Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Douglas Schirch"'
Autor:
Amelia A. Fuller, Amy B. Dounay, Mark A. T. Blaskovich, Kristiana Tenorio, Johannes Zuegg, Martin J. O'Donnell, Karl A. Hansford, Yanira Méndez, Sarah Burris-Hiday, Daniel G. Rivera, William L. Scott, J. Geno Samaritoni, Mark E. Cooper, Alysha G. Elliott, Douglas Schirch, Jacob R Hitchens
Publikováno v:
ACS Chemical Biology
New antibiotics are urgently needed to address increasing rates of multidrug resistant infections. Seventy-six diversely functionalized compounds, comprising five structural scaffolds, were synthesized and tested for their ability to inhibit microbia
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::20157c5b635cd20cc66ed91b47400431
https://doi.org/10.1021/acschembio.0c00732
https://doi.org/10.1021/acschembio.0c00732
Autor:
Isaac W. Lamb, Kristen Mudrack, Gerardo M. Ojeda, Amy B. Dounay, William L. Scott, Lukasz Popiolek, Douglas Schirch, Anna Malm, Anna Biernasiuk, Daniel G. Rivera, J. Geno Samaritoni, Martin J. O'Donnell
Publikováno v:
Journal of Chemical Education. 96:1731-1737
An experiment for the synthesis of N-acyl derivatives of natural amino acids has been developed as part of the Distributed Drug Discovery (D3) program. Students use solid-phase synthesis techniques to complete a three-step, combinatorial synthesis of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3d91349e7f4d2bf096551ec0bef582d7
https://doi.org/10.1021/acs.jchemed.8b00942
https://doi.org/10.1021/acs.jchemed.8b00942
Autor:
Douglas Schirch
Publikováno v:
ACS Symposium Series ISBN: 9780841236295
ACS Symposium Series
ACS Symposium Series
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3292c665037882be35a17996bcfefacd
https://doi.org/10.1021/bk-2019-1336.ch009
https://doi.org/10.1021/bk-2019-1336.ch009
Autor:
Justin B. Houseknecht, Alexey Leontyev, Vincent M. Maloney, Catherine O. Welder, Mary S. Lenczewski, Thomas P. Umile, Racquel C. DeCicco, Ryan C. Jeske, James A. Jones, Courtney L. Stanford, Kevin M. Shea, Julia E. Winter, Sarah E. Wegwerth, Brittland K. DeKorver, Layne A. Morsch, Dane DeSutter, Lawrence M. Goldman, Lauren M. Reutenauer, Douglas Schirch, James C. Shattuck, Matthew D. Casselman, Dorian A. Canelas, Jennifer L. Hill, Robert G. Carden, Matthew P. DeMatteo
Publikováno v:
Biochemistry. 35:15772-15783
A new rapid procedure for purifying 10-formyltetrahydrofolate dehydrogenase results in 90 mg of pure enzyme from two rabbit livers. This abundant liver enzyme is known to bind its product tetrahydropteroylpentaglutamate (H4PteGlu5) so tightly that it
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dc016a08396167c70aeded1f48956b46
https://doi.org/10.1021/bi9619684
https://doi.org/10.1021/bi9619684
Publikováno v:
The Journal of biological chemistry. 270(33)
Escherichia coli serine hydroxymethyltransferase is a 94-kDa homodimer. Each subunit contains a covalently attached pyridoxal-P, which is required for catalytic activity. At which step pyridoxal-P binds in the folding pathway of E. coli serine hydrox
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5c67df81a16b43ae596d0e95ab1aa4f9
https://pubmed.ncbi.nlm.nih.gov/7642604
https://pubmed.ncbi.nlm.nih.gov/7642604
Autor:
S Delle Fratte, Verne Schirch, Douglas Schirch, F Bossa, Sebastiana Angelaccio, Roberto Contestabile, Sandra Iurescia
Publikováno v:
Scopus-Elsevier
Serine hydroxymethyltransferase has a conserved lysine residue (Lys-229) that forms the internal aldimine with pyridoxal 5'-phosphate. In other pyridoxal 5'-phosphate enzymes investigated so far, this conserved lysine residue also plays a catalytic r
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c8bc664a24fb1ec628963decb9cad330
http://hdl.handle.net/11573/246082
http://hdl.handle.net/11573/246082
Autor:
Douglas Schirch, Sandra Iurescia, F Bossa, Schirch, Roberto Contestabile, Sebastiana Angelaccio, Delle Fratte S
Publikováno v:
Advances in Experimental Medicine and Biology ISBN: 9781461362876
Serine hydroxymethyltransferase (SHMT) is a pyridoxal phosphate requiring enzyme which catalyzes the reaction shown in Equation 1. This enzyme uses both the monoglutamate and polyglutamate forms of tetrahydrofolate (H4PteGlun) and 5,10-methylenetetra
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f7cf45baa12278e7385bb3ccdb83df99
https://doi.org/10.1007/978-1-4615-2960-6_148
https://doi.org/10.1007/978-1-4615-2960-6_148
Publikováno v:
European journal of biochemistry. 161(1)
Homogeneous preparations of cytosolic serine hydroxymethyltransferase from rabbit liver were incubated with several different proteases. Chymotrypsin rapidly cleaves a tetradecapeptide from the NH2-terminal end of the enzyme with the enzyme retaining
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7bdba97962038801939fa1f3bfb4c96a
https://pubmed.ncbi.nlm.nih.gov/3536510
https://pubmed.ncbi.nlm.nih.gov/3536510
Autor:
Douglas Schirch, John E. Wilson
Publikováno v:
Archives of biochemistry and biophysics. 257(1)
A reactive Glc analog, N-(bromoacetyl)-D-glucosamine (GlcNBrAc), has recently been used (D. M. Schirch and J. E. Wilson (1987) Arch. Biochem. Biophys. 254, 385-396) to label the Glc binding site of rat brain Type I hexokinase. This site has been loca
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1dd33901e8e2d9f4124977afb1af27f3
https://pubmed.ncbi.nlm.nih.gov/3631958
https://pubmed.ncbi.nlm.nih.gov/3631958