Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Lori G. Stinnett"'
Publikováno v:
Journal of Biological Chemistry. 279:47003-47009
R67 dihydrofolate reductase (R67 DHFR) catalyzes the transfer of a hydride ion from NADPH to dihydrofolate, generating tetrahydrofolate. The homotetrameric enzyme provides a unique environment for catalysis as both ligands bind within a single active
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4321e9e1beebf3b63d6dfb83d9fb6e86
https://doi.org/10.1074/jbc.m404485200
https://doi.org/10.1074/jbc.m404485200
Autor:
Lori G. Stinnett, Jun Wu, R. Derike Smiley, Michael Jackson, Elizabeth E. Howell, Michael Brad Strader, Shaileja Chopra
Publikováno v:
Biochemistry. 43:7403-7412
R67 dihydrofolate reductase (DHFR) is a novel protein that possesses 222 symmetry. A single active site pore traverses the length of the homotetramer. Although the 222 symmetry implies that four symmetry-related binding sites should exist for each su
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::558427096926d7ee8d7ce6aa70f71bef
https://doi.org/10.1021/bi049646k
https://doi.org/10.1021/bi049646k
Publikováno v:
Analytical Biochemistry. 301:153-156
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::984d85814e5fdd51be4578f0d1819724
https://doi.org/10.1006/abio.2001.5518
https://doi.org/10.1006/abio.2001.5518
Autor:
M.J. Jackson, Stephanie N. Hicks, Lori G. Stinnett, Elizabeth E. Howell, Arnold M. Saxton, R.D. Smiley
Publikováno v:
Analytical Biochemistry. 334:204-206
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::64da4e481f17b9b7a8f04a73b2fdc0b5
https://doi.org/10.1016/j.ab.2004.06.040
https://doi.org/10.1016/j.ab.2004.06.040
Autor:
Lori G. Stinnett, R. Derike Smiley, Kenneth H. Minor, Stephanie N. Hicks, Elizabeth E. Howell
Publikováno v:
The Journal of biological chemistry. 279(45)
R67 dihydrofolate reductase (R67 DHFR) is a novel protein encoded by an R-plasmid that confers resistance to the antibiotic, trimethoprim. This homotetrameric enzyme possesses 222 symmetry, which imposes numerous constraints on the single active site
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::100bf9c43d3d1f351c3cf98973f6d9b9
https://pubmed.ncbi.nlm.nih.gov/15333636
https://pubmed.ncbi.nlm.nih.gov/15333636
Autor:
Elizabeth E. Howell, Michael Brad Strader, Lori G. Stinnett, R.D. Smiley, Nathan C Verberkmoes
Publikováno v:
Biochemistry. 40(38)
R67 dihydrofolate reductase (DHFR) shares no sequence or structural homology with chromosomal DHFRs. This enzyme arose recently in response to the clinical use of the antibacterial drug trimethoprim. R67 DHFR is a homotetramer possessing a single act
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::755145c11d5c155fc0dcead722cd6543
https://pubmed.ncbi.nlm.nih.gov/11560482
https://pubmed.ncbi.nlm.nih.gov/11560482