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David C. Muddiman

Researcher at North Carolina State University

Publications -  356
Citations -  14095

David C. Muddiman is an academic researcher from North Carolina State University. The author has contributed to research in topics: Mass spectrometry & Electrospray ionization. The author has an hindex of 63, co-authored 327 publications receiving 12861 citations. Previous affiliations of David C. Muddiman include University of South Carolina & University of North Carolina at Greensboro.

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Generation and Detection of Multiply-Charged Peptides and Proteins by Matrix-Assisted Laser Desorption Electrospray Ionization (MALDESI) Fourier Transform Ion Cyclotron Resonance Mass Spectrometry

TL;DR: Analysis of peptides and proteins resulted in high resolving power single-acquisition FT-ICR mass spectra with average charge-states highly correlated to those obtained by nanoESI, thus, providing strong evidence that the ESI process dictates the observed charge-state distribution.
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MSiReader: An Open-Source Interface to View and Analyze High Resolving Power MS Imaging Files on Matlab Platform

TL;DR: MSiReader is introduced, a free open source application to read and analyze high resolution MSI data from the most common MSi data formats and is built on the Matlab platform and includes a large selection of data analysis tools and features.
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Quantitative mass spectral evidence for the absence of circulating brain natriuretic peptide (BNP-32) in severe human heart failure

TL;DR: An immunoaffinity purification assay is developed and used to isolate endogenous BNP-32 from New York Heart Association class IV patient plasma for subsequent analysis by nano-liquid chromatography (LC) electrospray ionization Fourier transform ion cyclotron resonance (FT-ICR) MS.
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Performance Characteristics of a New Hybrid Quadrupole Time-of-Flight Tandem Mass Spectrometer (TripleTOF 5600)

TL;DR: The TripleTOF 5600 System, a hybrid quadrupole time-of-flight mass spectrometer, was evaluated to explore the key figures of merit in generating peptide and protein identifications that included spectral acquisition rates, data quality, proteome coverage, and biological depth.
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Absolute Quantification of the Model Biomarker Prostate-Specific Antigen in Serum by LC-MS/MS Using Protein Cleavage and Isotope Dilution Mass Spectrometry

TL;DR: absolute quantification can be performed on the model biomarker PSA introduced into denatured serum when analyzed by LC-MS/MS, and concerns still exist regarding sensitivity compared to existing immunoassays as well as the reproducibility of PC-IDMS performed in different matrixes.