L'évolution de l'édition des ARN de transfert chez les jakobides

Mémoire numérisé par la Direction des bibliothèques de l'Université de Montréal.

Untangling Knots: Determining E-book Suitability for Course Reserves

E-books on their own are complex; they become even more so in the context of course reserves. In FY2016 the Resource Sharing & Reserves and Acquisitions units developed a new workflow for vetting requested e-books to ensure that they were suitable for course reserves (i.e. they permit unlimited simultaneous users) before posting links to them within the university’s online learning management system. In the Spring 2016 semester 46 e-books were vetted through this process, resulting in 18 purchases. Preliminary data analysis sheds light on the suitability of the Libraries’ current e-book collections for course reserves as well as faculty preferences, with potential implications for the Libraries’ ordering process. We hope this lightening talk will generate discussion about these issues among selectors, collection managers, and reserves staff alike.

PA Photos & Documents: Exploring Pennsylvania’s digitized documents and photographs

Presentation from the MARAC conference in Pittsburgh, PA on April 14–16, 2016. S24; - Pittsburgh Pop-Up #2.

“PROSPERING BECAUSE THAT’S ITS HISTORY”: BLACK RESILIENCE AND HONORS DEVELOPMENT IN HIGHER EDUCATION: MORGAN STATE UNIVERSITY AND THE STATE OF MARYLAND, 1867-1988

This study explores the origins and development of honors education at a Historically Black College and University (HBCU), Morgan State University, within the context of the Maryland higher education system. During the last decades, public and private institutions have invested in honors experiences for their high-ability students. These programs have become recruitment magnets while also raising institutional academic profiles, justifying additional campus resources. The history of higher education reveals simultaneous narratives such as the tension of post-desegregated Black colleges facing uncertain futures; and the progress of the rise and popularity of collegiate honors programs. Both accounts contribute to tracing seemingly parallel histories in higher education that speaks to the development of honors education at HBCUs. While the extant literature on honors development at Historically White Institutions (HWIs) of higher education has gradually emerged, our understanding of activity at HBCUs is spotty at best. One connection of these two phenomena is the development of honors programs at HBCUs. Using Morgan State University, I examine the role and purpose of honors education at a public HBCU through archival materials and oral histories. Major unexpected findings that constructed this historical narrative beyond its original scope were the impact of the 1935/6 Murray v Pearson, the first higher education desegregation case. Other emerging themes were Morgan’s decades-long efforts to resist state control of its governance, Maryland’s misuse of Morrill Act funds, and the border state’s resistance to desegregation. Also, the broader histories of Black education, racism, and Black citizenship from Dred Scott and Plessy, the 1863 Emancipation Proclamation to Brown, inform this study. As themes are threaded together, Critical Race Theory provides the framework for understanding the emerging themes. In the immediate wake of the post-desegregation era, HBCUs had to address future challenges such as purpose and mission. Competing with HWIs for high-achieving Black students was one of the unanticipated consequences of the Brown decision. Often marginalized from higher education research literature, this study will broaden the research repository of honors education by documenting HBCU contributions despite a challenging landscape.

Stock assessment of whaler and hammerhead sharks (Carcharhinidae and Sphyrnidae) in Queensland

This stock assessment provides detailed results for the most common sharks encountered by Queensland commercial fishers. These sharks come from the whaler (Carcharhinidae) and hammerhead (Sphyrnidae) families and comprise sharpnose sharks (Rhizoprionodon taylori and R. oligolinx), the milk shark (R. acutus), the creek whaler (Carcharhinus fitzroyensis), the hardnose shark (C. macloti), the spot-tail shark (C. sorrah), the Australian blacktip shark (C. tilstoni), the common blacktip shark (C. limbatus), the spinner shark (C. brevipinna), bull and pigeye sharks (C. leucas and C. amboinensis), the winghead shark (Eusphyra blochii), the scalloped hammerhead (Sphyrna lewini) and the great hammerhead (S. mokarran). Reef sharks were excluded because fishery observer data indicated that they were largely spatially segregated from sharks caught in the inshore net fisheries. The three common species of reef sharks in Queensland, which are all whaler sharks, are the grey reef shark Carcharhinus amblyrhynchos, the blacktip reef shark C. melanopterus and the whitetip reef shark Triaenodon obesus.

