A preservação digital dos periódicos científicos produzidos na UNICAMP: um relato de experiência

The present report describes how the State University of Campinas (Unicamp), one of the 100 best ranked Brazilian universities in the THE evaluation system, targets, through a partnership with Ibict, the digital preservation of scientific journals produced in multiple disciplines of its institutes, colleges, research centers and nuclei spread around its campus, that make use of the SEER (System Electronic Journal Publishing) platform, adapted from the international model OJS, through a pilot project using the LOCKSS methodology. The methodology, managed by Ibict and the institutions involved – including Unicamp, strives to ensure the security and fidelity of the content deposited in each institution-box through electronic archival, becoming a mirror of the content of all other institutions. The hope of the project is that all journals published within the university may join the initiative, preserving, in a rational and customized manner, the nowadays more widespread information resources (journals)

A preservação digital dos periódicos científicos produzidos na Unicamp: um relato de experiência

O presente relato descreve como a Universidade Estadual de Campinas (Unicamp), uma das 100 melhores universidades brasileiras no ranking do sistema de avaliação THE, busca, mediante parceria com o Ibict, realizar a preservação digital dos periódicos científicos produzidos em várias áreas dos institutos, faculdades, centros e núcleos de pesquisa dispersos no campus, que utilizam a plataforma do SEER (Sistema de Editoração Eletrônica de Revistas), adaptado do modelo internacional OJS, através de um projeto piloto utilizando-se da metodologia do LOCKSS. Essa metodologia, gerenciada pelo Ibict e as instituições envolvidas – entre elas a Unicamp, pretende garantir a segurança e fidelidade aos conteúdos depositados em cada caixa-instituição por meio de arquivamento eletrônico, tornando-se um espelho do conteúdo em todas as demais instituições. Espera-se, com esse projeto, que todos os periódicos editorados no âmbito da universidade possam aderir à iniciativa, preservando de modo racional e customizado os recursos informacionais (periódicos) mais difundidos na atualidade

A preservação digital dos periódicos científicos produzidos na UNICAMP: um relato de experiência

The present report describes how the State University of Campinas (Unicamp), one of the 100 best ranked Brazilian universities in the THE evaluation system, targets, through a partnership with Ibict, the digital preservation of scientific journals produced in multiple disciplines of its institutes, colleges, research centers and nuclei spread around its campus, that make use of the SEER (System Electronic Journal Publishing) platform, adapted from the international model OJS, through a pilot project using the LOCKSS methodology. The methodology, managed by Ibict and the institutions involved – including Unicamp, strives to ensure the security and fidelity of the content deposited in each institution-box through electronic archival, becoming a mirror of the content of all other institutions. The hope of the project is that all journals published within the university may join the initiative, preserving, in a rational and customized manner, the nowadays more widespread information resources (journals)

Arginine methylation analysis of the splicing-associated SR protein SFRS9/SRP30C

The human SFRS9/SRp30c belongs to the SR family of splicing regulators. Despite evidence that members of this protein family may be targeted by arginine methylation, this has yet to be experimentally addressed. In this study, we found that SFRS9 is a target for PRMT1-mediated arginine methylation in vitro, and that it is immunoprecipitated from HEK-293 lysates by antibodies that recognize both mono- and dimethylated arginines. We further observed that upon treatment with the methylation inhibitor Adox, the fluorescent EGFP-SFRS9 re-localizes to dot-like structures in the cell nucleus. In subsequent confocal analyses, we found that EGFP-SFRS9 localizes to nucleoli in Adox-treated cells. Our findings indicate the importance of arginine methylation for the subnuclear localization of SFRS9144657669CONSELHO NACIONAL DE DESENVOLVIMENTO CIENTÍFICO E TECNOLÓGICO - CNPQFUNDAÇÃO DE AMPARO À PESQUISA DO ESTADO DE SÃO PAULO - FAPESPsem informaçã

