Zobrazeno 1 - 10
of 22
pro vyhledávání: '"Barbara G Green"'
Publikováno v:
Bioorganic Chemistry. 29:211-222
The posttranslational deformylation of N-formyl-Met-polypeptides by the metalloenzyme, peptide defomylase, is essential for bacterial growth. Methionine hydroxamic acid derivatives were found to inhibit recombinant Escherichia coli peptide deformylas
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::61322aad426136b68b719bf438b64308
https://doi.org/10.1006/bioo.2001.1214
https://doi.org/10.1006/bioo.2001.1214
Publikováno v:
Archives of Biochemistry and Biophysics. 375:355-358
Peptide deformylase is an essential eubacterial metalloenzyme involved in the maturation of proteins by cleaving the N-formyl group from N-blocked methionine polypeptides. Biaryl acid analogs containing tetrazole, acyl sulfonamide, or carboxylate pha
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::75b4f92c23bcf27ec5fb7eec182d2170
https://doi.org/10.1006/abbi.1999.1673
https://doi.org/10.1006/abbi.1999.1673
Publikováno v:
Archives of Biochemistry and Biophysics. 367:297-302
Bacterial peptide deformylases (PDF, EC 3.5.1.27) are metalloenzymes that cleave the N-formyl groups from N-blocked methionine polypeptides. Peptide aldehydes containing a methional or norleucinal inhibited recombinant peptide deformylase from gram-n
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dfa5d3108f85aa791b6868dbe6474ebe
https://doi.org/10.1006/abbi.1999.1274
https://doi.org/10.1006/abbi.1999.1274
Autor:
Barbara G. Green, John W. Kozarich, Stephan K. Grant, Shrenik K. Shah, Philippe L. Durette, Janet Stiffey-Wilusz
Publikováno v:
Biochemistry. 37:4174-4180
Inducible nitric oxide synthase (iNOS; EC 1.14.13.39) catalyzes the NADPH-dependent oxidation of one of the free guanidino nitrogens of L-Arg to form nitric oxide and L-citrulline. Analogues of L-Arg and the inhibitor, L-N6-(1-iminoethyl)lysine, were
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c8e47b6b468c82d5c59522bd01468de8
https://doi.org/10.1021/bi972481d
https://doi.org/10.1021/bi972481d
Autor:
Kothandaraman Shankaran, John L. Humes, Barbara G. Green, Shrenik K. Shah, Karla L. Donnelly, Stephan K. Grant, Stephen G. Pacholok, Malcolm MacCoss
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 7:2887-2892
A series of benzoxazolones has been synthesized using modifications of literature methods. The synthetic benzoxazolone analogs, along with commercially available analogs, were evaluated as inhibitors of nitric oxide synthases (NOS). Structure-activit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::11c5d18952fe2afeed87a58f1778c155
https://doi.org/10.1016/s0960-894x(97)10101-9
https://doi.org/10.1016/s0960-894x(97)10101-9
Publikováno v:
Journal of Biological Chemistry. 272:977-983
Nitric-oxide synthases (NOS, EC 1.14.13.39) are heme-containing enzymes that catalyze the formation of nitric oxide from L-Arg. General cytochrome P-450 inhibitors and cytochrome P-450 isoform-selective substrates and inhibitors were used to characte
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::61e85e6eaf1a57ccf86abfe36e7520a2
https://doi.org/10.1074/jbc.272.2.977
https://doi.org/10.1074/jbc.272.2.977
Autor:
Renee M. Chabin, Daniel S. Fletcher, William A. Hanlon, Barbara G. Green, W. B. Knight, Thomas J. Lanza, Stephen G. Pacholok, John L. Humes, Malcolm MacCoss, Philippe L. Durette, Richard A. Mumford
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 5:271-274
Analogs of the monocyclic β-lactam human leukocyte elastase (HLE) inhibitor L-680,833 in which the carboxyl group is replaced by phosphorous acid moieties were synthesized and found to be potent inhibitors of the enzyme ( k inact / K i in the range
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ca84286af99004f9cc4d9ded5354ccc0
https://doi.org/10.1016/0960-894x(95)00022-l
https://doi.org/10.1016/0960-894x(95)00022-l
Publikováno v:
Biochemical and Biophysical Research Communications. 204:962-968
Nitric oxide synthase (NOS, EC 1.14.23) catalyzes the oxidation of the guanidino-nitrogen of L-arginine to form nitric oxide and L-citrulline. 2-Iminobiotin was found to be a reversible inhibitor of murine iNOS and rat n-cNOS with Ki values of 21.8 a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::268224627139f42c6bb625678c967bfc
https://doi.org/10.1006/bbrc.1994.2554
https://doi.org/10.1006/bbrc.1994.2554
Publikováno v:
Biochemical and Biophysical Research Communications. 197:523-528
Nitric oxide synthase (EC 1.14.23) substrate analog inhibitors N G -monomethyl-L-Arg, N G -nitro-L-Arg, N G -nitro-L-Arg methyl ester, and aminoguanidine were examined as potential inhibitors of rat liver arginase (EC 3.5.3.1). N G -nitro-L-Arg was f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7bedb9e8d5da602d766fb1d58ab47714
https://doi.org/10.1006/bbrc.1993.2510
https://doi.org/10.1006/bbrc.1993.2510
Autor:
Barbara G. Green, W. B. Knight, Lobner Jm, Poe M, Michael W. Lark, Vernon L. Moore, Joseph McDonnell
Publikováno v:
Connective Tissue Research. 30:1-9
In this study, we evaluated the in vitro and in vivo potency of human leukocyte elastase (HLE) and human cathepsin G (HCG) as proteoglycanases. In vitro evaluation was done using bovine nasal septum aggrecan and aggrecan/hyaluronan aggregate as subst
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::deafbfeb661fa6a333a833e1fedb7c3f
https://doi.org/10.3109/03008209309032926
https://doi.org/10.3109/03008209309032926