Year |
Citation |
Score |
2015 |
Reading E, Walton TA, Liko I, Marty MT, Laganowsky A, Rees DC, Robinson CV. The Effect of Detergent, Temperature, and Lipid on the Oligomeric State of MscL Constructs: Insights from Mass Spectrometry. Chemistry & Biology. 22: 593-603. PMID 26000747 DOI: 10.1016/J.Chembiol.2015.04.016 |
0.497 |
|
2015 |
Walton TA, Idigo CA, Herrera N, Rees DC. MscL: channeling membrane tension. PflüGers Archiv : European Journal of Physiology. 467: 15-25. PMID 24859800 DOI: 10.1007/S00424-014-1535-X |
0.48 |
|
2013 |
Walton TA, Rees DC. Structure and stability of the C-terminal helical bundle of the E. coli mechanosensitive channel of large conductance. Protein Science : a Publication of the Protein Society. 22: 1592-601. PMID 24038743 DOI: 10.1002/Pro.2360 |
0.515 |
|
2011 |
Gandhi CS, Walton TA, Rees DC. OCAM: a new tool for studying the oligomeric diversity of MscL channels. Protein Science : a Publication of the Protein Society. 20: 313-26. PMID 21280123 DOI: 10.1002/Pro.562 |
0.38 |
|
2010 |
Liu Z, Walton TA, Rees DC. A reported archaeal mechanosensitive channel is a structural homolog of MarR-like transcriptional regulators. Protein Science : a Publication of the Protein Society. 19: 808-14. PMID 20162616 DOI: 10.1002/Pro.360 |
0.386 |
|
2010 |
Gandhi CS, Walton TA, Rees DC. A Combined Spectroscopic and Biochemical Approach to Counting MscL Subunits Biophysical Journal. 98: 327a. DOI: 10.1016/J.Bpj.2009.12.1772 |
0.53 |
|
2009 |
Walton TA, Sandoval CM, Fowler CA, Pardi A, Sousa MC. The cavity-chaperone Skp protects its substrate from aggregation but allows independent folding of substrate domains. Proceedings of the National Academy of Sciences of the United States of America. 106: 1772-7. PMID 19181847 DOI: 10.1073/Pnas.0809275106 |
0.643 |
|
2008 |
Gatzeva-Topalova PZ, Walton TA, Sousa MC. Crystal structure of YaeT: conformational flexibility and substrate recognition. Structure (London, England : 1993). 16: 1873-81. PMID 19081063 DOI: 10.1016/J.Str.2008.09.014 |
0.506 |
|
2004 |
Walton TA, Sousa MC. Crystal structure of Skp, a prefoldin-like chaperone that protects soluble and membrane proteins from aggregation. Molecular Cell. 15: 367-74. PMID 15304217 DOI: 10.1016/J.Molcel.2004.07.023 |
0.719 |
|
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