MULTI IDENTITY CONFLICT: A CASE STUDY ON SUDANESE REFUGEES AND ASYLUM SEEKERS IN JORDAN

This inquiry was a completed as part of the requirements for earning a master of the arts degree in Peacebuilding and Conflict Transformation for the student William Clifton at SIT Graduate Institute. It was an independent practitioner inquiry based on the methodology of Grounded Theory that utilized qualitative research by way of in depth interviews and a focus group to understand how the identity shaped the experience of Sudanese migrants living in Jordan. In addition to these qualitative methods, a review of the literature was conducted on Sudanese populations in Sudan and in outside communities to help guide the process and provide information to compare as well as information about how these populations were treated by their host countries, with principal emphasis on the country of Jordan. The purpose of the research was to gain better understanding of this under researched minority population, to explore ways that identity conflict can affect them from various ways related to their identities, and to gather information about their level of institutional support and how that can be changed to further contribute to their well-being. The findings indicated that the participants expressed Geographical, Ethnic, and Religious Identities while also experiencing Racial Discrimination and Ascribed Identity. In addition, the participants expressed their reasons for coming to Jordan, described their livelihoods and institutional support. The author than wrote a 9 track diplomacy plan as a type of holistic intervention to serve the needs of that population

Multi Identity Conflict: A Case Study of Sudanese Refugees and Asylum Seekers in Jordan

This inquiry was a completed as part of the requirements for earning a Master\u27s of Arts degree in Peacebuilding and Conflict Transformation for the student William Clifton at SIT Graduate Institute. It was an independent practitioner inquiry based on the methodology of Grounded Theory that utilized qualitative research by way of in depth interviews and a focus group to understand how the identity shaped the experience of Sudanese migrants living in Jordan. In addition to these qualitative methods, a review of the literature was conducted on Sudanese populations in Sudan and in outside communities to help guide the process and provide information to compare as well as information about how these populations were treated by their host countries, with principal emphasis on the country of Jordan. The purpose of the research was to gain better understanding of this under researched minority population, to explore ways that identity conflict can affect them from various ways related to their identities, and to gather information about their level of institutional support and how that can be changed to further contribute to their well-being. The findings indicated that the participants expressed Geographical, Ethnic, and Religious Identities while also experiencing Racial Discrimination and Ascribed Identity. In addition, the participants expressed their reasons for coming to Jordan, described their livelihoods and institutional support. The author than wrote a 9 track diplomacy plan as a type of holistic intervention to serve the needs of that population

Process and apparatus for analyzing specimens for the presence of microorganisms therein

Microorganisms in a specimen are detected, identified, and enumerated by introducing the specimen into a sampling cartridge and diluting the specimen with a known volume of water within the cartridge. The cartridge has a manifold and several cassettes attached to the manifold. Each cassette contains a serpentine flow channel having a series of filters therein and a detection cell located downstream from each filter. The flow channel in each cassette also contains a culture medium which is freeze dried and is highly selective in the sense that it promotes the growth of one type of microorganism, but not others. The mixture of the specimen and water flows from the manifold into the flow channel of each cassette where it rehydrates the culture medium therein and further flows through the filters. Each filter removes a known proportion of the microorganisms from the mixture of specimen, water and medium, thereby effecting a serial dilution. After the cassettes are heated to incubate the microoganisms, the detection cells are observed for growth of the microorganisms therein which is manifested in a change in the light transmitting characteristics of the mixtures within the cells

Effects of local hypothermia-rewarming on physiology, metabolism and inflammation of acutely injured human spinal cord.

In five patients with acute, severe thoracic traumatic spinal cord injuries (TSCIs), American spinal injuries association Impairment Scale (AIS) grades A-C, we induced cord hypothermia (33 °C) then rewarming (37 °C). A pressure probe and a microdialysis catheter were placed intradurally at the injury site to monitor intraspinal pressure (ISP), spinal cord perfusion pressure (SCPP), tissue metabolism and inflammation. Cord hypothermia-rewarming, applied to awake patients, did not cause discomfort or neurological deterioration. Cooling did not affect cord physiology (ISP, SCPP), but markedly altered cord metabolism (increased glucose, lactate, lactate/pyruvate ratio (LPR), glutamate; decreased glycerol) and markedly reduced cord inflammation (reduced IL1β, IL8, MCP, MIP1α, MIP1β). Compared with pre-cooling baseline, rewarming was associated with significantly worse cord physiology (increased ICP, decreased SCPP), cord metabolism (increased lactate, LPR; decreased glucose, glycerol) and cord inflammation (increased IL1β, IL8, IL4, IL10, MCP, MIP1α). The study was terminated because three patients developed delayed wound infections. At 18-months, two patients improved and three stayed the same. We conclude that, after TSCI, hypothermia is potentially beneficial by reducing cord inflammation, though after rewarming these benefits are lost due to increases in cord swelling, ischemia and inflammation. We thus urge caution when using hypothermia-rewarming therapeutically in TSCI

