The DOI matches its Crossref record; 30 of the 30 references it cites were found in a registry or an index.
Immobilized Gallium(III) Affinity Chromatography of Phosphopeptides
Abstract
A novel procedure for micropurification of phosphorylated peptides, as a front end to mass spectrometric analysis, is described. As a result of a systematic study, we propose the use of an immobilized metal affinity chromatography (IMAC) in a microtip (Erdjument-Bromage, H.; et al. J. Chromatogr., A 1998, 826, 167-181) format, more specifically in combination with Ga(III) ions. Manual Ga-(III) IMAC is easy to perform; phosphopeptides are retrieved in a near-quantitative and highly selective manner, to yield a concentrated sample for direct analysis by matrix-assisted laser desorption/ionization time-of-flight and nanoelectrospray ionization mass spectrometry. Ga-(III) ions offer distinct advantages over the use of other metals, such as Fe(III) and Al(III), in terms of both selectivity and versatility, including facile base elution. Selectivity is best illustrated by effective enrichment of phosphopeptides that were present in a molar ratio of approximately 2% on a background of unphosphorylated protein, a situation very typical perhaps for protein phosphorylation states in the cell. The system was also used to retrieve and tentatively identify five previously uncharacterized phosphopeptides from a tryptic digest of human beta 4 integrin, isolated from cell extracts by immunoprecipitation.
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
Exploring the Metabolic and Genetic Control of Gene Expression on a Genomic Scale
DeRisi, J. L., Iyer, V. R., & Brown, P. O. (1997) · Science · doi:10.1126/science.278.5338.680 · Cited by 4,456
Mechanism of activation of protein kinase B by insulin and IGF-1.
Alessi, D. R., Andjelkovic, M., Caudwell, B., Cron, P., Morrice, N., Cohen, P., & Hemmings, B. A. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb01045.x · Cited by 3,004
Signaling Through Scaffold, Anchoring, and Adaptor Proteins
Pawson, T., & Scott, J. D. (1997) · Science · doi:10.1126/science.278.5346.2075 · Cited by 2,256
Error-Tolerant Identification of Peptides in Sequence Databases by Peptide Sequence Tags
Mann, M., & Wilm, M. (1994) · Analytical Chemistry · doi:10.1021/ac00096a002 · Cited by 1,468
Henzel, W. J., Billeci, T. M., Stults, J. T., Wong, S. C., Grimley, C., & Watanabe, C. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.11.5011 · Cited by 1,305
Use of mass spectrometric molecular weight information to identify proteins in sequence databases
Mann, M., Højrup, P., & Roepstorff, P. (1993) · Biological Mass Spectrometry · doi:10.1002/bms.1200220605 · Cited by 931
Isolation of phosphoproteins by immobilized metal (Fe3+) affinity chromatography
Andersson, L., & Porath, J. (1986) · Analytical Biochemistry · doi:10.1016/0003-2697(86)90523-3 · Cited by 774
Peptide Mass Maps: A Highly Informative Approach to Protein Identification
Yates, J. R., Speicher, S., Griffin, P. R., & Hunkapiller, T. (1993) · Analytical Biochemistry · doi:10.1006/abio.1993.1514 · Cited by 676
Structural basis for activation of the titin kinase domain during myofibrillogenesis
Mayans, O., van der Ven, P. F. M., Wilm, M., Mues, A., Young, P., Fürst, D. O., Wilmanns, M., & Gautel, M. (1998) · Nature · doi:10.1038/27603 · Cited by 361
Brain Regions Responsive to Novelty in the Absence of Awareness
Berns, G. S., Cohen, J. D., & Mintun, M. A. (1997) · Science · doi:10.1126/science.276.5316.1272 · Cited by 361
Phosphate groups as substrate determinants for casein kinase I action.
Flotow, H., Graves, P. R., Wang, A. Q., Fiol, C. J., Roeske, R. W., & Roach, P. J. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)77295-5 · Cited by 337
Large-Cage Zeolite Structures with Multidimensional 12-Ring Channels
Bu, X., Feng, P., & Stucky, G. D. (1997) · Science · doi:10.1126/science.278.5346.2080 · Cited by 329
Phosphopeptide Analysis by Matrix-Assisted Laser Desorption Time-of-Flight Mass Spectrometry
Annan, R. S., & Carr, S. A. (1996) · Analytical Chemistry · doi:10.1021/ac960221g · Cited by 310
Fragmentation of phosphopeptides in an ion trap mass spectrometer
DeGnore, J. P., & Qin, J. (1998) · Journal of the American Society for Mass Spectrometry · doi:10.1016/s1044-0305(98)00088-9 · Cited by 257
Huddleston, M. J., Annan, R. S., Bean, M. F., & Carr, S. A. (1993) · Journal of the American Society for Mass Spectrometry · doi:10.1016/1044-0305(93)80049-5 · Cited by 242
Neubauer, G., & Mann, M. (1999) · Analytical Chemistry · doi:10.1021/ac9804902 · Cited by 232
Mainiero, F., Pepe, A., Wary, K. K., Spinardi, L., Mohammadi, M., Schlessinger, J., & Giancotti, F. G. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb00126.x · Cited by 215
Erdjument-Bromage, H., Lui, M., Lacomis, L., Grewal, A., Annan, R. S., McNulty, D. E., Carr, S. A., & Tempst, P. (1998) · Journal of Chromatography A · doi:10.1016/s0021-9673(98)00705-5 · Cited by 211
Self-citationIdentification of phosphorylated sites in the mouse glucocorticoid receptor.
