Zobrazeno 1 - 10
of 100
pro vyhledávání: '"Frederick P. Schwarz"'
Publikováno v:
Biology, Vol 12, Iss 10, p 1277 (2023)
Bacteriophage endolysins degrade the bacterial peptidoglycan and are considered enzymatic alternatives to small-molecule antibiotics. In particular, the multimeric streptococcal endolysin PlyC has appealing antibacterial properties. However, a compre
Externí odkaz:
https://doaj.org/article/2cbd8116aed54495b8fe11f3f24006a5
Bacteriophage endolysins degrade the bacterial peptidoglycan and are considered enzymatic alternatives to small molecule antibiotics. In particular, the multimeric streptococcal endolysin PlyC has appealing antibacterial properties. However, a compre
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::031df307dcba7b491f7436108ddfbd4b
https://doi.org/10.1101/2022.01.06.475266
https://doi.org/10.1101/2022.01.06.475266
Autor:
Duilio Cascio, Ganesaratnam K. Balendiran, Frederick P. Schwarz, Richard Cuckovich, Michael R. Sawaya, Gomathinayagam Ponniah, Malkhey Verma
Publikováno v:
Journal of Biological Chemistry. 286:6336-6344
Diabetic tissues are enriched in an "activated" form of human aldose reductase (hAR), a NADPH-dependent oxidoreductase involved in sugar metabolism. Activated hAR has reduced sensitivity to potential anti-diabetes drugs. The C298S mutant of hAR repro
Effect of the phosphate substrate on drug-inhibitor binding to human purine nucleoside phosphorylase
Autor:
Frederick P. Schwarz, Niya A. Todorova
Publikováno v:
Archives of Biochemistry and Biophysics. 480:122-131
The thermodynamics of the drug-inhibitors acyclovir, ganciclovir, and 9-benzylguanine binding to human purine nucleoside phosphorylase (hsPNP) were determined from isothermal titration calorimetry as a function of the substrate phosphate ion (Pi) con
Autor:
Barry A. Fields, Xavier Ysern, Frederick P. Schwarz, Ana Cauerhff, William Dall'Acqua, Roy A. Mariuzza, Fernando A. Goldbaum, Emilio L. Malchiodi, Talapady N. Bhat, Bradford C. Braden, Roberto J. Poljak
Publikováno v:
Annals of the New York Academy of Sciences. 764:315-327
Publikováno v:
Pure and Applied Chemistry. 80:2025-2040
Isothermal titration calorimetry (ITC) is widely used to determine the thermodynamics of biological interactions including protein-protein, small molecule-protein, protein-DNA, small molecule-DNA, and antigen-antibody interactions. An ITC measurement
Autor:
Eugene Melamud, Zvi Kelman, Rajesh Kasiviswanathan, Frederick P. Schwarz, Mimi Han, Nozomi Sakakibara
Publikováno v:
Nucleic Acids Research
Minichromosome maintenance (MCM) helicases are the presumptive replicative helicases, thought to separate the two strands of chromosomal DNA during replication. In archaea, the catalytic activity resides within the C-terminal region of the MCM protei
Autor:
Niya A. Todorova, Frederick P. Schwarz
Publikováno v:
The Journal of Chemical Thermodynamics. 39:1038-1048
The thermodynamic parameters, Δ B G ∘ , Δ B H ∘ , Δ B S ∘ , and Δ B C p , of the drugs flurbiprofen (FLP), nabumetone (NAB), and naproxen (NPX) binding to β-cyclodextrin (βCD) and to γ-cyclodextrin (γCD) in 0.10 M sodium phosphate buffe
Publikováno v:
Biopolymers. 81:235-248
A comprehensive study of the thermal stabilization of defatted human albumin monomer by n-alkyl fatty acid anions (FAAs), formate through n-decanoate, was carried out by differential scanning calorimetry (DSC). The concentration of each ligand afford
Publikováno v:
Archives of Biochemistry and Biophysics. 438:162-173
The energetics of LRP binding to a 104 bp lac promoter determined from ITC measurements were compared to the energetics of binding to a shorter 40 bp DNA duplex with the 21 bp promoter binding site sequence. The promoter binding affinity of 2.47 +/-