E D Mihelich
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Explore the profile of E D Mihelich including associated specialties, affiliations and a list of published articles.
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14
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124
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Recent Articles
1.
Mihelich E, Schevitz R
Biochim Biophys Acta
. 1999 Nov;
1441(2-3):223-8.
PMID: 10570250
Human non-pancreatic secretory phospholipase A(2) (hnps-PLA(2)) is a group IIA enzyme that is massively over-expressed in a variety of severe inflammatory diseases. The enzyme degrades membrane phospholipids and it has...
2.
DILLARD R, Bach N, Draheim S, Berry D, Carlson D, Chirgadze N, et al.
J Med Chem
. 1996 Dec;
39(26):5119-36.
PMID: 9005255
Phospholipases (PLAs) produce rate-limiting precursors in the biosynthesis of various types of biologically active lipids involved in inflammatory processes. Increased levels of human nonpancreatic secretory phospholipase A2 (hnps-PLA2) have been...
3.
Draheim S, Bach N, DILLARD R, Berry D, Carlson D, Chirgadze N, et al.
J Med Chem
. 1996 Dec;
39(26):5159-75.
PMID: 8978844
The preceding papers of this series detail the development of functionalized indole-3-acetamides as inhibitors of hnps-PLA2. We describe here the extension of the structure-activity relationship to include a series of...
4.
DILLARD R, Bach N, Draheim S, Berry D, Carlson D, Chirgadze N, et al.
J Med Chem
. 1996 Dec;
39(26):5137-58.
PMID: 8978843
As reported in our previous paper, a series of indole-3-acetamides which possessed potency and selectivity as inhibitors of human nonpancreatic secretory phospholipase A2(hnps-PLA2) was developed. The design of these compounds...
5.
Fox N, Song M, Schrementi J, Sharp J, White D, Snyder D, et al.
Eur J Pharmacol
. 1996 Jul;
308(2):195-203.
PMID: 8840132
Transgenic mice were created which overexpress human secretory non-pancreatic phospholipase A2 (sPLA2) pansomatically as a potential disease and drug-testing model. The mice were produced using a DNA construct in which...
6.
Fleisch J, Armstrong C, Roman C, Mihelich E, Spaethe S, Jackson W, et al.
J Pharmacol Exp Ther
. 1996 Jul;
278(1):252-7.
PMID: 8764358
The primary objective of this study was to develop a functional assay that could provide rapid and reliable information on some pharmacologic characteristics of a novel inhibitor of human secretory...
7.
Schevitz R, Bach N, Carlson D, Chirgadze N, CLAWSON D, DILLARD R, et al.
Nat Struct Biol
. 1995 Jun;
2(6):458-65.
PMID: 7664108
A lead compound obtained from a high volume human non-pancreatic secretory phospholipase A2 (hnps-PLA2) screen has been developed into a potent inhibitor using detailed structural knowledge of inhibitor binding to...
8.
Snyder D, Sommers C, Bobbitt J, Mihelich E
J Pharmacol Exp Ther
. 1993 Sep;
266(3):1147-55.
PMID: 8371132
Contractile activities of nPLA2, pPLA2 and hPLA2 were characterized on pleural strips of guinea pig lung. The rank order of potency for these PLA2s was nPLA2 > pPLA2 > hPLA2....
9.
Snyder D, Sommers C, Bobbitt J, Mihelich E
J Pharmacol Exp Ther
. 1992 Sep;
262(3):1147-53.
PMID: 1527719
We have demonstrated previously that porcine pancreatic phospholipase A2 (PLA2)-induced contractions of guinea pig lung pleural strips can be abated by inhibitors of cyclooxygenase and 5-lipoxygenase pathways, suggesting the liberation...
10.
Cho H, Ho P, Mihelich E, Snyder D
J Pharmacol Methods
. 1991 Dec;
26(4):277-87.
PMID: 1661803
A quantitative method to assess relative potencies (IC50) of 5-lipoxygenase (5-LO) enzyme inhibitors was established in antigen-induced contractions of tracheas isolated from actively sensitized guinea pigs (Schultz-Dale model). The relative...