Boiling heat transfer inside parallel microchannels

Heat transfer study was carried out on convective boiling of R134a through nine horizontally positioned, parallel microchannels. The microchannels were of circular cross sections with internal diameter and length of 0.77 mm and 150 mm, respectively. The test conditions are as follows: mass velocity, G, of 250, 500, 750 and 1000 kg/m2s; inlet pressure, pin, of 600, 700, and 900 kPa and subcooling degrees of 1, 10 and 20oC. The experimental results for heat transfer coefficient are compared with seven correlations and semi-empirical models and the best predictions are obtained with the models of Sun and Mishima [13] and Thome et al. [15] for which the Mean Absolute Error was 14.4% and 14.9%, respectively.Papers presented to the 12th International Conference on Heat Transfer, Fluid Mechanics and Thermodynamics, Costa de Sol, Spain on 11-13 July 2016

Photography-based taxonomy is inadequate, unnecessary, and potentially harmful for biological sciences

The question whether taxonomic descriptions naming new animal species without type specimen(s) deposited in collections should be accepted for publication by scientific journals and allowed by the Code has already been discussed in Zootaxa (Dubois & Nemésio 2007; Donegan 2008, 2009; Nemésio 2009a–b; Dubois 2009; Gentile & Snell 2009; Minelli 2009; Cianferoni & Bartolozzi 2016; Amorim et al. 2016). This question was again raised in a letter supported by 35 signatories published in the journal Nature (Pape et al. 2016) on 15 September 2016. On 25 September 2016, the following rebuttal (strictly limited to 300 words as per the editorial rules of Nature) was submitted to Nature, which on 18 October 2016 refused to publish it. As we think this problem is a very important one for zoological taxonomy, this text is published here exactly as submitted to Nature, followed by the list of the 493 taxonomists and collection-based researchers who signed it in the short time span from 20 September to 6 October 2016

Mitochondrial physiology

As the knowledge base and importance of mitochondrial physiology to evolution, health and disease expands, the necessity for harmonizing the terminology concerning mitochondrial respiratory states and rates has become increasingly apparent. The chemiosmotic theory establishes the mechanism of energy transformation and coupling in oxidative phosphorylation. The unifying concept of the protonmotive force provides the framework for developing a consistent theoretical foundation of mitochondrial physiology and bioenergetics. We follow the latest SI guidelines and those of the International Union of Pure and Applied Chemistry (IUPAC) on terminology in physical chemistry, extended by considerations of open systems and thermodynamics of irreversible processes. The concept-driven constructive terminology incorporates the meaning of each quantity and aligns concepts and symbols with the nomenclature of classical bioenergetics. We endeavour to provide a balanced view of mitochondrial respiratory control and a critical discussion on reporting data of mitochondrial respiration in terms of metabolic flows and fluxes. Uniform standards for evaluation of respiratory states and rates will ultimately contribute to reproducibility between laboratories and thus support the development of data repositories of mitochondrial respiratory function in species, tissues, and cells. Clarity of concept and consistency of nomenclature facilitate effective transdisciplinary communication, education, and ultimately further discovery

Mitochondrial physiology

As the knowledge base and importance of mitochondrial physiology to evolution, health and disease expands, the necessity for harmonizing the terminology concerning mitochondrial respiratory states and rates has become increasingly apparent. The chemiosmotic theory establishes the mechanism of energy transformation and coupling in oxidative phosphorylation. The unifying concept of the protonmotive force provides the framework for developing a consistent theoretical foundation of mitochondrial physiology and bioenergetics. We follow the latest SI guidelines and those of the International Union of Pure and Applied Chemistry (IUPAC) on terminology in physical chemistry, extended by considerations of open systems and thermodynamics of irreversible processes. The concept-driven constructive terminology incorporates the meaning of each quantity and aligns concepts and symbols with the nomenclature of classical bioenergetics. We endeavour to provide a balanced view of mitochondrial respiratory control and a critical discussion on reporting data of mitochondrial respiration in terms of metabolic flows and fluxes. Uniform standards for evaluation of respiratory states and rates will ultimately contribute to reproducibility between laboratories and thus support the development of data repositories of mitochondrial respiratory function in species, tissues, and cells. Clarity of concept and consistency of nomenclature facilitate effective transdisciplinary communication, education, and ultimately further discovery

Analysis of the proteins Ki-1/57 and PRMT1: identification, mapping and characterization of the interaction with other proteins