Gulf of Carpentaria Developmental Finfish Trawl Fishery : Maximum Sustainable Yield

The Gulf of Carpentaria Finfish Trawl Fishery operates under developmental permits and harvests five main tropical snapper species. The fishery operates in eastern Gulf of Carpentaria waters and is managed by Fisheries Queensland on behalf of the Queensland Fishery Joint Authority. For the years 2004–2014, the fishery Total Allowable Commercial Catch (TACC) was fixed at 1250 t and substantially under-filled. In 2011 new stock analyses were published for the fishery. Results were presented to industry including the estimated equilibrium maximum sustainable yield (MSY) of 450 t for east Gulf of Carpentaria waters. The MSY value represented the maximum average combined species harvest that can be taken long-term; combining MSY harvests of the five main species. For the 2015 calendar year, a revised 450 t harvest quota was set for Crimson Snapper, Saddletail Snapper, Red Emperor and other Emperor species; plus a tonnage allowance for other permitted species. The revised quota tonnage represented a considerable reduction from the 1250 t set in previous years. Industry raised questions about not understanding how the MSY was arrived at and why it was less than early 1990s yield estimates. The purpose of this report is to explain the MSY estimates for east Gulf of Carpentaria waters. The 450 t MSY represents at present the best estimate available and is consistent with pre-2011 estimates.

Stout Whiting Fishery Summary : Commercial Quota Setting for 2017

This fishery assessment report describes the commercial stout whiting fishery operation along Australia’s east coast between Sandy Cape and the Queensland-New South Wales border. The fishery is identified by a T4 symbol. This study follows methods applied in (O'Neill & Leigh, 2016a) and extends the results of that study by using the latest data available up to end of March 2016. The fishery statistics reported herein are for fishing years 1991 to 2016. This study analysed stout whiting catch rates from both Queensland and New South Wales (NSW) for all vessels, areas and fishing gears. The 2016 catch rate index from Queensland and NSW waters was 0.86. This means that the 2016 catch rate index was 86% of the mean standardised catch rate. Results showed that there was a stable trend in catch rates from 2012 to 2016, as in the previous study (O'Neill & Leigh, 2016a), with the 2015 and 2014 catch rates 85% of the mean catch rate. The fish-length frequency and age-length-otolith data were translated using two models which showed: • Where patterns of fish age-abundance were estimated from the fish-length frequency and age-length data, there were slightly decreased estimated measures of fish survival at 38% for 2014, compared to fish survival estimates in 2013 at 40%. The 2014 and 2015 estimated age structure was dominated by 1+ and 2+ old fished, with a slightly higher frequency of age 2 - 3 fish for 2015. • Where only the age-length data were used, estimates showed that from 2011 to 2014 the survival index increased. The estimated survival index increased from 35% in 2013 to 64% in 2014, indicating stronger survival of fish as they recruited and aged. Together the stout whiting catch rate and survival indicators showed the recent fishery harvests were sustainable. Since 1997, T4 management (Stout Whiting Fishery) is centred on annual assessments of total allowable commercial catch (TACC). The TACC is assessed before the start of each fishing year using statistical assessment methodologies, namely evaluation of trends in fish catch rates and catch-at-age frequencies measured against management reference points. The TACC has been under-caught in many years. For setting the 2017 T4 stout whiting TACC, the calculations covered a range of settings to account for the variance in the data and provide options for quota change. The overall (averaged) results suggested: • The procedure where the quota was adjusted based on previous TACC setting in year 2016 gave a recommended TACC for 2017 of between 1100 and 1130 t. • The procedure that focussed directly on optimising the average harvest to match target reference points gave a recommended TACC for 2017 of between 860 and 890 t. Use of these estimates to set TACC will depend on management and industry aims for the fishery.

