2012
Folding mechanism of the metastable serpin α1-antitrypsin
Tsutsui 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.Peer-Reviewed Original Research
2011
Chapter Fifteen Probing Serpin Conformational Change Using Mass Spectrometry and Related Methods
Tsutsui Y, Sarkar A, Wintrode P. Chapter Fifteen Probing Serpin Conformational Change Using Mass Spectrometry and Related Methods. Methods In Enzymology 2011, 501: 325-350. PMID: 22078541, PMCID: PMC3679668, DOI: 10.1016/b978-0-12-385950-1.00015-8.Peer-Reviewed Original ResearchConceptsStructural mass spectrometry techniquesHydrogen/deuterium exchangeMass spectrometry techniquesDeuterium exchangeIon mobility mass spectrometrySpectrometry techniquesMass spectrometryMobility mass spectrometrySerpin polymersConformational flexibilitySerpin functionSerpin polymerizationChemical footprintingConformational changesThermodynamic metastabilitySpectrometryChapter FifteenSerpinsStructural distributionPolymerizationPolymersStabilityMisfoldingInhibitory mechanismFootprinting
2009
Local and Global Effects of a Cavity Filling Mutation in a Metastable Serpin
Sengupta 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.Peer-Reviewed Original Research
2008
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.Peer-Reviewed Original Research
2007
Cooperative Unfolding of a Metastable Serpin to a Molten Globule Suggests a Link Between Functional and Folding Energy Landscapes
Tsutsui 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.Peer-Reviewed Original ResearchConceptsMutagenesis studiesEquilibrium unfoldingMolten globuleCooperative structural unitDramatic conformational changeMultiple structural domainsNumerous mutagenesis studiesExchange mass spectrometryStable native stateNon-cooperative transitionPrevious mutagenesis studiesMolten globule formHydrogen-deuterium exchangeEquilibrium molten globuleFunctional intermediatesProtease-serpin complexesStructural domainsTarget proteasesConformational changesMetastable SerpinNative stateEquilibrium intermediatesCooperative unfoldingUnfolded stateGlobule form
2006
The Conformational Dynamics of a Metastable Serpin Studied by Hydrogen Exchange and Mass Spectrometry
Tsutsui 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.Peer-Reviewed Original Research