Year |
Citation |
Score |
2017 |
Hausrath AC, Kingston RL. Conditionally disordered proteins: bringing the environment back into the fold. Cellular and Molecular Life Sciences : Cmls. PMID 28597298 DOI: 10.1007/S00018-017-2558-1 |
0.574 |
|
2004 |
Dyer CM, Quillin ML, Campos A, Lu J, McEvoy MM, Hausrath AC, Westbrook EM, Matsumura P, Matthews BW, Dahlquist FW. Structure of the constitutively active double mutant CheYD13K Y106W alone and in complex with a FliM peptide. Journal of Molecular Biology. 342: 1325-35. PMID 15351654 DOI: 10.1016/J.Jmb.2004.07.084 |
0.538 |
|
2002 |
Hausrath AC, Matthews BW. Thermolysin in the absence of substrate has an open conformation. Acta Crystallographica. Section D, Biological Crystallography. 58: 1002-7. PMID 12037302 DOI: 10.1107/S090744490200584X |
0.577 |
|
2001 |
Hausrath AC, Capaldi RA, Matthews BW. The conformation of the epsilon- and gamma-subunits within the Escherichia coli F(1) ATPase. The Journal of Biological Chemistry. 276: 47227-32. PMID 11585832 DOI: 10.1074/Jbc.M107536200 |
0.503 |
|
1999 |
Hausrath AC, Grüber G, Matthews BW, Capaldi RA. Structural features of the gamma subunit of the Escherichia coli F(1) ATPase revealed by a 4.4-A resolution map obtained by x-ray crystallography. Proceedings of the National Academy of Sciences of the United States of America. 96: 13697-702. PMID 10570135 DOI: 10.1073/Pnas.96.24.13697 |
0.513 |
|
1999 |
Gassner NC, Baase WA, Hausrath AC, Matthews BW. Substitution with selenomethionine can enhance the stability of methionine-rich proteins. Journal of Molecular Biology. 294: 17-20. PMID 10556025 DOI: 10.1006/Jmbi.1999.3220 |
0.514 |
|
1998 |
McEvoy MM, Hausrath AC, Randolph GB, Remington SJ, Dahlquist FW. Two binding modes reveal flexibility in kinase/response regulator interactions in the bacterial chemotaxis pathway. Proceedings of the National Academy of Sciences of the United States of America. 95: 7333-8. PMID 9636149 DOI: 10.1073/Pnas.95.13.7333 |
0.554 |
|
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 |
0.581 |
|
1995 |
Holland DR, Hausrath AC, Juers D, Matthews BW. Structural analysis of zinc substitutions in the active site of thermolysin. Protein Science : a Publication of the Protein Society. 4: 1955-65. PMID 8535232 DOI: 10.1002/Pro.5560041001 |
0.612 |
|
1994 |
Hausrath AC, Matthews BW. Redetermination and refinement of the complex of benzylsuccinic acid with thermolysin and its relation to the complex with carboxypeptidase A. The Journal of Biological Chemistry. 269: 18839-42. PMID 8034637 DOI: 10.2210/Pdb1Hyt/Pdb |
0.476 |
|
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