Zobrazeno 1 - 10
of 17
pro vyhledávání: '"Hyunshun, Shin"'
Autor:
Andrew E. Huckleby, Jhawn G. Saul, Hyunshun Shin, Staci Desmarais, Apparao Bokka, Junha Jeon, Sung-Kun Kim
Publikováno v:
International Journal of Molecular Sciences; Volume 23; Issue 16; Pages: 9163
The emergence of resistant bacteria takes place, endangering the effectiveness of antibiotics. A reason for antibiotic resistance is the presence of lactamases that catalyze the hydrolysis of β-lactam antibiotics. An inhibitor of serine-β-lactamase
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::841fdefd66dd0d2dbd90f7626ff61722
Publikováno v:
Bioorganic & Medicinal Chemistry. 15:2617-2623
The first committed step in lipid A biosynthesis is catalyzed by uridine diphosphate-(3-O-(R-3-hydroxymyristoyl))-N-acetylglucosamine deacetylase (LpxC), a zinc-dependent deacetylase, and inhibitors of LpxC may be useful in the development of antibac
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4bf39fd85c8a58413497e28dbb6ce409
https://doi.org/10.1016/j.bmc.2007.01.044
https://doi.org/10.1016/j.bmc.2007.01.044
Autor:
Brendan Hilliard, Youhai H. Chen, Hyunshun Shin, David W. Christianson, Ruaidhrí J. Carmody, Galit Tsabary, Lingyun Xu
Publikováno v:
Immunology. 110:141-148
Using a high throughput gene microarray technology that detects approximately 22 000 genes, we found that arginase I was the most significantly up-regulated gene in the murine spinal cord during experimental autoimmune encephalomyelitis (EAE). By Nor
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::920fa1104bbee4965a85f991349ed463
https://doi.org/10.1046/j.1365-2567.2003.01713.x
https://doi.org/10.1046/j.1365-2567.2003.01713.x
Autor:
Evis, Cama, Diana M, Colleluori, Frances A, Emig, Hyunshun, Shin, Soo Woong, Kim, Noel N, Kim, Abdulmaged M, Traish, David E, Ash, David W, Christianson
Publikováno v:
Biochemistry. 42:8445-8451
Arginase is a binuclear manganese metalloenzyme that catalyzes the hydrolysis of l-arginine to form l-ornithine and urea. The X-ray crystal structure of a fully active, truncated form of human arginase II complexed with a boronic acid transition stat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c91f64da032c21f85b6daac5b2820034
https://doi.org/10.1021/bi034340j
https://doi.org/10.1021/bi034340j
Autor:
Heather Whitehead, Karl L Banta, Myung K Cho, Xian Zhou, Juliet V Spencer, Hyunshun Shin, Sung-Kun Kim
Publikováno v:
Biochemistry & Pharmacology: Open Access.
Cell proliferation can be regulated by small, aliphatic polyamines, and it is suggested that tumor tissues have significantly higher polyamine levels than surrounding tissues. The major biologically active polyamines present in mammalian cells are pu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::29b01ca00adbb9c26be85bec4fee1a20
https://doi.org/10.4172/2167-0501.1000111
https://doi.org/10.4172/2167-0501.1000111
Publikováno v:
Journal of the American Chemical Society. 126(33)
Arginase is a binuclear manganese metalloenzyme that catalyzes the hydrolysis of l-arginine to form l-ornithine and urea. Chiral L-amino acids bearing aldehyde side chains have been synthesized in which the electrophilic aldehyde C=O bond is isosteri
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9ff99bcddadd06a20ce9e2a0d29f5709
https://pubmed.ncbi.nlm.nih.gov/15315440
https://pubmed.ncbi.nlm.nih.gov/15315440
Publikováno v:
Journal of the American Chemical Society. 125(43)
Arginase is a binuclear manganese metalloenzyme that catalyzes the hydrolysis of L-arginine to form L-ornithine plus urea. Chiral L-amino acids bearing sulfonamide side chains have been synthesized in which the tetrahedral sulfonamide groups are desi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ab8773e2fef4564d49c61b0bd7d47736
https://pubmed.ncbi.nlm.nih.gov/14570477
https://pubmed.ncbi.nlm.nih.gov/14570477
Autor:
Kristin M. Rusche, Hyunshun Shin, David W. Christianson, Douglas A. Whittington, Carol A. Fierke
The outer leaflet of the outer membrane of the Gram-negative bacterium serves as a permeability barrier and is composed of lipopolysaccharide, also known as endotoxin. The membrane anchor of lipopolysaccharide is lipid A, the biosynthesis of which is
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3f8761b3589b1a4c337307a42c110dfc
https://europepmc.org/articles/PMC166197/
https://europepmc.org/articles/PMC166197/
Autor:
Lingyun Xu, Hilliard, Brendan, Carmody, Ruaidhrí J., Tsabary, Galit, Hyunshun Shin, Christiansont, David W., Chen, Youhai H.
Publikováno v:
Immunology; Sep2003, Vol. 110 Issue 1, p141-148, 8p
Autor:
Cama, Evis, Colleluori, Diana M., Emig, Frances A., Hyunshun Shin, Soo Woong Kim, Kim, Noel N., Traish, Abdulmaged M., Ash, David E., Christianson, David W.
Publikováno v:
Biochemistry; 7/22/2003, Vol. 42 Issue 28, p8445, 7p, 2 Color Photographs, 9 Diagrams, 1 Chart, 7 Graphs