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The purpose of this research was to study factors that facilitate technical knowledge sharing internally in international non-governmental organizations (INGOs) in Ecuador. Using a qualitative design, and semi-structured interviews this study examined knowledge sharing practices in four INGOS located in Quito, capital of Ecuador. The findings supported nine factors identified in the literature as influencing knowledge sharing practices. These factors included (1) organizational culture, (2) role in organization, (3) procedures for managing knowledge, (4) perceived value of knowledge sharing, (5) media used for sharing information, (6) management practices, (7) organizational structure, (8) mission and strategy, and (9) organizational climate and motivation. In addition, seventeen new factors emerged in the Ecuadorian context to influence knowledge sharing. All these factors not only support knowledge sharing in INGOs but also increase people’s skills for capacity building so that INGOs can fulfill their missions effectively.

The purpose of this research was to study factors that facilitate technical knowledge sharing internally in international non-governmental organizations (INGOs) in Ecuador. Using a qualitative design, and semi-structured interviews this study examined knowledge sharing practices in four INGOS located in Quito, capital of Ecuador. The findings supported nine factors identified in the literature as influencing knowledge sharing practices. These factors included (1) organizational culture, (2) role in organization, (3) procedures for managing knowledge, (4) perceived value of knowledge sharing, (5) media used for sharing information, (6) management practices, (7) organizational structure, (8) mission and strategy, and (9) organizational climate and motivation. In addition, seventeen new factors emerged in the Ecuadorian context to influence knowledge sharing. All these factors not only support knowledge sharing in INGOs but also increase people’s skills for capacity building so that INGOs can fulfill their missions effectively.

Chronic fibrosis caused by acute myocardial infarction (MI) leads to increased morbidity and mortality due to cardiac dysfunction. Despite care in the acute setting of MI, subsequent development of scar tissue and a lack of treatments for this maladaptive response lead to a poor prognosis. This has increased burdens on the cost of healthcare due to chronic disability. Here a novel therapeutic strategy that aims to mitigate myocardial fibrosis by utilizing injectable polymeric microstructural cues to attenuate the fibrotic response and improve functional outcomes is presented. Additionally, applications of integrated chemical functionalizations into discrete, micro-scale polymer structures are discussed in the realm of tissue engineering in order to impart enhancements in in vivo localization, three-dimensional manipulation and drug delivery.Polymeric microstructures, termed "microrods" and "microcubes", were fabricated using photolithographic techniques and studied in three-dimensional culture models of the fibrotic environment and by direct injection into the infarct zone of adult Sprague-Dawley rats. In vitro gene expression and functional and histological results were analyzed, showing a dose-dependent down-regulation fibrotic indicators and improvement in cardiac function. Furthermore, iron oxide nanoparticles and functionalized fluorocarbons were incorporated into the polymeric microdevices to promote in situ visualization by magnetic resonance imaging as well as to facilitate the manipulation and alignment of microstructural cues in a tissue-realistic environment. Lastly, successful encapsulation of native MGF peptide within microrods is demonstrated with release over two weeks as a proof of concept in the ability to locally deliver myogenic or supportive pharmacotherapeutics to the injured myocardium.This work demonstrates the efficacy and versatility of discrete microtopographical cues to attenuate the fibrotic response after MI and suggests a novel therapeu

Chronic fibrosis caused by acute myocardial infarction (MI) leads to increased morbidity and mortality due to cardiac dysfunction. Despite care in the acute setting of MI, subsequent development of scar tissue and a lack of treatments for this maladaptive response lead to a poor prognosis. This has increased burdens on the cost of healthcare due to chronic disability. Here a novel therapeutic strategy that aims to mitigate myocardial fibrosis by utilizing injectable polymeric microstructural cues to attenuate the fibrotic response and improve functional outcomes is presented. Additionally, applications of integrated chemical functionalizations into discrete, micro-scale polymer structures are discussed in the realm of tissue engineering in order to impart enhancements in in vivo localization, three-dimensional manipulation and drug delivery.Polymeric microstructures, termed "microrods" and "microcubes", were fabricated using photolithographic techniques and studied in three-dimensional culture models of the fibrotic environment and by direct injection into the infarct zone of adult Sprague-Dawley rats. In vitro gene expression and functional and histological results were analyzed, showing a dose-dependent down-regulation fibrotic indicators and improvement in cardiac function. Furthermore, iron oxide nanoparticles and functionalized fluorocarbons were incorporated into the polymeric microdevices to promote in situ visualization by magnetic resonance imaging as well as to facilitate the manipulation and alignment of microstructural cues in a tissue-realistic environment. Lastly, successful encapsulation of native MGF peptide within microrods is demonstrated with release over two weeks as a proof of concept in the ability to locally deliver myogenic or supportive pharmacotherapeutics to the injured myocardium.This work demonstrates the efficacy and versatility of discrete microtopographical cues to attenuate the fibrotic response after MI and suggests a novel therapeu

