Year |
Citation |
Score |
2020 |
Davey JA, Wilson CJ. Engineered signal-coupled inducible promoters: measuring the apparent RNA-polymerase resource budget. Nucleic Acids Research. PMID 32890400 DOI: 10.1093/Nar/Gkaa734 |
0.302 |
|
2020 |
Herde ZD, Short AE, Kay VE, Huang BD, Realff MJ, Wilson CJ. Engineering allosteric communication. Current Opinion in Structural Biology. 63: 115-122. PMID 32575020 DOI: 10.1016/J.Sbi.2020.05.004 |
0.344 |
|
2019 |
Rondon RE, Groseclose TM, Short AE, Wilson CJ. Transcriptional programming using engineered systems of transcription factors and genetic architectures. Nature Communications. 10: 4784. PMID 31636266 DOI: 10.1038/S41467-019-12706-4 |
0.309 |
|
2019 |
Rondon RE, Wilson CJ. Engineering a New Class of Anti-LacI Transcription Factors with Alternate DNA Recognition. Acs Synthetic Biology. PMID 30601657 DOI: 10.1021/Acssynbio.8B00324 |
0.333 |
|
2018 |
Wilson CJ, Bommarius AS, Champion JA, Chernoff YO, Lynn DG, Paravastu AK, Liang C, Hsieh MC, Heemstra JM. Biomolecular Assemblies: Moving from Observation to Predictive Design. Chemical Reviews. PMID 30281290 DOI: 10.1021/Acs.Chemrev.8B00038 |
0.326 |
|
2017 |
Davey JA, Wilson CJ. Deconstruction of complex protein signaling switches: a roadmap toward engineering higher-order gene regulators. Wiley Interdisciplinary Reviews. Nanomedicine and Nanobiotechnology. PMID 28185424 DOI: 10.1002/Wnan.1461 |
0.412 |
|
2016 |
Richards DH, Meyer S, Wilson CJ. 14 Ways to Re-route Cooperative Communication in the Lactose Repressor: Engineering Regulatory Proteins with Alternate Repressive Functions. Acs Synthetic Biology. PMID 27598336 DOI: 10.1021/Acssynbio.6B00048 |
0.331 |
|
2015 |
Choe JK, Richards DH, Wilson CJ, Mitch WA. Degradation of Amino Acids and Structure in Model Proteins and Bacteriophage MS2 by Chlorine, Bromine, and Ozone. Environmental Science & Technology. PMID 26488608 DOI: 10.1021/Acs.Est.5B03813 |
0.358 |
|
2015 |
Howell SC, Richards DH, Mitch WA, Wilson CJ. Leveraging the Mechanism of Oxidative Decay for Adenylate Kinase to Design Structural and Functional Resistances. Acs Chemical Biology. PMID 26266833 DOI: 10.1021/Acschembio.5B00431 |
0.362 |
|
2015 |
Wilson CJ. Rational protein design: developing next-generation biological therapeutics and nanobiotechnological tools. Wiley Interdisciplinary Reviews. Nanomedicine and Nanobiotechnology. 7: 330-41. PMID 25348497 DOI: 10.1002/Wnan.1310 |
0.397 |
|
2015 |
Wilson CJ. Understanding Enzyme Molecular Evolution toward Thermal Adaptation using Multistate Computational Protein Design Biophysical Journal. 108: 33a. DOI: 10.1016/J.Bpj.2014.11.209 |
0.332 |
|
2014 |
Tobin PH, Richards DH, Callender RA, Wilson CJ. Protein engineering: a new frontier for biological therapeutics. Current Drug Metabolism. 15: 743-56. PMID 25495737 DOI: 10.2174/1389200216666141208151524 |
0.305 |
|
2014 |
Tobin PH, Wilson CJ. Examining photoinduced energy transfer in Pseudomonas aeruginosa azurin. Journal of the American Chemical Society. 136: 1793-802. PMID 24467236 DOI: 10.1021/Ja412308R |
0.305 |
|
2014 |
Howell SC, Inampudi KK, Bean DP, Wilson CJ. Understanding thermal adaptation of enzymes through the multistate rational design and stability prediction of 100 adenylate kinases. Structure (London, England : 1993). 22: 218-29. PMID 24361272 DOI: 10.1016/J.Str.2013.10.019 |
0.316 |
|
2013 |
Meyer S, Ramot R, Kishore Inampudi K, Luo B, Lin C, Amere S, Wilson CJ. Engineering alternate cooperative-communications in the lactose repressor protein scaffold. Protein Engineering, Design & Selection : Peds. 26: 433-43. PMID 23587523 DOI: 10.1093/Protein/Gzt013 |
0.352 |
|
2013 |
Sivey JD, Howell SC, Bean DJ, McCurry DL, Mitch WA, Wilson CJ. Role of lysine during protein modification by HOCl and HOBr: halogen-transfer agent or sacrificial antioxidant? Biochemistry. 52: 1260-71. PMID 23327477 DOI: 10.1021/Bi301523S |
