Understanding Organisational Change in Museums: An Investigation of Evolving Museum Priorities and Practices at The National Museum of Natural Science, Taiwan

In this time of rapid political, economic, social and technological change, museums of all kinds face continuous pressures and demands from a variety of stakeholders. These demands are frequently competing (or at least in tension), arising from the different agendas, interests and requirements of diverse stakeholders which, in turn, raise questions around the purposes and priorities of museums. Although many literatures have contributed to the discussion around the museum’s purpose, there remains a lack of in-depth, grounded analysis that explores museums’ structures, processes, and practices and the role of individuals and broader forces for change in the making and reshaping of the organisation. In short, there has been relatively little scholarly attention given to the study of the museum as an ever-changing, dynamic and complex organisation. Drawing on organisational change studies, management theories and museum studies, this thesis seeks to understand the processes that contribute to the reshaping of the museum’s purpose, priorities and practices by staff and other agents through a qualitative investigation of change within a single institution. The aims of the research are to better understand the role of leadership in the process of change and the dynamic attitudes, values and power relations that underpin such processes. In order to explore the hidden complexities of the internal workings in the museum, this paper employs a single case study - the National Museum of Natural Science (NMNS) in Taiwan – that was investigated through an organisational ethnography approach. This thesis focuses on two main forces for change. One is the increasing influence of market forces that encourage the museum to move towards more business-like practices. The other is a growing appreciation of the social responsibility of the museum. These two predominantly external forces play out in a different ways and, at the same time, emerge as significant factors which influence the museum’s move away from traditional functions and conventional works and practices. By revealing various values, interests and power dynamics intersecting at the organisational and personal levels, the thesis aims to contribute an enhanced understanding of how and why change occurs in museums and how potentially competing interests can be negotiated

Changes in eGFR for (A) all patients (n = 40), and those evaluated at (B) 3 months after discharge (n = 11), (C) 6 months after discharge (n = 2), (D) 9 months after discharge (n = 6), and (E) 12 months after discharge (n = 21).

<p>Changes in eGFR for (A) all patients (n = 40), and those evaluated at (B) 3 months after discharge (n = 11), (C) 6 months after discharge (n = 2), (D) 9 months after discharge (n = 6), and (E) 12 months after discharge (n = 21).</p

Mean (±SD) eGFR and Cr of patients at admission and at 3 to 12 months after discharge (n = 40).

†<p>Paired t-test.</p

Baseline characteristics of study subjects admitted to the emergency department for renal infarction (n = 40).

<p>Baseline characteristics of study subjects admitted to the emergency department for renal infarction (n = 40).</p

Multivariate analysis of risk factors associated with chronic kidney disease at follow-up among patients admitted for renal infarction.

<p>OR: odds ratio; CI: confidence interval.</p>a<p>Median served as the cutoff value.</p

Protein Arginine Methyltransferase 8: Tetrameric Structure and Protein Substrate Specificity

Type I protein arginine methyltransferases (PRMTs) catalyze asymmetric dimethylation of various proteins, and their dysregulations often correlate with tumorigenesis or developmental deficiency. Recent studies have focused on the <i>in vivo</i> substrate identification and the enzyme mechanism with peptide substrates. However, how PRMTs recognize substrates at the protein level remains unknown. PRMT8 is one of the least characterized type I PRMTs, and its crystal structure has not been reported. Here, we report the crystal structure of the PRMT8:SAH complex, identify a new non-histone protein substrate NIFK, and uncover a previously unknown regulatory region specifically required for recognizing NIFK. Instead of the canonical dimeric structure for other type I PRMTs, PRMT8 exists as a tetramer in solution. Using X-ray crystallography in combination with small-angle X-ray scattering experiments, the dimer of dimers architecture in which two PRMT8 dimers are held together mainly by β strand interactions was proposed. Mutation of PRMT8-β15 impedes the methylation of NIFK but still allows methylation of the histone H2A/H2B dimer or a peptide substrate, suggesting a possible structural basis for recognition of protein substrates. Lastly, we observed two PRMT8 dimer orientations resulting in open (without SAH) and closed (with SAH bound) conformations. The comparison between open and closed conformations may provide useful information for PRMT1/8 inhibitor design