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Article ; Online: Hearing Health Healthcare Disparities in Appalachia.

Bush, Matthew L

Journal of Appalachian health

2021 Volume 3, Issue 4, Page(s) 5–10

Abstract: Hearing loss is a global public health issue with disproportionate negative impacts on those who live in rural regions, such as Appalachia. This commentary provides an overview of hearing health and healthcare disparities in rural regions along with ... ...

Abstract	Hearing loss is a global public health issue with disproportionate negative impacts on those who live in rural regions, such as Appalachia. This commentary provides an overview of hearing health and healthcare disparities in rural regions along with discussion of the significance of recent research findings which highlight the incidence of hearing loss and the shortage of hearing specialists in Appalachia.
Language	English
Publishing date	2021-10-25
Publishing country	United States
Document type	Journal Article
ISSN	2641-7804
ISSN (online)	2641-7804
DOI	10.13023/jah.0304.02
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Article ; Online: Quantitatively Differentiating Antibodies Using Charge-State Manipulation, Collisional Activation, and Ion Mobility-Mass Spectrometry.

Gozzo, Theresa A / Bush, Matthew F

Analytical chemistry

2023 Volume 96, Issue 1, Page(s) 505–513

Abstract: Antibody-based therapeutics continue to expand both in the number of products and in their use in patients. These heterogeneous proteins challenge traditional drug characterization strategies, but ion mobility (IM) and mass spectrometry (MS) approaches ... ...

Abstract	Antibody-based therapeutics continue to expand both in the number of products and in their use in patients. These heterogeneous proteins challenge traditional drug characterization strategies, but ion mobility (IM) and mass spectrometry (MS) approaches have eased the challenge of higher-order structural characterization. Energy-dependent IM-MS, e.g., collision-induced unfolding (CIU), has been demonstrated to be sensitive to subtle differences in structure. In this study, we combine a charge-reduction method, cation-to-anion proton-transfer reactions (CAPTR), with energy-dependent IM-MS and varied solution conditions to probe their combined effects on the gas-phase structures of IgG1κ and IgG4κ from human myeloma. CAPTR paired with MS-only analysis improves the confidence of charge-state assignments and the resolution of the interfering protein species. Collision cross-section distributions were determined for each of the charge-reduced products. Similarity scoring was used to quantitatively compare distributions determined from matched experiments analyzing samples of the two antibodies. Relative to workflows using energy-dependent IM-MS without charge-state manipulation, combining CAPTR and energy-dependent IM-MS enhanced the differentiation of these antibodies. Combined, these results indicate that CAPTR can benefit many aspects of antibody characterization and differentiation.
MeSH term(s)	Humans ; Proteins/chemistry ; Protons ; Anions/chemistry ; Cations/chemistry ; Antibodies ; Mass Spectrometry/methods
Chemical Substances	Proteins ; Protons ; Anions ; Cations ; Antibodies
Language	English
Publishing date	2023-12-26
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	1508-8
ISSN	1520-6882 ; 0003-2700
ISSN (online)	1520-6882
ISSN	0003-2700
DOI	10.1021/acs.analchem.3c04638
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Article ; Online: Effects of charge on protein ion structure: Lessons from cation-to-anion, proton-transfer reactions.

Gozzo, Theresa A / Bush, Matthew F

Mass spectrometry reviews

2023 Volume 43, Issue 3, Page(s) 500–525

Abstract: Collision cross-section values, which can be determined using ion mobility experiments, are sensitive to the structures of protein ions and useful for applications to structural biology and biophysics. Protein ions with different charge states can ... ...