Stout Whiting Fishery Summary : Queensland Total Allowable Catch for 2016

In Queensland, stout whiting are fished by Danish seine and fish otter-trawl methods between Sandy Cape and the Queensland-New South Wales border. The fishery is currently identified by a T4 symbol and is operated by two primary quota holders. Since 1997, T4 management has been informed by annual stock assessments in order to determine a total allowable commercial catch (TACC) quota. The TACC is assessed before the start of each fishing year using statistical methodologies. This includes evaluation of trends in fish catch-rates and catch-at-age frequencies against management reference points. The T4 stout whiting TACC for 2014 was adjusted down to 1150 t as a result of elevated estimates of fishing mortality and remained unchanged in 2015 (2013 TACC = 1350 t quota). Two T4 vessels fished for stout whiting in the 2015 fishing year, harvesting 663 t from Queensland waters. Annual T4 landings of stout whiting averaged about 713 t for the fishing years 2013–2015, with a maximum harvest in the last 10 fishing years of 1140 t and a maximum historical harvest of 2400 t in the 1995. Stout whiting catch rates from both Queensland and New South Wales were analysed for all vessels, areas and fishing gears. The 2015 catch rate index was equal to 0.85, down 15% compared to the 2010–2015 fishing year average (reference point =1). The stout whiting fish length and otolith weight frequencies indicated larger and older fish in the calendar year 2014. This data was translated to show improved measures of fish survival at about 38% per year and near the reference point of about 41%. Together, the stout whiting catch rate and survival indicators show the fishery was sustainable. Earlier population modelling conducted for the year 2013 also suggested the stock was sustainable, but the estimate was only marginally above the biomass for maximum sustainable yield. Irrespective, reasons for reduced catch rates should be examined further and interpreted with precaution, particularly given the TACC has been under-caught in many years. For setting of the 2016 TACC, alternate analyses and reference points were compared to address data uncertainties and provide options for quota change. The results were dependent on the stock indicator and harvest procedure used. Uncertainty in all TACC estimates should be considered as they were sensitive to the data inputs and assumptions. For the 2016 T4 fishing year, upper levels of harvest should be limited to 1000–1100 t following procedure equation 1, with target levels of harvest at 750–850 t for procedure equation 2. Use of these estimates to set TACC will depend on management and industry intentions.

Microfluidic platforms for the characterization of in meso membrane protein crystallization

