Zobrazeno 1 - 10 of 22 pro vyhledávání: '"Vijaykumar M. Baragi"'
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Akademický článek
Neuroimaging Markers for Determining Former American Football Players at Risk for Alzheimer's Disease
Autor: Vijaykumar M. Baragi, Ramtilak Gattu, Gabriela Trifan, John L Woodard, Kortney Meyers, Tim S. Halstead, Eric Hipple, Ewart Mark Haacke, Randall R Benson
Publikováno v: Neurotrauma Reports, Vol 3, Iss 1, Pp 398-414 (2022)
NFL players, by virtue of their exposure to traumatic brain injury (TBI), are at higher risk of developing dementia and Alzheimer's disease (AD) than the general population. Early recognition and intervention before the onset of clinical symptoms cou
Externí odkaz: https://doaj.org/article/8171ff7be19e445ca04e598f23e07a3e
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Evaluation of toxicokinetic variables and histologic appearance of arthropathic changes in juvenile rabbits after oral administration of an investigational fluoroquinolone, PD 117596
Autor: Robert E. Sigler, William D. Black, Ron J. Johnson, Vijaykumar M. Baragi, Alec W. Gough
Publikováno v: American Journal of Veterinary Research. 61:1396-1402
Objective—To compare toxicokinetic variables and associated tissue drug concentrations with severity of articular lesions in weight-bearing joints of juvenile rabbits after oral administration of a fluoroquinolone. Animals—Ten 6- to 7-week-old, 8
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::183f6b6faed60d8c6a4cc46e3669b871
https://doi.org/10.2460/ajvr.2000.61.1396
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A versatile assay for gelatinases using succinylated gelatin
Autor: Vijaykumar M. Baragi, Mahesh Mathrubutham, Howard G. Welgus, Paul J. Kuipers, Bonnie J. Shaw, Jon R. Cohen, Richard R. Renkiewicz, Srinivasa K. Rao
Publikováno v: Matrix Biology. 19:267-273
A spectrophotometric assay using succinylated gelatin as substrate is described for measuring the catalytic activity of gelatinases. The assay is based on measurement of primary amines exposed as a result of hydrolysis of the substrate by gelatinases
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::36d11b17c610a98d20ca8e91707bbb84
https://doi.org/10.1016/s0945-053x(00)00086-x
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Transcriptional downregulation of stromelysin by tetracycline
Autor: Vijaykumar M. Baragi, Carsten Jonat, Fu-Zon Chung
Publikováno v: Journal of Cellular Biochemistry. 60:341-347
We investigated the role of tetracycline in the transcriptional regulation of matrix metalloproteinases. Using interleukin-1β (IL-1) induced stromelysin as a model system, we describe the repression of the endogenous stromelysin RNA accumulation, as
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::38f937025b1a8a83d9a4ec9c09f3c76d
https://doi.org/10.1002/(sici)1097-4644(19960301)60:3<341::aid-jcb6>3.0.co
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Inhibition of Interleukin 1-lnduced Biosynthesis of Stromelysin by the Calcium Antagonist TMB-(8-(N, N-Diethylamino)octyl-3,4,5-trimethoxybenzoate HCl)
Autor: Vijaykumar M. Baragi, Wendy S. Rosebury, Ann Marie Sweet, Kathleen L. Hawkins, Mark A. Thompson, Katherine A. Toy
Publikováno v: Connective Tissue Research. 31:153-160
This study was done to identify agents that can inhibit interleukin 1 (IL1)-induced stromelysin biosynthesis and to gain insight into the mechanism of IL1 action. For this purpose, various agents known to modulate calcium-dependent signal transductio
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::0747790aca424e23baddcd11bc153ed8
https://doi.org/10.3109/03008209509028403
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Matrilysin Is Much More Efficient Than Other Matrix Metalloproteinases in the Proteolytic Inactivation of α1-Antitrypsin
Autor: Ulrike I. Sires, H. G. Welgus, C.J. Fliszar, Vijaykumar M. Baragi, Robert M. Senior, G. Murphy
Publikováno v: Biochemical and Biophysical Research Communications. 204:613-620
alpha 1-antitrypsin, the primary physiologic inhibitor of human leukocyte elastase, is proteolytically inactivated by several matrix metalloproteinases including interstitial collagenase, stromelysin and 92 kDa gelatinase. In this report, we describe
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8ef6e17d7f4212846b9a5f47b8bab003
https://doi.org/10.1006/bbrc.1994.2503
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Contribution of the C-terminal domain of metalloproteinases to binding by tissue inhibitor of metalloproteinases. C-terminal truncated stromelysin and matrilysin exhibit equally compromised binding affinities as compared to full-length stromelysin
Autor: Qi Zhuang Ye, M. C. Conroy, H. G. Welgus, J. M. Shipley, C. J. Fliszar, Vijaykumar M. Baragi
Publikováno v: Journal of Biological Chemistry. 269:12692-12697
In this study, we have used high resolution gel-filtration chromatography and measurements of Ki to compare the capacity of full-length native stromelysin, C-terminal truncated stromelysin (Phe100-Pro273), and matrilysin (the only metalloproteinase s
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::55e3afd34c5f098de74c962773aa1c75
https://doi.org/10.1016/s0021-9258(18)99931-x
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