P E Brandish
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Explore the profile of P E Brandish including associated specialties, affiliations and a list of published articles.
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7
Citations
379
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Recent Articles
1.
Zhao Y, Brandish P, Di Valentin M, DiValentin M, Schelvis J, Babcock G, et al.
Biochemistry
. 2000 Sep;
39(35):10848-54.
PMID: 10978171
The heme in soluble guanylate cyclases (sGC) as isolated is ferrous, high-spin, and 5-coordinate. [1H-[1,2,4]oxadiazolo-[4, 3-a]quinoxalin-1-one] (ODQ) has been used extensively as a specific inhibitor for sGC and as a...
2.
Denninger J, Schelvis J, Brandish P, Zhao Y, Babcock G, Marletta M
Biochemistry
. 2000 Apr;
39(14):4191-8.
PMID: 10747811
The enzyme-soluble guanylate cyclase (sGC), which converts GTP to cGMP, is a receptor for the signaling agent nitric oxide (NO). YC-1, a synthetic benzylindazole derivative, has been shown to activate...
3.
Zhao Y, Brandish P, Ballou D, Marletta M
Proc Natl Acad Sci U S A
. 1999 Dec;
96(26):14753-8.
PMID: 10611285
Nitric oxide (NO) functions as a signaling agent by activation of the soluble isoform of guanylate cyclase (sGC), a heterodimeric hemoprotein. NO binds to the heme of sGC and triggers...
4.
Brandish P, Buechler W, Marletta M
Biochemistry
. 1998 Dec;
37(48):16898-907.
PMID: 9836582
Soluble guanylate cyclase (sGC) catalyzes the conversion of GTP to cGMP and is activated several hundred-fold by binding of nitric oxide (*NO) to the heme prosthetic group. We have examined...
5.
Brandish P, Kimura K, Inukai M, Southgate R, Lonsdale J, Bugg T
Antimicrob Agents Chemother
. 1996 Jul;
40(7):1640-4.
PMID: 8807054
Using a continuous fluorescence-based enzyme assay, we have characterized the antibacterial agents tumicamycin and liposidomycin B as inhibitors of solubilized Escherichia coli phospho-N-acetylmuramyl-pentapeptide translocase. Tunicamycin exhibited reversible inhibition (Ki =...
6.
Brandish P, Burnham M, Lonsdale J, Southgate R, Inukai M, Bugg T
J Biol Chem
. 1996 Mar;
271(13):7609-14.
PMID: 8631795
Enzymes of the membrane cycle of reactions in bacterial peptidoglycan biosynthesis remain as unexploited potential targets for antibacterial agents. The first of these enzymes, phospho-N-acetylmuramyl-pentapeptide-translocase (EC 2.7.8.13), has been overexpresed...
7.
Bugg T, Brandish P
FEMS Microbiol Lett
. 1994 Jun;
119(3):255-62.
PMID: 8050708
The peptidoglycan layer of bacterial cell walls is biosynthesised using a lipid carrier undecaprenyl phosphate to assemble and transport the MurNAc(GlcNAc)-pentapeptide precursor. Similar lipid-linked cycles are involved in the biosynthesis...