The DOI matches its Crossref record; 29 of the 29 references it cites were found in a registry or an index.
Electron Capture Dissociation for Structural Characterization of Multiply Charged Protein Cations
Abstract
For proteins of < 20 kDa, this new radical site dissociation method cleaves different and many more backbone bonds than the conventional MS/MS methods (e.g., collisionally activated dissociation, CAD) that add energy directly to the even-electron ions. A minimum kinetic energy difference between the electron and ion maximizes capture; a 1 eV difference reduces capture by 10(3). Thus, in an FTMS ion cell with added electron trapping electrodes, capture appears to be achieved best at the boundary between the potential wells that trap the electrons and ions, now providing 80 +/- 15% precursor ion conversion efficiency. Capture cross section is dependent on the ionic charge squared (z2), minimizing the secondary dissociation of lower charge fragment ions. Electron capture is postulated to occur initially at a protonated site to release an energetic (approximately 6 eV) H. atom that is captured at a high-affinity site such as -S-S- or backbone amide to cause nonergodic (before energy randomization) dissociation. Cleavages between every pair of amino acids in mellitin (2.8 kDa) and ubiquitin (8.6 kDa) are represented in their ECD and CAD spectra, providing complete data for their de novo sequencing. Because posttranslational modifications such as carboxylation, glycosylation, and sulfation are less easily lost in ECD than in CAD, ECD assignments of their sequence positions are far more specific.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Electron Capture Dissociation of Multiply Charged Protein Cations. A Nonergodic Process
Zubarev, R. A., Kelleher, N. L., & McLafferty, F. W. (1998) · Journal of the American Chemical Society · doi:10.1021/ja973478k · Cited by 1,881
Self-citationInt. J. Mass Spectrom. Ion Processes
(1990) · International Journal of Mass Spectrometry and Ion Processes · doi:10.1016/0168-1176(90)80022-u · Cited by 1,003
INTERPRETATION OF MASS SPECTRA
(1992) · Analytical Chemistry · doi:10.1021/ac00037a717 · Cited by 944
Collision phenomena in ionized gases
Stewart, A. L. (1965) · Planetary and Space Science · doi:10.1016/0032-0633(65)90106-6 · Cited by 863
Infrared Multiphoton Dissociation of Large Multiply Charged Ions for Biomolecule Sequencing
Little, D. P., Speir, J. P., Senko, M. W., O'Connor, P. B., & McLafferty, F. W. (1994) · Analytical Chemistry · doi:10.1021/ac00090a004 · Cited by 753
Self-citationGauthier, J. W., Trautman, T. R., & Jacobson, D. B. (1991) · Analytica Chimica Acta · doi:10.1016/s0003-2670(00)80678-9 · Cited by 645
Tailored excitation for Fourier transform ion cyclotron mass spectrometry
Marshall, A. G., Wang, T. C. L., & Ricca, T. L. (1985) · Journal of the American Chemical Society · doi:10.1021/ja00312a015 · Cited by 631
Zubarev, R. A., Kruger, N. A., Fridriksson, E. K., Lewis, M. A., Horn, D. M., Carpenter, B. K., & McLafferty, F. W. (1999) · Journal of the American Chemical Society · doi:10.1021/ja981948k · Cited by 557
Self-citationAttomole Protein Characterization by Capillary Electrophoresis-Mass Spectrometry
Valaskovic, G. A., Kelleher, N. L., & McLafferty, F. W. (1996) · Science · doi:10.1126/science.273.5279.1199 · Cited by 398
Self-citationMirgorodskaya, E., Roepstorff, P., & Zubarev, R. A. (1999) · Analytical Chemistry · doi:10.1021/ac990578v · Cited by 381
Self-citationKelleher, N. L., Zubarev, R. A., Bush, K., Furie, B., Furie, B. C., McLafferty, F. W., & Walsh, C. T. (1999) · Analytical Chemistry · doi:10.1021/ac990684x · Cited by 368
Self-citationTandem Mass Spectrometry of Large Biomolecule Ions by Blackbody Infrared Radiative Dissociation
Price, W. D., Schnier, P. D., & Williams, E. R. (1996) · Analytical Chemistry · doi:10.1021/ac951038a · Cited by 314
Postseismic Rebound in Fault Step-Overs Caused by Pore Fluid Flow
Peltzer, G., Rosen, P., Rogez, F., & Hudnut, K. (1996) · Science · doi:10.1126/science.273.5279.1202 · Cited by 290
Jensen, P. K., Paša-Tolić, L., Anderson, G. A., Horner, J. A., Lipton, M. S., Bruce, J. E., & Smith, R. D. (1999) · Analytical Chemistry · doi:10.1021/ac990196p · Cited by 231
