NEOTROPICAL XENARTHRANS: a data set of occurrence of xenarthran species in the Neotropics

Xenarthrans – anteaters, sloths, and armadillos – have essential functions for ecosystem maintenance, such as insect control and nutrient cycling, playing key roles as ecosystem engineers. Because of habitat loss and fragmentation, hunting pressure, and conflicts with 24 domestic dogs, these species have been threatened locally, regionally, or even across their full distribution ranges. The Neotropics harbor 21 species of armadillos, ten anteaters, and six sloths. Our dataset includes the families Chlamyphoridae (13), Dasypodidae (7), Myrmecophagidae (3), Bradypodidae (4), and Megalonychidae (2). We have no occurrence data on Dasypus pilosus (Dasypodidae). Regarding Cyclopedidae, until recently, only one species was recognized, but new genetic studies have revealed that the group is represented by seven species. In this data-paper, we compiled a total of 42,528 records of 31 species, represented by occurrence and quantitative data, totaling 24,847 unique georeferenced records. The geographic range is from the south of the USA, Mexico, and Caribbean countries at the northern portion of the Neotropics, to its austral distribution in Argentina, Paraguay, Chile, and Uruguay. Regarding anteaters, Myrmecophaga tridactyla has the most records (n=5,941), and Cyclopes sp. has the fewest (n=240). The armadillo species with the most data is Dasypus novemcinctus (n=11,588), and the least recorded for Calyptophractus retusus (n=33). With regards to sloth species, Bradypus variegatus has the most records (n=962), and Bradypus pygmaeus has the fewest (n=12). Our main objective with Neotropical Xenarthrans is to make occurrence and quantitative data available to facilitate more ecological research, particularly if we integrate the xenarthran data with other datasets of Neotropical Series which will become available very soon (i.e. Neotropical Carnivores, Neotropical Invasive Mammals, and Neotropical Hunters and Dogs). Therefore, studies on trophic cascades, hunting pressure, habitat loss, fragmentation effects, species invasion, and climate change effects will be possible with the Neotropical Xenarthrans dataset

The Importance Of Standard Operating Procedures (sops) For Clinical Research Centers

[No abstract available]572132133ICH Harmonised Tripartite (1996) Guideline For Good Clinical Practice, , http://www.ich.org/fleadmin/Public_Web_Site/ICH_Products/Guidelines/Efcacy/E6_R1/Step4/E6_R1__Guide-line.pdf, International Conference on Harmonisation of Technical Requirements for Registration of Pharmaceuticals for Human Use(2006) Buenas Práticas Clínicas. Documento Das Américas, , Organização Panamericana de Saúde (OPAS), Washington (DC): OPAS2006Dainesi, L.S., Nunes, D.B., Procedimentos operacionais padronizados e o gerenciamento de qualidade em centros de pesquisa (2007) Rev Assoc Med Bras, 53 (1), p. 6Instrução Normativa Guia De Inspeção Em Boas Práticas Clínicas, , http://www.isaia.com.br/HP/aulas/instrucao_normativa_4_completa.pdf, Brasil. N. 4 de 11/05/2009. Agência Nacional de Vigilância Sanitária (ANVISA), [citado nov 2010]Reso-lução RDC 39/08 Aprova O Regulamento Para a Realização De Pesquisa Clínica E Dá Outras Providências, , http://www.anvisa.gov.br, Brasil. Agência Nacional de Vigilância Sanitária (ANVISA), [citado nov 2010]Barbosa, L.M., Laranjeira, L.N., Cesar, M.B., Miyaoka, T.M., Guimaraes, H.P., Avezum, A., Monitoria em estudos clínicos (2008) Rev Bras Hipertens, 15, pp. 39-41Lousana, G., Procedimento operacional padrão (POP) e sua importância na garantia de qualidade do centro de pesquisa (2008) Boas Práticas Clínicas Nos Centros De Pesquisa, pp. 47-53. , Lou-sana G. 2 a ed. Rio de Janeiro: Revinte

Detection of two partially structured species in the folding process of the amyloidogenic protein beta 2-microglobulin

beta 2-Microglobulin is a small, major histocompatibility complex class I-associated protein that undergoes aggregation and accumulates as amyloid deposits in human tissues as a consequence of long-term haemodialysis. The folding process of this amyloidogenic protein has been studied in vitro by diluting the guanidine hydrochloride-denatured protein in refolding buffer at pH 7.4 and monitoring the folding process by means of a number of spectroscopic probes that allow the native structure of the protein to be detected as it develops. These techniques include fluorescence spectroscopy, far and near-UV circular dichroism, 8-anilino-1-naphthalenesulfonic acid binding and double jump assays. All spectroscopic probes indicate that a significant amount of structure forms within the dead-time of stopped-flow measurements (<5 ms). The folding reaction goes to completion through a fast phase followed by a slow phase, whose rate constants are ca 5.1 and 0.0030 s(-1) in water, respectively. Unfolding-folding double jump experiments, together with the use of peptidyl prolyl isomerase, reveal that the slow phase of folding of beta 2-microglobulin is not fundamentally determined by cis/trans isomerisation of X-Pro peptide bonds. Other folding-unfolding double jump experiments also suggest that the fast and slow phases of folding are not related to independent folding of different populations of protein molecules. Rather, we provide evidence for a sequential mechanism of folding where denatured beta 2-microglobulin collapses to an ensemble of partially folded conformations (I(1)) which fold subsequently to a more highly structured species (I(2)) and, finally, attain the native state. The partially folded species I(2) appears to be closely similar to previously studied amyloidogenic forms of beta 2-microglobulin, such as those adopted by the protein at mildly acid pH values and by a variant with six residues deleted at the N terminus. Since amyloid formation in vivo originates from partial denaturation of beta 2-microglobulin under conditions favouring the folding process, the long-lived, partially structured species detected here might be significantly populated under some physiological conditions and hence might play an important role in the process of amyloid formation

“Separation and quantification of two beta2-microglobulin isoforms”.

The present patent refers to a method for the separation and quantification of physiologically relevant isoforms of beta2-microglobulin, in particular of the native form and of its amyloidogenic form, carried out by capillary electrophoresis under temperature-controlled conditions. This separation method faithfully reflects the existing ratios between the said isoforms in physiological solutions, buffers of ionic strength and pH corresponding to these of plasma, serum and urine and allow a precise evaluation of the concentrations present in the samples subjected to analysi