Membrane proteins, which reside in the membranes of cells, play a critical role in many important biological processes including cellular signaling, immune response, and material and energy transduction. Because of their key role in maintaining the environment within cells and facilitating intercellular interactions, understanding the function of these proteins is of tremendous medical and biochemical significance. Indeed, the malfunction of membrane proteins has been linked to numerous diseases including diabetes, cirrhosis of the liver, cystic fibrosis, cancer, Alzheimer's disease, hypertension, epilepsy, cataracts, tubulopathy, leukodystrophy, Leigh syndrome, anemia, sensorineural deafness, and hypertrophic cardiomyopathy.1-3 However, the structure of many of these proteins and the changes in their structure that lead to disease-related malfunctions are not well understood. Additionally, at least 60% of the pharmaceuticals currently available are thought to target membrane proteins, despite the fact that their exact mode of operation is not known.4-6 Developing a detailed understanding of the function of a protein is achieved by coupling biochemical experiments with knowledge of the structure of the protein. Currently the most common method for obtaining three-dimensional structure information is X-ray crystallography. However, no a priori methods are currently available to predict crystallization conditions for a given protein.7-14 This limitation is currently overcome by screening a large number of possible combinations of precipitants, buffer, salt, and pH conditions to identify conditions that are conducive to crystal nucleation and growth.7,9,11,15-24 Unfortunately, these screening efforts are often limited by difficulties associated with quantity and purity of available protein samples. While the two most significant bottlenecks for protein structure determination in general are the (i) obtaining sufficient quantities of high quality protein samples and (ii) growing high quality protein crystals that are suitable for X-ray structure determination,7,20,21,23,25-47 membrane proteins present additional challenges. For crystallization it is necessary to extract the membrane proteins from the cellular membrane. However, this process often leads to denaturation. In fact, membrane proteins have proven to be so difficult to crystallize that of the more than 66,000 structures deposited in the Protein Data Bank,48 less than 1% are for membrane proteins, with even fewer present at high resolution (< 2Å)4,6,49 and only a handful are human membrane proteins.49 A variety of strategies including detergent solubilization50-53 and the use of artificial membrane-like environments have been developed to circumvent this challenge.43,53-55 In recent years, the use of a lipidic mesophase as a medium for crystallizing membrane proteins has been demonstrated to increase success for a wide range of membrane proteins, including human receptor proteins.54,56-62 This in meso method for membrane protein crystallization, however, is still by no means routine due to challenges related to sample preparation at sub-microliter volumes and to crystal harvesting and X-ray data collection. This dissertation presents various aspects of the development of a microfluidic platform to enable high throughput in meso membrane protein crystallization at a level beyond the capabilities of current technologies. Microfluidic platforms for protein crystallization and other lab-on-a-chip applications have been well demonstrated.9,63-66 These integrated chips provide fine control over transport phenomena and the ability to perform high throughput analyses via highly integrated fluid networks. However, the development of microfluidic platforms for in meso protein crystallization required the development of strategies to cope with extremely viscous and non-Newtonian fluids. A theoretical treatment of highly viscous fluids in microfluidic devices is presented in Chapter 3, followed by the application of these strategies for the development of a microfluidic mixer capable of preparing a mesophase sample for in meso crystallization at a scale of less than 20 nL in Chapter 4. This approach was validated with the successful on chip in meso