Joseph A. Loo

About

Dr. Joseph A. Loo is a Professor in the Department of Biological Chemistry at the UCLA David Geffen School of Medicine and in the Department of Chemistry & Biochemistry at UCLA. He serves as the Faculty Director of the UCLA Mass Spectrometry and Proteomics Technology Center and is a member of several UCLA research institutes, including the UCLA/DOE Laboratory for Genomics and Proteomics, the UCLA Molecular Biology Institute, and the UCLA Jonsson Comprehensive Cancer Center. His expertise lies in the mass spectrometry characterization of proteins and their post-translational modifications, with a focus on developing bioanalytical methods for structural characterization of peptides and proteins, proteomics, and disease biomarkers. Dr. Loo has authored over 180 scientific publications and has significantly contributed to the application of electrospray ionization mass spectrometry (ESI-MS) for analyzing noncovalently-bound macromolecular assemblies and their interactions. His research includes profiling proteins in human salivary fluids for disease biomarker discovery and elucidating protein complexes and modifications in complex biological systems. He has received numerous awards and honors, including fellowships and recognition from professional societies, and has served on editorial boards for prominent journals in mass spectrometry and analytical chemistry.

Research topics

• Computer Science
• Chemistry
• Chromatography
• Computational biology
• Genetics
• Immunology
• Bioinformatics
• Cell biology
• Nanotechnology
• Medicine

Selected publications

• The Human Proteoform Project: Defining the human proteome

  Science Advances · 2021 · 236 citations

  Proteins are the primary effectors of function in biology, and thus, complete knowledge of their structure and properties is fundamental to deciphering function in basic and translational research. The chemical diversity of proteins is expressed in their many proteoforms, which result from combinations of genetic polymorphisms, RNA splice variants, and posttranslational modifications. This knowledge is foundational for the biological complexes and networks that control biology yet remains largel…

  DOI

• Amyloid fibrils in FTLD-TDP are composed of TMEM106B and not TDP-43

  Nature · 2022-03-28 · 178 citations

  articleOpen access
  PublisherOA PDFDOI

• Higher-order structural characterisation of native proteins and complexes by top-down mass spectrometry

  Chemical Science · 2020 · 152 citations

  , native mass spectrometry. Sequence, post-translational modifications, ligand/metal binding, protein folding, and complex stoichiometry can thus all be probed directly. Here, we review recent developments in this new and exciting field of research. While this work is written primarily from a mass spectrometry perspective, it is targeted to all bioanalytical scientists who are interested in applying these methods to their own biochemistry and chemical biology research.

  DOI

• Interlaboratory Study for Characterizing Monoclonal Antibodies by Top-Down and Middle-Down Mass Spectrometry

  Journal of the American Society for Mass Spectrometry · 2020 · 125 citations

  The Consortium for Top-Down Proteomics (www.topdownproteomics.org) launched the present study to assess the current state of top-down mass spectrometry (TD MS) and middle-down mass spectrometry (MD MS) for characterizing monoclonal antibody (mAb) primary structures, including their modifications. To meet the needs of the rapidly growing therapeutic antibody market, it is important to develop analytical strategies to characterize the heterogeneity of a therapeutic product's primary structure accu…

  DOI

• Evolution of Mass Spectrometers for High <i>m</i>/<i>z</i> Biological Ion Formation, Transmission, Analysis and Detection: A Personal Perspective

  Journal of the American Society for Mass Spectrometry · 2025-03-05 · 11 citations

  articleSenior authorCorresponding

  Mass spectrometry (MS) has become an essential tool in virtually all academic, pharmaceutical, and biopharmaceutical analytical laboratories. The specialized and bespoke area of MS research and application of high m/z ion (>m/z 6000 and high mass, >150 kDa) formation, transmission, analysis, and detection is a relatively new area of focus for MS that has seen dramatic acceleration in interest over the last two decades. Herein we delve into this exciting aspect of MS, discussing how MS instrument…

  PublisherDOI

Recent grants

• Advancing Mass Spectrometry Analyses of Proteins, Assemblies, and Proteoforms

  NIH · $1.9M · 2022–2027

• NIH Grant S10RR028893

  NIH · $2.7M · 2011

• Mass Spectrometry of Protein Assemblies

  NIH · $3.2M · 2004–2024

Frequent coauthors

• Rachel R. Ogorzalek Loo

  University of California, Los Angeles

  197 shared

• John R. Yates

  Scripps Research Institute

  112 shared

• Carolyn R. Bertozzi

  Stanford University

  87 shared

• Laura L. Kiessling

  Massachusetts Institute of Technology

  87 shared

• Anne B. McCoy

  University of Washington

  85 shared

• Kenneth M. Merz

  Michigan State University

  85 shared

• Gregory D. Scholes

  Princeton University

  85 shared

• Jillian M. Buriak

  University of Alberta

  85 shared

Labs

• Loo, Joseph A. LaboratoryPI

Awards & honors

• Clarkson U. American Chemical Society Analytical Chemistry D…
• Clarkson U. Chemical Rubber Company Achievement Award
• Clarkson U. George L. Jones, Jr. Memorial Award
• Clarkson U. Merck Chemistry Award
• Cornell Chemistry Teaching Assistant Award

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