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
2009
N-terminal Domains Elicit Formation of Functional Pmel17 Amyloid Fibrils*
Watt B, van Niel G, Fowler DM, Hurbain I, Luk KC, Stayrook SE, Lemmon MA, Raposo G, Shorter J, Kelly JW, Marks MS. N-terminal Domains Elicit Formation of Functional Pmel17 Amyloid Fibrils*. Journal Of Biological Chemistry 2009, 284: 35543-35555. PMID: 19840945, PMCID: PMC2790984, DOI: 10.1074/jbc.m109.047449.Peer-Reviewed Original ResearchConceptsFibril formationFormation of melanosomesMultivesicular compartmentsImperfect repeatsRPT domainTransmembrane proteinMelanosome maturationTerminal domainIntracellular traffickingMultivesicular bodiesAmyloid foldPrecursor organellesAmyloid-like fibrilsDownstream domainSubcellular organellesAmyloid conversionRegulatory rolePmel17RepeatsEarly stepsStructural coreAmyloid formationProteolytic fragmentsRecombinant fragmentsOrganelles