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Ranveer Singh Jayani

Researcher at University of California, San Diego

Publications -  13
Citations -  2014

Ranveer Singh Jayani is an academic researcher from University of California, San Diego. The author has contributed to research in topics: Enhancer & Chromatin. The author has an hindex of 11, co-authored 13 publications receiving 1728 citations. Previous affiliations of Ranveer Singh Jayani include Himachal Pradesh University & Howard Hughes Medical Institute.

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Microbial pectinolytic enzymes: A review

TL;DR: Pectinases are one of the most widely distributed enzymes in bacteria, fungi and plants as discussed by the authors, and they have a share of 25% in the global sales of food enzymes.
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Phase separation of ligand-activated enhancers licenses cooperative chromosomal enhancer assembly

TL;DR: In human breast cancer cells, the acute 17β-estradiol-dependent activation of functional enhancers requires assembly of an enhancer RNA–dependent ribonucleoprotein (eRNP) complex exhibiting properties of phase-separated condensates, which serve as determinants of rapid ligand-dependent alterations in chromosomal architecture and cooperative enhancer activation.
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Global Regulator SATB1 Recruits β-Catenin and Regulates TH2 Differentiation in Wnt-Dependent Manner

TL;DR: Chromatin organizer SATB1 and Wnt transducer β-catenin form a complex and regulate expression of GATA3 and TH2 cytokines in Wnt-dependent manner and orchestrate TH2 lineage commitment.
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p300-mediated Acetylation of Histone H3 Lysine 56 Functions in DNA Damage Response in Mammals

TL;DR: Interestingly, analysis of occurrence of H3K56 acetylation using ChIP-on-chip revealed its genome-wide spread, affecting genes involved in several pathways that are implicated in tumorigenesis such as cell cycle, DNA damage response, DNA repair, and apoptosis.
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Phosphorylation of SATB1, a global gene regulator, acts as a molecular switch regulating its transcriptional activity in vivo.

TL;DR: It is shown here that phosphorylation by PKC acts as a switch to determine whether SATB1 interacts with HDAC1 or PCAF, and it is proposed that a similar mechanism may dictate the ability of SATB 1 to function as a global regulator.