Figura, Kurt von

[["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","710"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Biochimica et Biophysica Acta (BBA) - Molecular Cell Research"],["dc.bibliographiccitation.lastpage","725"],["dc.bibliographiccitation.volume","1793"],["dc.contributor.author","Dierks, Thomas"],["dc.contributor.author","Schlotawa, Lars"],["dc.contributor.author","Frese, Marc-Andre"],["dc.contributor.author","Radhakrishnan, Karthikeyan"],["dc.contributor.author","von Figura, Kurt"],["dc.contributor.author","Schmidt, Bernhard"],["dc.date.accessioned","2018-11-07T08:30:52Z"],["dc.date.available","2018-11-07T08:30:52Z"],["dc.date.issued","2009"],["dc.description.abstract","Multiple sulfatase deficiency (MSD), mucolipidosis (MIL) II/III and Niemann-Pick type C1 (NPC1) disease are rare but fatal lysosomal storage disorders caused by the genetic defect of non-lysosomal proteins. The NPC1 protein mainly localizes to late endosomes and is essential for cholesterol redistribution from endocytosed LDL to cellular membranes. NPC1 deficiency leads to lysosomal accumulation of a broad range of lipids. The precise functional mechanism of this membrane protein, however, remains puzzling. ML II, also termed I cell disease. and the less severe ML III result from deficiencies of the Golgi enzyme N-acetylglucosamine 1-phosphotransferase leading to a global defect of lysosome biogenesis. In patient cells, newly synthesized lysosomal proteins are not equipped with the critical lysosomal trafficking marker mannose 6-phosphate, thus escaping from lysosomal sorting at the trans Golgi network. MSD affects the entire sulfatase family, at least seven members of which are lysosomal enzymes that are specifically involved in the degradation of sulfated glycosaminoglycans, sulfolipids or other sulfated molecules. The combined deficiencies of all sulfatases result from a defective post-translational modification by the ER-localized formylglycine-generating enzyme (FGE), which oxidizes a specific cysteine residue to formylglycine, the catalytic residue enabling a unique mechanism of sulfate ester hydrolysis. This review gives an update on the molecular bases of these enigmatic diseases, which have been challenging researchers since many decades and so far led to a number of surprising findings that give deeper insight into both the cell biology and the pathobiochemistry underlying these complex disorders. In case of MSD, considerable progress has been made in recent years towards an understanding of disease-causing FGE mutations. First approaches to link molecular parameters with clinical manifestation have been described and even therapeutical options have been addressed. Further. the discovery of FGE as an essential sulfatase activating enzyme has considerable impact on enzyme replacement or gene therapy of lysosomal storage disorders caused by single sulfatase deficiencies. (C) 2008 Elsevier B.V. All rights reserved."],["dc.identifier.doi","10.1016/j.bbamcr.2008.11.015"],["dc.identifier.isi","000265369800011"],["dc.identifier.pmid","19124046"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/16996"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Elsevier Science Bv"],["dc.relation.issn","0167-4889"],["dc.title","Molecular basis of multiple sulfatase deficiency, mucolipidosis II/III and Niemann-Pick C1 disease - Lysosomal storage disorders caused by defects of non-lysosomal proteins"],["dc.type","review"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["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.journal","Journal of Bone and Mineral Research"],["dc.bibliographiccitation.volume","16"],["dc.contributor.author","Everts, V."],["dc.contributor.author","Suter, A."],["dc.contributor.author","von Figura, Kurt"],["dc.contributor.author","Beertsen, W."],["dc.contributor.author","Saftig, P."],["dc.date.accessioned","2018-11-07T08:42:46Z"],["dc.date.available","2018-11-07T08:42:46Z"],["dc.date.issued","2001"],["dc.format.extent","S451"],["dc.identifier.isi","000170709001316"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/19779"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Soc Bone & Mineral Res"],["dc.publisher.place","Washington"],["dc.relation.issn","0884-0431"],["dc.title","Acid