D
Dunja Skoko
Researcher at University of Illinois at Chicago
Publications - 13
Citations - 1299
Dunja Skoko is an academic researcher from University of Illinois at Chicago. The author has contributed to research in topics: DNA & DNA condensation. The author has an hindex of 9, co-authored 13 publications receiving 1200 citations. Previous affiliations of Dunja Skoko include Laboratory of Molecular Biology & National Institutes of Health.
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Journal ArticleDOI
Probing protein heterogeneity in the plasma membrane using PALM and pair correlation analysis
Prabuddha Sengupta,Tijana Jovanovic-Talisman,Tijana Jovanovic-Talisman,Dunja Skoko,Malte Renz,Sarah L. Veatch,Jennifer Lippincott-Schwartz +6 more
TL;DR: PC-PALM is an effective tool with broad applicability for analysis of protein heterogeneity and function, adaptable to other single-molecule strategies, and shows dramatic changes in glycosylphosphatidylinositol (GPI)-anchored protein arrangement under varying perturbations.
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Near-field-magnetic-tweezer manipulation of single DNA molecules.
TL;DR: The magnetic manipulation system can be combined with manipulation and force measurement using glass micropipettes to allow rapid switching between measurements in fixed-force and fixed-extension ensembles and is demonstrated to study formation of DNA loops by an enzyme which strongly binds two copies of a specific 6-base-pair sequence.
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Mechanism of chromosome compaction and looping by the Escherichia coli nucleoid protein Fis.
Dunja Skoko,Daniel Yoo,Hua Bai,Bernhard Schnurr,Jie Yan,Sarah M. McLeod,John F. Marko,Reid C. Johnson +7 more
TL;DR: Results suggest that Fis may play a role in vivo as a domain barrier element by organizing DNA loops within the E. coli chromosome through Fis-mediated DNA looping.
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Micromechanical analysis of the binding of DNA-bending proteins HMGB1, NHP6A, and HU reveals their ability to form highly stable DNA-protein complexes.
TL;DR: It is observed that protein transport along DNA by direct transfers occurs even for proteins such as NHP6A and HU that have only one DNA-binding domain, and this rapid protein exchange in the presence of competitor DNA must occur only via "direct" DNA-DNA contact.
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Defining a Centromere-like Element in Bacillus subtilis by Identifying the Binding Sites for the Chromosome-Anchoring Protein RacA
Sigal Ben-Yehuda,Sigal Ben-Yehuda,Masya Fujita,Xiaole Shirley Liu,Boris Gorbatyuk,Dunja Skoko,Jie Yan,John F. Marko,Jun Liu,Patrick Eichenberger,David Z. Rudner,Richard Losick +11 more
TL;DR: It is proposed that interactions between DNA bound RacA molecules cause the centromere-like element in the vicinity of the origin of replication to fold up into a higher order complex that fastens the chromosome to the cell pole.