209 research outputs found
Small heat-shock proteins: important players in regulating cellular proteostasis
Small heat-shock proteins (sHsps) are a diverse family of intra-cellular molecular chaperone proteins that play a critical role in mitigating and preventing protein aggregation under stress conditions such as elevated temperature, oxidation and infection. In doing so, they assist in the maintenance of protein homeostasis (proteostasis) thereby avoiding the deleterious effects that result from loss of protein function and/or protein aggregation. The chaperone properties of sHsps are therefore employed extensively in many tissues to prevent the development of diseases associated with protein aggregation. Significant progress has been made of late in understanding the structure and chaperone mechanism of sHsps. In this review, we discuss some of these advances, with a focus on mammalian sHsp hetero-oligomerisation, the mechanism by which sHsps act as molecular chaperones to prevent both amorphous and fibrillar protein aggregation, and the role of post-translational modifications in sHsp chaperone function, particularly in the context of disease.SM was supported by a Royal Society Dorothy Hodgkin Fellowship, HE is supported by an Australian Research Council Future Fellowship (FT110100586) and JC is supported by a National Health and Medical Research Council Project Grant (#1068087)
How students can develop skills to cope with academic stress
The University of Cumbria's Sarah Meehan (Mental Health Caseworker) and Liz Mallabon (Principal Lecturer in Outdoor Studies) explain how students can develop skills to cope with academic stress
Reduced erbium-doped ceria nanoparticles: one nano-host applicable for simultaneous optical down- and up-conversions
This paper introduces a new synthesis procedure to form erbium-doped ceria nanoparticles (EDC NPs) that can act as an optical medium for both up-conversion and down-conversion in the same time. This synthesis process results qualitatively in a high concentration of Ce(3+) ions required to obtain high fluorescence efficiency in the down-conversion process. Simultaneously, the synthesized nanoparticles contain the molecular energy levels of erbium that are required for up-conversion. Therefore, the synthesized EDC NPs can emit visible light when excited with either UV or IR photons. This opens new opportunities for applications where emission of light via both up- and down-conversions from a single nanomaterial is desired such as solar cells and bio-imaging
Herstory Writers Workshop
Herstory Writerâs Workshop, founded in 1996 by Erika Duncan, was involved
on the LIU Post campus this semester providing internships that enhanced
studentâs writing skills while serving as an opportunity for civic engagement.
Herstory runs these workshops at many Long Island campuses such
as Hofstra, Adelphi, and St. Josephâs. During the workshops, high school
students and college students write and share their personal memoirs
involving social issues such as immigration, substance abuse, gender
identity, gang involvement, poverty, and health care. During the Spring 2017
semester, about ten Westbury High School students were brought by school
bus to attend weekly workshops with LIU Post students, faculty, and two
trained Herstory Facilitators. Desks in the classroom in Kahn Hall were set
in a circle to facilitate the seminar style of pedagogy. Students worked on
their writing throughout the week and read their work to each other in the
Kahn Hall classroom each week. Feedback from peers and the facilitators
was shared. This poster highlights Herstoryâs role in addressing the issue
of social amelioration among the American youth. We also present quotations
from our fellow peers on how the internship has had a positive impact
on their lives. Herstoryâs purpose is âBringing unheard voices into the public
arenaâŠto change hearts, minds, and policy.â Ultimately, this poster will shed
light on Herstoryâs goals, purpose, and overall concern with social justice
The trauma of the body in the drama of Artaud, Beckett and Genet: a paradox of the speaking being
The mind-body problem has perplexed scholars, philosophers and thinkers for centuries if not millennia. This doctoral thesis addresses an epistemology of the body in its regard to subjectivity through an analysis of the drama of Artaud, Beckett and Genet. A fundamental premise in this study is that there is a traumatic and alienating dimension to embodiment which is resistant to expression within representation systems. In particular, the ideas of Jacques Lacan, as they concern language, the body and trauma are applied to considering the representation of the body within the dramatic works. Hence, a fundamental principle in this thesis is that the human being is a divided subject regarding the body. The structure of this thesis is interdisciplinary and creates a dialogue between psychoanalytic studies, theatre studies, disability studies, and the subject of the body in the dramatic works of the three authors. The purpose of this encounter between disciplines is to formulate a mutually augmenting dialectic where the end âproductâ regarding a knowledge of the body is a synthesis of this work. This approach aims to avoid the limitations of applying a theory to a subject that presumes a knowledge of the body a priori. Through a reading of specific texts and performances, this proposal challenges narratives and simplifications of the relationship between mind and body that permeate sociocultural discourse. The structure of the thesis consists of an overview of the background to the topic of the body and the context of the authors in chapter 1. A Lacanian account of the body and its application to theatre in Chapter 2. Chapters 3 and 4, focus on analyses of specific dramatic works. Finally, in chapter 5, I provide a comparative analysis of the theme of the body in the work of the three authors
