2012
Crystal Structure of a Proteolytic Fragment of ADAMTS13 Reveals Alternative Disulfide Pairings in the Cysteine-Rich Domain
Skipwith C, Stayrook S, Rottensteiner H, Scheiflinger F, Zheng X. Crystal Structure of a Proteolytic Fragment of ADAMTS13 Reveals Alternative Disulfide Pairings in the Cysteine-Rich Domain. Blood 2012, 120: 3363. DOI: 10.1182/blood.v120.21.3363.3363.Peer-Reviewed Original ResearchIntermolecular disulfide bondsSpacer domainExosite interactionsProteolytic fragmentsDisulfide bondsNon-catalytic domainStably transfected Chinese hamster ovary cellsCysteine-rich domainChinese hamster ovary cellsDisulfide pairing patternADAMTS13 spacer domainHamster ovary cellsCys-richCrystallization screeningCysteine residuesDiffracting crystalsVon Willebrand factorX-ray diffractionFree cysteine residuesDisulfide bond pairingsDisulfide pairingPairing patternsCA domainOvary cellsResidues
2008
Structural basis for the function and inhibition of an influenza virus proton channel
Stouffer A, Acharya R, Salom D, Levine A, Di Costanzo L, Soto C, Tereshko V, Nanda V, Stayrook S, DeGrado W. Structural basis for the function and inhibition of an influenza virus proton channel. Nature 2008, 451: 596-599. PMID: 18235504, PMCID: PMC3889492, DOI: 10.1038/nature06528.Peer-Reviewed Original Research