Zobrazeno 1 - 10
of 1 095
pro vyhledávání: '"R. Bauerle"'
Autor:
Squire J. Booker, Ryan J. Martinie, Carsten Krebs, Matthew R. Bauerle, Mohamed Almarei, James D. Gumkowski, Patrick S. Corrigan, Alexey Silakov, Juan Pan, Amie K. Boal
Publikováno v:
Biochemistry. 58:3169-3184
Cfr is a radical S-adenosylmethionine (SAM) RNA methylase linked to multidrug antibiotic resistance in bacterial pathogens. It catalyzes a chemically challenging C-C bond-forming reaction to methylate C8 of A2503 (Escherichia coli numbering) of 23S r
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f7c9590ed60eae307acd7841e8f2ed44
https://doi.org/10.1021/acs.biochem.9b00197
https://doi.org/10.1021/acs.biochem.9b00197
Publikováno v:
Biochemistry. 57:4431-4439
Cfr is a radical S-adenosylmethionine (RS) methylase that appends methyl groups to C8 and C2 of adenosine 2503 in 23S ribosomal RNA. Methylation of C8 confers resistance to several classes of antibiotics that bind in or near the peptidyl transferase
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0a07bde5e11423e2f840bb1583866ed0
https://doi.org/10.1021/acs.biochem.8b00347
https://doi.org/10.1021/acs.biochem.8b00347
Autor:
James D, Gumkowski, Ryan J, Martinie, Patrick S, Corrigan, Juan, Pan, Matthew R, Bauerle, Mohamed, Almarei, Squire J, Booker, Alexey, Silakov, Carsten, Krebs, Amie K, Boal
Publikováno v:
Biochemistry
Cfr is a radical S-adenosylmethionine (SAM) RNA methylase linked to multi-drug antibiotic resistance in bacterial pathogens. It catalyzes a chemically challenging C-C-bond forming reaction to methylate C8 of A2503 [Escherichia coli (Ec) numbering) of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::79c386cf30fbc6dcbffbd07ca389d436
https://pubmed.ncbi.nlm.nih.gov/31246421
https://pubmed.ncbi.nlm.nih.gov/31246421
Autor:
Matthew I. Radle, Tyler L. Grove, Amie K. Boal, Alexey Silakov, Matthew R. Bauerle, Michael Green, Amy C. Rosenzweig, Squire J. Booker
Publikováno v:
Journal of the American Chemical Society
RlmN and Cfr are methyltransferases/methylsynthases that belong to the radical S-adenosylmethionine superfamily of enzymes. RlmN catalyzes C2 methylation of adenosine 2503 (A2503) of 23S rRNA, while Cfr catalyzes C8 methylation of the exact same nucl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::15105d2bee02115c4903db82cd2b1cac
http://europepmc.org/articles/PMC4227720
http://europepmc.org/articles/PMC4227720
Autor:
Elisa Granjo, Natália Mundim Tôrres, P. Manata, Alexandre Quintanilha, R. Bauerle, Ricardo Sampaio
Publikováno v:
International Journal of Hematology. 76:153-156
Hereditary spherocytosis (HS) is a common inherited hemolytic anemia due to red cell membrane defects. Extramedullary hematopoiesis is a compensatory response to insufficient bone marrow blood cell production. The preferred sites of extramedullary he
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2182bb616b5fd1258e2b21e6daa758f1
https://doi.org/10.1007/bf02982578
https://doi.org/10.1007/bf02982578
Publikováno v:
The Journal of biological chemistry. 290(7)
Radical S-adenosylmethionine (SAM) enzymes use the oxidizing power of a 5'-deoxyadenosyl 5'-radical to initiate an amazing array of transformations, usually through the abstraction of a target substrate hydrogen atom. A common reaction of radical SAM
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b2b2a0cf277de4dcd75c1b19b13264e2
https://pubmed.ncbi.nlm.nih.gov/25477520
https://pubmed.ncbi.nlm.nih.gov/25477520
Publikováno v:
The FASEB Journal. 26
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3a21c5e996e32be95dd95543a74ca6fd
https://doi.org/10.1096/fasebj.26.1_supplement.963.13
https://doi.org/10.1096/fasebj.26.1_supplement.963.13
Publikováno v:
European Neuropsychopharmacology. 21:S382-S383
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::61214cbdb66948035f1e236bf3b19849
https://doi.org/10.1016/s0924-977x(11)70614-9
https://doi.org/10.1016/s0924-977x(11)70614-9
Publikováno v:
Journal of molecular biology. 301(2)
The crystal structure of the phenylalanine-regulated 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase (DAHPS) from Escherichia coli in complex with Mn(2+) and the substrate analog, 2-phosphoglycolate (PGL), was determined by molecular replacement
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::99a92d120c5133decf5635a0a54a38dc
https://pubmed.ncbi.nlm.nih.gov/10926516
https://pubmed.ncbi.nlm.nih.gov/10926516
Publikováno v:
Journal of molecular biology. 301(2)
The crystal structure of 3-deoxy-d-manno-octulosonate-8-phosphate synthase (KDOPS) from Escherichia coli was determined by molecular replacement using coordinates given to us by Radaev and co-workers prior to publication. The KDOPS crystals reported
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::0f355a4030ab8e21e975ce2fb4e9cb7a
https://pubmed.ncbi.nlm.nih.gov/10926505
https://pubmed.ncbi.nlm.nih.gov/10926505