phosphatase deficiency leads to accumulation of osteopontin in the subosteoclastic resorption area."],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","541"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Cell"],["dc.bibliographiccitation.lastpage","552"],["dc.bibliographiccitation.volume","121"],["dc.contributor.author","Dierks, T."],["dc.contributor.author","Dickmanns, A."],["dc.contributor.author","Preusser-Kunze, A."],["dc.contributor.author","Schmidt, Bernhard"],["dc.contributor.author","Mariappan, M."],["dc.contributor.author","Von Figura, K."],["dc.contributor.author","Ficner, R."],["dc.contributor.author","Rudolph, M."],["dc.date.accessioned","2017-09-07T11:54:25Z"],["dc.date.available","2017-09-07T11:54:25Z"],["dc.date.issued","2005"],["dc.description.abstract","Sulfatases are enzymes essential for degradation and remodeling of sulfate esters. Formylglycine (FGly), the key catalytic residue in the active site, is unique to sulfatases. In higher eukaryotes, FGly is generated from a cysteine precursor by the FGly-generating enzyme (FGE). Inactivity of FGE results in multiple sulfatase deficiency (MSD), a fatal autosomal recessive syndrome. Based on the crystal structure, we report that FGE is a single-domain monomer with a surprising paucity of secondary structure and adopts a unique fold. The effect of all 18 missense mutations found in MSD patients is explained by the FGE structure, providing a molecular basis of MSD. The catalytic mechanism of FGly generation was elucidated by six high-resolution structures of FGE in different redox environments. The structures allow formulation of a novel oxygenase mechanism whereby FGE utilizes molecular oxygen to generate FGly via a cysteine sulfenic acid intermediate."],["dc.identifier.doi","10.1016/j.cell.2005.03.001"],["dc.identifier.gro","3143846"],["dc.identifier.isi","000229331200011"],["dc.identifier.pmid","15907468"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?goescholar/3452"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1405"],["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","0092-8674"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Molecular basis for multiple sulfatase deficiency and mechanism for formylglycine generation of the human formylglycine-generating enzyme"],["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"]]

[["dc.bibliographiccitation.firstpage","5615"],["dc.bibliographiccitation.issue","15"],["dc.bibliographiccitation.journal","Molecular and Cellular Biology"],["dc.bibliographiccitation.lastpage","5620"],["dc.bibliographiccitation.volume","26"],["dc.contributor.author","Thiel, Christian"],["dc.contributor.author","Luebke, Torben"],["dc.contributor.author","Matthijs, Gert"],["dc.contributor.author","von Figura, Kurt"],["dc.contributor.author","Koerner, Christian"],["dc.date.accessioned","2018-11-07T09:30:01Z"],["dc.date.available","2018-11-07T09:30:01Z"],["dc.date.issued","2006"],["dc.description.abstract","Mutations in the cytosolic enzyme phosphomannomutase.2 (PMM2), which catalyzes the conversion of mannose-6-phosphate to mannose-l-phosphate, cause the most common form of congenital disorders of glycosylation, termed CDG-Ia. It is an inherited multisystemic disease with severe neurological impairment. To study the pathophysiology of CDG-Ia and to investigate possible therapeutic approaches, we generated a mouse model for CDG-Ia by targeted disruption of the Pmm2 gene. Heterozygous mutant mice appeared normal in development, gross anatomy, and fertility. In contrast, embryos homozygous for the Pmm2-null allele were recovered in embryonic development at days 2.5 to 3.5. These results indicate that Pmm2 is essential for early development of mice. Mating experiments of heterozygous mice with wild-type mice could further show that transmission of the female Pmm2-null allele is impaired."],["dc.identifier.doi","10.1128/MCB.02391-05"],["dc.identifier.isi","000239286600007"],["dc.identifier.pmid","16847317"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/31202"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Soc Microbiology"],["dc.relation.issn","0270-7306"],["dc.title","Targeted disruption of the mouse phosphomannomutase 2 gene causes early embryonic lethality"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Acta