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Alice Barkan
Researcher at University of Oregon
Publications - 120
Citations - 11270
Alice Barkan is an academic researcher from University of Oregon. The author has contributed to research in topics: RNA & Gene. The author has an hindex of 56, co-authored 119 publications receiving 10137 citations. Previous affiliations of Alice Barkan include Max Delbrück Center for Molecular Medicine & University of California, Berkeley.
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Journal ArticleDOI
Pentatricopeptide repeat proteins in plants
Alice Barkan,Ian Small +1 more
TL;DR: Recent breakthroughs in understanding how PPR proteins recognize RNA sequences through modular base-specific contacts will help match proteins to potential binding sites and provide a pathway toward designing synthetic RNA-binding proteins aimed at desired targets.
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Redesigning photosynthesis to sustainably meet global food and bioenergy demand
Donald R. Ort,Donald R. Ort,Sabeeha S. Merchant,Jean Alric,Alice Barkan,Robert E. Blankenship,Ralph Bock,Roberta Croce,Maureen R. Hanson,Julian M. Hibberd,Stephen P. Long,Thomas A. Moore,James V. Moroney,Krishna K. Niyogi,Krishna K. Niyogi,Martin A. J. Parry,Pamela Peralta-Yahya,Roger C. Prince,Kevin Redding,Martin H. Spalding,Klaas J. van Wijk,Wim F. J. Vermaas,Susanne von Caemmerer,Andreas P.M. Weber,Todd O. Yeates,Joshua S. Yuan,Xin-Guang Zhu +26 more
TL;DR: This work explores an array of prospective redesigns of plant systems at various scales aimed at increasing crop yields through improved photosynthetic efficiency and performance, and suggests some proposed redesigns are certain to face obstacles that will require alternate routes.
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A Combinatorial Amino Acid Code for RNA Recognition by Pentatricopeptide Repeat Proteins
TL;DR: The pentatricopeptide repeat (PPR) is a helical repeat motif found in an exceptionally large family of RNA-binding proteins that functions in mitochondrial and chloroplast gene expression as mentioned in this paper.
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Site-specific binding of a PPR protein defines and stabilizes 5′ and 3′ mRNA termini in chloroplasts
TL;DR: Findings show that PPR10 serves as a barrier to RNA decay from either the 5′ or 3′ direction and that a bound protein provides an alternative to an RNA hairpin as a Barrier to 3′ exonucleases, implying that protein ‘caps’ at both 5′ and 3′ ends can define the termini of chloroplast mRNA segments.
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Participation of nuclear genes in chloroplast gene expression.
TL;DR: The convergence of biochemical approaches with those of classical and reverse genetics, and the contributions from large scale genomic sequencing should result in rapid advances in the understanding of the regulatory interactions that govern plastid gene expression.