The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Direct Profiling of Proteins in Biological Tissue Sections by MALDI Mass Spectrometry
Abstract
The direct profiling of proteins present in tissue sections for several organs of the mouse has been accomplished using matrix-assisted laser desorption ionization (MALDI) mass spectrometry (MS). Fresh tissue was sectioned and blotted on a conductive polyethylene membrane. The dried membrane blot was coated with matrix, typically sinapinic acid, and directly analyzed in the mass spectrometer. Generally, well over 100 peptide/protein signals in the 2000-30,000 Da range were observed, with 30-50 having relatively high signal intensities. Analysis of different areas of the same tissue gave remarkably similar mass spectra with greater than 90% homology. However, different parts of a segmented tissue, such as the proximal, intermediate, and distal colon, gave some unique protein signals. After treatment of the tissue blot with protease and subsequent MALDI MS analysis using postsource decay methods for peptide sequencing, some of the proteins were identified. The unique protein profiles measured from these tissue blots also showed differences from strain to strain of the mouse, with genetically similar strains having very similar patterns.
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
Molecular Imaging of Biological Samples: Localization of Peptides and Proteins Using MALDI-TOF MS
Caprioli, R. M., Farmer, T. B., & Gile, J. (1997) · Analytical Chemistry · doi:10.1021/ac970888i · Cited by 2,234
Self-citation
Cited by
The Desorption Process in MALDI
Dreisewerd, K. (2003) · Chemical Reviews · doi:10.1021/cr010375i · Cited by 709
Lemaire, K., Ravier, M. A., Schraenen, A., Creemers, J. W. M., Van de Plas, R., Granvik, M., Van Lommel, L., Waelkens, E., Chimienti, F., Rutter, G. A., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0906587106 · Cited by 330
Stoeckli, M., Staab, D., & Schweitzer, A. (2007) · International Journal of Mass Spectrometry · doi:10.1016/j.ijms.2006.10.007 · Cited by 295
Self-citationMethods for samples preparation in proteomic research
Bodzon-Kulakowska, A., Bierczynska-Krzysik, A., Dylag, T., Drabik, A., Suder, P., Noga, M., Jarzebinska, J., & Silberring, J. (2007) · Journal of Chromatography B · doi:10.1016/j.jchromb.2006.10.040 · Cited by 254
Proteomics in Diagnostic Pathology
Chaurand, P., Sanders, M. E., Jensen, R. A., & Caprioli, R. M. (2004) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)63367-6 · Cited by 253
Self-citation
Metadata
- Authors
- Chaurand, P., Stoeckli, M., & Caprioli, R. M.
- Venue
- Analytical Chemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 1999-10-29
- Volume
- 71
- Issue
- 23
- Pages
- 5263-5270
- ISSN
- 0003-2700 (ISSN-L)
- 1520-6882
- OpenAlex
- W1970209157
- Cited by
- 282
- References
- 1
- FWCI
- 6.40
- 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
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: Direct Profiling of Proteins in Biological Tissue Sections by MALDI Mass Spectrometry. https://app.cochat.ai/papers/10.1021/ac990781q
- The paper
- Chaurand, P., Stoeckli, M., & Caprioli, R. M. (1999). Direct Profiling of Proteins in Biological Tissue Sections by MALDI Mass Spectrometry. Analytical Chemistry. https://doi.org/10.1021/ac990781q
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.