Abstract	Collision cross-section values, which can be determined using ion mobility experiments, are sensitive to the structures of protein ions and useful for applications to structural biology and biophysics. Protein ions with different charge states can exhibit very different collision cross-section values, but a comprehensive understanding of this relationship remains elusive. Here, we review cation-to-anion, proton-transfer reactions (CAPTR), a method for generating a series of charge-reduced protein cations by reacting quadrupole-selected cations with even-electron monoanions. The resulting CAPTR products are analyzed using a combination of ion mobility, mass spectrometry, and collisional activation. We compare CAPTR to other charge-manipulation strategies and review the results of various CAPTR-based experiments, exploring their contribution to a deeper understanding of the relationship between protein ion structure and charge state.
MeSH term(s)	Protons ; Ions/chemistry ; Proteins ; Anions ; Cations/chemistry ; Mass Spectrometry/methods
Chemical Substances	Protons ; Ions ; Proteins ; Anions ; Cations
Language	English
Publishing date	2023-05-02
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	1491946-1
ISSN	1098-2787 ; 0277-7037
ISSN (online)	1098-2787
ISSN	0277-7037
DOI	10.1002/mas.21847
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Article ; Online: Proceedings of CI 2022DC Symposium: Emerging Issues in Cochlear Implantation.

Sorkin, Donna / Bush, Matthew / Park, Lisa

Otology & neurotology : official publication of the American Otological Society, American Neurotology Society [and] European Academy of Otology and Neurotology

2023 Volume 44, Issue 8, Page(s) e612

MeSH term(s)	Humans ; Cochlear Implantation ; Cochlear Implants
Language	English
Publishing date	2023-08-03
Publishing country	United States
Document type	Editorial
ZDB-ID	2036790-9
ISSN	1537-4505 ; 1531-7129
ISSN (online)	1537-4505
ISSN	1531-7129
DOI	10.1097/MAO.0000000000003980
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Zs.A 1554: Show issues

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Article: Towards IM

Zercher, Benjamin P / Feng, Yuan / Bush, Matthew F

International journal of mass spectrometry

2023 Volume 495

Abstract: Increasing the dimensionality of ion mobility (IM) presents an enticing opportunity to increase the information content and selectivity of many analyses. However, for implementations of IM that use constant electrostatic gradients to separate ions in a ... ...

Abstract	Increasing the dimensionality of ion mobility (IM) presents an enticing opportunity to increase the information content and selectivity of many analyses. However, for implementations of IM that use constant electrostatic gradients to separate ions in a buffer gas, technical challenges have limited the adoption of the technique and number of dimensions within individual experiments. Here, we introduce a strategy to "reset" the potentials of ions between IM dimensions. To achieve this, mobility-selected ions are trapped between dimensions of IM, using a combination of RF and electrostatic fields, while the subsequent dimension of IM is devoid of any drift field. By applying an incremental voltage ramp, the potential of the trapping region is elevated, simultaneously establishing the drift field in the subsequent dimension of IM. The trapped ions are then released and separated. We measured similar arrival-time distributions of protein ions using this strategy and a method without potential resetting, suggesting that potential resetting can be performed without additional losses or activation of ions. The findings of those experiments were corroborated by ion trajectory simulations, which exhibited a very small changes in ion position and no significant changes in effective temperatures during potential resetting. Finally, we demonstrate that IM information can be preserved during potential resetting by selecting subpopulations of 9+ cytochrome
Language	English
Publishing date	2023-10-17
Publishing country	Netherlands
Document type	Journal Article
ISSN	1387-3806
ISSN	1387-3806
DOI	10.1016/j.ijms.2023.117163
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Article ; Online: The actinobacterial WhiB-like (Wbl) family of transcription factors.

Bush, Matthew J

Molecular microbiology

2018 Volume 110, Issue 5, Page(s) 663–676

Abstract: The WhiB-like (Wbl) family of proteins are exclusively found in Actinobacteria. Wbls have been shown to play key roles in virulence and antibiotic resistance in Mycobacteria and Corynebacteria, reflecting their importance during infection by the human ... ...