Ancestral coatomer element 1 (ACE1) proteins assemble latticework coats for COPII vesicles and the nuclear pore complex. The ACE1 protein Sec31 and Sec13 make a 2:2 tetramer that forms the edge element of the COPII outer coat. In this study, we report that the COPII accessory protein Sec16 also contains an ACE1. The 165-kD crystal structure of the central domain of Sec16 in complex with Sec13 was solved at 2.7-Å resolution. Sec16 and Sec13 also make a 2:2 tetramer, another edge element for the COPII system. Domain swapping at the ACE1–ACE1 interface is observed both in the prior structure of Sec13–Sec31 and in Sec13–Sec16. A Sec31 mutant in which domain swapping is prevented adopts an unprecedented laminated structure, solved at 2.8-Å resolution. Our in vivo data suggest that the ACE1 element of Sec31 can functionally replace the ACE1 element of Sec16. Our data support Sec16 as a scaffold for the COPII system and a template for the Sec13–Sec31 coat., Pew Charitable Trusts (Pew Scholar Award), National Center for Research Resources (U.S.) (Award RR-15301), United States. Dept. of Energy. Office of Basic Energy Sciences (Contract DE-AC02-06CH11357)

http://archive.org/details/ananuykinterpret1094515989

Nuclear pore complexes (NPCs) perforate the nuclear envelope and represent the exclusive passageway into and out of the nucleus of the eukaryotic cell. Apart from their essential transport function, components of the NPC have important, direct roles in nuclear organization and in gene regulation. Because of its central role in cell biology, it is of considerable interest to determine the NPC structure at atomic resolution. The complexity of these large, 40–60 MDa protein assemblies has for decades limited such structural studies. More recently, exploiting the intrinsic modularity of the NPC, structural biologists are making progress toward understanding this nanomachine in molecular detail. Structures of building blocks of the stable, architectural scaffold of the NPC have been solved, and distinct models for their assembly proposed. Here we review the status of the field and lay out the challenges and the next steps toward a full understanding of the NPC at atomic resolution., Pew Charitable Trusts (Scholars Program), National Institutes of Health (U.S.) (Grant GM077537)

Thesis (Ph. D.)--Massachusetts Institute of Technology, Dept. of Biology, 2010., This electronic version was submitted by the student author. The certified thesis is available in the Institute Archives and Special Collections., Cataloged from student submitted PDF version of thesis., Includes bibliographical references (p. 127-142)., The Nuclear Pore Complex (NPC) is a ~50 MDa protein complex that forms the sole conduit for macromolecular transport across the nuclear envelope. It assembles from ~30 proteins, termed nucleoporins or nups, symmetrically arranged about a central 8-fold axis. Some nucleoporins also contribute to other structures or perform diverse other functions. A subset forms a stably-associated core scaffold for the NPC, organized into two large subcomplexes, the Y-complex and the Nic96-complex. Studies using electron microscopy and X-ray crystallography have begun to elucidate the architecture of the NPC scaffold. To better understand the NPC and related proteins, two studies were performed: 1. The crystal structure of the C-terminal a-helical domain of Nup133 in complex with the C terminus of Nup107 revealed (with a prior structure of the N-terminal β-propeller domain of Nup133) the complete structure of Nup133 and its connection to the Y-complex. This contributes to a nearly complete molecular model of the Y-complex. Nup107-Nup133 forms the distal half of the stalk of the Y-complex. Sequence similarity between Nup133 and another nucleoporin, Nup170, was detected, and structural similarity proven by solving the structure of the a-helical domain of Nup170. Nup170 is a member of the Nic96-complex. Similarity between Nup133 and Nup170 suggests that the Y-complex and the Nic96-complex employ the same architectural principles. 2. Four nucleoporins contain an a-helical domain structurally related to the COPII coat protein Sec31. This domain is called the ancestral coatomer element 1 (ACE1). Sec13-Sec31 and Nup84-Nup145C-Sec13 complexes form analogous edge elements for the COPII coat and the NPC. A sequence-based search for other ACE1s identified the COPII accessory protein Sec16. Sec16 and Sec13 were shown to form a 2:2 heterotetramer. A crystal structure of Sec13-Sec16 revealed similarities to the Sec13-Sec31 edge element. Together with other structural and in vivo data, this result, by James Richardson Ross Whittle., Ph.D.