crystallization of the membrane protein bacteriorhodopsin. In summary, this is the first report of a microfluidic platform capable of performing in meso crystallization on-chip, representing a 1000x reduction in the scale at which mesophase trials can be prepared. Once protein crystals have formed, they are typically harvested from the droplet they were grown in and mounted for crystallographic analysis. Despite the high throughput automation present in nearly all other aspects of protein structure determination, the harvesting and mounting of crystals is still largely a manual process. Furthermore, during mounting the fragile protein crystals can potentially be damaged, both from physical and environmental shock. To circumvent these challenges an X-ray transparent microfluidic device architecture was developed to couple the benefits of scale, integration, and precise fluid control with the ability to perform in situ X-ray analysis (Chapter 5). This approach was validated successfully by crystallization and subsequent on-chip analysis of the soluble proteins lysozyme, thaumatin, and ribonuclease A and will be extended to microfluidic platforms for in meso membrane protein crystallization. The ability to perform in situ X-ray analysis was shown to provide extremely high quality diffraction data, in part as a result of not being affected by damage due to physical handling of the crystals. As part of the work described in this thesis, a variety of data collection strategies for in situ data analysis were also tested, including merging of small slices of data from a large number of crystals grown on a single chip, to allow for diffraction analysis at biologically relevant temperatures. While such strategies have been applied previously,57,59,61,67 they are potentially challenging when applied via traditional methods due to the need to grow and then mount a large number of crystals with minimal crystal-to-crystal variability. The integrated nature of microfluidic platforms easily enables the generation of a large number of reproducible crystallization trials. This, coupled with in situ analysis capabilities has the potential of being able to acquire high resolution structural data of proteins at biologically relevant conditions for which only small crystals, or crystals which are adversely affected by standard cryocooling techniques, could be obtained (Chapters 5 and 6). While the main focus of protein crystallography is to obtain three-dimensional protein structures, the results of typical experiments provide only a static picture of the protein. The use of polychromatic or Laue X-ray diffraction methods enables the collection of time resolved structural information. These experiments are very sensitive to crystal quality, however, and often suffer from severe radiation damage due to the intense polychromatic X-ray beams. Here, as before, the ability to perform in situ X-ray analysis on many small protein crystals within a microfluidic crystallization platform has the potential to overcome these challenges. An automated method for collecting a "single-shot" of data from a large number of crystals was developed in collaboration with the BioCARS team at the Advanced Photon Source at Argonne National Laboratory (Chapter 6). The work described in this thesis shows that, even more so than for traditional structure determination efforts, the ability to grow and analyze a large number of high quality crystals is critical to enable time resolved structural studies of novel proteins. In addition to enabling X-ray crystallography experiments, the development of X-ray transparent microfluidic platforms also has tremendous potential to answer other scientific questions, such as unraveling the mechanism of in meso crystallization. For instance, the lipidic mesophases utilized during in meso membrane protein crystallization can be characterized by small angle X-ray diffraction analysis. Coupling in situ analysis with microfluidic platforms capable of preparing these difficult mesophase samples at very small volumes has tremendous potential to enable the high throughput analysis of these systems on a scale that is not reasonably achievable using conventional sample preparation strategies (Chapter 7). In collaboration