J
Joseph A. Loo
Researcher at University of California, Los Angeles
Publications - 434
Citations - 28705
Joseph A. Loo is an academic researcher from University of California, Los Angeles. The author has contributed to research in topics: Mass spectrometry & Electrospray ionization. The author has an hindex of 89, co-authored 413 publications receiving 26162 citations. Previous affiliations of Joseph A. Loo include University of Massachusetts Amherst & Ohio State University.
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Studying noncovalent protein complexes by electrospray ionization mass spectrometry
TL;DR: Several applications of ESI-MS are discussed, including protein interactions with metal ions and nucleic acids and subunit protein structures (quaternary structure) and mass spectrometry offers advantages in speed and sensitivity.
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New developments in biochemical mass spectrometry: electrospray ionization
TL;DR: Fundamental considerations suggest even more impressive developments may be anticipated related to detection sensitivity and methods for obtaining structural information, as well as new developments related to ESI-MS.
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Target identification using drug affinity responsive target stability (DARTS)
Brett Lomenick,Rui Hao,Nao Jonai,Randall Chin,Mariam Aghajan,Sarah Warburton,Jianing Wang,Raymond Wu,Fernando Gomez,Joseph A. Loo,James A. Wohlschlegel,Thomas M. Vondriska,Jerry Pelletier,Harvey R. Herschman,Jon Clardy,Catherine F. Clarke,Jing Huang +16 more
TL;DR: In this paper, drug affinity responsive target stability (DARTS) is proposed to identify known small-molecule-protein interactions and reveal the eukaryotic translation initiation machinery as a molecular target for the longevity enhancing plant natural product resveratrol.
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Principles and practice of electrospray ionization—mass spectrometry for large polypeptides and proteins
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How many human proteoforms are there
Ruedi Aebersold,Jeffrey N. Agar,I. Jonathan Amster,Mark S. Baker,Carolyn R. Bertozzi,Emily S. Boja,Catherine E. Costello,Benjamin F. Cravatt,Catherine Fenselau,Benjamin A. Garcia,Ying Ge,Jeremy Gunawardena,Ronald C. Hendrickson,Paul J. Hergenrother,Christian G. Huber,Alexander R. Ivanov,Ole N. Jensen,Michael C. Jewett,Neil L. Kelleher,Laura L. Kiessling,Nevan J. Krogan,Martin R. Larsen,Joseph A. Loo,Rachel R. Ogorzalek Loo,Emma Lundberg,Emma Lundberg,Michael J. MacCoss,Parag Mallick,Vamsi K. Mootha,Milan Mrksich,Tom W. Muir,Steven M. Patrie,James J. Pesavento,Sharon J. Pitteri,Henry Rodriguez,Alan Saghatelian,Wendy Sandoval,Hartmut Schlüter,Salvatore Sechi,Sarah A. Slavoff,Lloyd M. Smith,Michael Snyder,Paul M. Thomas,Mathias Uhlén,Jennifer E. Van Eyk,Marc Vidal,David R. Walt,Forest M. White,Evan R. Williams,Therese Wohlschlager,Vicki H. Wysocki,Nathan A. Yates,Nicolas L. Young,Bing Zhang +53 more
TL;DR: This work frames central issues regarding determination of protein-level variation and PTMs, including some paradoxes present in the field today, and uses this framework to assess existing data and ask the question, "How many distinct primary structures of proteins (proteoforms) are created from the 20,300 human genes?"