Thesis (Ph. D.)--Massachusetts Institute of Technology, Dept. of Biology, 2010., This electronic version was submitted by the student author. The certified thesis is available in the Institute Archives and Special Collections., Cataloged from student submitted PDF version of thesis., Includes bibliographical references (p. 127-142)., The Nuclear Pore Complex (NPC) is a ~50 MDa protein complex that forms the sole conduit for macromolecular transport across the nuclear envelope. It assembles from ~30 proteins, termed nucleoporins or nups, symmetrically arranged about a central 8-fold axis. Some nucleoporins also contribute to other structures or perform diverse other functions. A subset forms a stably-associated core scaffold for the NPC, organized into two large subcomplexes, the Y-complex and the Nic96-complex. Studies using electron microscopy and X-ray crystallography have begun to elucidate the architecture of the NPC scaffold. To better understand the NPC and related proteins, two studies were performed: 1. The crystal structure of the C-terminal a-helical domain of Nup133 in complex with the C terminus of Nup107 revealed (with a prior structure of the N-terminal β-propeller domain of Nup133) the complete structure of Nup133 and its connection to the Y-complex. This contributes to a nearly complete molecular model of the Y-complex. Nup107-Nup133 forms the distal half of the stalk of the Y-complex. Sequence similarity between Nup133 and another nucleoporin, Nup170, was detected, and structural similarity proven by solving the structure of the a-helical domain of Nup170. Nup170 is a member of the Nic96-complex. Similarity between Nup133 and Nup170 suggests that the Y-complex and the Nic96-complex employ the same architectural principles. 2. Four nucleoporins contain an a-helical domain structurally related to the COPII coat protein Sec31. This domain is called the ancestral coatomer element 1 (ACE1). Sec13-Sec31 and Nup84-Nup145C-Sec13 complexes form analogous edge elements for the COPII coat and the NPC. A sequence-based search for other ACE1s identified the COPII accessory protein Sec16. Sec16 and Sec13 were shown to form a 2:2 heterotetramer. A crystal structure of Sec13-Sec16 revealed similarities to the Sec13-Sec31 edge element. Together with other structural and in vivo data, this result, by James Richardson Ross Whittle., Ph.D.

Thesis (Ph. D.)--Massachusetts Institute of Technology, Dept. of Biology, 2010., This electronic version was submitted by the student author. The certified thesis is available in the Institute Archives and Special Collections., Cataloged from student submitted PDF version of thesis., Includes bibliographical references (p. 127-142)., The Nuclear Pore Complex (NPC) is a ~50 MDa protein complex that forms the sole conduit for macromolecular transport across the nuclear envelope. It assembles from ~30 proteins, termed nucleoporins or nups, symmetrically arranged about a central 8-fold axis. Some nucleoporins also contribute to other structures or perform diverse other functions. A subset forms a stably-associated core scaffold for the NPC, organized into two large subcomplexes, the Y-complex and the Nic96-complex. Studies using electron microscopy and X-ray crystallography have begun to elucidate the architecture of the NPC scaffold. To better understand the NPC and related proteins, two studies were performed: 1. The crystal structure of the C-terminal a-helical domain of Nup133 in complex with the C terminus of Nup107 revealed (with a prior structure of the N-terminal β-propeller domain of Nup133) the complete structure of Nup133 and its connection to the Y-complex. This contributes to a nearly complete molecular model of the Y-complex. Nup107-Nup133 forms the distal half of the stalk of the Y-complex. Sequence similarity between Nup133 and another nucleoporin, Nup170, was detected, and structural similarity proven by solving the structure of the a-helical domain of Nup170. Nup170 is a member of the Nic96-complex. Similarity between Nup133 and Nup170 suggests that the Y-complex and the Nic96-complex employ the same architectural principles. 2. Four nucleoporins contain an a-helical domain structurally related to the COPII coat protein Sec31. This domain is called the ancestral coatomer element 1 (ACE1). Sec13-Sec31 and Nup84-Nup145C-Sec13 complexes form analogous edge elements for the COPII coat and the NPC. A sequence-based search for other ACE1s identified the COPII accessory protein Sec16. Sec16 and Sec13 were shown to form a 2:2 heterotetramer. A crystal structure of Sec13-Sec16 revealed similarities to the Sec13-Sec31 edge element. Together with other structural and in vivo data, this result, by James Richardson Ross Whittle., Ph.D.

