Zobrazeno 1 - 10
of 21
pro vyhledávání: '"Mira Sastri"'
Autor:
Ping Zhang, Matthias J Knape, Lalima G Ahuja, Malik M Keshwani, Charles C King, Mira Sastri, Friedrich W Herberg, Susan S Taylor
Publikováno v:
PLoS Biology, Vol 13, Iss 7, p e1002192 (2015)
To provide tight spatiotemporal signaling control, the cyclic adenosine monophosphate (cAMP)-dependent protein kinase (PKA) holoenzyme typically nucleates a macromolecular complex or a "PKA signalosome." Using the RIIβ holoenzyme as a prototype, we
Externí odkaz:
https://doaj.org/article/f3af226096054bbfacdf5c8046e4a3ce
Publikováno v:
PLoS ONE, Vol 6, Iss 4, p e18713 (2011)
The mechanism of PKAc-dependent NF-κB activation and subsequent translocation into the nucleus is not well defined. Previously, we showed that A kinase interacting protein 1 (AKIP1) was important for binding and retaining PKAc in the nucleus. Since
Externí odkaz:
https://doaj.org/article/e5b9e0b1bb7c484e916576d26d0b2b26
Autor:
Kristofer J. Haushalter, Jan M. Schilling, Hemal H. Patel, Guy Perkins, Mira Sastri, Young Duk Song, Stefan Strack, Susan S. Taylor
Publikováno v:
Am J Physiol Heart Circ Physiol
Type I PKA regulatory α-subunit (RIα; encoded by the Prkar1a gene) serves as the predominant inhibitor protein of the catalytic subunit of cAMP-dependent protein kinase (PKAc). However, recent evidence suggests that PKA signaling can be initiated b
Autor:
Mira, Sastri, Manjula, Darshi, Mason, Mackey, Ranjan, Ramachandra, Saeyeon, Ju, Sebastien, Phan, Stephen, Adams, Kathryn, Stein, Christopher R, Douglas, Jiwan John, Kim, Mark H, Ellisman, Susan S, Taylor, Guy A, Perkins
Publikováno v:
Journal of cell science. 130(19)
Each mitochondrial compartment contains varying protein compositions that underlie a diversity of localized functions. Insights into the localization of mitochondrial intermembrane space-bridging (MIB) components will have an impact on our understand
Autor:
Ranjan Ramachandra, Mira Sastri, Manjula Darshi, Christopher Douglas, Saeyeon Ju, Susan S. Taylor, Jiwan John Kim, Kathryn Stein, Mason R. Mackey, Guy Perkins, Sebastien Phan, Mark H. Ellisman, Stephen R. Adams
Publikováno v:
Journal of Cell Science.
Each mitochondrial compartment contains varying protein compositions that underlie a diversity of localized functions. Insights into the localization of mitochondrial intermembrane space-bridging (MIB) components will have an impact on our understand
Autor:
Mark H. Ellisman, Mira Sastri, John D. Scott, Susan S. Taylor, Mason R. Mackey, Michele E. Day, Guido M. Gaietta, Antonius Koller, Guy Perkins
Publikováno v:
The Journal of Cell Biology
PKA RIα subunit is localized to MVBs by the A-kinase–anchoring protein AKAP11 when disassociated from the PKA catalytic subunit.
Although RII protein kinase A (PKA) regulatory subunits are constitutively localized to discrete cellular compart
Although RII protein kinase A (PKA) regulatory subunits are constitutively localized to discrete cellular compart
Autor:
Mira Sastri, Matthias J. Knape, Friedrich W. Herberg, Charles C. King, Malik M. Keshwani, Ping Zhang, Susan S. Taylor, Lalima G. Ahuja
Publikováno v:
PLoS Biology, Vol 13, Iss 7, p e1002192 (2015)
PLoS Biology
PLoS Biology
To provide tight spatiotemporal signaling control, the cyclic adenosine monophosphate (cAMP)-dependent protein kinase (PKA) holoenzyme typically nucleates a macromolecular complex or a “PKA signalosome.” Using the RIIβ holoenzyme as a prototype,
Publikováno v:
Proceedings of the National Academy of Sciences. 102:349-354
The genetic variability and covalent modifications associated with the amino terminus of the protein kinase A (PKA) catalytic (C) subunit suggest that it may contribute to protein–protein interactions and/or localization. By using a yeast two-hybri
Publikováno v:
Journal of Molecular Biology. 307:1035-1047
The three-dimensional crystal structure of the empty capsid of Physalis mottle tymovirus has been determined to 3.2 A resolution. The empty capsids crystallized in the space group P1, leading to 60-fold non-crystallographic redundancy. The known stru
Autor:
C. N. Hiremath, Handanahal S. Savithri, Sanjay Krishna, S. K. Munshi, Mathur R. N. Murthy, D. Prahadeeswaran, Mira Sastri
Publikováno v:
Journal of Molecular Biology. 289:919-934
The structure of the T=3 single stranded RNA tymovirus, physalis mottle virus (PhMV), has been determined to 3.8\AA resolution. PhMV crystals belong to the rhombohedral space group R 3, with one icosahedral particle in the unit cell leading to 20-fol