Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Brett Feeney"'
Autor:
A. Clay Clark, Benjamin G. Bobay, John Cavanagh, Linda M. Benson, Mark A. Strauch, Stephen Naylor, Brett Feeney, Richele J. Thompson, Michael B. Goshe
Publikováno v:
Biochemistry. 43:16106-16118
Global transition state regulator proteins represent one of the most diverse classes of prokaryotic transcription factors. One such transition state regulator, AbrB from Bacillus subtilis, is known to bind more than 60 gene targets yet displays speci
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d6103cb509a7085bb1fae1c17926cbf4
https://doi.org/10.1021/bi048399h
https://doi.org/10.1021/bi048399h
Publikováno v:
Biochemistry. 42:12298-12310
We have examined the enzymatic activity of an uncleavable procaspase-3 mutant (D9A/D28A/D175A), which contains the wild-type catalytic residues in the active site. The results are compared to those for the mature caspase-3. Although at pH 7.5 and 25
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2324e83c9737d8bb36640a202991e3f4
https://doi.org/10.1021/bi034998x
https://doi.org/10.1021/bi034998x
Publikováno v:
Journal of molecular biology. 369(1)
Caspase recruitment domains (CARDs) are members of the death domain superfamily and contain six antiparallel helices in an alpha-helical Greek key topology. We have examined the equilibrium and kinetic folding of the CARD of Apaf-1 (apoptotic proteas
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5d5a808725551afc0fbcab7fb9fac5c4
https://pubmed.ncbi.nlm.nih.gov/17408690
https://pubmed.ncbi.nlm.nih.gov/17408690
During maturation, procaspase-3 is cleaved at D175, which resides in a linker that connects the large and small subunits. The intersubunit linker also connects two active site loops that rearrange following cleavage and, in part, form the so-called l
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::92a15da93255547fabcdc2cb91b8158b
https://europepmc.org/articles/PMC3119718/
https://europepmc.org/articles/PMC3119718/
Autor:
A. Clay Clark, Brett Feeney
Changes in ionic homeostasis are early events leading up to the commitment to apoptosis. Although the direct effects of cations on caspase-3 activity have been examined, comparable studies on procaspase-3 are lacking. In addition, the effects of salt
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7c9b8181a8f3d24712b0d2c861e00881
https://europepmc.org/articles/PMC3119714/
https://europepmc.org/articles/PMC3119714/
Publikováno v:
Protein expression and purification. 47(1)
Coupled with over-expression in host organisms, fusion protein systems afford economical methods to obtain large quantities of target proteins in a fast and efficient manner. Some proteases used for these purposes cleave C-terminal to their recogniti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3e03d800fb43f5d772320ef32a05cca9
https://pubmed.ncbi.nlm.nih.gov/16289916
https://pubmed.ncbi.nlm.nih.gov/16289916
Publikováno v:
The Biochemical journal. 384(Pt 3)
We have examined the role of a salt bridge between Lys242 and Glu246 in loop L4 of procaspase 3 and of mature caspase 3, and we show that the interactions are required for stabilizing the active site. Replacing either of the residues with an alanine
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bc177a0aa2ee660378c90ad7adbde975
https://pubmed.ncbi.nlm.nih.gov/15312047
https://pubmed.ncbi.nlm.nih.gov/15312047
Autor:
Bobay, Benjamin G., Benson, Linda, Naylor, Stephen, Brett Feeney, Clark, A. Clay, Goshe, Michael B., Strauch, Mark A., Thompson, Richele, Cavanagh, John
Publikováno v:
Biochemistry; 12/28/2004, Vol. 43 Issue 51, p16106-16118, 13p