A
Amy-Joan L. Ham
Researcher at Vanderbilt University
Publications - 57
Citations - 6578
Amy-Joan L. Ham is an academic researcher from Vanderbilt University. The author has contributed to research in topics: Phosphorylation & Shotgun proteomics. The author has an hindex of 37, co-authored 57 publications receiving 6073 citations. Previous affiliations of Amy-Joan L. Ham include Veterans Health Administration & Belmont University.
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Journal ArticleDOI
Multi-site assessment of the precision and reproducibility of multiple reaction monitoring–based measurements of proteins in plasma
Terri A. Addona,Susan E. Abbatiello,Birgit Schilling,Steven J. Skates,D. R. Mani,David M. Bunk,Clifford H. Spiegelman,Lisa J. Zimmerman,Amy-Joan L. Ham,Hasmik Keshishian,Steven C. Hall,Simon Allen,Ronald K. Blackman,Christoph H. Borchers,Charles Buck,Helene L. Cardasis,Michael P. Cusack,Nathan G. Dodder,Bradford W. Gibson,Jason M. Held,Tara Hiltke,Angela M. Jackson,Eric B. Johansen,Christopher R. Kinsinger,Jing Li,Mehdi Mesri,Thomas A. Neubert,Richard K. Niles,Trenton C. Pulsipher,David F. Ransohoff,Henry Rodriguez,Paul A. Rudnick,Derek Smith,David L. Tabb,Tony J. Tegeler,Asokan Mulayath Variyath,Lorenzo Vega-Montoto,Asa Wahlander,Sofia Waldemarson,Mu Wang,Jeffrey R. Whiteaker,Lei Zhao,N. Leigh Anderson,Susan J. Fisher,Daniel C. Liebler,Amanda G. Paulovich,Fred E. Regnier,Paul Tempst,Steven A. Carr +48 more
TL;DR: A multilaboratory study to assess reproducibility, recovery, linear dynamic range and limits of detection and quantification of multiplexed, MRM-based assays, conducted by NCI-CPTAC demonstrates that these assays can be highly reproducible within and across laboratories and instrument platforms.
Journal ArticleDOI
A dynamic pathway for calcium-independent activation of CaMKII by methionine oxidation
Jeffrey R. Erickson,Mei Ling A. Joiner,Xiaoqun Guan,William Kutschke,Jinying Yang,Carmine V. Oddis,Ryan K. Bartlett,John S. Lowe,Susan E. O'Donnell,Nukhet Aykin-Burns,Matthew C. Zimmerman,Kathy Zimmerman,Amy-Joan L. Ham,Robert M. Weiss,Douglas R. Spitz,Madeline A. Shea,Roger J. Colbran,Peter J. Mohler,Mark E. Anderson +18 more
TL;DR: It is shown that oxidation of paired regulatory domain methionine residues sustains CaMKII activity in the absence of Ca2+/CaM and highlights the critical importance of oxidation-dependent CaMK II activation to AngII and ischemic myocardial apoptosis.
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Repeatability and Reproducibility in Proteomic Identifications by Liquid Chromatography−Tandem Mass Spectrometry
David L. Tabb,Lorenzo Vega-Montoto,Lorenzo Vega-Montoto,Paul A. Rudnick,Asokan Mulayath Variyath,Asokan Mulayath Variyath,Amy-Joan L. Ham,David M. Bunk,Lisa E. Kilpatrick,Dean Billheimer,Ronald K. Blackman,Helene L. Cardasis,Helene L. Cardasis,Steven A. Carr,Karl R. Clauser,Jacob D. Jaffe,Kevin A. Kowalski,Thomas A. Neubert,Fred E. Regnier,Birgit Schilling,Tony J. Tegeler,Mu Wang,Pei Wang,Jeffrey R. Whiteaker,Lisa J. Zimmerman,Susan J. Fisher,Bradford W. Gibson,Christopher R. Kinsinger,Mehdi Mesri,Henry Rodriguez,Stephen E. Stein,Paul Tempst,Amanda G. Paulovich,Daniel C. Liebler,Cliff Spiegelman +34 more
TL;DR: The most repeatable peptides were those corresponding to conventional tryptic cleavage sites, those that produced intense MS signals, and those that resulted from proteins generating many distinct peptides.
Journal ArticleDOI
Proteomic Analysis of Exosomes from Mutant KRAS Colon Cancer Cells Identifies Intercellular Transfer of Mutant KRAS
Michelle Demory Beckler,James N. Higginbotham,Jeffrey L. Franklin,Jeffrey L. Franklin,Amy-Joan L. Ham,Patrick J. Halvey,Imade E. Imasuen,Corbin W. Whitwell,Ming Li,Daniel C. Liebler,Robert J. Coffey,Robert J. Coffey +11 more
TL;DR: A comprehensive proteomic analysis of exosomes from parental DLD-1 cells that contain both wild-type and G13D mutant KRAS alleles and isogenically matched derivative cell lines, DKO-1 (mutant KRAS allele only) and DKs-8 (wild-type KRas allele only), showing Mutant KRAS status dramatically affects the composition of the exosome proteome.
Journal ArticleDOI
Sample preparation and digestion for proteomic analyses using spin filters
TL;DR: The use of commercially available microcentrifugation devices (spin filters) for cleanup and digestion of protein samples for mass spectrometry analyses provides digestion efficiencies comparable to standard in‐solution digests, avoids lengthy dialysis steps, and allows rapid cleanup of samples containing salts, some detergents, and acidic or basic buffers.