Abstract	The WhiB-like (Wbl) family of proteins are exclusively found in Actinobacteria. Wbls have been shown to play key roles in virulence and antibiotic resistance in Mycobacteria and Corynebacteria, reflecting their importance during infection by the human pathogens Mycobacterium tuberculosis, Mycobacterium leprae and Corynebacterium diphtheriae. In the antibiotic-producing Streptomyces, several Wbls have important roles in the regulation of morphological differentiation, including WhiB, a protein that controls the initiation of sporulation septation and the founding member of the Wbl family. In recent years, genome sequencing has revealed the prevalence of Wbl paralogues in species throughout the Actinobacteria. Wbl proteins are small (generally ~80-140 residues) and each contains four invariant cysteine residues that bind an O
MeSH term(s)	Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Corynebacterium/genetics ; Corynebacterium/metabolism ; Gene Expression Regulation, Bacterial ; Mycobacterium/genetics ; Mycobacterium/metabolism ; Streptomyces/genetics ; Streptomyces/metabolism ; Transcription Factors/genetics ; Transcription Factors/metabolism
Chemical Substances	Bacterial Proteins ; Transcription Factors ; whiB protein, Streptomyces
Language	English
Publishing date	2018-10-25
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	619315-8
ISSN	1365-2958 ; 0950-382X
ISSN (online)	1365-2958
ISSN	0950-382X
DOI	10.1111/mmi.14117
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Zs.A 2502: Show issues

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Article: Defining Disparities in Cochlear Implantation through the Social Determinants of Health.

Schuh, Marissa / Bush, Matthew L

Seminars in hearing

2021 Volume 42, Issue 4, Page(s) 321–330

Abstract: Hearing loss is a global public health problem with high prevalence and profound impacts on health. Cochlear implantation (CI) is a well-established evidence-based treatment for hearing loss; however, there are significant disparities in utilization, ... ...

Abstract	Hearing loss is a global public health problem with high prevalence and profound impacts on health. Cochlear implantation (CI) is a well-established evidence-based treatment for hearing loss; however, there are significant disparities in utilization, access, and clinical outcomes among different populations. While variations in CI outcomes are influenced by innate biological differences, a wide array of social, environmental, and economic factors significantly impact optimal outcomes. These differences in hearing health are rooted in inequities of health-related socioeconomic resources. To define disparities and advance equity in CI, there is a pressing need to understand and target these social factors that influence equitable outcomes, access, and utilization. These factors can be categorized according to the widely accepted framework of social determinants of health, which include the following domains: healthcare access/quality, education access/quality, social and community context, economic stability, and neighborhood and physical environment. This article defines these domains in the context of CI and examines the published research and the gaps in research of each of these domains. Further consideration is given to how these factors can influence equity in CI and how to incorporate this information in the evaluation and management of patients receiving cochlear implants.
Language	English
Publishing date	2021-12-09
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	604961-8
ISSN	1098-8955 ; 0734-0451
ISSN (online)	1098-8955
ISSN	0734-0451
DOI	10.1055/s-0041-1739282
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Zs.B 2630: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular ab Jg. 2022: Lesesaal (EG)
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Article ; Online: Drugs Form Ternary Complexes with Human Liver Fatty Acid Binding Protein (FABP1) and FABP1 Binding Alters Drug Metabolism.

Yabut, King Clyde B / Martynova, Alice / Nath, Abhinav / Zercher, Benjamin P / Bush, Matthew F / Isoherranen, Nina

Molecular pharmacology

2024

Abstract: Liver fatty acid binding protein (FABP1) binds diverse endogenous lipids and is highly expressed in the human liver. Binding to FABP1 alters the metabolism and homeostasis of endogenous lipids in the liver. Drugs have also been shown to bind to rat FABP1, ...

Abstract	Liver fatty acid binding protein (FABP1) binds diverse endogenous lipids and is highly expressed in the human liver. Binding to FABP1 alters the metabolism and homeostasis of endogenous lipids in the liver. Drugs have also been shown to bind to rat FABP1, but limited data is available for human FABP1 (hFABP1). FABP1 has a large binding pocket and up to two fatty acids can bind to FABP1 simultaneously. We hypothesized that drug binding to hFABP1 results in formation of ternary complexes and that FABP1 binding alters drug metabolism. To test these hypotheses, native protein mass spectrometry (MS) and fluorescent 11-(dansylamino)undecanoic acid (DAUDA) displacement assays were used to characterize drug binding to hFABP1, and diclofenac oxidation by cytochrome P450 2C9 (CYP2C9) was studied in the presence and absence of hFABP1. DAUDA binding to hFABP1 involved high (K
Language	English
Publishing date	2024-04-05
Publishing country	United States
Document type	Journal Article
ZDB-ID	124034-1
ISSN	1521-0111 ; 0026-895X
ISSN (online)	1521-0111
ISSN	0026-895X
DOI	10.1124/molpharm.124.000878
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Article: Drugs Form Ternary Complexes with Human Liver Fatty Acid Binding Protein (FABP1) and FABP1 Binding Alters Drug Metabolism.

