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1821. Partida
- Type:
- Media
- Description/Abstract:
- Produced on ¾" tape at Center for Contemporary Art, Santa Fe; features music by the Memluks, a band from Norman, OK, and appearances by my friend Willy.
- Creator/Author:
- Woodman, Charles
- Submitter:
- Charles Woodman
- Date Uploaded:
- 03/20/2017
- Date Modified:
- 05/07/2019
- Date Created:
- 1985-01-31
- License:
- All rights reserved
1822. Personal Jesus
- Type:
- Media
- Description/Abstract:
- The image was filmed off a decorative plate with a live camera which was being processed dimming, and then coming to brightness then back again. It looks like the hue was off too, giving Jesus a green tint. Produced during a residency at the Experimental TV Center.
- Creator/Author:
- Woodman, Charles
- Submitter:
- Charles Woodman
- Date Uploaded:
- 03/19/2017
- Date Modified:
- 05/07/2019
- Date Created:
- 1993-06-01
- License:
- All rights reserved
1823. Mixed Fish with Clouds
- Type:
- Media
- Description/Abstract:
- This is an early installation video shown at a gallery at Millersville University and projected onto the ceiling. All footage is original.
- Creator/Author:
- Woodman, Charles
- Submitter:
- Charles Woodman
- Date Uploaded:
- 03/19/2017
- Date Modified:
- 05/07/2019
- Date Created:
- 1994-06-01
- License:
- All rights reserved
- Type:
- Student Work
- Description/Abstract:
- Submitted to the Faculty of the Information Engineering Technology Program in Partial Fulfillment of the Requirements for the Degree of Bachelor of Science in Information Engineering Technology
- Creator/Author:
- Morrison, Matthew Edward
- Submitter:
- CECH Library Service
- Date Uploaded:
- 03/09/2017
- Date Modified:
- 05/23/2019
- Date Created:
- 2003-03-14
- License:
- Attribution-NonCommercial-NoDerivs 4.0 International
- Type:
- Article
- Description/Abstract:
- Background: Acid -glucosidase is trafficked to the lysosome by LIMP-2. Results: A unique 11-amino acid sequence on acid -glucosidase was critical for its LIMP-2-dependent targeting to the lysosome. Conclusion: This sequence is essential for oligosaccharide-independent targeting of synthesized acid -glucosidase to the lysosome. Significance: Modification of this sequence has basic/therapeutic implications for Gaucher disease and its comorbidities (e.g. Parkinson disease).
- Creator/Author:
- Grabowski, Gregory A.; Haffey, Wendy D.; Greis, Kenneth D., and Llou, Benjamin
- Submitter:
- Kenneth Greis
- Date Uploaded:
- 03/03/2017
- Date Modified:
- 04/07/2017
- Date Created:
- 2014-09
- License:
- All rights reserved
- Type:
- Article
- Description/Abstract:
- OBJECTIVE: Damage to hair from UV exposure has been well reported in the literature and is known to be a highly complex process involving initiation via absorption of UV light followed by formation and propagation of reactive oxygen species (ROS). The objective of this work was to understand these mechanisms, explain the role of copper in accelerating the formation of ROS and identify strategies to reduce the hair damage caused by these reactive species. METHODS: The location of copper in hair was measured by Transmission electron microscopy–(TEM) X-ray energy dispersive spectroscopy (XEDS) and levels measured by ICP-OES. Protein changes were measured as total protein loss via the Lowry assay, and MALDI ToF was used to identify the biomarker protein fragments. TBARS assay was used to measure lipid peroxide formation. Sensory methods and dry combing friction were used to measure hair damage due to copper and UV exposure and to demonstrate the efficacy of N,N’ ethylenediamine disuccinic acid (EDDS) and histidine chelants to reduce this damage. RESULTS: In this work, a biomarker protein fragment formed during UV exposure is identified using mass spectrometry. This fragment originates from the calcium-binding protein S100A3. Also shown is the accelerated formation of this peptide fragment in hair containing low levels of copper absorbed from hair during washing with tap water containing copper ions. Transmission electron microscopy (TEM) X-ray energy dispersive spectroscopy (XEDS) studies indicate copper is located in the sulphur-poor endo-cuticle region, a region where the S100A3 protein is concentrated. A mechanism for formation of this peptide fragment is proposed in addition to the possible role of lipids in UV oxidation. A shampoo and conditioner containing chelants (EDDS in shampoo and histidine in conditioner) is shown to reduce copper uptake from tap water and reduce protein loss and formation of S100A3 protein fragment. In addition, the long-term consequences of UV oxidation and additional damage induced by copper are illustrated in a fourmonth wear study where hair was treated with a consumer relevant protocol of hair colouring treatments, UV exposure and regular shampoo and conditioning. CONCLUSIONS: The role of copper in accelerating UV damage to hair has been demonstrated as well as the ability of chelants such as EDDS and histidine in shampoo and conditioner products to reduce this damage.