0.383 |
|
2012 |
Ramot R, Kishore Inampudi K, Wilson CJ. Lactose repressor experimental folding landscape: fundamental functional unit and tetramer folding mechanisms. Biochemistry. 51: 7569-79. PMID 22931511 DOI: 10.1021/Bi300545F |
0.404 |
|
2010 |
Miller C, Davlieva M, Wilson C, White KI, Couñago R, Wu G, Myers JC, Wittung-Stafshede P, Shamoo Y. Experimental evolution of adenylate kinase reveals contrasting strategies toward protein thermostability. Biophysical Journal. 99: 887-96. PMID 20682267 DOI: 10.1016/J.Bpj.2010.04.076 |
0.364 |
|
2008 |
Couñago R, Wilson CJ, Peña MI, Wittung-Stafshede P, Shamoo Y. An adaptive mutation in adenylate kinase that increases organismal fitness is linked to stability-activity trade-offs. Protein Engineering, Design & Selection : Peds. 21: 19-27. PMID 18093993 DOI: 10.1093/Protein/Gzm072 |
0.36 |
|
2007 |
Zong C, Wilson CJ, Shen T, Wittung-Stafshede P, Mayo SL, Wolynes PG. Establishing the entatic state in folding metallated Pseudomonas aeruginosa azurin. Proceedings of the National Academy of Sciences of the United States of America. 104: 3159-64. PMID 17301232 DOI: 10.1073/Pnas.0611149104 |
0.35 |
|
2007 |
Wilson CJ, Zhan H, Swint-Kruse L, Matthews KS. The lactose repressor system: paradigms for regulation, allosteric behavior and protein folding. Cellular and Molecular Life Sciences : Cmls. 64: 3-16. PMID 17103112 DOI: 10.1007/S00018-006-6296-Z |
0.624 |
|
2007 |
Wilson CJ, Zhan H, Swint-Kruse L, Matthews KS. Ligand interactions with lactose repressor protein and the repressor-operator complex: the effects of ionization and oligomerization on binding. Biophysical Chemistry. 126: 94-105. PMID 16860458 DOI: 10.1016/J.Bpc.2006.06.005 |
0.606 |
|
2006 |
Chen M, Wilson CJ, Wu Y, Wittung-Stafshede P, Ma J. Correlation between protein stability cores and protein folding kinetics: a case study on Pseudomonas aeruginosa apo-azurin. Structure (London, England : 1993). 14: 1401-10. PMID 16962971 DOI: 10.1016/J.Str.2006.07.007 |
0.432 |
|
2006 |
Zong C, Wilson CJ, Shen T, Wolynes PG, Wittung-Stafshede P. Phi-value analysis of apo-azurin folding: comparison between experiment and theory. Biochemistry. 45: 6458-66. PMID 16700556 DOI: 10.1021/Bi060025W |
0.351 |
|
2005 |
Wilson CJ, Das P, Clementi C, Matthews KS, Wittung-Stafshede P. The experimental folding landscape of monomeric lactose repressor, a large two-domain protein, involves two kinetic intermediates. Proceedings of the National Academy of Sciences of the United States of America. 102: 14563-8. PMID 16203983 DOI: 10.1073/Pnas.0505808102 |
0.595 |
|
2005 |
Das P, Wilson CJ, Fossati G, Wittung-Stafshede P, Matthews KS, Clementi C. Characterization of the folding landscape of monomeric lactose repressor: quantitative comparison of theory and experiment. Proceedings of the National Academy of Sciences of the United States of America. 102: 14569-74. PMID 16203982 DOI: 10.1073/Pnas.0505844102 |
0.586 |
|
2005 |
Wilson CJ, Wittung-Stafshede P. Snapshots of a dynamic folding nucleus in zinc-substituted Pseudomonas aeruginosa azurin. Biochemistry. 44: 10054-62. PMID 16042382 DOI: 10.1021/Bi050342N |
0.349 |
|
2005 |
Wilson CJ, Wittung-Stafshede P. Role of structural determinants in folding of the sandwich-like protein Pseudomonas aeruginosa azurin. Proceedings of the National Academy of Sciences of the United States of America. 102: 3984-7. PMID 15753320 DOI: 10.1073/Pnas.0501038102 |
0.41 |
|
2004 |
Wilson CJ, Apiyo D, Wittung-Stafshede P. Role of cofactors in metalloprotein folding. Quarterly Reviews of Biophysics. 37: 285-314. PMID 16194296 DOI: 10.1017/S003358350500404X |
0.396 |
|
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