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Emine Kaya

Researcher at Ludwig Maximilian University of Munich

Publications -  9
Citations -  1528

Emine Kaya is an academic researcher from Ludwig Maximilian University of Munich. The author has contributed to research in topics: Amino acid & Click chemistry. The author has an hindex of 8, co-authored 9 publications receiving 1288 citations. Previous affiliations of Emine Kaya include Protein Sciences & University of California, Berkeley.

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Journal ArticleDOI

Structures of Cas9 Endonucleases Reveal RNA- Mediated Conformational Activation

TL;DR: To compare the architectures and domain organization of diverse Cas9 proteins, the atomic structures of Cas9 from Streptococcus pyogenes and Actinomyces naeslundii and AnaCas9 were determined by x-ray crystallography and three-dimensional reconstructions of apo-SpyCas9, SpyCas9:RNA, and SpyCas 9:RNA:DNA were obtained by negative-stain single-particle electron microscopy.
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A genetically encoded norbornene amino acid for the mild and selective modification of proteins in a copper-free click reaction.

TL;DR: This project shows that requirments for the incorporation of special unnatural amino acid into proteins to enable site-specific bioorthogonal functionalization can be met with a specially encoded norbornene amino acid which reacts selectively with nitrile imines.
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RNA-dependent RNA targeting by CRISPR-Cas9

TL;DR: It is shown that Cas9 enzymes from both subtypes II-A and II-C can recognize and cleave single-stranded RNA by an RNA-guided mechanism that is independent of a protospacer-adjacent motif (PAM) sequence in the target RNA.
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The archaeal cofactor F0 is a light-harvesting antenna chromophore in eukaryotes

TL;DR: The results show that the F0/F420 coenzyme system, so far believed to be strictly limited to the archael kingdom of life, is far more widespread than anticipated.
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Synthesis of Threefold Glycosylated Proteins using Click Chemistry and Genetically Encoded Unnatural Amino Acids

TL;DR: In vivo incorporation of up to three artificial alkyne or alkene amino acids into the yellow fluorescent protein (YFP) and the subsequent glycosylation of these sites with different sugar azides using the Huisgen–Meldal–Sharpless click chemistry method, which was used in this group for the synthesis of multiple sugar modified oligonucleotides.