Kristof Nolan
Affiliations: | 2011-2016 | Molecular Genetics, Biochemistry and Microbiology | University of Cincinnati, Cincinnati, OH |
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Parents
Sign in to add mentor| Thomas B. Thompson | grad student | 2011-2016 | University of Cincinnati | |
| (Thesis:Structure function of DAN family BMP inhibitors) | ||||
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Publications
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| Gipson GR, Nolan K, Kattamuri C, et al. (2023) Formation and characterization of BMP2/GDF5 and BMP4/GDF5 heterodimers. Bmc Biology. 21: 16 |
| Kattamuri C, Nolan K, Thompson TB. (2017) Correction: Analysis and identification of the Grem2 heparin/heparan sulfate-binding motif. The Biochemical Journal. 474: 1529 |
| Bylund J, Awgulewitsch CP, Trinh LT, et al. (2017) Coordinated proliferation and differentiation of human iPS cell-derived cardiac progenitor cells depends on BMP signaling regulation by Gremlin 2. Stem Cells and Development |
| Kattamuri C, Nolan K, Thompson TB. (2017) Analysis and identification of the Grem2 heparin/heparan-sulfate binding motif. The Biochemical Journal |
| Nolan K, Kattamuri C, Rankin SA, et al. (2016) Structure of Gremlin-2 in Complex with GDF5 Gives Insight into DAN-Family-Mediated BMP Antagonism. Cell Reports |
| Sanders LN, Schoenhard JA, Saleh MA, et al. (2016) The BMP Antagonist Gremlin 2 Limits Inflammation After Myocardial Infarction. Circulation Research |
| Nolan K, Kattamuri C, Luedeke DM, et al. (2015) Structure of neuroblastoma suppressor of tumorigenicity 1 (NBL1): insights for the functional variability across bone morphogenetic protein (BMP) antagonists. The Journal of Biological Chemistry. 290: 4759-71 |
| Nolan K, Thompson TB. (2014) The DAN family: modulators of TGF-β signaling and beyond. Protein Science : a Publication of the Protein Society. 23: 999-1012 |
| Nolan K, Kattamuri C, Luedeke DM, et al. (2013) Structure of protein related to Dan and Cerberus: insights into the mechanism of bone morphogenetic protein antagonism. Structure (London, England : 1993). 21: 1417-29 |
| Kattamuri C, Luedeke DM, Nolan K, et al. (2012) Members of the DAN family are BMP antagonists that form highly stable noncovalent dimers. Journal of Molecular Biology. 424: 313-27 |