Year |
Citation |
Score |
2010 |
Takenoya M, Nikolakakis K, Sagermann M. Crystallographic insights into the pore structures and mechanisms of the EutL and EutM shell proteins of the ethanolamine-utilizing microcompartment of Escherichia coli. Journal of Bacteriology. 192: 6056-63. PMID 20851901 DOI: 10.1128/Jb.00652-10 |
0.356 |
|
2009 |
Chapleau RR, Sagermann M. Real-time in vivo imaging of mercury uptake in Caenorhabditis elegans through the foodchain. Toxicology. 261: 136-42. PMID 19460414 DOI: 10.1016/J.Tox.2009.05.005 |
0.63 |
|
2009 |
Sagermann M, Ohtaki A, Nikolakakis K. Crystal structure of the EutL shell protein of the ethanolamine ammonia lyase microcompartment. Proceedings of the National Academy of Sciences of the United States of America. 106: 8883-7. PMID 19451619 DOI: 10.1073/Pnas.0902324106 |
0.347 |
|
2009 |
Nikolakakis K, Ohtaki A, Newton K, Chworos A, Sagermann M. Preliminary structural investigations of the Eut-L shell protein of the ethanolamine ammonia-lyase metabolosome of Escherichia coli Acta Crystallographica Section F: Structural Biology and Crystallization Communications. 65: 128-132. PMID 19194002 DOI: 10.1107/S1744309108042127 |
0.342 |
|
2009 |
Sagermann M, Chapleau RR, DeLorimier E, Lei M. Using affinity chromatography to engineer and characterize pH-dependent protein switches. Protein Science : a Publication of the Protein Society. 18: 217-28. PMID 19177365 DOI: 10.1002/Pro.23 |
0.677 |
|
2008 |
Chapleau RR, Blomberg R, Ford PC, Sagermann M. Design of a highly specific and noninvasive biosensor suitable for real-time in vivo imaging of mercury (II) uptake. Protein Science : a Publication of the Protein Society. 17: 614-22. PMID 18305194 DOI: 10.1110/Ps.073358908 |
0.664 |
|
2006 |
Sagermann M, Baase WA, Matthews BW. Sequential reorganization of beta-sheet topology by insertion of a single strand. Protein Science : a Publication of the Protein Society. 15: 1085-92. PMID 16597830 DOI: 10.1110/Ps.052018006 |
0.555 |
|
2004 |
Sagermann M, Baase WA, Mooers BH, Gay L, Matthews BW. Relocation or duplication of the helix A sequence of T4 lysozyme causes only modest changes in structure but can increase or decrease the rate of folding. Biochemistry. 43: 1296-301. PMID 14756565 DOI: 10.1021/Bi035702Q |
0.68 |
|
2003 |
Sagermann M, Gay L, Matthews BW. Long-distance conformational changes in a protein engineered by modulated sequence duplication. Proceedings of the National Academy of Sciences of the United States of America. 100: 9191-5. PMID 12869697 DOI: 10.1073/Pnas.1633549100 |
0.584 |
|
2002 |
Sagermann M, Matthews BW. Crystal structures of a T4-lysozyme duplication-extension mutant demonstrate that the highly conserved beta-sheet region has low intrinsic folding propensity. Journal of Molecular Biology. 316: 931-40. PMID 11884133 DOI: 10.1006/Jmbi.2001.5376 |
0.603 |
|
2002 |
Sagermann M, Mårtensson LG, Baase WA, Matthews BW. A test of proposed rules for helix capping: implications for protein design. Protein Science : a Publication of the Protein Society. 11: 516-21. PMID 11847274 DOI: 10.1110/Ps.39802 |
0.613 |
|
2001 |
Sagermann M, Stevens TH, Matthews BW. Crystal structure of the regulatory subunit H of the V-type ATPase of Saccharomyces cerevisiae. Proceedings of the National Academy of Sciences of the United States of America. 98: 7134-9. PMID 11416198 DOI: 10.1073/Pnas.131192798 |
0.515 |
|
2000 |
Sagermann M, Matthews BW. Cloning, expression and crystallization of VMA13p, an essential subunit of the vacuolar H+-ATPase of Saccharomyces cerevisiae. Acta Crystallographica. Section D, Biological Crystallography. 56: 475-7. PMID 10739925 DOI: 10.1107/S0907444900000950 |
0.538 |
|
1999 |
Sagermann M, Baase WA, Matthews BW. Structural characterization of an engineered tandem repeat contrasts the importance of context and sequence in protein folding. Proceedings of the National Academy of Sciences of the United States of America. 96: 6078-83. PMID 10339544 DOI: 10.1073/Pnas.96.11.6078 |
0.642 |
|
1997 |
Grüber G, Hausrath A, Sagermann M, Capaldi RA. An improved purification of ECF1 and ECF1F0 by using a cytochrome bo- deficient strain of Escherichia coli facilitates crystallization of these complexes Febs Letters. 410: 165-168. PMID 9237622 DOI: 10.1016/S0014-5793(97)00528-0 |
0.622 |
|
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