Saftig, Paul

[["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.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","897"],["dc.bibliographiccitation.issue","11"],["dc.bibliographiccitation.journal","Cell Biology International"],["dc.bibliographiccitation.lastpage","902"],["dc.bibliographiccitation.volume","27"],["dc.contributor.author","Schellens, JPM"],["dc.contributor.author","Saftig, P."],["dc.contributor.author","von Figura, Kurt"],["dc.contributor.author","Everts, V."],["dc.date.accessioned","2018-11-07T10:42:09Z"],["dc.date.available","2018-11-07T10:42:09Z"],["dc.date.issued","2003"],["dc.description.abstract","Transport of lysosomal enzymes is mediated by two mannose 6-phosphate receptors: a cation dependent (CD-MPR) and a cation independent receptor (CI-MPR). In the present study the effect of MPR-deficiency on the lysosomal system of neonatal mouse hepatocytes was studied by ultrastructural morphometric analyses. The volume density of the lysosomal system in hepatocytes of mice that lack both receptors was significantly increased in comparison with controls and with mice deficient for CI-MPR only. This higher volume density was due to a nine-fold increase of residual bodies. In CI-MPR-deficient mice the volume density of the lysosomal system was not different from controls and no increase of residual bodies was observed. It is concluded that in hepatocytes of MPR-deficient neonatal mice lysosomal storage occurs when both MPRs are lacking, whereas deficiency of CI-MPR only has no effect on the ultrastructure of the lysosomal system. (C) 2003 Elsevier Ltd. All rights reserved."],["dc.identifier.doi","10.1016/j.cellbi.2003.07.001"],["dc.identifier.isi","000186532600002"],["dc.identifier.pmid","14585283"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/46721"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Academic Press Ltd Elsevier Science Ltd"],["dc.relation.issn","1065-6995"],["dc.title","Deficiency of mannose 6-phosphate receptors and lysosomal storage: a morphometric analysis of hepatocytes of neonatal mice"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","3355"],["dc.bibliographiccitation.issue","9"],["dc.bibliographiccitation.journal","Molecular Biology of the Cell"],["dc.bibliographiccitation.lastpage","3368"],["dc.bibliographiccitation.volume","13"],["dc.contributor.author","Eskelinen, E. L."],["dc.contributor.author","Illert, A. L."],["dc.contributor.author","Tanaka, Y."],["dc.contributor.author","Schwarzmann, G."],["dc.contributor.author","Blanz, J."],["dc.contributor.author","von Figura, Kurt"],["dc.contributor.author","Saftig, P."],["dc.date.accessioned","2018-11-07T10:07:50Z"],["dc.date.available","2018-11-07T10:07:50Z"],["dc.date.issued","2002"],["dc.description.abstract","In LAMP-2-deficient mice autophagic vacuoles accumulate in many tissues, including liver, pancreas, muscle, and heart. Here we extend the phenotype analysis using cultured hepatocytes. In LAMP-2-deficient hepatocytes the half-life of both early and late autophagic vacuoles was prolonged as evaluated by quantitative electron microscopy. However, an endocytic tracer reached the autophagic vacuoles, indicating delivery of endo/lysosomal constituents to autophagic vacuoles. Enzyme activity measurements showed that the trafficking of some lysosomal enzymes to lysosomes was impaired.,Immunoprecipitation of metabolically labeled cathepsin D indicated reduced intracellular retention and processing in the knockout cells. The steady-state level of 300-kDa mannose 6-phosphate receptor was slightly lower in LAMP-2-deficient hepatocytes, whereas that of 46-kDa mannose 6-phosphate receptor was decreased to 30% of controls due to a shorter half-life. Less receptor was found in the Golgi region and in vesicles and tubules surrounding multivesicular endosomes, suggesting impaired recycling from endosomes to the Golgi. More receptor was found in autophagic vacuoles, which may explain its shorter half-life. Our data indicate that in hepatocytes LAMP-2 deficiency either directly or indirectly leads to impaired recycling of 46-kDa