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Stephen Fried

As seen in: Medium, The New York Times, Yahoo Life, Nature, The Washington Post, The Atlantic, Vanity Fair, ACS Publications, Smithsonian Magazine, Science Magazine and
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Articles

Structural basis of kinesin-1 autoinhibition and its control of microtubule-based motility

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By Takuya Yahagi, Piero Lamelza, Lou-Anne Chevrollier, Yuqi Tang, Kyoko Okada, Stephen Fried, Richard J. McKenney, Jawdat Al-Bassam
| Science Magazine Verified
Abstract INTRODUCTION RESULTS DISCUSSION MATERIALS AND METHODS Acknowledgments Supplementary Materials REFERENCES Information & Authors Metrics & Citations View Options References Figures Tables Media Share Abstract Kinesin-1 was the first microtubule motor identified, responsible for anterograde transport of diverse cargo in eukaryotic cells. Defects or misregulation of kinesin-1 is linked to multiple neurological disorders, and various pathogens exploit kinesin-1 to transport their cargo.
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Remembering Isaiah Zagar

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By Stephen Fried
| Philadelphia Magazine Verified
Opinion Remembering Isaiah Zagar A longtime friend and admirer reflects on Philly’s one-of-a-kind outsider artist, who died this week. Get a compelling long read and must-have lifestyle tips in your inbox every Sunday morning — great with coffee! Isaiah Zagar / Photograph courtesy of Philadelphia’s Magic Gardens Isaiah Zagar, arguably Philadelphia’s most prolific, inspired, daring, death-defying, adored and debated artist, died this week, just shy of his 87th birthday.
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Cryo-EM structures of plant Augmin reveal coiled-coil assembly, antiparallel dimerization, and NEDD1 binding - Nature Communications

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By Yuh-Ru Julie Lee, Shubham Mittal, Faruck Morcos, Stephen Fried
| Nature Verified
Abstract Microtubule (MT) branch nucleation requires Augmin and NEDD1 proteins, which recruit and activate the gamma-tubulin ring complex (γ-TuRC). Augmin is a fork-shaped assembly of eight coiled-coil subunits, while NEDD1 is a β-propeller protein bridging MTs, Augmin, and γ-TuRC. We reconstitute Arabidopsis thaliana Augmin assemblies and determine 3.7-7.3-Å cryo-EM structures of its V-junction and extended regions using crosslinking mass spectrometry.
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