This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. The seven mammalian isoforms of 14-3-3 family of proteins play diverse roles in intracellular signaling. Most 14-3-3 proteins form homodimers and mixed heterodimers between different isotypes, with overlapping roles in ligand binding. One mammalian isoform, 14-3-3 sigma, appears to play a unique role in the cellular response to DNA damage and in human oncogenesis. The biological and structural basis for these 14-3-3 sigma-specific functions is unknown. To understand the basis for preferential homodimerization of 14-3-3 sigma and to shed light on mechanisms of its unique functional specificity we have conducted biochemical and structural studies on the sigma isoform. The paper on this work was published in J. Biol. Chem.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
3P41RR015301-05S1
Application #
7369490
Study Section
Special Emphasis Panel (ZRG1)
Project Start
2005-06-01
Project End
2007-05-31
Budget Start
2005-06-01
Budget End
2007-05-31
Support Year
5
Fiscal Year
2006
Total Cost
$1,331
Indirect Cost
Name
Cornell University
Department
Chemistry
Type
Schools of Arts and Sciences
DUNS #
872612445
City
Ithaca
State
NY
Country
United States
Zip Code
14850
Chen, Wenyang; Mandali, Sridhar; Hancock, Stephen P et al. (2018) Multiple serine transposase dimers assemble the transposon-end synaptic complex during IS607-family transposition. Elife 7:
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Uppalapati, Maruti; Lee, Dong Jun; Mandal, Kalyaneswar et al. (2016) A Potent d-Protein Antagonist of VEGF-A is Nonimmunogenic, Metabolically Stable, and Longer-Circulating in Vivo. ACS Chem Biol 11:1058-65
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