mannose 6-phosphate receptors and partial mistargeting of a subset of lysosomal enzymes. Autophagic vacuoles may accumulate due to impaired capacity for lysosomal degradation."],["dc.identifier.doi","10.1091/mbc.E02-02-0114"],["dc.identifier.isi","000178268300030"],["dc.identifier.pmid","12221139"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/39356"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Soc Cell Biology"],["dc.relation.issn","1059-1524"],["dc.title","Role of LAMP-2 in lysosome biogenesis and autophagy"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","6539"],["dc.bibliographiccitation.issue","28"],["dc.bibliographiccitation.journal","Journal of Neuroscience"],["dc.bibliographiccitation.lastpage","6549"],["dc.bibliographiccitation.volume","25"],["dc.contributor.author","D'Hooge, R."],["dc.contributor.author","Lullmann-Rauch, R."],["dc.contributor.author","Beckers, T."],["dc.contributor.author","Balschun, D."],["dc.contributor.author","Schwake, M."],["dc.contributor.author","Reiss, K."],["dc.contributor.author","von Figura, Kurt"],["dc.contributor.author","Saftig, P."],["dc.date.accessioned","2018-11-07T08:42:56Z"],["dc.date.available","2018-11-07T08:42:56Z"],["dc.date.issued","2005"],["dc.description.abstract","Mice with alpha-mannosidase gene inactivation provide an experimental model for alpha-mannosidosis, a lysosomal storage disease with severe neuropsychological and psychopathological complications. Neurohistological alterations in these mice were similar to those in patients and included vacuolations and axonal spheroids in the CNS and peripheral nervous system. Vacuolation was most prominent and evenly distributed in neuronal perikarya of the hippocampal CA2 and CA3 regions, whereas CA1 and dentate gyrus were weakly or not affected. Field potential recordings from CA1 region in hippocampal slices showed enhanced theta burst-induced long-term potentiation (LTP) in alpha-mannosidase-deficient mice. Longitudinal assessment in age-matched alpha-mannosidase-deficient and wild-type littermates, using an extended test battery, demonstrated a neurocognitive and psychotiform profile that may relate to the psychopathological alterations in clinical alpha-mannosidosis. Brainstem auditory-evoked potentials and basic neuromotor abilities were not impaired and did not deteriorate with age. Exploratory and conflict tests revealed consistent decreases in exploratory activity and emotional blunting in the knock-out group. alpha-Mannosidosis mice were also impaired in aversively motivated learning and acquisition of signal-shock associations. Acquisition and reversal learning in the water maze task, passive avoidance learning in the step-through procedure, as well as emotional response conditioning in an operant procedure were all impaired. Acquisition or shaping of an appetitive instrumental conditioning task was unchanged. Appetitive odor discrimination learning was only marginally impaired during shaping, whereas both the discrimination and reversal subtasks were normal. We propose that prominent storage and enhanced LTP in hippocampus have contributed to these specific behavioral alterations in alpha-mannosidase-deficient mice."],["dc.identifier.doi","10.1523/JNEUROSCI.0283-05.2005"],["dc.identifier.isi","000230478100007"],["dc.identifier.pmid","16014715"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/19824"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.relation.issn","0270-6474"],["dc.title","Neurocognitive and psychotiform behavioral alterations and enhanced hippocampal long-term potentiation in transgenic mice displaying neuropathological features of human alpha-mannosidosis"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1733"],["dc.bibliographiccitation.issue","11"],["dc.bibliographiccitation.journal","Journal of Clinical Investigation"],["dc.bibliographiccitation.lastpage","1745"],["dc.bibliographiccitation.volume","111"],["dc.contributor.author","Friedrich, Bianca"],["dc.contributor.author","Tepel, C."],["dc.contributor.author","Reinheckel, T."],["dc.contributor.author","Deussing, J. M."],["dc.contributor.author","von