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Jayson A. Falkner

Researcher at University of Michigan

Publications -  11
Citations -  851

Jayson A. Falkner is an academic researcher from University of Michigan. The author has contributed to research in topics: Peptide spectral library & Mass spectrometry data format. The author has an hindex of 10, co-authored 11 publications receiving 813 citations. Previous affiliations of Jayson A. Falkner include University of Colorado Boulder.

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A HUPO test sample study reveals common problems in mass spectrometry–based proteomics

Alexander W. Bell, +101 more
- 01 Jun 2009 - 
TL;DR: Central analysis determined missed identifications, environmental contamination, database matching and curation of protein identifications as sources of problems in liquid chromatography–mass spectrometry–based proteomics.
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Human Proteinpedia enables sharing of human protein data.

Suresh Mathivanan, +163 more
- 01 Feb 2008 - 
TL;DR: MMCD is a practical tool for expediting the time-consuming steps of identifying and researching small molecules and is compatible with both NMR and MS data and facilitates high-throughput metabolomics investigations.
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A Spectral Clustering Approach to MS/MS Identification of Post-Translational Modifications

TL;DR: A novel algorithm is described, "Bonanza", for clustering spectra without knowledge of peptide or protein identifications, which significantly more spectra can be identified with this approach, including spectra with unexpected potential modifications or amino-acid substitutions.
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Rapid optimization of MRM-MS instrument parameters by subtle alteration of precursor and product m/z targets.

TL;DR: A workflow functional on both Waters Quattro Premier and ABI 4000 QTRAP triple quadrupole instruments that allows rapid determination of the optimal value of any programmable instrument parameter for each MRM transition is devised.
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Exploring protein-ligand recognition with Binding MOAD.

TL;DR: It is determined that most cavities and ligands are well buried in the complexes of Binding MOAD, which fits with the common paradigm that a large degree of contact between the ligand and protein is significant in molecular recognition.