Zobrazeno 1 - 10 of 51 pro vyhledávání: '"Richard E. Galardy"'
1
SUBTILOPEPTIDASE A CLEAVAGE IN THE CYCLIC REGION OF THE PEPTIDE ANTIBIOTIC POLYMYXIN B1
Autor: John A. Sogn, W. A. Gibbons, Richard E. Galardy, Morton P. Printz, Richard S. Bockman, Lyman C. Craig
Publikováno v: International Journal of Peptide and Protein Research. 5:455-461
Digestion of a commercial mixture of the peptides polymyxin B1 and B2 with subtilopeptidase A yielded a peptide whose amino acid composition corresponded to the ring fragment common to both antibiotics. However, in contrast to the earlier chemical st
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4069165d9869dbdaeb74f00fd0539a6e
https://doi.org/10.1111/j.1399-3011.1973.tb02351.x
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2
s-Cis and s-trans isomerism in acylproline analogs
Autor: Richard E. Galardy, Jeffrey R. Alger, Maria Liakopoulou-Kyriakides
Publikováno v: International Journal of Peptide and Protein Research. 19:123-132
N-Acetyl-2,3-dehydroproline, N-acetyl-5-oxo-L-proline, N-acrylyl-L-proline, N-acetyl-L-azetidine-2-carboxylic acid and N-acetyl-D,L-pipecolic acid have been examined in 2H2O by 1H and 13Cn.m.r. for the purpose of finding s-cis or s-trans locked acylp
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c8aacbdd1964cdf2bc3554f9c25377cc
https://doi.org/10.1111/j.1399-3011.1982.tb02599.x
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3
s-cis, s-trans Isomerism about the Ala-Pro peptide bond in Nα-phospho- and Nα-phosphono-l-alanyl-l-prolines by 31P n.m.r
Autor: E. Carroll Teater, Damian Grobelny, Umesh B. Goli, Richard E. Galardy
Publikováno v: International Journal of Peptide and Protein Research. 32:292-297
Nα-(Phenethylphosphono)-l-alanyl-l-proline 1, a potent inhibitor of angiotensin converting enzyme, exhibits two 31P n.m.r. resonances (intensity ratio one to one), which exchange with a constant (k1) of about 1 s−1 and a free energy of activation
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::82cd31b3b428a50737b89b3c9f5b71e9
https://doi.org/10.1111/j.1399-3011.1988.tb01263.x
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4
Matrix Metalloproteinase Inhibitors: A Structure−Activity Study
Autor: Daniel E. Levy, France Lapierre, Weisheng Liang, Wenqing Ye, Christopher W. Lange, Xiaoyuan Li, Damian Grobelny, Marie Casabonne, David Tyrrell, Kevin Holme, Alex Nadzan, Richard E. Galardy
Publikováno v: Journal of Medicinal Chemistry. 41:199-223
Modifications around the dipeptide-mimetic core of a hydroxamic acid based matrix metalloproteinase inhibitor were studied. These variations incorporated a variety of natural, unnatural, and synthetic amino acids in addition to modifications of the P
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c3305083e8dd9cc67803fbd243001f88
https://doi.org/10.1021/jm970494j
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5
A MATRIX METALLOPROTEINASE INHIBITOR PREVENTS PROCESSING OF TUMOR NECROSIS FACTOR α (TNFα) AND ABROGATES ENDOTOXIN-INDUCED LETHALITY
Autor: Riadh Ksontini, Lyle L. Moldawer, Carmen C. Solorzano, Sally L. D. MacKay, Jeffrey H. Pruitt, Gregory Schultz, Cynthia L. Tannahill, Troy Auffenberg, Edward M. Copeland, Richard E. Galardy
Publikováno v: Shock. 7:427-431
Excessive tumor necrosis factor alpha (TNF alpha) production in response to Gram-negative bacteremia or endotoxemia can often lead to hypotension, shock, and increased mortality. Current approaches used to block the deleterious effects of exaggerated
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6107610bc740f5bca5a49a71f94ef0bf
https://doi.org/10.1097/00024382-199706000-00007
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6
Matrix metalloproteinase inhibitors reduce phorbol ester-induced cutaneous inflammation and hyperplasia
Autor: Walter M. Holleran, Wen Ni Gao, Peter M. Elias, Peng Cho Tang, Daniel Levy, Richard E. Galardy
Publikováno v: Archives of Dermatological Research. 289:138-144
Matrix metalloproteinases (MMPs) are a family of zinc-dependent proteases which play key roles in extracellular matrix remodeling, connective tissue damage, inflammation and cell proliferation in a variety of tissues. Since MMP inhibitors have been r
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f4fa030154094eef03ba3bd8af2dbce6
https://doi.org/10.1007/s004030050169
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8
92-kD type IV collagenase mediates invasion of human cytotrophoblasts
Autor: Clifford Librach, King Chiu, Susan J. Fisher, Damian Grobelny, Marilyn L. Fitzgerald, Caroline H. Damsky, Richard E. Galardy, Zena Werb, Nanci M. Corwin, Ruth A. Esteves
Publikováno v: The Journal of Cell Biology
The specialized interaction between embryonic and maternal tissues is unique to mammalian development. This interaction begins with invasion of the uterus by the first differentiated embryonic cells, the trophoblasts, and culminates in formation of t
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4bc4995c5d4277e4d0d5b4e48a652786
http://europepmc.org/articles/PMC2288933
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9
Matrix metalloproteinase expression in human retinal microvascular cells
Autor: Polyxenie E. Spoerri, Richard E. Galardy, Maria B. Grant, Sergio Caballero, Alexander V. Ljubimov, Roy W. Tarnuzzer, Kathryn E Bass
Publikováno v: Diabetes. 47(8)
The degree of hyperglycemia correlates with the development of diabetic retinopathy. We investigated the effect of glucose on the expression of matrix metalloproteinase (MMP)-2 and MMP-9 (72-kDa and 92-kDa type IV collagenases, respectively) by human
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::db66d83d1e828c1416ac01cd88a76309
https://pubmed.ncbi.nlm.nih.gov/9703333
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10
Administration of a matrix metalloproteinase inhibitor after hemorrhage improves cardiovascular and hepatocellular function
Autor: Ping Wang, Zheng F. Ba, Richard E. Galardy, Irshad H. Chaudry
Publikováno v: Shock (Augusta, Ga.). 6(5)
Although matrix metalloproteinase inhibitors prevent the increase in soluble tumor necrosis factor-α during endotoxemia, it remains unknown whether a novel matrix metalloproteinase inhibitor, GM6001, improves cardiovascular and hepatocellular functi
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5e03be29b2246ab7b28d428045bbcf78
https://pubmed.ncbi.nlm.nih.gov/8946655
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