Yuko Tsutsui
Research Scientist in Pharmacology
Research & Publications
Biography
News
Coauthors
Selected Publications
- Biochemical and structural basis for differential inhibitor sensitivity of EGFR with distinct exon 19 mutationsvan Alderwerelt van Rosenburgh I, Lu D, Grant M, Stayrook S, Phadke M, Walther Z, Goldberg S, Politi K, Lemmon M, Ashtekar K, Tsutsui Y. Biochemical and structural basis for differential inhibitor sensitivity of EGFR with distinct exon 19 mutations. Nature Communications 2022, 13: 6791. PMID: 36357385, PMCID: PMC9649653, DOI: 10.1038/s41467-022-34398-z.
- Structural basis for ligand reception by anaplastic lymphoma kinaseLi T, Stayrook SE, Tsutsui Y, Zhang J, Wang Y, Li H, Proffitt A, Krimmer SG, Ahmed M, Belliveau O, Walker IX, Mudumbi KC, Suzuki Y, Lax I, Alvarado D, Lemmon MA, Schlessinger J, Klein DE. Structural basis for ligand reception by anaplastic lymphoma kinase. Nature 2021, 600: 148-152. PMID: 34819665, PMCID: PMC8639777, DOI: 10.1038/s41586-021-04141-7.
- Structural Insights into Pseudokinase Domains of Receptor Tyrosine KinasesSheetz J, Mathea S, Karvonen H, Malhotra K, Chatterjee D, Niininen W, Perttila R, Preuss F, Suresh K, Stayrook S, Tsutsui Y, Radhakrishnan R, Ungureanu D, Knapp S, Lemmon M. Structural Insights into Pseudokinase Domains of Receptor Tyrosine Kinases. The FASEB Journal 2021, 35 DOI: 10.1096/fasebj.2021.35.s1.02446.
- Imatinib Binding to Human c-Src is Coupled to Inter-Domain Allostery and Suggest a Novel Kinase Inhibition StrategyTsutsui Y, Deredge D, Wintrode P, Hays F. Imatinib Binding to Human c-Src is Coupled to Inter-Domain Allostery and Suggest a Novel Kinase Inhibition Strategy. Biophysical Journal 2017, 112: 63a. DOI: 10.1016/j.bpj.2016.11.381.
- Imatinib binding to human c-Src is coupled to inter-domain allostery and suggests a novel kinase inhibition strategyTsutsui Y, Deredge D, Wintrode P, Hays F. Imatinib binding to human c-Src is coupled to inter-domain allostery and suggests a novel kinase inhibition strategy. Scientific Reports 2016, 6: 30832. PMID: 27480221, PMCID: PMC4969603, DOI: 10.1038/srep30832.
- Conformation-Dependent Human p52Shc Phosphorylation by Human c‑SrcTsutsui Y, Johnson J, Demeler B, Kinter M, Hays F. Conformation-Dependent Human p52Shc Phosphorylation by Human c‑Src. Biochemistry 2015, 54: 3469-3482. PMID: 25961473, DOI: 10.1021/acs.biochem.5b00122.
- Overproduction and biophysical characterization of human HSP70 proteinsBoswell-Casteel R, Johnson J, Duggan K, Tsutsui Y, Hays F. Overproduction and biophysical characterization of human HSP70 proteins. Protein Expression And Purification 2014, 106: 57-65. PMID: 25266791, PMCID: PMC4248018, DOI: 10.1016/j.pep.2014.09.013.
- Human p52Shc Conformational Bias and Localization in c-SRC ActivationTsutsui Y, Hays F. Human p52Shc Conformational Bias and Localization in c-SRC Activation. Biophysical Journal 2014, 106: 466a-467a. DOI: 10.1016/j.bpj.2013.11.2642.
- Folding mechanism of the metastable serpin α1-antitrypsinTsutsui Y, Dela Cruz R, Wintrode P. Folding mechanism of the metastable serpin α1-antitrypsin. Proceedings Of The National Academy Of Sciences Of The United States Of America 2012, 109: 4467-4472. PMID: 22392975, PMCID: PMC3311335, DOI: 10.1073/pnas.1109125109.
- Chapter Fifteen Probing Serpin Conformational Change Using Mass Spectrometry and Related MethodsTsutsui Y, Sarkar A, Wintrode P. Chapter Fifteen Probing Serpin Conformational Change Using Mass Spectrometry and Related Methods. 2011, 501: 325-350. PMID: 22078541, PMCID: PMC3679668, DOI: 10.1016/b978-0-12-385950-1.00015-8.
- Local and Global Effects of a Cavity Filling Mutation in a Metastable SerpinSengupta T, Tsutsui Y, Wintrode P. Local and Global Effects of a Cavity Filling Mutation in a Metastable Serpin. Biochemistry 2009, 48: 8233-8240. PMID: 19624115, PMCID: PMC2746415, DOI: 10.1021/bi900342d.
- The Structural Basis of Serpin Polymerization Studied by Hydrogen/Deuterium Exchange and Mass Spectrometry*Tsutsui Y, Kuri B, Sengupta T, Wintrode P. The Structural Basis of Serpin Polymerization Studied by Hydrogen/Deuterium Exchange and Mass Spectrometry*. Journal Of Biological Chemistry 2008, 283: 30804-30811. PMID: 18794298, PMCID: PMC2576545, DOI: 10.1074/jbc.m804048200.
- Cooperative Unfolding of a Metastable Serpin to a Molten Globule Suggests a Link Between Functional and Folding Energy LandscapesTsutsui Y, Wintrode P. Cooperative Unfolding of a Metastable Serpin to a Molten Globule Suggests a Link Between Functional and Folding Energy Landscapes. Journal Of Molecular Biology 2007, 371: 245-255. PMID: 17568610, DOI: 10.1016/j.jmb.2007.05.039.
- Hydrogen/deuterium exchange-mass spectrometry: a powerful tool for probing protein structure, dynamics and interactions.Tsutsui Y, Wintrode P. Hydrogen/deuterium exchange-mass spectrometry: a powerful tool for probing protein structure, dynamics and interactions. Current Medicinal Chemistry 2007, 14: 2344-58. PMID: 17896983, DOI: 10.2174/092986707781745596.
- The Conformational Dynamics of a Metastable Serpin Studied by Hydrogen Exchange and Mass SpectrometryTsutsui Y, Liu L, Gershenson A, Wintrode P. The Conformational Dynamics of a Metastable Serpin Studied by Hydrogen Exchange and Mass Spectrometry. Biochemistry 2006, 45: 6561-6569. PMID: 16716066, DOI: 10.1021/bi060431f.