[Jewish citizens in Oberbrechen 1711-1941].

This collection contains a partial translation by Justin J. Mueller of "Jüdische Mitbürger in Oberbrechen 1711-1941" by Eugen Caspary, 1975. Caspary's work appeared in a volume entitled "Geschichte von Oberbrechen" by Hellmuth Gensicke and Egon Eichhorn, 1975. The translation deals mainly with the named inhabitants of Oberbrechen, augmented by personal and family histories. Surnames include: Stern family, Besmann family, Blumenthal famil, Liechtenstein family.Processed for digitizatio

Hermann Stern (1887-1981) : Lives as examples of Jewish migration in the 20th century /

English translation by Justin J. Mueller of part of an article by Eugen Caspary, describing Hermann Stern's life. A copy of the original article is included in this folder.The original article was published in: Caspary, Eugen : Limburg-Weilburg. Beitraege zur Geschichte des Kreises Limburg/Lahn, Landkreis Limburg-Weilburg, 1986, LBI Library call number DD 901 L69 L5.Hermann Stern (1887-1981), a descendant of a Jewish family that lived in Oberbrechen since at least at the end of the 18th century, emigrated to the United States in 1903. He settled in North Dakota, and managed successfully a chain of mean's wear shops, a business owned by his uncle M.G. Strauss, who originally was from Heringen. During 1933-1945 he enabled over 100 Jewish families to emigrate to the United States.digitize

Jüdisches Jahrbuch für Groß-Berlin : ein Wegweiser durch die jüdischen Einrichtungen und Organisationen Berlins /

"Jüdisches Jahrbuch" was a yearbook published for the Berlin Jewish community. The "Jahrbuch" was a guidebook to Jewish organizations and establishments in Germany and in Berlin in particular. It included an index of Jewish clubs and societies, contact information for Jewish communities in other German cities, and lists of Jewish newspapers along with other valuable information. Issues of the "Jahrbuch" also included a literary part in which authors wrote on the history of the Jewish community or about contemporary Jewish topics.[1. Ausg.] (1926): Stamp "Cosman Werner Bibliothek" on title page, with "Cancelled" stamp over it.2. Ausgage (1928): Stamp "der Jüdischen Gemeinde Spandau" on title page.[Vol.] (1929): Bookplate on inside cover "Eigentum der Bibliothek des Rabbiner-Seminars zu Berlin, Geschenk von Rabb. Dr. Artur Liebermann im Jahre 1930"; Stamp on title page "Rabbiner-Seminar zu Berlin".[Vol.] (1930): Stamp on title page "Bibliothek der Synagogen-Gemeinde zu Liegnitz".[Vol.] (1931): Stamp on title page "Bibliothek der Synagogen-Gemeinde zu Liegnitz".[Vol.] (1932): Stamp on half-title page "Rabbiner-Seminar zu Berlin".Recataloging - edited record, edited item recordDescription based on: [1. Ausg.] (1926)Lastest issue consulted: [Vol.] (1932)CATALOGING COMPLETE 20180424. Information verified against digital surrogates.Digital imageDescription based on print version record

Origin of spectral red-shift and polarization patterns of self-assembled InGaN nanostructures on GaN nanowires

The luminescence of InxGa1 amp; 8722;xN nanowires NWs is frequently reported with large red shifts as compared to the theoretical value expected from the average In content. Both compositional fluctuations and radial built in fields were considered accountable for this effect, depending on the size, structure, composition, and surrounding medium of the NWs. In the present work, the emission properties of InGaN GaN NWs grown by plasma assisted molecular beam epitaxy are investigated in a comprehensive study combining ultraviolet Raman and photoluminescence spectroscopy PL on vertical arrays, polarization dependent PL on bundles of a few NWs, scanning transmission electron microscopy, energy dispersive X ray spectroscopy, and calculations of the band profiles. The roles of inhomogeneous In distribution and radial fields in the context of optical emission properties are addressed. The radial built in fields are found to be modest, with a maximum surface band bending below 350 meV. On the other hand, variations in the local In content have been observed that give rise to potential fluctuations whose impact on the emission properties is shown to prevail over band bending effects. Two luminescence bands with large positive and moderate negative polarization ratios of amp; 8776; 80 and amp; 8804; amp; 8722;60 , respectively, were observed. The red shift in the luminescence is associated with In rich inclusions in the NWs due to thermodynamic decomposition during growth. The negative polarization anisotropy is suggested to result from spontaneously formed superlattices in the In rich regions of the NWs. The NWs show a preferred orthogonal absorption due to the dielectric boundary conditions and highlight the extreme sensitivity of these structures towards light polarizatio