Orientador: Jorg KobargTese (doutorado) - Universidade Estadual de Campinas, Instituto de BiologiaResumo: A proteína Ki-1/57 que é encontrada tanto no núcleo quanto no citoplasma está associada com atividade de proteína quinase serina/treonina e é fosforilada nestes resíduos após ativação celular. Neste trabalho verificamos que Ki-1/57 interage com a proteína Chromatin-Helicase-DNA-binding domain 3 (CHD3) e com a proteína adaptadora/sinalizadora RACK1 no núcleo. Pelo sistema do duplo híbrido de levedura (SDHL) a proteína arginina metiltransferase 1 (PRMT1) foi selecionada como outra proteína de interação. A PRMT1 integra uma família representada por nove enzimas humanas que catalisam reações de metilação em resíduos de arginina. Em seguida, usando agora a PRMT1 como isca - no SDHL - identificamos as proteínas Ki-1/57 e hnRNPQ, juntamente com outras 13. A maioria delas contêm motivos ¿RGG-box¿ em suas seqüências de aminoácidos, que são conhecidos alvos para metilação. Posteriormente verificamos que Ki-1/57 e seu provável parálogo CGI-55 conservam dois motivos ¿RGG/RXR-box¿ e que são substratos in vitro para a metilação de argininas pela PRMT1. Estudos de mapeamento mostraram que todos os fragmentos contendo o motivo ¿RGG/RXR-box¿ interagem com a PRMT1 e são alvos à metilação in vitro. Ki-1/57 endógena, imunoprecipitada de células L540, mostrou ser metilada in vivo, além de ser um alvo a metilação pela PRMT1 in vitro, somente quando as células são previamente tratadas com o inibidor da metilação Adox. Tratamento das células Hela com o inibidor da metilação (Adox) causa desaparecimento da imuno-marcação citoplasmática de Ki-1/57 e relativa redistribuição do parálogo CGI-55 para o citosol. Assim, pode ser especulado que a metilação destas proteínas deve ser um evento importante para suas localizações subcelulares e conseqüentemente para suas funções. Em resumo, nossos dados sugerem que o SDHL é um método efetivo na identificação de novos substratos celulares para a PRMT1 e poderia ser estendido para a identificação e caracterização de novos substratos para os outros integrantes da família das PRMTs humanasAbstract: The protein Ki-1/57 that is found both in the cytoplasm and nucleus is associated with serine/threonine protein kinase activity and gets phosphorylated on serine and threonine residues upon cellular activation. We demonstrated that Ki-1/57 interacts with the Chromatin-Helicase-DNA-binding domain protein 3 (CHD3) and with the adaptor/signaling protein RACK1 in the nucleus. By utilizing the yeast two-hybrid system (YTHS), we were further able to find the protein arginine-methylatranseferase-1 (PRMT1) as another interacting protein. PRMT1 is a member of the family constituted by 9 human enzymes that catalyze methylation reactions on arginine residues. Afterwards, by using PRMT1 as bait in the YTHS we identified both Ki-1/57 and NSAP1 as interacting proteins, along with 13 other proteins. The majority of them present RGG-box clusters in their amino acid sequences, which are known to be targets for arginine methylation. We further found that Ki-1/57 and its putative paralogue CGI-55 have two RGG/RXR-box clusters conserved between them and that they are substrates for arginine-methylation by PRMT1 in vitro. In mapping studies, we observed that all Ki-1/57 protein fragments containing the RGG/RXRbox clusters interact with PRMT1 and are targets for methylation in vitro. Endogenous cellular Ki-1/57 seems to be methylated in vivo and is a target for methylation by PRMT1 in vitro, only when cells have been previously treated with the methylation inhibitor Adox. Treatment of Hela cells with the inhibitor of methylation (Adox) causes the disappearance of the immuno-staining of Ki-1/57 in the cytoplasm and a relative redistribution of the paralogue CGI-55 to the cytosol. It can therefore be speculated that the methylation of these proteins is important for their sub-cellular localization and in consequence for their function. In summary our data suggest that the YTHS is an effective method for the identification of novel cellular PRMT substrates and could be extended for the identification and characterization of novel substrates to the other components of the human PRMT1 familyDoutoradoBioquimicaDoutor em Biologia Funcional e Molecula