Thesis (Ph. D.)--Massachusetts Institute of Technology, Dept. of Biology, 2010., This electronic version was submitted by the student author. The certified thesis is available in the Institute Archives and Special Collections., Cataloged from student submitted PDF version of thesis., Includes bibliographical references (p. 127-142)., The Nuclear Pore Complex (NPC) is a ~50 MDa protein complex that forms the sole conduit for macromolecular transport across the nuclear envelope. It assembles from ~30 proteins, termed nucleoporins or nups, symmetrically arranged about a central 8-fold axis. Some nucleoporins also contribute to other structures or perform diverse other functions. A subset forms a stably-associated core scaffold for the NPC, organized into two large subcomplexes, the Y-complex and the Nic96-complex. Studies using electron microscopy and X-ray crystallography have begun to elucidate the architecture of the NPC scaffold. To better understand the NPC and related proteins, two studies were performed: 1. The crystal structure of the C-terminal a-helical domain of Nup133 in complex with the C terminus of Nup107 revealed (with a prior structure of the N-terminal β-propeller domain of Nup133) the complete structure of Nup133 and its connection to the Y-complex. This contributes to a nearly complete molecular model of the Y-complex. Nup107-Nup133 forms the distal half of the stalk of the Y-complex. Sequence similarity between Nup133 and another nucleoporin, Nup170, was detected, and structural similarity proven by solving the structure of the a-helical domain of Nup170. Nup170 is a member of the Nic96-complex. Similarity between Nup133 and Nup170 suggests that the Y-complex and the Nic96-complex employ the same architectural principles. 2. Four nucleoporins contain an a-helical domain structurally related to the COPII coat protein Sec31. This domain is called the ancestral coatomer element 1 (ACE1). Sec13-Sec31 and Nup84-Nup145C-Sec13 complexes form analogous edge elements for the COPII coat and the NPC. A sequence-based search for other ACE1s identified the COPII accessory protein Sec16. Sec16 and Sec13 were shown to form a 2:2 heterotetramer. A crystal structure of Sec13-Sec16 revealed similarities to the Sec13-Sec31 edge element. Together with other structural and in vivo data, this result, by James Richardson Ross Whittle., Ph.D.

Weekly publication. Teaneck Edition.

Weekly publication. Teaneck Edition.

Scott Helms, conductor.; Soloists: Deborah Collins, mallet percussion, James Jones, mallet percussion, Linette Richardson, mallet percussion, Ryan Schwartz, mallet percussion, Randall Sorensen, trumpet.; Includes a list of the personnel of the Concert Band, with section leaders., Series XLVII, Number 189., This archival material has been provided for educational purposes. Ball State University Libraries recognizes that some historic items may include offensive content. Our statement regarding objectionable content is available at: https://dmr.bsu.edu/digital/about

Scott Helms, conductor.; Soloists: Deborah Collins, mallet percussion, James Jones, mallet percussion, Linette Richardson, mallet percussion, Ryan Schwartz, mallet percussion, Randall Sorensen, trumpet.; Includes a list of the personnel of the Concert Band, with section leaders., Series XLVII, Number 189., This archival material has been provided for educational purposes. Ball State University Libraries recognizes that some historic items may include offensive content. Our statement regarding objectionable content is available at: https://dmr.bsu.edu/digital/about

Michigan Quarterly Review: vol. XXXVIII, no. 2, (dlps) act2080.0038.210, http://hdl.handle.net/2027/spo.act2080.0038.210, This work is protected by copyright and may be linked to without seeking permission. Permission must be received for subsequent distribution in print or electronically. Please contact mpub-help@umich.edu for more information.

Michigan Quarterly Review: vol. XXXVIII, no. 2, (dlps) act2080.0038.210, http://hdl.handle.net/2027/spo.act2080.0038.210, This work is protected by copyright and may be linked to without seeking permission. Permission must be received for subsequent distribution in print or electronically. Please contact mpub-help@umich.edu for more information.

An IBM System/360 based interpreter program for the AN/UYK-7 multiprocessing computer system is presented. The program provides interpretive execution of the AN/UYK-7 instruction set, an interrupt-handling capability, a variable-sized simulated memory and a multiprocessing capability for up to three central processors. Input/output is limited to a card reader and a line printer. Various segments of the program are discussed and a detailed User's Manual is provided. (Author)