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Institution

Roosevelt University

EducationChicago, Illinois, United States
About: Roosevelt University is a education organization based out in Chicago, Illinois, United States. It is known for research contribution in the topics: Electron paramagnetic resonance & Population. The organization has 751 authors who have published 1482 publications receiving 44299 citations.


Papers
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Journal ArticleDOI
TL;DR: The Racial Microaggression Scale distress subscales may aid health professionals in assessing the distress elicited by different types of microaggressions, and this may facilitate diagnosis and treatment planning in order to provide multiculturally competent care for African American, Latino, and Asian American clients.
Abstract: Racial microaggressions are everyday subtle or ambiguous racially related insults, slights, mistreatment, or invalidations. Racial microaggressions are a type of perceived racism that may negativel...

46 citations

Journal ArticleDOI
TL;DR: It is concluded that a clear understanding of the effects of habitat loss and fragmentation on functional diversity will improve predictions of the resiliency and resistance of plant communities to varying scales of disturbance.
Abstract: Habitat loss and fragmentation result in significant landscape changes that ultimately affect plant diversity and add uncertainty to how natural areas will respond to future global change. This uncertainty is important given that the loss of biodiversity often includes losing key ecosystem functions. Few studies have explored the effects of landscape changes on plant functional diversity and evidence so far has shown far more pervasive effects than previously reported by species richness and composition studies. Here we present a review on the impact of habitat loss and fragmentation on (1) individual functional traits—related to persistence, dispersal and establishment—and (2) functional diversity. We also discuss current knowledge gaps and propose ways forward. From the literature review we found that studies have largely focused on dispersal traits, strongly impacted by habitat loss and fragmentation, while traits related to persistence were the least studied. Furthermore, most studies did not distinguish habitat loss from spatial fragmentation and were conducted at the plot or fragment-level, which taken together limits the ability to generalize the scale-dependency of landscape changes on plant functional diversity. For future work, we recommend (1) clearly distinguishing the effects of habitat loss from those of fragmentation, and (2) recognizing the scale-dependency of predicted responses when functional diversity varies in time and space. We conclude that a clear understanding of the effects of habitat loss and fragmentation on functional diversity will improve predictions of the resiliency and resistance of plant communities to varying scales of disturbance.

46 citations

Journal ArticleDOI
TL;DR: Stabilizing the native pCRP conformation represents a promising anti-inflammatory therapeutic strategy by attenuation of leukocyte recruitment and ROS formation, the primary pathomechanisms of IRI.
Abstract: Introduction: C-reactive protein circulates as a pentameric protein (pCRP). pCRP is a well-established diagnostic marker as plasma levels rise in response to tissue injury and inflammation. We recently described pro-inflammatory properties of CRP, which are mediated by conformational changes from pCRP to bioactive isoforms expressing pro-inflammatory neo-epitopes (pCRP* and mCRP). Here, we investigate the role of CRP isoforms in renal ischemia/reperfusion injury (IRI). Methods: Rat kidneys in animals with and without intraperitoneally injected pCRP were subjected to IRI by the time of pCRP exposure and were subsequently analyzed for monocyte infiltration, caspase-3 expression and tubular damage. Blood urea nitrogen (BUN) was analyzed pre-ischemia and post-reperfusion. CRP effects on leukocyte recruitment were investigated via intravital imaging of rat striated muscle IRI. Localized conformational CRP changes were analyzed by immunohistochemistry using conformation specific antibodies. 1,6-bis(phosphocholine)-hexane (1,6-bisPC), which stabilizes CRP in its native pentameric form was used to validate CRP effects. Leukocyte activation was assessed by quantification of reactive oxygen species (ROS) induction by CRP isoforms ex vivo and in vitro through electron spin resonance (ESR) spectroscopy. Signaling pathways were analyzed by disrupting lipid rafts with nystatin and subsequent ROS detection. In order to confirm the translational relevance of our findings, biopsies of microsurgical human free tissue transfers before and after IRI were examined by immunofluorescence for CRP deposition and co-localization of CD68+ leukocytes. Results: The application of pCRP aggravates tissue damage in renal IRI. 1,6-bisPC reverses these effects via inhibition of the conformational change that leads to exposure of pro-inflammatory epitopes in CRP (pCRP* and mCRP). Structurally altered CRP induces leukocyte-endothelial interaction and induces ROS formation in leukocytes, the latter can be abrogated by blocking lipid raft dependent signaling pathways with Nystatin. Stabilizing pCRP in its native pentameric state abrogates these pro-inflammatory effects. Importantly, these findings are confirmed in human IRI challenged muscle tissue. Conclusion: These results suggest that CRP is a potent modulator of IRI. Stabilizing the native pCRP conformation represents a promising anti-inflammatory therapeutic strategy by attenuation of leukocyte recruitment and ROS formation, the primary pathomechanisms of IRI.

