| Year |
Citation |
Score |
| 2014 |
McDowell GS, Gunsalus KT, MacKellar DC, Mazzilli SA, Pai VP, Goodwin PR, Walsh EM, Robinson-Mosher A, Bowman TA, Kraemer J, Erb ML, Schoenfeld E, Shokri L, Jackson JD, Islam A, ... ... Krukenberg KA, et al. Shaping the Future of Research: a perspective from junior scientists. F1000research. 3: 291. PMID 25653845 DOI: 10.12688/F1000Research.5878.2 |
0.636 |
|
| 2014 |
Polka JK, Krukenberg KA. Making science a desirable career. Science (New York, N.Y.). 346: 1422. PMID 25504725 DOI: 10.1126/Science.346.6215.1422 |
0.315 |
|
| 2014 |
McDowell GS, Krukenberg K, Polka J. The Future of Research Symposium: Facilitating Postdoctoral Involvement in the Future of Science Postdoc Journal. DOI: 10.14304/Surya.Jpr.V2N9.9 |
0.307 |
|
| 2012 |
Schneidman-Duhovny D, Rossi A, Avila-Sakar A, Kim SJ, Velázquez-Muriel J, Strop P, Liang H, Krukenberg KA, Liao M, Kim HM, Sobhanifar S, Dötsch V, Rajpal A, Pons J, Agard DA, et al. A method for integrative structure determination of protein-protein complexes. Bioinformatics (Oxford, England). 28: 3282-9. PMID 23093611 DOI: 10.1093/Bioinformatics/Bts628 |
0.483 |
|
| 2012 |
Tan ES, Krukenberg KA, Mitchison TJ. Large-scale preparation and characterization of poly(ADP-ribose) and defined length polymers. Analytical Biochemistry. 428: 126-36. PMID 22743307 DOI: 10.1016/J.Ab.2012.06.015 |
0.328 |
|
| 2012 |
Cunningham CN, Southworth DR, Krukenberg KA, Agard DA. The conserved arginine 380 of Hsp90 is not a catalytic residue, but stabilizes the closed conformation required for ATP hydrolysis. Protein Science : a Publication of the Protein Society. 21: 1162-71. PMID 22653663 DOI: 10.1002/Pro.2103 |
0.715 |
|
| 2011 |
Krukenberg KA, Street TO, Lavery LA, Agard DA. Conformational dynamics of the molecular chaperone Hsp90. Quarterly Reviews of Biophysics. 44: 229-55. PMID 21414251 DOI: 10.1017/S0033583510000314 |
0.703 |
|
| 2010 |
Street TO, Krukenberg KA, Rosgen J, Bolen DW, Agard DA. Osmolyte-induced conformational changes in the Hsp90 molecular chaperone. Protein Science : a Publication of the Protein Society. 19: 57-65. PMID 19890989 DOI: 10.1002/Pro.282 |
0.642 |
|
| 2009 |
Krukenberg KA, Böttcher UM, Southworth DR, Agard DA. Grp94, the endoplasmic reticulum Hsp90, has a similar solution conformation to cytosolic Hsp90 in the absence of nucleotide. Protein Science : a Publication of the Protein Society. 18: 1815-27. PMID 19554567 DOI: 10.1002/Pro.191 |
0.643 |
|
| 2009 |
Krukenberg KA, Southworth DR, Street TO, Agard DA. pH-dependent conformational changes in bacterial Hsp90 reveal a Grp94-like conformation at pH 6 that is highly active in suppression of citrate synthase aggregation. Journal of Molecular Biology. 390: 278-91. PMID 19427321 DOI: 10.1016/J.Jmb.2009.04.080 |
0.63 |
|
| 2008 |
Förster F, Webb B, Krukenberg KA, Tsuruta H, Agard DA, Sali A. Integration of small-angle X-ray scattering data into structural modeling of proteins and their assemblies. Journal of Molecular Biology. 382: 1089-106. PMID 18694757 DOI: 10.1016/J.Jmb.2008.07.074 |
0.543 |
|
| 2008 |
Cunningham CN, Krukenberg KA, Agard DA. Intra- and intermonomer interactions are required to synergistically facilitate ATP hydrolysis in Hsp90. The Journal of Biological Chemistry. 283: 21170-8. PMID 18492664 DOI: 10.1074/Jbc.M800046200 |
0.705 |
|
| 2008 |
Krukenberg KA, Förster F, Rice LM, Sali A, Agard DA. Multiple conformations of E. coli Hsp90 in solution: insights into the conformational dynamics of Hsp90. Structure (London, England : 1993). 16: 755-65. PMID 18462680 DOI: 10.1016/J.Str.2008.01.021 |
0.714 |
|
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