Figura, Kurt"],["dc.contributor.author","Herzog, V."],["dc.contributor.author","Peters, C."],["dc.contributor.author","Saftig, P."],["dc.contributor.author","Brix, K."],["dc.date.accessioned","2018-11-07T10:38:39Z"],["dc.date.available","2018-11-07T10:38:39Z"],["dc.date.issued","2003"],["dc.description.abstract","Thyroid function depends on processing of the prohormone thyroglobulin by sequential proteolytic events. From in vitro analysis it is known that cysteine proteinases mediate proteolytic processing of thyroglobulin. Here, we have analyzed mice with deficiencies in cathepsins B, K, L, B and K, or K and L in order to investigate which of the cysteine proteinases is most important for proteolytic processing of thyroglobulin in vivo. Immunolabeling demonstrated a rearrangement of the endocytic system and a redistribution of extracellularly located enzymes in thyroids of cathepsin-deficient mice. Cathepsin L was upregulated in thyroids of cathepsin K-/- or B-/-/K-/- mice, suggesting a compensation of cathepsin L for cathepsin K deficiency. Impaired proteolysis resulted in the persistence of thyroglobulin in the thyroids of mice with deficiencies in cathepsin B or L. The typical multilayered appearance of extracellularly stored thyroglobulin was retained in cathepsin K-/- mice only. These results suggest that cathepsins B and L are involved in the solubilization of thyroglobulin from its covalently cross-linked storage form. Cathepsin K-/-/L-/- mice had significantly reduced levels of free thyroxine, indicating that utilization of luminal thyroglobulin for thyroxine liberation is mediated by a combinatory action of cathepsins K and L."],["dc.identifier.doi","10.1172/JCI200315990"],["dc.identifier.isi","000183313400017"],["dc.identifier.pmid","12782676"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/45858"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.relation.issn","1558-8238"],["dc.relation.issn","0021-9738"],["dc.title","Thyroid functions of mouse cathepsins B, K, and L"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1713"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","American Journal Of Pathology"],["dc.bibliographiccitation.lastpage","1728"],["dc.bibliographiccitation.volume","167"],["dc.contributor.author","Koike, M."],["dc.contributor.author","Shibata, M."],["dc.contributor.author","Waguri, S."],["dc.contributor.author","Yoshimura, K."],["dc.contributor.author","Tanida, I."],["dc.contributor.author","Kominami, E."],["dc.contributor.author","Gotow, T."],["dc.contributor.author","Peters, C."],["dc.contributor.author","von Figura, Kurt"],["dc.contributor.author","Mizushima, N."],["dc.contributor.author","Saftig, P."],["dc.contributor.author","Uchiyama, Y."],["dc.date.accessioned","2018-11-07T10:53:39Z"],["dc.date.available","2018-11-07T10:53:39Z"],["dc.date.issued","2005"],["dc.description.abstract","In cathepsin D-deficient (CD-/-) and cathepsins B and L double-deficient (CB-/-CL-/-) mice, abnormal vacuolar structures accumulate in neurons of the brains. Many of these structures resemble autophagosomes in which part of the cytoplasm is retained but their precise nature and biogenesis remain unknown. We show here how autophagy contributes to the accumulation of these vacuolar structures in neurons deficient in cathepsin D or both cathepsins B and L by demonstrating an increased conversion of the molecular form of MAP1-LC3 for autophagosome formation from the cytosolic form (LC3-I) to the membrane-bound form (LC3-II). in both CD-/- and CB-/-CL-/- mouse brains, the membrane-bound LC3-II form predominated whereas MAP1-LC3 signals accumulated in granular structures located in neuronal perikarya and axons of these mutant brains and were localized to the membranes of autophagosomes, evidenced by immunofluorescence microscopy and freeze-fracture-replica immunoelectron microscopy. Moreover, as in CD-/- neurons, autofluorescence and subunit c of mitochondrial ATP synthase accumulated in CB-/-CL-/- neurons. This suggests that not only CD-/- but also