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Bryan Roth on Muck Rack

Bryan Roth

(He/Him)
  • Insights Director, Sightlines
  • Analyst, Feel Goods Company
North Carolina
As seen in: Sightlines, Nature, Wiley Online Library, PLOS Biology, Frontiers, JAMA (The Journal of the American Medical Association), Science Magazine, Paste, BioRxiv, Cell Press, Paperblog English and
Covers:  Beer, Beverage Alcohol, Spirits, Wine, Hard Seltzer
@feelgoodscomp analyst. @sightlines_news insights. @peterfrost: "A bright, shining light in an otherwise empty world." @andwoo: “Never meet your heroes.”

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Bryan Roth’s Biography

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My background includes just about anything asked of a modern journalist, although writing has always been at the center. Focus on beverage alcohol as a reporter and data journalist.

Articles

A suite of engineered mice for interrogating psychedelic drug actions

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By Yi-Ting Chiu, Ariel Y. Deutch, Wei Wang, Gavin Schmitz, D. Dewran Kocak, Pierre Llorach, Bei Liu, Noah Sciaky, Kunjie Hua, Chongguang Chen, Sarah Mott, Jesse K Niehaus, Jeffrey F. DiBerto, Justin G. English, Jessica Walsh, Grégory Scherrer, Melissa Herman, Zhuhao Wu, William C. Wetsel, Bryan Roth, Karen Lu Huang, Kasey R. Bowyer
| Nature Verified
Abstract Psychedelic drugs, such as lysergic acid diethylamide and psilocybin, have emerged as potentially transformative therapeutics for various neuropsychiatric conditions, including depression, anxiety, post-traumatic stress disorder, migraine and cluster headaches. Classical psychedelics exert their effects through activation of 5-hydroxytryptamine 2A receptors (HTR2As).
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Structural characterization of kappa-opioid receptor dimer in complex with two G proteins

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By Yuxi Zhao, Chanjuan Xu, YUE WANG, Hong Shan, Jing L. Wang, Yuxuan Liu, Xin Luo Luo, Junrui Li, Mingyang Li, Yini Liu, Kai Wu, Bryan Roth, Xi-Ping Huang, H. Xu, Jianfeng Liu, Youwen Zhuang
| Nature Verified
Abstract The κ-opioid receptor (κOR) represents a promising non-addictive analgesic target due to its critical role in pain and reward pathways. Despite evidence of κOR dimerization, its molecular basis and pharmacological significance remain elusive.
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De novo design of miniproteins targeting GPCRs

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By Edin Muratspahić, David Feldman, Xiangli Qu, Paula Rivera-Sánchez, Jan Hendrik Voss, Emil P. T. Hertz, Mads Jeppesen, Federica Dimitri, Kensuke Sakamoto, Amrita Nallathambi, Jianjun Cao, Brian P. Cary, Matthew Belousoff, Peter Keov, Phuc Trinh, Qingchao Chen, Yue Ren, Sudha Mishra, Annu Dalal, Ramanuj Banerjee, Manisankar Ganguly, Isaac Sappington, Thomas Schlichthaerle, Jason Zhang, Arvind Pillai, Brian Coventry, Ljubica Mihaljevic, Magnus Krogstad Bauer, Susana Torres, Amir Motmaen, Gyu Lee, Long Tran, Xinru Wang, Inna Goreshnik, Dionne Vafeados, Justin E. Svendsen, Parisa Hosseinzadeh, Matthäus Brandt, Yann Waltenspühl, Kristine Deibler, Anja Bennett, Jendrik Schöppe, Xiaoli Yan, William Cao, Ayodeji A. Asuni, Justin G. English, Lance Stewart, Lauren Kay Halloran, Jamie B. Spangler, André Lieber, Arun Shukla, Patrick Sexton, Bryan Roth, Brian Krumm, Denise Wootten, Christopher Tate, Christoffer Norn, David Baker, Ana-Maria Bratovianu, Pia Peceli, Justyn Fine, Shachie Sinha, Karthik Varappalayam Karuppusamy, Nicolai Lindegaard, Lukas Deweid, Tiantang Dong, Luke Oostdyk, Lakshmi Anantharaman, Johan J. Weisser, Jesper Frank Bastlund, Christoffer Bundgaard
| Nature Verified
Abstract G protein-coupled receptors (GPCRs) play key roles in physiology and are central targets for drug discovery and development1,2, but the design of protein agonists and antagonists has been challenging as GPCRs are integral membrane proteins and conformationally dynamic3–6. Here we describe computational de novo design methods and a high-throughput “receptor diversion” microscopy-based screen for generating GPCR binding miniproteins with high affinity, potency and selectivity.
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