulfatase deficiency; protein modification; sulfatase"],["dc.subject.ddc","610"],["dc.title","Sequence determinants directing conversion of cysteine to formylglycine in eukaryotic sulfatases"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","914"],["dc.bibliographiccitation.journal","American Journal of Human Genetics"],["dc.bibliographiccitation.lastpage","922"],["dc.bibliographiccitation.volume","58"],["dc.contributor.author","Stockler, Sylvia"],["dc.contributor.author","Isbrandt, Dirk"],["dc.contributor.author","Hanefeld, Folker"],["dc.contributor.author","Schmidt, Bernhard"],["dc.contributor.author","Figura, Kurt von"],["dc.date.accessioned","2019-07-10T08:12:46Z"],["dc.date.available","2019-07-10T08:12:46Z"],["dc.date.issued","1996"],["dc.description.abstract","In two children with an accumulation of guanidinoacetate in brain and a deficiency of creatine in blood, a severe deficiency of guanidinoacetate methyltransferase (GAMT) activity was detected in the liver. Two mutant GAMT alleles were identified that carried a single base substitution within a 5' splice site or a 13-nt insertion and gave rise to four mutant transcripts. Three of the transcripts encode truncated polypeptides that lack a residue known to be critical for catalytic activity of GAMT. Deficiency of GAMT is the first inborn error of creatine metabolism. It causes a severe developmental delay and extrapyramidal symptoms in early infancy and is treatable by oral substitution with creatine."],["dc.format.mimetype","application/pdf"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?goescholar/3442"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/61031"],["dc.language.iso","en"],["dc.notes.intern","Migrated from goescholar"],["dc.publisher","Cell Press"],["dc.relation.issn","0002-9297"],["dc.rights","Goescholar"],["dc.rights.access","openAccess"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.subject","Guanidinoacetate methyltransferase deficiency"],["dc.subject.ddc","610"],["dc.title","Guanidinoacetate methyltransferase deficiency: the first inborn error of creatine metabolism in man"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","15781"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Scientific Reports"],["dc.bibliographiccitation.volume","7"],["dc.contributor.author","Candiello, Ermes"],["dc.contributor.author","Mishra, Ratnakar"],["dc.contributor.author","Schmidt, Bernhard"],["dc.contributor.author","Jahn, Olaf"],["dc.contributor.author","Schu, Peter"],["dc.date.accessioned","2019-07-09T11:44:40Z"],["dc.date.available","2019-07-09T11:44:40Z"],["dc.date.issued","2017-11-17"],["dc.description.abstract","AP-1/σ1B-deficiency causes X-linked intellectual disability. AP-1/σ1B -/- mice have impaired synaptic vesicle recycling, fewer synaptic vesicles and enhanced endosome maturation mediated by AP-1/σ1A. Despite defects in synaptic vesicle recycling synapses contain two times more endocytic AP-2 clathrin-coated vesicles. We demonstrate increased formation of two classes of AP-2/clathrin coated vesicles. One which uncoats readily and a second with a stabilised clathrin coat. Coat stabilisation is mediated by three molecular mechanisms: reduced recruitment of Hsc70 and synaptojanin1 and enhanced μ2/AP-2 phosphorylation and activation. Stabilised AP-2 vesicles are enriched in the structural active zone proteins Git1 and stonin2 and synapses contain more Git1. Endocytosis of the synaptic vesicle exocytosis regulating Munc13 isoforms are differentially effected. Regulation of synaptic protein endocytosis by the differential stability of AP-2/clathrin coats is a novel molecular mechanism of synaptic plasticity."],["dc.identifier.doi","10.1038/s41598-017-16055-4"],["dc.identifier.pmid","29150658"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/14858"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/59063"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.relation.issn","2045-2322"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.subject.ddc","610"],["dc.title","Differential regulation of synaptic AP-2/clathrin vesicle uncoating in synaptic plasticity."],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","271"],["dc.bibliographiccitation.journal","Cell"],["dc.bibliographiccitation.lastpage","278"],["dc.bibliographiccitation.volume","82"],["dc.contributor.author","Schmidt, Bernhard"],["dc.contributor.author","Selmer, Thorsten"],["dc.contributor.author","Ingendoh, Arnd"],["dc.contributor.author","Figura, Kurt von"],["dc.date.accessioned","2019-07-10T08:12:46Z"],["dc.date.available","2019-07-10T08:12:46Z"],["dc.date.issued","1995"],["dc.description.abstract","Multiple sulfatase deficiency (MSD) is a lysosomal storage disorder characterized by a decreased activity of all known sulfatases. The deficiency of sulfatases was proposed to result from the lack of a co- or posttranslational modification that is common to all sulfatases and required for their catalytic activity. Structural analysis of two catalytically active sulfatases revealed that a cysteine residue that is predicted from the cDNA sequence and conserved among all known sulfatases is replaced by a 2-amino-3-oxopropionic acid residue, while in sulfatases derived from Mp. cells, this cysteine residue is retained. It is proposed that the co- or posttranslational conversion of a cysteine to 2-amino- 3-oxopropionic acid is required for generating catalytically active sulfatases and that deficiency of this protein modification is the cause of