Schnier, P. D., Gross, D. S., & Williams, E. R. (1995) · Journal of the American Chemical Society · doi:10.1021/ja00130a015 · Cited by 216
High-resolution tandem FT mass spectrometry above 10 kDa
McLafferty, F. W. (1994) · Accounts of Chemical Research · doi:10.1021/ar00047a009 · Cited by 194
Self-citationMcLafferty, F. W., Fridriksson, E. K., Horn, D. M., Lewis, M. A., & Zubarev, R. A. (1999) · Science · doi:10.1126/science.284.5418.1289 · Cited by 166
Self-citationSequence Information from 42−108-mer DNAs (Complete for a 50-mer) by Tandem Mass Spectrometry
Little, D. P., Aaserud, D. J., Valaskovic, G. A., & McLafferty, F. W. (1996) · Journal of the American Chemical Society · doi:10.1021/ja9533611 · Cited by 145
Self-citationThe barrier to internal rotation in ethane
Pitzer, R. M. (1983) · Accounts of Chemical Research · doi:10.1021/ar00090a004 · Cited by 129
Andersen, J., Svensson, B., & Roepstorff, P. (1996) · Nature Biotechnology · doi:10.1038/nbt0496-449 · Cited by 113
High‐resolution tandem mass spectra of 37‐67 kDa proteins
Speir, J. P., Senko, M. W., Little, D. P., Loo, J. A., & McLafferty, F. W. (1995) · Journal of Mass Spectrometry · doi:10.1002/jms.1190300108 · Cited by 86
Self-citationSurface-Induced Dissociation of Multiply Protonated Peptides
McCormack, A. L., Jones, J., & Wysocki, V. H. (1992) · Journal of the American Society for Mass Spectrometry · doi:10.1016/1044-0305(92)80010-i · Cited by 81
Schnier, P. D., Jurchen, J. C., & Williams, E. R. (1999) · The Journal of Physical Chemistry B · doi:10.1021/jp9833193 · Cited by 60
Chen, X., Asmar, F., Wang, H., & Weiner, B. R. (1991) · The Journal of Physical Chemistry · doi:10.1021/j100170a007 · Cited by 55
Negative ions, mass selection, and photoelectrons
Boesl, U., & Knott, W. J. (1998) · Mass Spectrometry Reviews · Cited by 38
Two-dimensional mass spectrometry of biomolecules at the subfemtomole level
McLafferty, F. W., Kelleher, N. L., Begley, T. P., Fridriksson, E. K., Zubarev, R. A., & Horn, D. M. (1998) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(98)80085-9 · Cited by 34
Self-citationRowe, B. R., Mitchell, J. B., & Canosa, A. (1993) · NATO ASI series. Series B : Physics · doi:10.1007/978-1-4615-2976-7 · Cited by 34
Determination of organosulfur compounds extracted from marine sediments
Bates, T. S., & Carpenter, R. (1979) · Analytical Chemistry · doi:10.1021/ac50040a023 · Cited by 26
Enhanced specificity for aromatics using 2e mass spectrometry
Robinson, M., Bostwick, D. E., Abbey, L. E., et al. (1988) · Rapid Communications in Mass Spectrometry · doi:10.1002/rcm.1290021007 · Cited by 23
Cited by
Peptide and protein sequence analysis by electron transfer dissociation mass spectrometry
Syka, J. E. P., Coon, J. J., Schroeder, M. J., Shabanowitz, J., & Hunt, D. F. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0402700101 · Cited by 2,370
Mass Spectrometry in Proteomics
Aebersold, R., & Goodlett, D. R. (2001) · Chemical Reviews · doi:10.1021/cr990076h · Cited by 1,238
Multivalent engagement of chromatin modifications by linked binding modules
Ruthenburg, A. J., Li, H., Patel, D. J., & David Allis, C. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2298 · Cited by 1,013
Automated reduction and interpretation of
Horn, D. M., Zubarev, R. A., & McLafferty, F. W. (2000) · Journal of the American Society for Mass Spectrometry · doi:10.1016/s1044-0305(99)00157-9 · Cited by 507
Self-citationPrecision proteomics: The case for high resolution and high mass accuracy
Mann, M., & Kelleher, N. L. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0800788105 · Cited by 450
Self-citation
Metadata
- Authors
- Zubarev, R. A., Horn, D. M., Fridriksson, E. K., Kelleher, N. L., Kruger, N. A., Lewis, M. A., Carpenter, B. K., & McLafferty, F. W.
- Venue
- Analytical Chemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 2000-01-05
- Volume
- 72
- Issue
- 3
- Pages
- 563-573
- ISSN
- 0003-2700 (ISSN-L)
- 1520-6882
- OpenAlex
- W2048527293
- Cited by
- 986
- References
- 29
- FWCI
- 20.27
- Type
- journal article
- Language
- en
- Open access
- closed
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
