Zobrazeno 1 - 10
of 30
pro vyhledávání: '"Trevor Selwood"'
Autor:
Jessica L. Schneck, Charlie Y. Mo, Zachary M Hostetler, Anthony J. Jurewicz, Paul M. Keller, Trevor Selwood, Amy Quinn, Andrew J. Pope, Matthew J. Culyba, Widdowson Katherine L, Rahul M. Kohli, Jeffrey M. Kubiak
Publikováno v:
ACS Infectious Diseases. 4:349-359
The RecA/LexA axis of the bacterial DNA damage (SOS) response is a promising, yet non-traditional drug target. The SOS response is initiated upon genotoxic stress, when RecA, a DNA damage sensor, induces LexA, the SOS repressor, to undergo autoproteo
Autor:
Trevor Selwood, Brian J. Larsen, Charlie Y. Mo, Matthew J. Culyba, Zachary M. Hostetler, Rahul M. Kohli, Allen B. Reitz, Simon D. P. Baugh
Publikováno v:
Frontiers in Microbiology
Frontiers in Microbiology, Vol 9 (2018)
Frontiers in Microbiology, Vol 9 (2018)
Many antibiotics, either directly or indirectly, cause DNA damage thereby activating the bacterial DNA damage (SOS) response. SOS activation results in expression of genes involved in DNA repair and mutagenesis, and the regulation of the SOS response
Publikováno v:
Current Chemical Biology. 7:196-206
The molecular mechanisms whereby small molecules that contaminate our environment cause physiological effects are largely unknown, in terms of both targets and mechanisms. The essential human enzyme porphobilinogen synthase (HsPBGS, a.k.a. 5-aminolev
Publikováno v:
ChemMedChem. 6:1067-1073
An in vitro evaluation of the Johns Hopkins Clinical Compound Library demonstrates that certain drugs can alter the quaternary structure of an essential human protein. Human porphobilinogen synthase (HsPBGS) is an essential enzyme involved in heme bi
Publikováno v:
Biochemistry. 47:3245-3257
A morpheein is a homo-oligomeric protein that can adopt different nonadditive quaternary assemblies (morpheein forms) with different functionalities. The human porphobilinogen synthase (PBGS) morpheein forms are a high activity octamer, a low activit
Publikováno v:
Biochemistry. 44:3580-3590
Human tryptase-beta (HTbeta) is a serine protease with an atypical tetrameric structure and an unusual dependence on heparin binding or high salt for functional and structural stability. In the absence of heparin and at physiological salt, pH, and te
Publikováno v:
Biochemistry. 41:3329-3340
Recombinant human tryptases (rHTs) corresponding to alpha and beta isoforms were characterized. rHTbeta was similar to tryptase isolated from skin (HST); it was a tetramer, hydrolyzed model substrates efficiently, and was functionally unstable when i
Autor:
Harvey Rubin, Richard W. Scott, Damian G. Weaver, H. Marie Loughran, Allen B. Reitz, Katie B. Freeman, Michael J. Costanzo, Trevor Selwood, Jay E. Wrobel, Takahiro Yano
Publikováno v:
Bioorganicmedicinal chemistry letters. 25(2)
The Gram-negative bacterium Acinetobacter baumannii is an opportunistic pathogen in humans and infections are poorly treated by current therapy. Recent emergence of multi-drug resistant strains and the lack of new antibiotics demand an immediate acti
Publikováno v:
Biochemistry. 37:13174-13183
The conformational changes accompanying spontaneous inactivation and dextran sulfate (DS) mediated reactivation of the serine protease human tryptase were investigated by analysis of (i) intrinsic fluorescence, (ii) inhibitor binding, and (iii) catal
Publikováno v:
bchm. 379:167-174
Expression of recombinant human chymase and tryptase was achieved in a baculovirus-insect cell system using a fusion protein construct. Recombinant baculovirus was produced with DNA coding for a NH2-ubiquitin-chymase-COOH or NH2-ubiquitin-tryptase-CO