with the LS-CAT team at the Advanced Photon Source, an experimental station for small angle X-ray analysis coupled with the high quality visualization capabilities needed to target specific microfluidic samples on a highly integrated chip is under development. Characterizing the phase behavior of these mesophase systems and the effects of various additives present in crystallization trials is key for developing an understanding of how in meso crystallization occurs. A long term goal of these studies is to enable the rational design of in meso crystallization experiments so as to avoid or limit the need for high throughput screening efforts. In summary, this thesis describes the development of microfluidic platforms for protein crystallization with in situ analysis capabilities. Coupling the ability to perform in situ analysis with the small scale, fine control, and the high throughput nature of microfluidic platforms has tremendous potential to enable a new generation of crystallographic studies and facilitate the structure determination of important biological targets. The development of platforms for in meso membrane protein crystallization is particularly significant because they enable the preparation of highly viscous mixtures at a previously unachievable scale. Work in these areas is ongoing and has tremendous potential to improve not only current the methods of protein crystallization and crystallography, but also to enhance our knowledge of the structure and function of proteins which could have a significant scientific and medical impact on society as a whole. The microfluidic technology described in this thesis has the potential to significantly advance our understanding of the structure and function of membrane proteins, thereby aiding the elucidation of human biology, the development of pharmaceuticals with fewer side effects for a wide range of diseases. References (1) Quick, M.; Javitch, J. A. P Natl Acad Sci USA 2007, 104, 3603. (2) Trubetskoy, V. S.; Burke, T. J. Am Lab 2005, 37, 19. (3) Pecina, P.; Houstkova, H.; Hansikova, H.; Zeman, J.; Houstek, J. Physiol Res 2004, 53, S213. (4) Arinaminpathy, Y.; Khurana, E.; Engelman, D. M.; Gerstein, M. B. Drug Discovery Today 2009, 14, 1130. (5) Overington, J. P.; Al-Lazikani, B.; Hopkins, A. L. Nat Rev Drug Discov 2006, 5, 993. (6) Dauter, Z.; Lamzin, V. S.; Wilson, K. S. Current Opinion in Structural Biology 1997, 7, 681. (7) Hansen, C.; Quake, S. R. Current Opinion in Structural Biology 2003, 13, 538. (8) Govada, L.; Carpenter, L.; da Fonseca, P. C. A.; Helliwell, J. R.; Rizkallah, P.; Flashman, E.; Chayen, N. E.; Redwood, C.; Squire, J. M. J Mol Biol 2008, 378, 387. (9) Hansen, C. L.; Skordalakes, E.; Berger, J. M.; Quake, S. R. P Natl Acad Sci USA 2002, 99, 16531. (10) Leng, J.; Salmon, J.-B. Lab Chip 2009, 9, 24. (11) Zheng, B.; Gerdts, C. J.; Ismagilov, R. F. Current Opinion in Structural Biology 2005, 15, 548. (12) Lorber, B.; Delucas, L. J.; Bishop, J. B. J Cryst Growth 1991, 110, 103. (13) Talreja, S.; Perry, S. L.; Guha, S.; Bhamidi, V.; Zukoski, C. F.; Kenis, P. J. A. The Journal of Physical Chemistry B 2010, 114, 4432. (14) Chayen, N. E. Current Opinion in Structural Biology 2004, 14, 577. (15) He, G. W.; Bhamidi, V.; Tan, R. B. H.; Kenis, P. J. A.; Zukoski, C. F. Cryst Growth Des 2006, 6, 1175. (16) Zheng, B.; Tice, J. D.; Roach, L. S.; Ismagilov, R. F. Angew Chem Int Edit 2004, 43, 2508. (17) Li, L.; Mustafi, D.; Fu, Q.; Tereshko, V.; Chen, D. L. L.; Tice, J. D.; Ismagilov, R. F. P Natl Acad Sci USA 2006, 103, 19243. (18) Song, H.; Chen, D. L.; Ismagilov, R. F. Angew Chem Int Edit 2006, 45, 7336. (19) van der Woerd, M.; Ferree, D.; Pusey, M. Journal of Structural Biology 2003, 142, 180. (20) Ng, J. D.; Gavira, J. A.; Garcia-Ruiz, J. M. Journal of Structural Biology 2003, 142, 218. (21) Talreja, S.; Kenis, P. J. A.; Zukoski, C. F. Langmuir 2007, 23, 4516. (22) Hansen, C. L.; Quake, S. R.; Berger, J. M. US, 2007. (23) Newman, J.; Fazio, V. J.; Lawson, B.; Peat, T. S. Cryst Growth Des 2010, 10, 2785. (24) Newman, J.; Xu, J.; Willis, M. C. Acta Crystallographica Section D 2007, 63, 826. (25) Collingsworth, P. D.; Bray, T. L.; Christopher, G. K. J Cryst Growth 2000, 219, 283. (26) Durbin, S. D.; Feher, G. Annu Rev Phys Chem 1996, 