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Your search keyword '"Smerdon, S.J."' showing total 35 results
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35 results on '"Smerdon, S.J."'

1. A unified polymerase mechanism for nonhomologous DNA and RNA polymerases

Author

Steitz, T.A., Smerdon, S.J., Jager, J., Joyce, C.M., and Pelletier, H.

Subjects
Biochemical genetics -- Research, DNA polymerases -- Research, Science and technology, Research
Abstract

Extrapolating from the co-crystal structure of rat DNA polymerase β pol β) complexed with primer-template, dideoxycytidine triphosphate (DDCTP), and two metal ions, H. Pelletier et al. (1) recently concluded that [...]

Published
1994

2. Structural basis of asymmetry in the human immunodeficiency virus type 1 reverse transcriptase heterodimer

Author

Wang, J., Smerdon, S.J., Jager, J., Kohlstaedt, L.A., Rice, P.A., Friedman, J.M., and Steitz, T.A.

Subjects
Reverse transcriptase -- Research, HIV (Viruses) -- Genetic aspects, Science and technology
Abstract

The structure of HIV-1 reverse transcriptase reveals a peculiar aspect of polymerase domain, assuming a different structure in the two subunits p51 and p66. However, it has the same polypeptide chain sequence as other transcriptases. The two subunits interact to produce one polymerase cleft that binds primer-template.

Published
1994

9. PIH1D1 N-terminal domain

Author

Smerdon, S.J., primary, Boulton, S.J., additional, Stach, L., additional, Flower, T.G., additional, and Horejsi, Z., additional

Published
2014
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11. Human Mob1-phosphopeptide complex

Author

Stach, L., primary, Ogrodowicz, R.W., additional, Rock, J.M., additional, Lim, D., additional, Yaffe, M.B., additional, Amon, A., additional, and Smerdon, S.J., additional

Published
2013
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21. crystal structure of the rpr of pcf11

Author

Noble, C.G., primary, Hollingworth, D., additional, Martin, S.R., additional, Adeniran, V.E., additional, Smerdon, S.J., additional, Kelly, G., additional, Taylor, I.A., additional, and Ramos, A., additional

Published
2005
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27. 14-3-3 ZETA/PHOSPHOPEPTIDE COMPLEX

Author

Yaffe, M.B., primary, Rittinger, K., additional, Volinia, S., additional, Caron, P.R., additional, Aitken, A., additional, Leffers, H., additional, Gamblin, S.J., additional, Smerdon, S.J., additional, and Cantley, L.C., additional

Published
1999
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34. NF-κB1 p105 Negatively Regulates TPL-2 MEK Kinase Activity.

Author

Beinke, S., Deka, J., Lang, V., Belich, M.P., Walker, P.A., Howell, S., Smerdon, S.J., Gamblin, S.J., and Ley, S.C.

Subjects
CARCINOGENS, GENETIC mutation
Abstract

Activation of the oncogenic potential of the MEK kinase TPL-2 (Cot) requires deletion of its C terminus. This mutation also weakens the interaction of TPL-2 with NF-κB1 p105 in vitro, although it is unclear whether this is important for the activation of TPL-2 oncogenicity. It is demonstrated here that TPL-2 stability in vivo relies on its high-affinity, stoichiometric association with NF-κB1 p105. Formation of this complex occurs as a result of two distinct interactions. The TPL-2 C terminus binds to a region encompassing residues 497 to 534 of p105, whereas the TPL-2 kinase domain interacts with the p105 death domain. Binding to the p105 death domain inhibits TPL-2 MEK kinase activity in vitro, and this inhibition is significantly augmented by concomitant interaction of the TPL-2 C terminus with p105. In cotransfected cells, both interactions are required for inhibition of TPL-2 MEK kinase activity and, consequently, the catalytic activity of a C-terminally truncated oncogenic mutant of TPL-2 is not affected by p105. Thus, in addition to its role as a precursor for p50 and cytoplasmic inhibitor of NF-κB, p105 is a negative regulator of TPL-2. Insensitivity of C-terminally truncated TPL-2 to this regulatory mechanism is likely to contribute to its ability to transform cells. [ABSTRACT FROM AUTHOR]

Published
2003
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35. The structural basis of Arfaptin-mediated cross-talk between Rac and Arf signalling pathways.

Author

Tarricone, C., Xiao, B., Justin, N., Walker, P.A., Rittinger, K., Gamblin, S.J., and Smerdon, S.J.

Subjects
PROTEIN binding, G proteins, GUANOSINE triphosphatase, BIOCHEMICAL mechanism of action
Abstract

Focuses on a study which examined the role of the cross-talk between small-G protein families in signaling. Mechanism of Arfaptin (Arf) binding to guanosine triphosphate (GTP)-bound Arf1 and Arf6; Significance of the coordinated action of Arf and Rho family GTPases in cellular processes; X-ray structures of Arfaptin; Differences between the molecular mechanisms of Rho and Ras family signaling.

Published
2001
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