CB-/-CL-/- mice could be useful animal models for neuronal ceroid-lipofuscinosis/Batten disease. These data strongly argue for a major involvement of autophagy in the pathogenesis of Batten disease/lysosomal storage disorders."],["dc.identifier.doi","10.1016/S0002-9440(10)61253-9"],["dc.identifier.isi","000233573600022"],["dc.identifier.pmid","16314482"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/49395"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Soc Investigative Pathology, Inc"],["dc.relation.issn","0002-9440"],["dc.title","Participation of autophagy in storage of lysosomes in neurons from mouse models of neuronal ceroid-lipofuscinoses (Batten disease)"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","37"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Trends in Molecular Medicine"],["dc.bibliographiccitation.lastpage","39"],["dc.bibliographiccitation.volume","7"],["dc.contributor.author","Saftig, P."],["dc.contributor.author","Tanaka, Y."],["dc.contributor.author","Lullmann-Rauch, R."],["dc.contributor.author","von Figura, Kurt"],["dc.date.accessioned","2018-11-07T09:40:13Z"],["dc.date.available","2018-11-07T09:40:13Z"],["dc.date.issued","2001"],["dc.description.abstract","Danon disease ('lysosomal glycogen storage disease with normal acid maltase') is characterized by a cardiomyopathy, myopathy and variable mental retardation. Mutations in the coding sequence of the lysosomal-associated membrane protein 2 (LAMP-2) were shown to cause a LAMP-2 deficiency in patients with Danon disease. LAMP-2 deficient mice manifest a similar vacuolar cardioskeletal myopathy. In addition to the patient reports LAMP-2 deficiency in mice causes pancreatic, hepatocytic, endothelial and leucocyte vacuolation. LAMP-2 deficient mice represent a valuable animal model of Danon disease. They will further be used to study the exact role of LAMP-P in autophagy and to analyse the consequences of an impaired autophagic pathway in various tissues."],["dc.identifier.doi","10.1016/S1471-4914(00)01868-2"],["dc.identifier.isi","000169932200010"],["dc.identifier.pmid","11427988"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/33461"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Elsevier Sci Ltd"],["dc.relation.issn","1471-4914"],["dc.title","Disease model: LAMP-2 enlightens Danon disease"],["dc.type","review"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","281"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Basic Research in Cardiology"],["dc.bibliographiccitation.lastpage","291"],["dc.bibliographiccitation.volume","101"],["dc.contributor.author","Stypmann, J."],["dc.contributor.author","Janssen, PML"],["dc.contributor.author","Prestle, J."],["dc.contributor.author","Engelen, M. A."],["dc.contributor.author","Kogler, Harald"],["dc.contributor.author","Lullmann-Rauch, R."],["dc.contributor.author","Eckardt, Lars"],["dc.contributor.author","von Figura, Kurt"],["dc.contributor.author","Landgrebe, J."],["dc.contributor.author","Mleczko, A."],["dc.contributor.author","Saftig, P."],["dc.date.accessioned","2018-11-07T09:33:52Z"],["dc.date.available","2018-11-07T09:33:52Z"],["dc.date.issued","2006"],["dc.description.abstract","Mutations in the highly glycosylated lysosome associated membrane protein-2 (LAMP-2) cause, as recently shown, familial Danon disease with mental retardation, mild myopathy and fatal cardiomyopathy. Extent and basis of the contractile dysfunction is not completely understood. In LAMP-2 deficient mice, we investigated cardiac function in vivo using Doppler-echocardiography and contractile function in vitro in isolated myocardial trabeculae. LAMP-2 deficient mice displayed reduced ejection fraction (EF) (58.9 +/- 3.4 vs. 80.7 +/- 5.1%, P < 0.05) and reduced cardiac output (8.3 +/- 3.1 vs. 14.7 +/- 3.6 ml/min, P < 0.05) as compared to wild-type controls. Isolated multicellular muscle preparations from LAMP-2 deficient mice confirmed depressed force development (3.2 +/- 0.6 vs. 8.4 +/- 0.9 mN/mm(2), P < 0.01). All groups showed similar force-frequency behaviour when normalised to baseline force. Post-rest