45 citations

Journal ArticleDOI
TL;DR: The last two decades of research performed on hyperthermophiles and reverse gyrase are summarized in an effort to provide an up to date synopsis of their invariable association.
Abstract: With the discovery of reverse gyrase in 1972, from Yellowstone National Park, isolated from Sulfolobus acidocaldarius, it has been speculated as to why reverse gyrase can be found in all hyperthermophiles and just what exactly its role is in hyperthermophilic organisms. Hyperthermophiles have been defined as organisms with an optimal growth temperature of above 85°C. Reverse gyrase is responsible for the introduction of positive supercoils into closed circular DNA. This review of reverse gyrase in hyperthermophilic microorganisms summarizes the last two decades of research performed on hyperthermophiles and reverse gyrase in an effort to provide an up to date synopsis of their invariable association. From the data gathered for this review it is reasonable to hypothesize that reverse gyrase is closely tied to hyperthermophilic life.

45 citations

Journal ArticleDOI
TL;DR: A modified reaction mechanism for this intriguing DNA repair enzyme is proposed, suggesting that some protein residue(s), which is capable of exchanging a proton with the aqueous buffer, is involved in the enzyme catalysis.
Abstract: 5-Thyminyl-5,6-dihydrothymine (commonly called spore photoproduct or SP) is the exclusive DNA photodamage product in bacterial endospores. It is generated in the bacterial sporulation phase and repaired by a radical SAM enzyme, spore photoproduct lyase (SPL), at the early germination phase. SPL utilizes a special [4Fe-4S] cluster to reductively cleave S-adenosylmethionine (SAM) to generate a reactive 5'-dA radical. The 5'-dA radical is proposed to abstract one of the two H-atoms at the C6 carbon of SP to initiate the repair process. Via organic synthesis and DNA photochemistry, we selectively labeled the 6-H(proS) or 6-H(proR) position with a deuterium in a dinucleotide SP TpT substrate. Monitoring the deuterium migration in enzyme catalysis (employing Bacillus subtilis SPL) revealed that it is the 6-H(proR) atom of SP that is abstracted by the 5'-dA radical. Surprisingly, the abstracted deuterium was not returned to the resulting TpT after enzymatic catalysis; an H-atom from the aqueous buffer was incorporated into TpT instead. This result questions the currently hypothesized SPL mechanism which excludes the involvement of protein residue(s) in SPL reaction, suggesting that some protein residue(s), which is capable of exchanging a proton with the aqueous buffer, is involved in the enzyme catalysis. Moreover, evidence has been obtained for a possible SAM regeneration after each catalytic cycle; however, such a regeneration process is more complex than currently thought, with one or even more protein residues involved as well. These observations have enabled us to propose a modified reaction mechanism for this intriguing DNA repair enzyme.

45 citations


Authors

Showing all 758 results

NameH-indexPapersCitations
C. N. R. Rao133164686718
David Henry8954745563
Kim R. Dunbar7447020262
John F. McDonald6533316812
John Storey6236315276
Sarah N. Mattson5815111907
Joshua Telser4918719135
Paul L. Ornstein451616673
John Bacsa431857791
Eric J. Schelter411645045
Andrew Ozarowski401634546
Robert F. Inger3812111729
Oglesby Paul35877274
Michael Shatruk341653292
Christopher B. Keys331074263
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Performance
Metrics
No. of papers from the Institution in previous years
YearPapers
20231
20229
202173
202072
201965
201853