A novel homozygous ARL13B variant in patients with Joubert syndrome impairs its guanine nucleotide-exchange factor activity

ARL13B encodes for the ADP-ribosylation factor-like 13B GTPase, which is required for normal cilia structure and Sonic hedgehog (Shh) signaling. Disruptions in cilia structure or function lead to a class of human disorders called ciliopathies. Joubert syndrome is characterized by a wide spectrum of symptoms, including a variable degree of intellectual disability, ataxia, and ocular abnormalities. Here we report a novel homozygous missense variant c.[223G>A] (p.(Gly75Arg) in the ARL13B gene, which was identified by whole-exome sequencing of a trio from a consanguineous family with multiple-affected individuals suffering from intellectual disability, ataxia, ocular defects, and epilepsy. The same variant was also identified in a second family. We saw a striking difference in the severity of ataxia between affected male and female individuals in both families. Both ARL13B and ARL13B-c.[223G>A] (p.(Gly75Arg) expression rescued the cilia length and Shh defects displayed by Arl13b hennin (null) cells, indicating that the variant did not disrupt either ARL13B function. In contrast, ARL13B-c.[223G>A] (p.(Gly75Arg) displayed a marked loss of ARL3 guanine nucleotide-exchange factor activity, with retention of its GTPase activities, highlighting the correlation between its loss of function as an ARL3 guanine nucleotide-exchange factor and Joubert syndrome

Mutations in INPP5E, encoding inositol polyphosphate-5-phosphatase E, link phosphatidyl inositol signaling to the ciliopathies.

Phosphotidylinositol (PtdIns) signaling is tightly regulated both spatially and temporally by subcellularly localized PtdIns kinases and phosphatases that dynamically alter downstream signaling events. Joubert syndrome is characterized by a specific midbrain-hindbrain malformation ('molar tooth sign'), variably associated retinal dystrophy, nephronophthisis, liver fibrosis and polydactyly and is included in the newly emerging group of 'ciliopathies'. In individuals with Joubert disease genetically linked to JBTS1, we identified mutations in the INPP5E gene, encoding inositol polyphosphate-5-phosphatase E, which hydrolyzes the 5-phosphate of PtdIns(3,4,5)P3 and PtdIns(4,5)P2. Mutations clustered in the phosphatase domain and impaired 5-phosphatase activity, resulting in altered cellular PtdIns ratios. INPP5E localized to cilia in major organs affected by Joubert syndrome, and mutations promoted premature destabilization of cilia in response to stimulation. These data link PtdIns signaling to the primary cilium, a cellular structure that is becoming increasingly recognized for its role in mediating cell signals and neuronal function.Journal ArticleResearch Support, N.I.H. ExtramuralResearch Support, Non-U.S. Gov'tSCOPUS: ar.jinfo:eu-repo/semantics/publishe

CEP41 is mutated in Joubert syndrome and is required for tubulin glutamylation at the cilium

Tubulin glutamylation is a post-translational modification that occurs predominantly in the ciliary axoneme and has been suggested to be important for ciliary function. However, its relationship to disorders of the primary cilium, termed ciliopathies, has not been explored. Here we mapped a new locus for Joubert syndrome (JBTS), which we have designated as JBTS15, and identified causative mutations in CEP41, which encodes a 41-kDa centrosomal protein. We show that CEP41 is localized to the basal body and primary cilia, and regulates ciliary entry of TTLL6, an evolutionarily conserved polyglutamylase enzyme. Depletion of CEP41 causes ciliopathy-related phenotypes in zebrafish and mice and results in glutamylation defects in the ciliary axoneme. Our data identify CEP41 mutations as a cause of JBTS and implicate tubulin post-translational modification in the pathogenesis of human ciliary dysfunction