The search campaign to identify and Image the Philae Lander on the surface of comet 67P/Churyumov-Gerasimenko

On the 12th of November 2014, the Rosetta Philae Lander descended to make the first soft touchdown on the surface of a comet – comet 67P/Churyumov- Gerasimenko. That soft touchdown did occur but due to the failure in the firing of its two harpoons, Philae bounced and travelled across the comet making contact with the surface twice more before finally landing in a shaded rocky location somewhere on the southern hemisphere of the comet. The search campaign, led by ESA, involved multiple teams across Europe with a wide range of techniques used in support of it. This search campaign would continue through 2015 where a prime candidate on the surface was identified and on into 2016 to end on the 2nd of September 2016 when a definitive and conclusive image was taken of the lander on the surface of the comet, confirming the prime candidate to indeed be Philae

Crystal structure of avian carboxypeptidase D domain II: a prototype for the regulatory metallocarboxypeptidase subfamily

10 pages, 4 figures, 1 table.-- PMID: 10545093 [PubMed].-- PMCID: PMC1171647.The crystal structure of domain II of duck carboxypeptidase D, a prohormone/propeptide processing enzyme integrated in a three repeat tandem in the natural system, has been solved, constituting a prototype for members of the regulatory metallocarboxypeptidase subfamily. It displays a 300 residue N-terminal a/b-hydrolase subdomain with overall topological similarity to and general coincidence of the key catalytic residues with the archetypal pancreatic carboxypeptidase A. However, numerous significant insertions/deletions in segments forming the funnel-like access to the active site explain differences in specificity towards larger protein substrates or inhibitors. This a/bhydrolase subdomain is followed by a C-terminal 80 residue b-sandwich subdomain, unique for these regulatory metalloenzymes and topologically related to transthyretin and sugar-binding proteins. The structure described here establishes the fundamentals for a better understanding of the mechanism ruling events such as prohormone processing and will enable modelling of regulatory carboxypeptidases as well as a more rational design of inhibitors of carboxypeptidase D.This work was supported by grants PB95-0224 and BIO98-0362 from the Ministerio de Educación y Cultura (Spain), by grant 1997SGR-275 and the Centre de Referència en Biotecnologia, both from the Generalitat de Catalunya, by grant DK-51271 from the National Institutes of Health and by the US–Spain Science & Technology Program, 1999. The support provided by the TMR/LSF programme to the EMBL Hamburg Outstation (ref. ERBFMGECT980134) is gratefully acknowledged.Peer reviewe

Crystal structure of avian carboxypeptidase D domain II: a prototype for the regulatory metallocarboxypeptidase subfamily.

The crystal structure of domain II of duck carboxypeptidase D, a prohormone/propeptide processing enzyme integrated in a three repeat tandem in the natural system, has been solved, constituting a prototype for members of the regulatory metallocarboxypeptidase subfamily. It displays a 300 residue N-terminal alpha/beta-hydrolase subdomain with overall topological similarity to and general coincidence of the key catalytic residues with the archetypal pancreatic carboxypeptidase A. However, numerous significant insertions/deletions in segments forming the funnel-like access to the active site explain differences in specificity towards larger protein substrates or inhibitors. This alpha/beta-hydrolase subdomain is followed by a C-terminal 80 residue beta-sandwich subdomain, unique for these regulatory metalloenzymes and topologically related to transthyretin and sugar-binding proteins. The structure described here establishes the fundamentals for a better understanding of the mechanism ruling events such as prohormone processing and will enable modelling of regulatory carboxypeptidases as well as a more rational design of inhibitors of carboxypeptidase D

Documentació relativa al canvi de la propietat del teatre després de la incautació de 1936 per part de la Generalitat

Documents presentats a la Cambra de la Propietat al desembre de 1941, on es recull la incautació del Liceu per part de la Generalitat el 1936, amb els noms de Ll. Companys i V. Gassol. Per la Junta estan els noms M. de Senmenat, F. Fagés i J.M. Bartr

Pulmonary complications in patients with staphylococcal sepsis

Background: The aim of the present study was to determine the pulmonary findings in patients with sepsis caused by Staphylococcus aureus