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Lihi Shaulov

Researcher at Technion – Israel Institute of Technology

Publications -  14
Citations -  730

Lihi Shaulov is an academic researcher from Technion – Israel Institute of Technology. The author has contributed to research in topics: Biology & Nuclear pore. The author has an hindex of 9, co-authored 11 publications receiving 629 citations. Previous affiliations of Lihi Shaulov include Bar-Ilan University.

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Structural Basis of DNA Recognition by p53 Tetramers

TL;DR: High-resolution crystal structures of sequence-specific complexes between the core domain of human p53 and different DNA half-sites are presented and establish a structural framework for understanding the mechanisms of specificity, affinity, and cooperativity of DNA binding by p53.
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A novel lineage of myoviruses infecting cyanobacteria is widespread in the oceans.

TL;DR: The genome of this phage encodes an entirely unique set of structural proteins not found in any currently known phage, indicating that it uses lineage-specific genes for virion morphogenesis and represents a previously unknown lineage of myoviruses.
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Importin beta regulates the seeding of chromatin with initiation sites for nuclear pore assembly.

TL;DR: It is shown that the initial step of chromatin seeding is negatively regulated by importin beta, and suggested that initiation sites for NPC assembly contain single copies of Chromatin-bound ELYS/Nup107-160 and that the lateral oligomerization of these subunits depends on the recruitment of membrane components.
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Sequence-dependent cooperative binding of p53 to DNA targets and its relationship to the structural properties of the DNA targets

TL;DR: It is demonstrated that the CWWG motif, found in the center of each consensus p53 half-site, is a key player in p53/DNA interactions and binds to p53 consensus sites containing CATG with relatively low cooperativity, as both dimers and tetramers, and with even lower cooperativity to such sites containing spacer sequences.
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A dominant-negative form of POM121 binds chromatin and disrupts the two separate modes of nuclear pore assembly

TL;DR: It is shown that a soluble internal fragment of the membrane nucleoporin POM121 has a dominant-negative effect on both modes of assembly in a cell-free reconstitution system and links nuclear membrane formation and expansion to nuclear pore biogenesis.