scispace - formally typeset
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.

Papers
More filters
Journal ArticleDOI

Structural Characterization of Native Proteins and Protein Complexes by Electron Ionization Dissociation-Mass Spectrometry.

TL;DR: The capabilities of another activation method, 30 eV electron ionization dissociation (EID), for the top-down MS characterization of native protein-ligand and protein-protein complexes and the structural changes due to Cu-binding and a point mutation were revealed by EID-MS.
Journal ArticleDOI

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

TL;DR: In this paper , the authors extracted amyloid fibrils from four patients representing four of the five FTLD-TDP subclasses, and determined their structures by cryo-electron microscopy.
Journal ArticleDOI

Use of electrospray ionization mass spectrometry to probe antisense peptide interactions

TL;DR: Electrospray ionization mass spectrometry with a magnetic sector instrument has been used to test for non-covalent interactions between human angiotensin II and eight synthetic octapeptides that are considered complementary peptides or analogues of these antisense peptides.
Journal ArticleDOI

Capillary isotachophoresis with UV and tandem mass spectrometric detection for peptides and proteins.

TL;DR: The application of capillary isotachophoresis (CITP) and combined CITP‐mass spectrometry (MS) for peptides and proteins is demonstrated, showing the potential for rapid sequence determination.
Journal ArticleDOI

Glycoprofiling of the Human Salivary Proteome

TL;DR: This starting 2-D gel glycosylation reference map shows that the scientifically accepted, individual oligosaccharide variability is not limited to a few large glycoproteins such as MUC5B, but are found on most members of the salivary proteome.