Paediatrica"],["dc.bibliographiccitation.volume","96"],["dc.contributor.author","von Figura, Kurt"],["dc.date.accessioned","2018-11-07T11:03:18Z"],["dc.date.available","2018-11-07T11:03:18Z"],["dc.date.issued","2007"],["dc.format.extent","5"],["dc.identifier.doi","10.1111/j.1651-2227.2007.00197.x"],["dc.identifier.isi","000245177900002"],["dc.identifier.pmid","17391431"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/51586"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Blackwell Publishing"],["dc.relation.issn","0803-5253"],["dc.title","Structure-function relationship for lysosomal enzymes"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.subtype","letter_note"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Neurobiology of Aging"],["dc.bibliographiccitation.volume","23"],["dc.contributor.author","Hartmann, Daniel"],["dc.contributor.author","De Strooper, B."],["dc.contributor.author","Serneels, L."],["dc.contributor.author","Craessaerts, K."],["dc.contributor.author","Herreman, A."],["dc.contributor.author","Annaert, W."],["dc.contributor.author","Brabant, V."],["dc.contributor.author","Luebke, Torben"],["dc.contributor.author","Illert, A. L."],["dc.contributor.author","von Figura, Kurt"],["dc.contributor.author","Saftig, P."],["dc.date.accessioned","2018-11-07T10:23:07Z"],["dc.date.available","2018-11-07T10:23:07Z"],["dc.date.issued","2002"],["dc.format.extent","S183"],["dc.identifier.isi","000177465300670"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/42396"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Elsevier Science Inc"],["dc.publisher.place","New york"],["dc.relation.issn","0197-4580"],["dc.title","Deficiency for the disintegrin metalloprotease ADAM10 causes disturbed alpha-secretase function and a notch deficiency-related phenotype in mice"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","681"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","The EMBO Journal"],["dc.bibliographiccitation.lastpage","686"],["dc.bibliographiccitation.volume","8"],["dc.contributor.author","Braulke, T."],["dc.contributor.author","Tippmer, S."],["dc.contributor.author","Neher, Erwin"],["dc.contributor.author","von Figura, K."],["dc.date.accessioned","2022-03-01T11:45:56Z"],["dc.date.available","2022-03-01T11:45:56Z"],["dc.date.issued","1989"],["dc.identifier.doi","10.1002/j.1460-2075.1989.tb03426.x"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103506"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.issn","0261-4189"],["dc.title","Regulation of the mannose 6-phosphate/IGF II receptor expression at the cell surface by mannose 6-phosphate, insulin like growth factors and epidermal growth factor."],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","18"],["dc.bibliographiccitation.journal","New England Journal of Medicine"],["dc.bibliographiccitation.lastpage","22"],["dc.bibliographiccitation.volume","324"],["dc.contributor.author","Polten, Andreas"],["dc.contributor.author","Fluharty, Arvan L."],["dc.contributor.author","Fluharty, Claire B."],["dc.contributor.author","Kappler, Joachim"],["dc.contributor.author","Figura, Kurt von"],["dc.contributor.author","Gieselmann, Volkmar"],["dc.date.accessioned","2019-07-10T08:12:45Z"],["dc.date.available","2019-07-10T08:12:45Z"],["dc.date.issued","1991"],["dc.description.abstract","Metachromatic leukodystrophy is an autosomal recessive inherited lysosomal storage disorder caused by a deficiency of arylsulfatase A. Three forms of the disease can be distinguished according to severity and the age at onset: late infantile (1 to 2 years), juvenile (3 to 16), and adult (> 16)."],["dc.format.mimetype","application/pdf"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?goescholar/3437"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/61026"],["dc.language.iso","en"],["dc.notes.intern","Migrated from goescholar"],["dc.publisher","Massachusetts Medical Society"],["dc.relation.issn","0028-4793"],["dc.rights","Goescholar"],["dc.rights.access","openAccess"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.subject","metachromatic leukodystrophy"],["dc.subject.ddc","610"],["dc.title","Molecular basis of different forms of metachromatic leukodystrophy"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]