47, 171. (27) Talreja, S.; Kim, D. Y.; Mirarefi, A. Y.; Zukoski, C. F.; Kenis, P. J. A. J Appl Crystallogr 2005, 38, 988. (28) Yoshizaki, I.; Nakamura, H.; Sato, T.; Igarashi, N.; Komatsu, H.; Yoda, S. J Cryst Growth 2002, 237, 295. (29) Anderson, M. J.; Hansen, C. L.; Quake, S. R. P Natl Acad Sci USA 2006, 103, 16746. (30) Hansen, C. L.; Sommer, M. O. A.; Quake, S. R. P Natl Acad Sci USA 2004, 101, 14431. (31) Lounaci, M.; Rigolet, P.; Abraham, C.; Le Berre, M.; Chen, Y. Microelectron Eng 2007, 84, 1758. (32) Zheng, B.; Roach, L. S.; Ismagilov, R. F. J Am Chem Soc 2003, 125, 11170. (33) Zhou, X.; Lau, L.; Lam, W. W. L.; Au, S. W. N.; Zheng, B. Anal. Chem. 2007. (34) Cherezov, V.; Caffrey, M. J Appl Crystallogr 2003, 36, 1372. (35) Qutub, Y.; Reviakine, I.; Maxwell, C.; Navarro, J.; Landau, E. M.; Vekilov, P. G. J Mol Biol 2004, 343, 1243. (36) Rummel, G.; Hardmeyer, A.; Widmer, C.; Chiu, M. L.; Nollert, P.; Locher, K. P.; Pedruzzi, I.; Landau, E. M.; Rosenbusch, J. P. Journal of Structural Biology 1998, 121, 82. (37) Gavira, J. A.; Toh, D.; Lopez-Jaramillo, J.; Garcia-Ruiz, J. M.; Ng, J. D. Acta Crystallogr D 2002, 58, 1147. (38) Stevens, R. C. Current Opinion in Structural Biology 2000, 10, 558. (39) Baker, M. Nat Methods 2010, 7, 429. (40) McPherson, A. In Current Topics in Membranes, Volume 63; Volume 63 ed.; DeLucas, L., Ed.; Academic Press: 2009, p 5. (41) Gabrielsen, M.; Gardiner, A. T.; Fromme, P.; Cogdell, R. J. In Current Topics in Membranes, Volume 63; Volume 63 ed.; DeLucas, L., Ed.; Academic Press: 2009, p 127. (42) Page, R. In Methods in Molecular Biology: Structural Proteomics - High Throughput Methods; Kobe, B., Guss, M., Huber, T., Eds.; Humana Press: Totowa, NJ, 2008; Vol. 426, p 345. (43) Caffrey, M. Ann Rev Biophys 2009, 38, 29. (44) Doerr, A. Nat Methods 2006, 3, 244. (45) Brostromer, E.; Nan, J.; Li, L.-F.; Su, X.-D. Biochemical and Biophysical Research Communications 2009, 386, 634. (46) Li, G.; Chen, Q.; Li, J.; Hu, X.; Zhao, J. Anal Chem 2010, 82, 4362. (47) Jia, Y.; Liu, X.-Y. The Journal of Physical Chemistry B 2006, 110, 6949. (48) RCSB Protein Data Bank. http://www.rcsb.org/ (July 11, 2010). (49) Membrane Proteins of Known 3D Structure. http://blanco.biomol.uci.edu/Membrane_Proteins_xtal.html (July 11, 2010). (50) Michel, H. Trends Biochem Sci 1983, 8, 56. (51) Rosenbusch, J. P. Journal of Structural Biology 1990, 104, 134. (52) Garavito, R. M.; Picot, D. Methods 1990, 1, 57. (53) Kulkarni, C. V. 2010; Vol. 12, p 237. (54) Landau, E. M.; Rosenbusch, J. P. P Natl Acad Sci USA 1996, 93, 14532. (55) Pebay-Peyroula, E.; Rummel, G.; Rosenbusch, J. P.; Landau, E. M. Science 1997, 277, 1676. (56) Cherezov, V.; Liu, W.; Derrick, J. P.; Luan, B.; Aksimentiev, A.; Katritch, V.; Caffrey, M. Proteins: Structure, Function, and Bioinformatics 2008, 71, 24. (57) Cherezov, V.; Rosenbaum, D. M.; Hanson, M. A.; Rasmussen, S. G. F.; Thian, F. S.; Kobilka, T. S.; Choi, H. J.; Kuhn, P.; Weis, W. I.; Kobilka, B. K.; Stevens, R. C. Science 2007, 318, 1258. (58) Cherezov, V.; Yamashita, E.; Liu, W.; Zhalnina, M.; Cramer, W. A.; Caffrey, M. J Mol Biol 2006, 364, 716. (59) Jaakola, V. P.; Griffith, M. T.; Hanson, M. A.; Cherezov, V.; Chien, E. Y. T.; Lane, J. R.; IJzerman, A. P.; Stevens, R. C. Science 2008, 322, 1211. (60) Rosenbaum, D. M.; Cherezov, V.; Hanson, M. A.; Rasmussen, S. G. F.; Thian, F. S.; Kobilka, T. S.; Choi, H. J.; Yao, X. J.; Weis, W. I.; Stevens, R. C.; Kobilka, B. K. Science 2007, 318, 1266. (61) Wacker, D.; Fenalti, G.; Brown, M. A.; Katritch, V.; Abagyan, R.; Cherezov, V.; Stevens, R. C. J Am Chem Soc 2010, 132, 11443. (62) Höfer, N.; Aragão, D.; Caffrey, M. Biophys J 2010, 99, L23. (63) Li, L.; Ismagilov, R. F. Ann Rev Biophys 2010. (64) Pal, R.; Yang, M.; Lin, R.; Johnson, B. N.; Srivastava, N.; Razzacki, S. Z.; Chomistek, K. J.; Heldsinger, D. C.; Haque, R. M.; Ugaz, V. M.; Thwar, P. K.; Chen, Z.; Alfano, K.; Yim, M. B.; Krishnan, M.; Fuller, A. O.; Larson, R. G.; Burke, D. T.; Burns, M. A. Lab Chip 2005, 5, 1024. (65) Jayashree, R. S.; Gancs, L.; Choban, E. R.; Primak, A.; Natarajan, D.; Markoski, L. J.; Kenis, P. J. A. J Am Chem Soc 2005, 127, 16758. (66) Wootton, R. C. R.; deMello, A. J. Chem Commun 2004, 266. (67) McPherson, A. J Appl Crystallogr 2000, 33, 397.