- Creator/Author:
- McComb, D. W.; Marsh, J. M.; Sun, Y.; Chaudhary, T.; Flagler, M. J.; Coderch, L.; Mamak, M.; Greis, Kenneth D.; Rubio, L.; Williams, R. E. A., and Davis, M. G.
- Submitter:
- Kenneth Greis
- Date Uploaded:
- 03/03/2017
- Date Modified:
- 04/07/2017
- Date Created:
- 2015-04
- License:
- All rights reserved
- Type:
- Article
- Description/Abstract:
- In the pharmaceutical industry, there is a tremendous need for qualitative and quantitative analysis of target analytes such as peptides, proteins, drugs, metabolites, biomarkers, impurities, and degradation products in various mixtures including synthetic reactions, in vitro cultures, biological fluids, drug substances, finished products, and many others. To provide adequate specificity for analysis in these complex mixtures, multidimensional analytical techniques are required. Mass spectrometry plays a central role in many of these multidimensional approaches to mixture analysis because it provides an unparalleled combination of sensitivity and specificity that is useful for both molecular identification and quantitative applications. Recent innovations in mass spectrometry and industrial implementation of these advances have transformed many aspects of pharmaceutical research and development. Data that were previously unattainable, or were not collected due to exorbitant cost or time constraints, can now be obtained using mass spectrometry-based technologies. The impact of these innovations has been most dramatically felt in early stages of discovery, as more data are available to make critical decisions, such as selecting compounds for advancement to costly preclinical and clinical trials. New MS technologies have also accelerated the progression of drug candidates through development and toward regulatory approval. Here, five major categories of pharmaceutical applications of mass spectrometry are reviewed. They are new chemical entity characterization, biomacromolecule characterization, bioanalytical quantitation, metabolite identification, and impurity and degradation product identification. A brief historical perspective and evolution of technologies for each application area are presented. Those discussions are followed with a description of the current strategies for implementation of the tremendous capabilities of the state-of-the-art approaches, along with representative applications. In addition, emerging technologies for each application area are presented to indicate the future directions of instrumentation for mixture analysis in the pharmaceutical industry. (Int J Mass Spectrom 212 (2001) 135–196) © 2001 Elsevier Science B.V.
- Creator/Author:
- Harbol, Kevin L.; Greis, Kenneth D.; Hoke, Steven H.; Morand, Kenneth L.; Baker, Timothy R., and Dobson, Roy L. M.
- Submitter:
- Kenneth Greis
- Date Uploaded:
- 03/03/2017
- Date Modified:
- 04/07/2017
- Date Created:
- 2001-11
- License:
- All rights reserved
- Type:
- Article
- Description/Abstract:
- Candida albicans is a leading pathogen in infections of central venous catheters, which are frequently infused with heparin. Binding of C. albicans to medically relevant concentrations of soluble and plate-bound heparin was demonstrable by confocal microscopy and enzyme-linked immunosorbent assay (ELISA). A sequencebased search identified 34 C. albicans surface proteins containing ≥1 match to linear heparin-binding motifs. The virulence factor Int1 contained the most putative heparin-binding motifs (n = 5); peptides encompassing 2 of 5 motifs bound to heparin-Sepharose. Alanine substitution of lysine residues K805/K806 in 804QKKHQIHK811 (motif 1 of Int1) markedly attenuated biofilm formation in central venous catheters in rats, whereas alanine substitution of K1595/R1596 in 1593FKKRFFKL1600 (motif 4 of Int1) did not impair biofilm formation. Affinity-purified immunoglobulin G (IgG) recognizing motif 1 abolished biofilm formation in central venous catheters; preimmune IgG had no effect. After heparin treatment of C. albicans, soluble peptides from multiple C. albicans surface proteins were detected, such as Eno1, Pgk1, Tdh3, and Ssa1/2 but not Int1, suggesting that heparin changes candidal surface structures and may modify some antigens critical for immune recognition. These studies define a new mechanism of biofilm formation for C. albicans and a novel strategy for inhibiting catheter-associated biofilms.
