Výsledky vyhledávání - "Tammy L. Domanski"

Extracytoplasmic Stress Responses Induced by Antimicrobial Cationic Polyethylenimines

Autor: Virginia F. Smith, Kyle D. Checchi, Blaine A. Lander, Daniel D. Isaac, Stephen A. Koplin, Tammy L Domanski, Shirley Lin

Publikováno v: Current Microbiology. 65:488-492

The ability of an antimicrobial, cationic polyethylenimine (PEI+) to induce the three known extracytoplasmic stress responses of Escherichia coli was quantified. Exposure of E. coli to PEI+ in solution revealed specific, concentration-dependent induc

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::96d1c1dc5103013d5cdb75f91092f75e
https://doi.org/10.1007/s00284-012-0182-8

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Evaluation of the antimicrobial activity of cationic polyethylenimines on dry surfaces

Autor: Tammy L Domanski, Stephen A. Koplin, Shirley Lin

Publikováno v: Biotechnology Progress. 24:1160-1165

The antimicrobial activity of cationic N-dodecyl-N-methylpolyethylenimine (PEI+) against S. aureus, A. baumannii, and E. coli was evaluated when the polymer was applied as a coating to various surfaces using a paint-like procedure. Antimicrobial acti

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::32a51a02a22059e444a3f49e6b8a8320
https://doi.org/10.1002/btpr.32

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Midazolam Oxidation by Cytochrome P450 3A4 and Active-Site Mutants: an Evaluation of Multiple Binding Sites and of the Metabolic Pathway That Leads to Enzyme Inactivation

Autor: James R. Halpert, Tammy L. Domanski, You Qun He, Kishore K. Khan

Publikováno v: Molecular Pharmacology. 61:495-506

Midazolam (MDZ) oxidation by recombinant CYP3A4 purified from Escherichia coli and 30 mutants generated at 15 different substrate recognition site positions has been studied to determine the role of individual residues in regioselectivity and to inve

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d74d12e43a826575bd8cd46a0b3a77f6
https://doi.org/10.1124/mol.61.3.495

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The Role of Cytochrome 2B1 Substrate Recognition Site Residues 115, 294, 297, 298, and 362 in the Oxidation of Steroids and 7-Alkoxycoumarins

Autor: Qinmi Wang, Emily E. Scott, James R. Halpert, Tammy L. Domanski, You-Qun He

Publikováno v: Archives of Biochemistry and Biophysics. 394:21-28

At least two substitutions were made at each of five amino acid residues in rat cytochrome P450 2B1 that align to residues of known importance in other P450s. The mutants were histidine tagged for purification from Escherichia coli, and the proteins

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d7be07d04ff9ff0355c89e376e968e2d
https://doi.org/10.1006/abbi.2001.2504

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Phenylalanine and Tryptophan Scanning Mutagenesis of CYP3A4 Substrate Recognition Site Residues and Effect on Substrate Oxidation and Cooperativity

Autor: You-Ai He, Fabienne Roussel, Qinmi Wang, Tammy L. Domanski, James R. Halpert, Kishore K. Khan

Publikováno v: Biochemistry. 40:10150-10160

Phenylalanine and/or tryptophan scanning mutagenesis was performed at 15 sites within CYP3A4 proposed to be involved in substrate specificity or cooperativity. The sites were chosen on the basis of previous studies or from a comparison with the struc

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::149a68f3537f328a82952fa11937d3d8
https://doi.org/10.1021/bi010758a

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[Untitled]

Autor: Arne Zibat, You-Ai He, Hans-Peter Klenk, Regina Eiselt, Romy Mueller, Urs A. Meyer, James R. Halpert, Tammy L. Domanski, Elisabeth Hustert, Elena Presecan-Siedel, Ulrich M. Zanger, Jürgen Brockmöller, Leszek Wojnowski, Kishore K. Khan

Publikováno v: Pharmacogenetics. 11:447-458

The genetic component of the inter-individual variability in CYP3A4 activity has been estimated to be between 60% and 90%, but the underlying genetic factors remain largely unknown. A study of 213 Middle and Western European DNA samples resulted in t

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::4cb47b7abfe83a1a6dc106ca07e6efd7
https://doi.org/10.1097/00008571-200107000-00008

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Influence of P450 3A4 SRS-2 Residues on Cooperativity and/or Regioselectivity of Aflatoxin B1 Oxidation

Autor: Huifen Faye Wang, Qinmi Wang, Grazyna D. Szklarz, Tammy L. Domanski, Linlong Xue, James R. Halpert, Maria Almira Correia

Publikováno v: Chemical Research in Toxicology. 14:483-491

The major human liver drug-metabolizing cytochrome P450 enzymes P450 3A4 and P450 3A5 share >85% amino acid sequence identity yet exhibit different regioselectivity toward aflatoxin B(1) (AFB(1)) biotransformation [Gillam et al. (1995) Arch. Biochem.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d58db40bb94e4aa7e721a9b54e780b7b
https://doi.org/10.1021/tx000218z

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Analysis of Four Residues within Substrate Recognition Site 4 of Human Cytochrome P450 3A4: Role in Steroid Hydroxylase Activity and α-Naphthoflavone Stimulation

Autor: James R. Halpert, Greg R. Harlow, Juping Liu, Tammy L. Domanski

Publikováno v: Archives of Biochemistry and Biophysics. 350:223-232

Sequence alignment of human cytochrome P450 3A4 with bacterial enzymes of known structure has provided a basis from which to predict residues involved in substrate oxidation. Substitutions were made at four residues (I301, F304, A305, and T309) predi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::58ff44cf5595e77f8be2064a427c1545
https://doi.org/10.1006/abbi.1997.0525

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