MSD."],["dc.format.mimetype","application/pdf"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?goescholar/3441"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/61030"],["dc.language.iso","en"],["dc.notes.intern","Migrated from goescholar"],["dc.publisher","Cell Press"],["dc.relation.issn","0092-8674"],["dc.rights","Goescholar"],["dc.rights.access","openAccess"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.subject","novel amino acid modification"],["dc.subject.ddc","610"],["dc.title","A novel amino acid modification in sulfatases that is defective in multiple sulfatase deficiency"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","4391"],["dc.bibliographiccitation.issue","12"],["dc.bibliographiccitation.journal","The EMBO Journal"],["dc.bibliographiccitation.lastpage","4399"],["dc.bibliographiccitation.volume","11"],["dc.contributor.author","Lehmann, Lutz E."],["dc.contributor.author","Eberle, Wolfgang"],["dc.contributor.author","Krull, Sabine"],["dc.contributor.author","Prill, Volkmar"],["dc.contributor.author","Schmidt, Bernhard"],["dc.contributor.author","Sander, Chris"],["dc.contributor.author","Figura, Kurt von"],["dc.contributor.author","Peters, Christoph"],["dc.date.accessioned","2019-07-10T08:12:45Z"],["dc.date.available","2019-07-10T08:12:45Z"],["dc.date.issued","1992"],["dc.description.abstract","Lysosomal acid phosphatase (LAP) is rapidly internalized from the cell surface due to a tyrosine-containing internalization signal in its 19 amino acid cytoplasmic tail. Measuring the internalization of a series of LAP cytoplasmic tail truncation and substitution mutants revealed that the N-terminal 12 amino acids of the cytoplasmic tail are sufficient for rapid endocytosis and that the hexapeptide 411-PGYRHV416 is the tyrosinecontaining internalization signal. Truncation and substitution mutants of amino acid residues following Val416 can prevent internalization even though these residues do not belong to the internalization signal. It was shown recently that part of the LAP cytoplasmic tail peptide corresponding to 410-PPGY413 forms a wellordered β turn structure in solution. Two-dimensional NNMR spectroscopy of two modified LAP tail peptides, in which the single tyrosine was substituted either by phenylalanine or by alanine, revealed that the tendency to form a β turn is reduced by 25% in the phenylalaninecontaining peptide and by ~ 50% in the alaninecontaining mutant peptide. Our results suggest, that in the short cytoplasmic tail of LAP tyrosine is required for stabilization of the tight turn and that the aromatic ring system of the tyrosine residue is a contact point to the putative cytoplasmic receptor."],["dc.format.mimetype","application/pdf"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?goescholar/3439"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/61028"],["dc.language.iso","en"],["dc.notes.intern","Migrated from goescholar"],["dc.publisher","Nature Publishing Group"],["dc.relation.issn","0261-4189"],["dc.rights","Goescholar"],["dc.rights.access","openAccess"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.subject","2D-NMR; endocytosis; internalization signal; lysosomal acid phosphatase"],["dc.subject.ddc","610"],["dc.title","The internalization signal in the cytoplasmic tail of lysosomal acid phosphatase consists of the hexapeptide PGYRHV"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","435"],["dc.bibliographiccitation.journal","Cell"],["dc.bibliographiccitation.lastpage","444"],["dc.bibliographiccitation.volume","113"],["dc.contributor.author","Dierks, Thomas"],["dc.contributor.author","Schmidt, Bernhard"],["dc.contributor.author","Borissenko, Ljudmila V."],["dc.contributor.author","Peng, Jianhe"],["dc.contributor.author","Preusser, Andrea"],["dc.contributor.author","Mariappan, Malaiyalam"],["dc.contributor.author","Figura, Kurt von"],["dc.date.accessioned","2019-07-10T08:12:47Z"],["dc.date.available","2019-07-10T08:12:47Z"],["dc.date.issued","2003"],["dc.description.abstract","Cα-formylglycine (FGly) is the catalytic residue in the active site of eukaryotic sulfatases. It is posttranslationally generated from a cysteine in the endoplasmic reticulum. The genetic defect of FGly formation causes multiple sulfatase deficiency (MSD), a lysosomal storage disorder. We purified the FGly generating enzyme (FGE) and identified its gene and nine mutations in seven Mp. patients. In patient fibroblasts, the activity of sulfatases is partially restored by transduction of FGE encoding cDNA, but not by cDNA carrying an MSD mutation. The gene encoding FGE is highly conserved among pro- and eukaryotes and has a paralog of unknown function in vertebrates. FGE is localized in the endoplasmic reticulum and is predicted to have a tri-partite domain structure."],["dc.format.mimetype","application/pdf"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?goescholar/3451"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/61038"],["dc.language.iso","en"],["dc.notes.intern","Migrated from goescholar"],["dc.publisher","Cell Press"],["dc.relation.issn","0092-8674"],["dc.rights","Goescholar"],["dc.rights.access","openAccess"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.subject","multiple sulfatase deficiency; gene mutation; Cα-Formylglycine generating enzyme"],["dc.subject.ddc","610"],["dc.title","Multiple sulfatase deficiency is caused by mutations in the gene encoding the human Cα-Formylglycine generating enzyme"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]