- Creator/Author:
- Andes, David R.; Lu, Jason Long; Tan, Queenie K., G.; Hostetter, Margaret K.; Greis, Kenneth D.; Zhang, Minlu; Orsborn, Kris I.; Porollo, Alexey, and Green, Julianne V.
- Submitter:
- Kenneth Greis
- Date Uploaded:
- 03/03/2017
- Date Modified:
- 04/07/2017
- Date Created:
- 2013-07
- License:
- All rights reserved
- Type:
- Article
- Description/Abstract:
- Data-independent acquisition (DIA)-based proteomics has become increasingly complicated in recent years because of the vast number of workflows described, coupled with a lack of studies indicating a rational framework for selecting effective settings to use. To address this issue and provide a resource for the proteomics community, we compared 12 DIA methods that assay tryptic peptides using various mass-isolation windows. Our findings indicate that the most sensitive single injection LC-DIA method uses 6 m/z isolation windows to analyze the densely populated tryptic peptide range from 450 to 730 m/z, which allowed quantification of 4465 Escherichia coli peptides. In contrast, using the sequential windowed acquisition of all theoretical fragmentions (SWATH) approach with 26 m/z isolation windows across the entire 400–1200 m/z range, allowed quantification of only 3309 peptides. This reduced sensitivity with 26 m/z windows is caused by an increase in co-eluting compounds with similar precursor values detected in the same tandemMS spectra, which lowers the signal-to-noise of peptide fragment-ion chromatograms and reduces the amount of low abundance peptides that can be quantified from 410 to 920 m/z. Above 920 m/z, more peptides were quantified with 26 m/z windows because of substantial peptide 13C isotope distributions that parse peptide ions into separate isolation windows. Because reproducible quantification has been a long-standing aimof quantitative proteomics, and is a socalled trait of DIA, we sought to determine whether precursor-level chromatograms used in some methods rather than their fragment-level counterparts have similar precision. Our data show that extracted fragment-ion chromatograms are the reason DIA provides superior reproducibility. Copyright © 2015 John Wiley & Sons, Ltd.
- Creator/Author:
- Haffey, Wendy D.; Norris, Jeremy L.; McCullumsmith, Robert E.; Heaven, Michael R.; Cobbs, Archie L.; Funk, Adam J., and Greis, Kenneth D.
- Submitter:
- Kenneth Greis
- Date Uploaded:
- 03/03/2017
- Date Modified:
- 04/07/2017
- Date Created:
- 2016-01
- License:
- All rights reserved
- Type:
- Article
- Description/Abstract:
- Commonly used methods for isolated enzyme inhibitor screening typically rely on fluorescent or chemiluminescent detection techniques that are often indirect and/or coupled assays. Mass spectrometry (MS) has been widely reported for measuring the conversion of substrates to products for enzyme assays and has more recently been demonstrated as an alternative readout system for inhibitor screening. In this report, a high-throughput mass spectrometry (HTMS) readout platform, based on the direct measurement of substrate conversion to product, is presented. The rapid ionization and desorption features of a new generation matrix-assisted laser desorption ionization-triple quadrupole (MALDI-QqQ) mass spectrometer are shown to improve the speed of analysis to greater than 1 sample per second while maintaining excellent Z′ values. Furthermore, the readout was validated by demonstrating the ability to measure IC50 values for several known kinase inhibitors against cyclic AMP–dependent protein kinase (PKA). Finally, when the assay performance was compared with a common ADPaccumulation readout system, this HTMS approach produced better signal-to-background ratios, higher Z′ values, and a reagent cost of about $0.03 per well compared with about $0.60 per well for the fluorescence assay. Collectively, these data demonstrate that a MALDI-QqQ-MS–based readout platform offers significant advantages over the commonly used assays in terms of speed, sensitivity, reproducibility, and reagent cost. (Journal of Biomolecular Screening 2008:1007-1013)
- Creator/Author:
- Rathore, Rakesh; Corr, Jay; Scott, George; Greis, Kenneth D., and Vollmerhaus, Pauline
- Submitter:
- Kenneth Greis
- Date Uploaded:
- 03/03/2017
- Date Modified:
- 04/07/2017
- Date Created:
- 2008-12
- License:
- All rights reserved