potentiation was significantly depressed at intervals > 15 s in LAMP-2 deficient mice (P < 0.05). Although attenuated in absolute force development, the normalised inotropic response to increased calcium and beta-adrenoreceptor stimulation was unaltered. Electron microscopic analysis revealed autophagic vacuoles in LAMP-2 deficient cardiomyocytes. Protein analysis showed unaltered levels of SERCA2a, calsequestrin and phospholamban. Cardiac contractile function in LAMP-2 deficient mice as a model for Danon disease is significantly attenuated. The occurrence of autophagic vacuoles in LAMP-2 deficient myocytes is likely to be causal for the depressed contractile function resulting in an attenuated cardiac pump reserve."],["dc.identifier.doi","10.1007/s00395-006-0591-6"],["dc.identifier.isi","000238516400002"],["dc.identifier.pmid","16604439"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/32058"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Dr Dietrich Steinkopff Verlag"],["dc.relation.issn","0300-8428"],["dc.title","LAMP-2 deficient mice show depressed cardiac contractile function without significant changes in calcium handling"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","631"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","Human Molecular Genetics"],["dc.bibliographiccitation.lastpage","646"],["dc.bibliographiccitation.volume","12"],["dc.contributor.author","Gamp, A. C."],["dc.contributor.author","Tanaka, Y."],["dc.contributor.author","Lullmann-Rauch, R"],["dc.contributor.author","Wittke, D"],["dc.contributor.author","D'Hooge, R."],["dc.contributor.author","De Deyn, P. P."],["dc.contributor.author","Moser, Tobias"],["dc.contributor.author","Maier, H"],["dc.contributor.author","Hartmann, D."],["dc.contributor.author","Reiss, K"],["dc.contributor.author","Illert, A. L."],["dc.contributor.author","von Figura, K"],["dc.contributor.author","Saftig, Paul"],["dc.date.accessioned","2017-09-07T11:45:02Z"],["dc.date.available","2017-09-07T11:45:02Z"],["dc.date.issued","2003"],["dc.description.abstract","In previous overexpression studies we revealed a role for the lysosomal membrane protein LIMP-2/LGP85 in lysosomal biogenesis. LIMP-2-deficient mice show an increased postnatal mortality which is associated with a development of a uni- or bilateral hydronephrosis caused by an obstruction of the ureteropelvic junction. An accumulation of lysosomes in epithelial cells of the ureter adjacent to the ureteral lumen and a disturbed apical expression of uroplakin was observed, suggesting an impairment of membrane transport processes. Serious hearing impairment in LIMP-2-deficient animals was indicated by deficits in acoustic startle responses, in brainstem evoked auditory potentials and a reduced endochondral potential. LIMP-2-deficient mice suffer from a massive decline of spiral ganglia in the cochlea concomitant with that of the inner and outer hair cells. These pathological changes begin at the age of 3 months and are probably secondary to a degeneration of the stria vascularls. LIMP-2-deficient mice are also characterized, by a peripheral demyelinating neuropathy. Demyelinization was found to be associated with a massive loss of peripheral myelin proteins and an increased activity and expression of lysosomal proteins highlighting a hitherto unknown role of the lysosomal compartment in the development of this myelination disorder. The phenotype of LIMP-2-deficient mice stimulates the search for mutations in human disorders associated with degeneration of the stria vascularis and/or demyelinization of peripheral nerves."],["dc.identifier.doi","10.1093/hmg/ddg062"],["dc.identifier.gro","3144122"],["dc.identifier.isi","000181931000006"],["dc.identifier.pmid","12620969"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1711"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Oxford Univ Press"],["dc.relation.issn","0964-6906"],["dc.title","LIMP-2/LGP85 deficiency causes ureteric pelvic junction obstruction, deafness and peripheral neuropathy in mice"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]