High-Performance Mass Spectrometry: Fourier Transform Ion Cyclotron Resonance at 14.5 Tesla

Schaub, Tanner; Hendrickson, Christopher L.; Horning, Stevan; Quinn, John; Senko, Michael W.; Marshall, Alan G.

doi:10.1021/ac800386h

Cited by 186 publications

(219 citation statements)

References 38 publications

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“…HDX was quenched by 1:1 (vol/vol) addition of protease type XIII solution in 1.0% formic acid. Microelectrosprayed (21) HDX samples were directed to a custom-built hybrid linear trap quadrupole 14.5-Tesla FT-ICR mass spectrometer (22). Data were analyzed by using an in-house analysis package.…”

Section: Hdx Fourier Transform Ion Cyclotron Resonance (Ft-icr) Mass mentioning

confidence: 99%

KIT kinase mutants show unique mechanisms of drug resistance to imatinib and sunitinib in gastrointestinal stromal tumor patients

Gajiwala

Christensen

et al. 2009

Proc. Natl. Acad. Sci. U.S.A.

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344

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Most gastrointestinal stromal tumors (GISTs) exhibit aberrant activation of the receptor tyrosine kinase (RTK) KIT. The efficacy of the inhibitors imatinib mesylate and sunitinib malate in GIST patients has been linked to their inhibition of these mutant KIT proteins. However, patients on imatinib can acquire secondary KIT mutations that render the protein insensitive to the inhibitor. Sunitinib has shown efficacy against certain imatinib-resistant mutants, although a subset that resides in the activation loop, including D816H/V, remains resistant. Biochemical and structural studies were undertaken to determine the molecular basis of sunitinib resistance. Our results show that sunitinib targets the autoinhibited conformation of WT KIT and that the D816H mutant undergoes a shift in conformational equilibrium toward the active state. These findings provide a structural and enzymologic explanation for the resistance profile observed with the KIT inhibitors. Prospectively, they have implications for understanding oncogenic kinase mutants and for circumventing drug resistance.kinase inhibitor ͉ signal transduction ͉ targeted therapy ͉ resistance mechanism ͉ cancer

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Section: Hdx Fourier Transform Ion Cyclotron Resonance (Ft-icr) Mass mentioning

confidence: 99%

KIT kinase mutants show unique mechanisms of drug resistance to imatinib and sunitinib in gastrointestinal stromal tumor patients

Gajiwala

Christensen

et al. 2009

Proc. Natl. Acad. Sci. U.S.A.

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344

315

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“…After ionization, the sample was introduced into a custombuilt hybrid LTQ 14.5 T FT-ICR mass spectrometer (Thermo Fisher Scientific) (20). Over a period of 6.5 min, 319 mass spectra were collected from m/z 400 to 1,300, at high mass resolving power (m/⌬m 50% ϭ 200,000 at m/z 400, in which ⌬m 50% is the peak full width at half-maximum peak height).…”

Section: Hdx and Liquid Chromatography (Lc)-electrospray Ionization mentioning

confidence: 99%

The N-terminal Domain of Escherichia coli Assimilatory NADPH-Sulfite Reductase Hemoprotein Is an Oligomerization Domain That Mediates Holoenzyme Assembly

Askenasy

Pennington

Tao

et al. 2015

Journal of Biological Chemistry

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Background: Assimilatory NADPH-sulfite reductase (SiR) is an essential metalloenzyme for sulfur metabolism made from two subunits. Results: We defined how the subunits of SiR assemble, with or without cofactors. Conclusion: One region of the metalloenzyme interacted either with its reductase partner when cofactors were formed or with itself when they were not. Significance: We propose a novel mechanism to regulate SiR assembly.

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“…However, the ''database congestion'' for larger peptides (Ͼ2 kDa) eases somewhat to often rule out all but one peptide sequence given the measured mass, at least for unmodified peptides. Model experiments have already indicated the potential for low ppb accuracy (27). Measurements around 30 ppb may soon become routine for well defined peaks.…”

Section: On a Fourier Transform Instrument At High Resolution (B) (Imentioning

confidence: 99%

Precision proteomics: The case for high resolution and high mass accuracy

Mann

Kelleher

2008

Proc. Natl. Acad. Sci. U.S.A.

408

354

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Proteomics has progressed radically in the last 5 years and is now on par with most genomic technologies in throughput and comprehensiveness. Analyzing peptide mixtures by liquid chromatography coupled to high-resolution mass spectrometry (LC-MS) has emerged as the main technology for in-depth proteome analysis whereas two-dimensional gel electrophoresis, low-resolution MALDI, and protein arrays are playing niche roles. MS-based proteomics is rapidly becoming quantitative through both label-free and stable isotope labeling technologies. The latest generation of mass spectrometers combines extremely high resolving power, mass accuracy, and very high sequencing speed in routine proteomic applications. Peptide fragmentation is mostly performed in lowresolution but very sensitive and fast linear ion traps. However, alternative fragmentation methods and high-resolution fragment analysis are becoming much more practical. Recent advances in computational proteomics are removing the data analysis bottleneck. Thus, in a few specialized laboratories, ''precision proteomics'' can now identify and quantify almost all fragmented peptide peaks. Huge challenges and opportunities remain in technology development for proteomics; thus, this is not ''the beginning of the end'' but surely ''the end of the beginning.''

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High-Performance Mass Spectrometry: Fourier Transform Ion Cyclotron Resonance at 14.5 Tesla

Cited by 186 publications

References 38 publications

KIT kinase mutants show unique mechanisms of drug resistance to imatinib and sunitinib in gastrointestinal stromal tumor patients

KIT kinase mutants show unique mechanisms of drug resistance to imatinib and sunitinib in gastrointestinal stromal tumor patients

The N-terminal Domain of Escherichia coli Assimilatory NADPH-Sulfite Reductase Hemoprotein Is an Oligomerization Domain That Mediates Holoenzyme Assembly

Precision proteomics: The case for high resolution and high mass accuracy

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