Exploring Health in Military Families: Does Continuity of Care Influence Patient Satisfaction?

To ensure mission-readiness for military members, support for their families is essential. Military family health and health care satisfaction has been a neglected area of study in this population. Satisfaction can be defined in terms of patient-, provider-, and practice-level factors and is influenced by continuity of care, which is often poor in transient military populations. Using a modified patient satisfaction survey, this study found that both the number of moves and assigned providers were significantly associated with continuity of care in military spouses. Further, continuity of care was a significant predictor of satisfaction with military health care.

Pinning Down Identity in Social Media: Food Cultural Transfer on Pinterest

This research has been conducted within the realm of where today’s digital media society and the timeless concept of cultural identity overlap. The aim of this thesis is to explore the nature of online cultural identity management. By focusing on the social media platform, Pinterest, this study considers the food-pinning behavior of a group of Americans living in Finland and connects their online actions with their cultural identity. Through an examination of Pinterest as a social space, and even a third place, the relative theoretical literature provides and interesting background for a contemporary discussion on the matter. Literature on food as a cultural marker is also brought into consideration. Using the methods of introspection and an adapted version of virtual ethnography, a study was conducted, and ultimately, the analysis of data obtained from the Pinterest boards of ten individuals shows that the vast majority of food-related information in this setting is US-sourced. A questionnaire provides further insight into the individuals’ Pinterest usage. I argue that pinning is an act of online identity management, whether it is a conscious act or a situational effect, and that using Pinterest maintains and even strengthens these individuals’ cultural identity as Americans. This study adds to current discussions pertaining to transnationalism, globalization, and online cultural identity, as well as opens channels for further research on this dynamic topic, which is needed to understand ourselves as cultural beings in the digital age.

"Let Us Sing as We Go": The Role of Music in the United States Suffrage Movement

Music played a prominent role in the United States women’s suffrage movement (1848–1920). Suffragists left behind hundreds of compositions supporting their cause and historical accounts indicate that musical performances were common at suffrage events. With only a few exceptions, scholars have disregarded the music used in this movement, and have underemphasized its significance. This study examines the use of music in the suffrage movement from three perspectives: music with lyrics, titles, and images that espouse women’s enfranchisement; music performed at national suffrage conventions held by the National American Woman Suffrage Association; and music accompanying suffrage parades. Though the music used varies in each case, it is clear that music played an important role in unifying suffragists and underscoring the ideals and goals of the movement.

Clima psicológico e desempenho organizacional nas secções de uma autarquia local

Dissertação de Mestrado apresentada ao Instituto Superior de Psicologia Aplicada para a obtenção do grau de Mestre na especificidade de Psicologia Social e das Organizações

Dysfonctions mitochondriales associées à l’acidose lactique du Saguenay-Lac-Saint-Jean révélées par l’étude d’un nouveau modèle murin de la maladie

Le syndrome de Leigh version canadienne-française (LSFC) est une maladie autosomale récessive causée par une mutation du gène LRPPRC, encodant une protéine du même nom. LRPPRC est impliquée dans la traduction des gènes mitochondriaux qui encodent certains complexes de la chaine respiratoire. Les répercussions biochimiques incluent un déficit tissu spécifique de la cytochrome c oxydase (COX), principalement dans le foie et le cerveau, et la survenue de crises d’acidose fatales chez 80 % des enfants atteints avant l’âge de 3-4 ans. L’identification d’options thérapeutiques demeure encore un défi de taille et ceci est en partie relié au manque de connaissances des fonctions biologiques de LRPPRC et des mécanismes impliqués dans la pathogenèse du LSFC, au niveau des dysfonctions mitochondriales résultantes. Afin d’étudier ces mécanismes, le consortium de l’acidose lactique, dont fait partie notre laboratoire, a récemment développé un modèle murin portant une ablation de LRPPRC spécifique au foie (souris H-Lrpprc-/-). L’objectif principal est de déterminer si ce modèle reproduit le phénotype pathologique observé dans les cultures de fibroblastes humains issus de biopsies de peau de patients LSFC. Dans le cadre des travaux de ce mémoire, nous avons amorcé la caractérisation de ce nouveau modèle, en examinant le phénotype général, l’histopathologie hépatique et les fonctions mitochondriales, et en nous focalisant principalement sur les fonctions respiratoires et la capacité à oxyder divers types de substrats. Nous avons observé un retard de croissance, une hépatomégalie ainsi que plusieurs anomalies histologiques du foie chez la souris HLrpprc-/-. De plus, l’ablation de LRPPRC induit un déficit du complexe IV, mais aussi de l’ATP synthase, et affecte l’oxydation des acides gras à longues chaines. À la lumière de ces résultats, nous croyons que le modèle murin H-Lrpprc-/- contribuera à l’avancement des connaissances générales sur LRPPRC, nous permettant de mieux comprendre l’influence de la protéine sur les fonctions mitochondriales.