Small heat-shock proteins: important players in regulating cellular proteostasis
Small heat-shock proteins (sHsps) are a diverse family of intra-cellular molecular chaperone proteins that play a critical role in mitigating and preventing protein aggregation under stress conditions such as elevated temperature, oxidation and infection. In doing so, they assist in the maintenance of protein homeostasis (proteostasis) thereby avoiding the deleterious effects that result from loss of protein function and/or protein aggregation. The chaperone properties of sHsps are therefore employed extensively in many tissues to prevent the development of diseases associated with protein aggregation. Significant progress has been made of late in understanding the structure and chaperone mechanism of sHsps. In this review, we discuss some of these advances, with a focus on mammalian sHsp hetero-oligomerisation, the mechanism by which sHsps act as molecular chaperones to prevent both amorphous and fibrillar protein aggregation, and the role of post-translational modifications in sHsp chaperone function, particularly in the context of disease
Combination of hydrogel nanoparticles and proteomics to reveal secreted proteins associated with decidualization of human uterine stromal cells
<p>Abstract</p> <p>Background</p> <p>Identification of secreted proteins of low abundance is often limited by abundant and high molecular weight (MW) proteins. We have optimised a procedure to overcome this limitation.</p> <p>Results</p> <p>Low MW proteins in the conditioned media of cultured cells were first captured using dual-size exclusion/affinity hydrogel nanoparticles and their identities were then revealed by proteomics.</p> <p>Conclusions</p> <p>This technique enables the analysis of secreted proteins of cultured cells low MW and low abundance.</p
Parentsâ Perceptions of the Philly Goat Projectâs All Abilities RAMble: A Qualitative Study of Animal-Assisted Intervention for Intellectual and Developmental Disorders
Individuals with intellectual and developmental disabilities (IDD) are a growing population. Considering the wide diversity in IDD and the financial burden of traditional treatment modalities, Animal-Assisted Interventions (AAI) has emerged as an innovative and non-traditional treatment for individuals with a range of disabilities, including individuals with IDD. To the authorsâ knowledge, the present study was one of the first to explore a goat-assisted therapy experience for children with IDD. This study explored the experiences of 23 children with the All Abilities RAMble â a goat-assisted therapeutic activity offered by the Philly Goat Project (PGP). Key themes in our study included the RAMble activating joy, RAMble as a place to practice skills, RAMble as a unique service providing transferable skills, RAMble as a personalized and child-directed program, and RAMble providing a sense of community. This research provides valuable insight into the childâs experience with goat-assisted therapy, which can inform future goat-assisted therapy interventions for children with IDD. The results suggest there are several positive impacts from the All Abilities RAMble, further supported by the literature on AAI and IDD. Additionally, the emergence of social skill(s) and communication skill development, transferability of acquired skills, and sense of community prompted provided strength in this exploratory inquiry of this specific form of AAI. Goat-assisted therapeutic activities, such as the PGP All Abilities RAMble, is an opportunity to practice skills and develop relationships that are often under-examined in this specific population. This study demonstrates the need for more empirical research on goat-specific AAI with children with IDD, and their families. Future research recommendations include exploration of siblings and parentsâ experience at the RAMble and further inquiry into what contributes to outdoor or nature-based programming beneficial to people with disabilities
The interaction of unfolding α-lactalbumin and malate dehydrogenase with the molecular chaperone αB-crystallin: a light and X-ray scattering investigation
Purpose: The molecular chaperone αB-crystallin is found in high concentrations in the lens and is present in all major body tissues. Its structure and the mechanism by which it protects its target protein from aggregating and precipitating are not known. Methods: Dynamic light scattering and X-ray solution scattering techniques were used to investigate structural features of the αB-crystallin oligomer when complexed with target proteins under mild stress conditions, i.e., reduction of α- lactalbumin at 37 °C and malate dehydrogenase when heated at 42 °C. In this investigation, the size, shape and particle distribution of the complexes were determined in real-time following the induction of stress. Results: Overall, it is observed that the mass distribution, hydrodynamic radius, and spherical shape of the αB-crystallin oligomer do not alter significantly when it complexes with its target protein. Conclusions: The data are consistent with the target protein being located in the outer protein shell of the αB-crystallin oligomer where it is readily accessible for possible refolding via the action of other molecular chaperones. © 2010 Molecular Vision
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