N
Nikolina Sekulic
Researcher at University of Oslo
Publications - 30
Citations - 1686
Nikolina Sekulic is an academic researcher from University of Oslo. The author has contributed to research in topics: Nucleosome & Histone H3. The author has an hindex of 17, co-authored 28 publications receiving 1462 citations. Previous affiliations of Nikolina Sekulic include University of Pennsylvania & University of Illinois at Chicago.
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Journal ArticleDOI
The structure of (CENP-A–H4) 2 reveals physical features that mark centromeres
TL;DR: DNA topological analysis indicates that CENP-A-containing nucleosomes are octameric with conventional left-handed DNA wrapping, in contrast to other recent proposals, indicating specificity for an unconventional nucleosome shape.
Journal ArticleDOI
CENP-C reshapes and stabilizes CENP-A nucleosomes at the centromere
Samantha J. Falk,Lucie Y. Guo,Nikolina Sekulic,Evan M. Smoak,Tomoyasu Mani,Glennis A. Logsdon,Kushol Gupta,Lars E.T. Jansen,Gregory D. Van Duyne,Sergei A. Vinogradov,Michael A. Lampson,Ben E. Black +11 more
TL;DR: This work finds that CENP-C affects nucleosome shape and dynamics in a manner analogous to allosteric regulation of enzymes, and is a prime candidate to stabilize centromeric chromatin.
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The octamer is the major form of CENP-A nucleosomes at human centromeres
Dan Hasson,Tanya Panchenko,Kevan J. Salimian,Mishah Uzziel Salman,Nikolina Sekulic,Alicia Alonso,Peter E. Warburton,Peter E. Warburton,Ben E. Black +8 more
TL;DR: It is shown that the predominant form of the CENP-A particle at human centromeres is an octameric nucleosome, the fundamental unit of the chromatin that epigenetically specifies centromere location in mammals.
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The CENP-L-N Complex Forms a Critical Node in an Integrated Meshwork of Interactions at the Centromere-Kinetochore Interface.
TL;DR: It is found that the CCAN does not assemble as a linear hierarchy, and instead, each sub-complex requires multiple non-redundant interactions for its localization to centromeres and the structural integrity of the overall assembly.
Journal ArticleDOI
HJURP Uses Distinct CENP-A Surfaces to Recognize and to Stabilize CENP-A/Histone H4 for Centromere Assembly
Emily A. Bassett,Jamie E. DeNizio,Meghan C. Barnhart-Dailey,Tanya Panchenko,Nikolina Sekulic,Danielle J. Rogers,Daniel R. Foltz,Ben E. Black +7 more
TL;DR: It is found that whereas surface-exposed residues in the CENP-A targeting domain (CATD) are the primary sequence determinants for HJURP recognition, buried CATD residues that generate rigidity with H4 are also required for efficient incorporation into centromeres.