Zobrazeno 1 - 10
of 25
pro vyhledávání: '"Joseph F. Krebs"'
Publikováno v:
Nucleic Acids Research
The RNA-dependent protein kinase (PKR) is activated by binding to double-stranded RNA (dsRNA). Activation of PKR by short-interfering RNAs (siRNAs) and stimulation of the innate immune response has been suggested to explain certain off-target effects
Autor:
Kevin J. Tomaselli, Julia Herrmann, Robert O. Sayers, Joe C. Wu, Lalitha Kodandapani, Kathy G. Jahangiri, Craig D. Fisher, David T. Winn, Edward D. Robinson, Steven P. Meduna, Robert J. Ternansky, Pauline Yeo, Karen L. Valentino, Jose-Luis Diaz, Vincent J. Kalish, Steven D. Linton, Kristen Sebring, Robert A. Armstrong, Joseph F. Krebs, Niel C. Hoglen, Alfred P. Spada, Brad P. Hirakawa, Ning Chen, Brett R. Ullman, Brett Weylan Ching, Cheng-zhi Zhang, Xu Bai, Xin Gu, Kip Nalley, Long-Shiuh Chen, Patricia L. Gladstone, Jeff McQuiston, Teresa Aja, Todd Groessl, Donald S. Karanewsky, Suzanne Weeks, Lawrence C. Fritz, Patricia C. Contreras
Publikováno v:
Journal of Medicinal Chemistry. 48:6779-6782
A series of oxamyl dipeptides were optimized for pan caspase inhibition, anti-apoptotic cellular activity and in vivo efficacy. This structure-activity relationship study focused on the P4 oxamides and warhead moieties. Primarily on the basis of in v
Autor:
Anu Srinivasan, Lawrence C. Fritz, Joseph F. Krebs, Kevin J. Tomaselli, Joe C. Wu, Angela M. Wong
Publikováno v:
Biochemistry. 39:16056-16063
Heavy membrane preparations from 697 lymphoblastoid cells contain a tightly bound caspase zymogen. This heavy membrane-bound procaspase can be efficiently liberated from membrane preparations using detergents. Alternatively, the procaspase can be rap
Autor:
Christian Leist, Kim Hoang, Anu Srinivasan, Donald S. Karanewsky, Tam Vu, Lawrence C. Fritz, Robert C. Armstrong, Joe C. Wu, Bryan Pham, Teresa Aja, Rob Sayers, Albert Schmitz, Angela M. Wong, Joseph F. Krebs, Aileen Aboy, Kevin J. Tomaselli
Publikováno v:
The Journal of Cell Biology
The mechanism by which membrane-bound Bcl-2 inhibits the activation of cytoplasmic procaspases is unknown. Here we characterize an intracellular, membrane-associated form of procaspase-3 whose activation is controlled by Bcl-2. Heavy membranes isolat
Autor:
Joseph A. Trapani, Kevin J. Tomaselli, Teresa Fernandes-Alnemri, Lawrence C. Fritz, Emad S. Alnemri, Lijuan Wang, Florencia Bullrich, Joseph F. Krebs, Robert C. Armstrong, Gerald Litwack, Srinivasa M. Srinivasula
Publikováno v:
Proceedings of the National Academy of Sciences. 93:7464-7469
Emerging evidence suggests that an amplifiable protease cascade consisting of multiple aspartate specific cysteine proteases (ASCPs) is responsible for the apoptotic changes observed in mammalian cells undergoing programmed cell death. Here we descri
Autor:
Joseph F. Krebs, Jialing Xiang, Smita Gaur, Lawrence C. Fritz, Xu Bai, Kevin J. Tomaselli, Stanley J. Korsmeyer, Teresa Aja, Donald S. Karanewsky, Robert C. Armstrong, Kim Hoang
Publikováno v:
Journal of Biological Chemistry. 271:16850-16855
The human proto-oncogene bcl-2 and its Caenorhabditis elegans homologue ced-9 inhibit programmed cell death. In contrast, members of the human interleukin-1beta converting enzyme (ICE) family of cysteine proteases and their C. elegans homologue CED-3
Publikováno v:
Biochemistry. 34:3981-3989
The activities and structures of certain L198 variants of human carbonic anhydrase II (CAII) have been reported recently [Krebs, J. F., Rana, F., Dluhy, R. A., & Fierke, C. A. (1993) Biochemistry 32, 4496-4505; Nair, S. K., & Christianson, D. W. (199
Publikováno v:
Biochemistry. 34:720-723
The chemical interactions between a catalytic antibody Fv fragment and ester substrates were examined using pneumatically assisted electrospray (ion spray) mass spectrometry. Upon addition of the p-nitrophenyl ester substrate to the antibody fragment
Autor:
Gary Siuzdak, Anthony J. Berdis, David B. Smithrud, Stephen J. Benkovic, John D. Stewart, Joseph F. Krebs
Publikováno v:
Proceedings of the National Academy of Sciences. 91:7404-7409
Antibody 43C9 accelerates the hydrolysis of a p-nitroanilide by a factor of 2.5 x 10(5) over the background rate in addition to catalyzing the hydrolysis of a series of aromatic esters. Since this represents one of the largest rate accelerations achi
Publikováno v:
Journal of Biological Chemistry. 268:27458-27466
Amino acid substitutions at Thr199 of human carbonic anhydrase II (CAII) (Thr199-->Ser, Ala, Val, and Pro) were characterized to investigate the importance of a conserved hydrogen bonding network. The three-dimensional structures of azide-bound and s