Zobrazeno 1 - 10
of 16
pro vyhledávání: '"G N, DeMartino"'
Autor:
L R Dick, C Aldrich, S C Jameson, C R Moomaw, B C Pramanik, C K Doyle, G N DeMartino, M J Bevan, J M Forman, C A Slaughter
Publikováno v:
The Journal of Immunology. 152:3884-3894
The identification of genes in the class II region of the MHC that are homologous to genes encoding subunits of the proteasome has led to intense interest in the possible role of this enzyme in the proteolytic processing of polypeptide Ags. We have t
Autor:
G N, DeMartino, G A, Ordway
Publikováno v:
Exercise and sport sciences reviews. 26
Publikováno v:
Journal of molecular biology. 273(3)
Control and targeting of the proteolytic activity of the major intracellular protease, the proteasome, is accomplished by various regulatory protein complexes that may form higher-order assemblies with the proteasome. An activator of proteolytic acti
Publikováno v:
The Journal of biological chemistry. 269(50)
PA28, one of a series of a positive allosteric regulators of the 20 S proteasome, stimulates the enzyme's peptidase activities in an ATP-independent manner by binding to the terminal rings of the 20 S complex. PA28 has a native molecular mass of 180,
Autor:
G N, DeMartino, C R, Moomaw, O P, Zagnitko, R J, Proske, M, Chu-Ping, S J, Afendis, J C, Swaffield, C A, Slaughter
Publikováno v:
The Journal of biological chemistry. 269(33)
PA700 is a 700,000-dalton multisubunit protein that activates multiple proteolytic activities of the 20 S proteasome by a mechanism dependent upon ATP hydrolysis (Ma, C.-P., Vu, J.H., Proske, R.J., Slaughter, C.A., and DeMartino, G.N. (1994) J. Biol.
Autor:
L R, Dick, C, Aldrich, S C, Jameson, C R, Moomaw, B C, Pramanik, C K, Doyle, G N, DeMartino, M J, Bevan, J M, Forman, C A, Slaughter
Publikováno v:
Journal of immunology (Baltimore, Md. : 1950). 152(8)
The identification of genes in the class II region of the MHC that are homologous to genes encoding subunits of the proteasome has led to intense interest in the possible role of this enzyme in the proteolytic processing of polypeptide Ags. We have t
Publikováno v:
The Journal of biological chemistry. 269(5)
In order to identify protein complexes consisting of the proteasome and specific proteasome regulators, crude soluble lysates of red blood cells were fractionated by gel filtration chromatography and by velocity sedimentation centrifugation. The frac
Publikováno v:
The Journal of biological chemistry. 268(30)
PA28, a protein activator of the 20 S proteasome, was previously identified in soluble extracts of bovine red blood cells (Ma, C.-P., Slaughter, C. A., and DeMartino, G. N. (1992) J. Biol. Chem. 267, 10515-10523). To determine whether this regulatory
Publikováno v:
The Journal of biological chemistry. 267(15)
A protein that greatly stimulates the multiple peptidase activities of the 20 S proteasome (also known as macropain, the multicatalytic protease complex, and 20 S protease) has been purified from bovine red blood cells and from bovine heart. The acti
Autor:
G N, DeMartino, A L, Goldberg
Publikováno v:
The Journal of biological chemistry. 254(10)
Extracts from rat liver contain a sulfhydryl-dependent endoprotease which degrades [methyl-14C]globin or 125I-hemoglobin to acid-soluble peptides. This enzyme was isolated from the 100,000 x g supernatant of the homogenate. It showed a pH optimum bet