Yabut, King Clyde B / Martynova, Alice / Nath, Abhinav / Zercher, Benjamin P / Bush, Matthew F / Isoherranen, Nina

bioRxiv : the preprint server for biology

2024

Abstract	Liver fatty acid binding protein (FABP1) binds diverse endogenous lipids and is highly expressed in the human liver. Binding to FABP1 alters the metabolism and homeostasis of endogenous lipids in the liver. Drugs have also been shown to bind to rat FABP1, but limited data is available for human FABP1 (hFABP1). FABP1 has a large binding pocket and multiple fatty acids can bind to FABP1 simultaneously. We hypothesized that drug binding to hFABP1 results in formation of ternary complexes and that FABP1 binding alters drug metabolism. To test these hypotheses native protein mass spectrometry (MS) and fluorescent 11-(dansylamino)undecanoic acid (DAUDA) displacement assays were used to characterize drug binding to hFABP1 and diclofenac oxidation by cytochrome P450 2C9 (CYP2C9) was studied in the presence and absence of hFABP1. DAUDA binding to hFABP1 involved high (K
Language	English
Publishing date	2024-01-19
Publishing country	United States
Document type	Preprint
DOI	10.1101/2024.01.17.576032
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Article ; Online: Metastability of Protein Solution Structures in the Absence of a Solvent: Rugged Energy Landscape and Glass-like Behavior.

Cropley, Tyler C / Liu, Fanny C / Chai, Mengqi / Bush, Matthew F / Bleiholder, Christian

Journal of the American Chemical Society

2024

Abstract: Native ion mobility/mass spectrometry is well-poised to structurally screen proteomes but characterizes protein structures in the absence of a solvent. This raises long-standing unanswered questions about the biological significance of protein structures ...

Abstract	Native ion mobility/mass spectrometry is well-poised to structurally screen proteomes but characterizes protein structures in the absence of a solvent. This raises long-standing unanswered questions about the biological significance of protein structures identified through ion mobility/mass spectrometry. Using newly developed computational and experimental ion mobility/ion mobility/mass spectrometry methods, we investigate the unfolding of the protein ubiquitin in a solvent-free environment. Our data suggest that the folded, solvent-free ubiquitin observed by ion mobility/mass spectrometry exists in a largely native fold with an intact β-grasp motif and α-helix. The ensemble of folded, solvent-free ubiquitin ions can be partitioned into kinetically stable subpopulations that appear to correspond to the structural heterogeneity of ubiquitin in solution. Time-resolved ion mobility/ion mobility/mass spectrometry measurements show that folded, solvent-free ubiquitin exhibits a strongly stretched-exponential time dependence, which simulations trace to a rugged energy landscape with kinetic traps. Unfolding rate constants are estimated to be approximately 800 to 20,000 times smaller than in the presence of water, effectively quenching the unfolding process on the time scale of typical ion mobility/mass spectrometry measurements. Our proposed unfolding pathway of solvent-free ubiquitin shares substantial characteristics with that established for the presence of solvent, including a polarized transition state with significant native content in the N-terminal β-hairpin and α-helix. Our experimental and computational data suggest that (1) the energy landscape governing the motions of folded, solvent-free proteins is rugged in analogy to that of glassy systems; (2) large-scale protein motions may at least partially be determined by the amino acid sequence of a polypeptide chain; and (3) solvent facilitates, rather than controls, protein motions.
Language	English
Publishing date	2024-04-10
Publishing country	United States
Document type	Journal Article
ZDB-ID	3155-0
ISSN	1520-5126 ; 0002-7863
ISSN (online)	1520-5126
ISSN	0002-7863
DOI	10.1021/jacs.3c12892
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