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Bruce D. Pascal
Researcher at Scripps Research Institute
Publications - 56
Citations - 4296
Bruce D. Pascal is an academic researcher from Scripps Research Institute. The author has contributed to research in topics: Protein structure & Ligand (biochemistry). The author has an hindex of 27, co-authored 55 publications receiving 3325 citations. Previous affiliations of Bruce D. Pascal include Scripps Health & Florida State University.
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Journal ArticleDOI
Crystal structure of rhodopsin bound to arrestin by femtosecond X-ray laser
Yanyong Kang,X. Edward Zhou,Xiang Gao,Yuanzheng He,Wei Liu,Andrii Ishchenko,Anton Barty,Thomas A. White,Oleksandr Yefanov,Gye Won Han,Qingping Xu,Parker W. de Waal,Jiyuan Ke,M. H. Eileen Tan,Chenghai Zhang,Arne Moeller,Graham M. West,Bruce D. Pascal,Ned Van Eps,Lydia N. Caro,Sergey A. Vishnivetskiy,Regina J. Lee,Kelly Suino-Powell,Xin Gu,Kuntal Pal,Jinming Ma,Xiaoyong Zhi,Sébastien Boutet,Garth J. Williams,Marc Messerschmidt,Cornelius Gati,Nadia A. Zatsepin,Dingjie Wang,Daniel James,Shibom Basu,Shatabdi Roy-Chowdhury,Chelsie E. Conrad,Jesse Coe,Haiguang Liu,Stella Lisova,Christopher Kupitz,Ingo Grotjohann,Raimund Fromme,Yi Jiang,Minjia Tan,Huaiyu Yang,Jun Li,Meitian Wang,Zhong Zheng,Dianfan Li,Nicole Howe,Yingming Zhao,Jörg Standfuss,Kay Diederichs,Yuhui Dong,Clinton S. Potter,Bridget Carragher,Martin Caffrey,Hualiang Jiang,Henry N. Chapman,John C. H. Spence,Petra Fromme,Uwe Weierstall,Oliver P. Ernst,Vsevolod Katritch,Vsevolod V. Gurevich,Patrick R. Griffin,Wayne L. Hubbell,Raymond C. Stevens,Vadim Cherezov,Karsten Melcher,H. Eric Xu +71 more
TL;DR: The crystal structure of a constitutively active form of human rhodopsin bound to a pre-activated form of the mouse visual arrestin is determined by serial femtosecond X-ray laser crystallography and provides a basis for understanding GPCR-mediated arrestin-biased signalling.
Journal ArticleDOI
Recommendations for performing, interpreting and reporting hydrogen deuterium exchange mass spectrometry (HDX-MS) experiments.
Glenn R. Masson,John E. Burke,Natalie G. Ahn,Ganesh S. Anand,Christoph H. Borchers,Sébastien Brier,George M. Bou-Assaf,John R. Engen,S. Walter Englander,Johan H. Faber,Rachel Garlish,Patrick R. Griffin,Michael L. Gross,Miklos Guttman,Yoshitomo Hamuro,Albert J. R. Heck,Damian Houde,Roxana E. Iacob,Thomas J. D. Jørgensen,Igor A. Kaltashov,Judith P. Klinman,Lars Konermann,Petr Man,Leland Mayne,Bruce D. Pascal,Dana Reichmann,Mark Skehel,Joost Snijder,Timothy S. Strutzenberg,Eric S. Underbakke,Cornelia Wagner,Thomas E. Wales,Benjamin T. Walters,David D. Weis,Derek J. Wilson,Patrick L. Wintrode,Zhongqi Zhang,Jie Zheng,David C. Schriemer,Kasper D. Rand +39 more
TL;DR: Recommendations arising from community discussions emerging out of the first International Conference on Hydrogen-Exchange Mass Spectrometry (IC-HDX; 2017) are provided, meant to represent both a consensus viewpoint and an opportunity to stimulate further additions and refinements as the field advances.
Journal ArticleDOI
Irisin Mediates Effects on Bone and Fat via αV Integrin Receptors
Hyeonwoo Kim,Christiane D. Wrann,Mark P. Jedrychowski,Sara Vidoni,Yukiko Kitase,Kenichi Nagano,Chuan Zhou,Joshua Chou,Virginia-Jeni A. Parkman,Scott J. Novick,Timothy S. Strutzenberg,Bruce D. Pascal,Phuong T. Le,Daniel J. Brooks,Alexander M. Roche,Kaitlyn K. Gerber,Laura Mattheis,Wei Chen,Hua Tu,Mary L. Bouxsein,Patrick R. Griffin,Roland Baron,Clifford J. Rosen,Lynda F. Bonewald,Bruce M. Spiegelman +24 more
TL;DR: Irisin is secreted by muscle, increases with exercise, and mediates certain favorable effects of physical activity as discussed by the authors, however, the skeletal response to exercise is less clear, and the receptor for irisin has not been identified.
Journal ArticleDOI
HP1 reshapes nucleosome core to promote phase separation of heterochromatin
Serena Sanulli,Michael J. Trnka,Venkatasubramanian Dharmarajan,Ryan W. Tibble,Bruce D. Pascal,Alma L. Burlingame,Patrick R. Griffin,John D. Gross,Geeta J. Narlikar +8 more
TL;DR: The results indicate that Swi6 couples its oligomerization to the phase separation of chromatin by a counterintuitive mechanism, namely the dynamic exposure of buried nucleosomal regions, which increases opportunities for multivalent interactions between nucleosomes, thereby promoting phase separation.
Journal ArticleDOI
Probing Protein Ligand Interactions by Automated Hydrogen/Deuterium Exchange Mass Spectrometry
Michael J. Chalmers,Scott A. Busby,Bruce D. Pascal,Yuanjun He,Christopher L. Hendrickson,Alan G. Marshall,Patrick R. Griffin +6 more
TL;DR: The utility of this system to differentiate structural perturbations in the ligand-binding domain (LBD) of the nuclear receptor PPARgamma induced upon binding a full agonist and a partial agonist is demonstrated.