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Eva Nogales

Researcher at University of California, Berkeley

Publications -  253
Citations -  28553

Eva Nogales is an academic researcher from University of California, Berkeley. The author has contributed to research in topics: Microtubule & Tubulin. The author has an hindex of 84, co-authored 244 publications receiving 24906 citations. Previous affiliations of Eva Nogales include University of California & California Institute for Quantitative Biosciences.

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Structure of the alpha beta tubulin dimer by electron crystallography.

TL;DR: An atomic model of the αβ tubulin dimer fitted to a 3.7-Å density map obtained by electron crystallography of zinc-induced tubulin sheets is presented.
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High-resolution model of the microtubule.

TL;DR: A high-resolution model of the microtubule has been obtained by docking the crystal structure of tubulin into a 20 A map of themicrotubule, and the excellent fit indicates the similarity of the tubulin conformation in both polymers and defines the orientation of the Tubulin structure within the micro Tubule.
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Refined structure of alpha beta-tubulin at 3.5 A resolution.

TL;DR: In this paper, a refined model of the alpha-beta-tubulin dimer was presented, which includes residues alpha: 2-34, alpha:61-439, beta:2-437, one molecule of GTP, one of GDP, and one of taxol, as well as one magnesium ion near the M-loop in the alpha subunit.
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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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Structural Insights into Microtubule Function

TL;DR: The recent high-resolution analysis of the structure of tubulin and the microtubule has brought new insight to the study of microtubules function and regulation, as well as the mode of action of antimitotic drugs that disrupt normal micro Tubulin behavior.