Technical manual, operator and organizational manual : grader, road, motorized, DED, type 1, 6 wheel, 4 wheel drive, front wheel steering, 12-foot blade, Caterpillar model 120, FSN 3805-466-0084.

Includes index.

Die Schweriner Falschungen : Diplomatische Untersuchungen zur mecklenburgischen und pommerschen Geschichte im 12. und 13. Jahrhunder. Teil 1: Vier Falschungen aus der papstlicen Kanzlei.

Thesis (doctoral)--Georg-August-Universitat zu Gottingen.

Fragm. lat. II 34 - Biblia glossata (Dt 4,43 - 5,9; 12,15 - 13,16)

Trägerband: 'Spirae 3a Julii 1655'; Vorbesitzer: Stadtarchiv Frankfurt am Main

Ethane-1,2-diaminium 4,5-dichlorophthalate

In the structure of the title compound, C2H10N22+·C8H2Cl2O42-, the dications and dianions form hydrogen-bonded ribbon substructures which enclose conjoint cyclic R21(7), R12(7) and R42(8) associations and extend down the c-axis direction. These ribbons inter-associate down b, giving a two-dimensional sheet structure. In the dianions, one of the carboxylate groups is essentially coplanar with the benzene ring, while the other is normal to it [C-C-C-O torsion angles = 177.67 (12) and 81.94 (17)°, respectively].

Néstor-Guillermo Progeria Syndrome: a biochemical insight into Barrier-to-Autointegration Factor 1, alanine 12 threonine mutation

Background Premature aging syndromes recapitulate many aspects of natural aging and provide an insight into this phenomenon at a molecular and cellular level. The progeria syndromes appear to cause rapid aging through disruption of normal nuclear structure. Recently, a coding mutation (c.34G > A [p.A12T]) in the Barrier to Autointegration Factor 1 (BANF1) gene was identified as the genetic basis of Néstor-Guillermo Progeria syndrome (NGPS). This mutation was described to cause instability in the BANF1 protein, causing a disruption of the nuclear envelope structure. Results Here we demonstrate that the BANF1 A12T protein is indeed correctly folded, stable and that the observed phenotype, is likely due to the disruption of the DNA binding surface of the A12T mutant. We demonstrate, using biochemical assays, that the BANF1 A12T protein is impaired in its ability to bind DNA while its interaction with nuclear envelope proteins is unperturbed. Consistent with this, we demonstrate that ectopic expression of the mutant protein induces the NGPS cellular phenotype, while the protein localizes normally to the nuclear envelope. Conclusions Our study clarifies the role of the A12T mutation in NGPS patients, which will be of importance for understanding the development of the disease.