Quantum Electronics

Contains research objectives and summary of research on eight research projects split into four sections.Joint Services Electronics Program (Contract DAAB07-76-C-1400)U. S. Air Force - Office of Scientific Research (Grant AFOSR-76-3042)U. S. Air Force - Office of Scientific Research (Contract F44620-76-C-0079

Ribosomal oxygenases are structurally conserved from prokaryotes to humans

2-Oxoglutarate (2OG)-dependent oxygenases have important roles in the regulation of gene expression via demethylation of N-methylated chromatin components1,2 and in the hydroxylation of transcription factors3 and splicing factor proteins4. Recently, 2OG-dependent oxygenases that catalyse hydroxylation of transfer RNA5,6,7 and ribosomal proteins8 have been shown to be important in translation relating to cellular growth, TH17-cell differentiation and translational accuracy9,10,11,12. The finding that ribosomal oxygenases (ROXs) occur in organisms ranging from prokaryotes to humans8 raises questions as to their structural and evolutionary relationships. In Escherichia coli, YcfD catalyses arginine hydroxylation in the ribosomal protein L16; in humans, MYC-induced nuclear antigen (MINA53; also known as MINA) and nucleolar protein 66 (NO66) catalyse histidine hydroxylation in the ribosomal proteins RPL27A and RPL8, respectively. The functional assignments of ROXs open therapeutic possibilities via either ROX inhibition or targeting of differentially modified ribosomes. Despite differences in the residue and protein selectivities of prokaryotic and eukaryotic ROXs, comparison of the crystal structures of E. coli YcfD and Rhodothermus marinus YcfD with those of human MINA53 and NO66 reveals highly conserved folds and novel dimerization modes defining a new structural subfamily of 2OG-dependent oxygenases. ROX structures with and without their substrates support their functional assignments as hydroxylases but not demethylases, and reveal how the subfamily has evolved to catalyse the hydroxylation of different residue side chains of ribosomal proteins. Comparison of ROX crystal structures with those of other JmjC-domain-containing hydroxylases, including the hypoxia-inducible factor asparaginyl hydroxylase FIH and histone Nε-methyl lysine demethylases, identifies branch points in 2OG-dependent oxygenase evolution and distinguishes between JmjC-containing hydroxylases and demethylases catalysing modifications of translational and transcriptional machinery. The structures reveal that new protein hydroxylation activities can evolve by changing the coordination position from which the iron-bound substrate-oxidizing species reacts. This coordination flexibility has probably contributed to the evolution of the wide range of reactions catalysed by oxygenases

High-Frequency (> 100 GHz) Electronic Devices

Contains reports on five research projects and a list of publications.MIT Lincoln LaboratoryNational Aeronautics and Space Administration Grant NAG2-693National Science Foundation Grant ECS 91-09330Defense Advanced Research Projects Agency Contract MDA972-90-C-0021U.S. Army - Research Office Grant DAAL03-92-G-025

Quantum Electronics

Contains thirteen research projects split into three sections.U.S. Air Force - Rome Air Development Center (Contract F19628-80-C-0077)National Science Foundation (Grant PHY79-09739)Joint Services Electronics Program (Contract DAAG29-78-C-0020)Joint Services Electronics Program (Contract DAAG29-80-C-0104)U.S. Air Force Geophysics Laboratory (AFSC) (Contract F19628-79-C-0082)National Science Foundation (Grant ECS79-19475)National Science Foundation (Grant DAR80-08752)National Science Foundation (Grant ENG79-09980

Quantum Electronics

Contains reports on three research projects.National Science Foundation (Grant PHY77-07156)Joint Services Electronics Program (Contract DAABO7-76-C-1400)U. S. Air Force - Office of Scientific Research (Grant AFOSR-76-3042)U. S. Air Force - Office of Scientific Research (Contract F-44620-76-C-0079)M.I.T. Sloan Fund for Basic Researc