Bodwell, J. E., Ortí, E., Coull, J. M., Pappin, D. J., Smith, L. I., & Swift, F. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)89482-4 · Cited by 202
The intracellular functions of alpha6beta4 integrin are regulated by EGF.
Mainiero, F., Pepe, A., Yeon, M., Ren, Y., & Giancotti, F. G. (1996) · The Journal of cell biology · doi:10.1083/jcb.134.1.241 · Cited by 185
Wisniewski, D., Strife, A., Swendeman, S., Erdjument-Bromage, H., Geromanos, S., Kavanaugh, W. M., Tempst, P., & Clarkson, B. (1999) · Blood · doi:10.1182/blood.v93.8.2707 · Cited by 162
Self-citationModel studies on iron(III) ion affinity chromatography
Muszyńska, G., Dobrowolska, G., Medin, A. S., Medin, A. S., Ekman, P., & Porath, J. O. (1992) · Journal of Chromatography A · doi:10.1016/0021-9673(92)85524-w · Cited by 110
Identification of the phosphorylation site of an 8.3 kDa protein from photosystem II of spinach
Michel, H., & Bennett, J. (1987) · FEBS Letters · doi:10.1016/0014-5793(87)81565-x · Cited by 107
Chapline, C., Cottom, J. E., Tobin, H., Hulmes, J. D., Crabb, J. W., & Jaken, S. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.31.19482 · Cited by 86
Betts, J. C., Blackstock, W. P., Ward, M. A., & Anderton, B. H. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.20.12922 · Cited by 60
Affolter, M., Watts, J. D., Krebs, D. L., et al. (1994) · Analytical Biochemistry · doi:10.1006/abio.1994.1549 · Cited by 50
Immobilized Fe3+ affinity chromatographic isolation of phosphopeptides
Scanff, P., Yvon, M., & Pélissier, J. P. (1991) · Journal of Chromatography A · doi:10.1016/s0021-9673(01)83951-0 · Cited by 48
LC/MS and LC/MS/MS Screening for the Sites of Post-Translational Modification in Proteins
Covey, T. R., Shushan, B. I., Bonner, R. F., Schröder, W., & Hucho, F. (1991) · Birkhäuser Basel eBooks · doi:10.1007/978-3-0348-5678-2_25 · Cited by 46
Recognition of phosphate groups by immobilized aluminium(III) ions
Andersson, L. (1991) · Journal of Chromatography A · doi:10.1016/s0021-9673(01)83941-8 · Cited by 40
InJection adaptable Fine Ionization Source (‘JaFIS’) for continuous flow nano‐electrospray
Geromanos, S. J., Philip, J., Freckleton, G., & Tempst, P. (1998) · Rapid Communications in Mass Spectrometry · doi:10.1002/(sici)1097-0231(19980515)12:9<551::aid-rcm198>3.0.co;2-y · Cited by 32
Self-citation
Cited by
Protein Analysis by Shotgun/Bottom-up Proteomics
Zhang, Y., Fonslow, B. R., Shan, B., Baek, M.-C., & Yates, J. R. (2013) · Chemical Reviews · doi:10.1021/cr3003533 · Cited by 1,491
Phosphorylation and Functional Inactivation of TSC2 by Erk
Ma, L., Chen, Z., Erdjument-Bromage, H., Tempst, P., & Pandolfi, P. P. (2005) · Cell · doi:10.1016/j.cell.2005.02.031 · Cited by 1,268
Self-citationPinkse, M. W. H., Uitto, P. M., Hilhorst, M. J., Ooms, B., & Heck, A. J. R. (2004) · Analytical Chemistry · doi:10.1021/ac0498617 · Cited by 891
Proteomics: the first decade and beyond
Patterson, S. D., & Aebersold, R. H. (2003) · Nature Genetics · doi:10.1038/ng1106 · Cited by 745
Interpreting the protein language using proteomics
Jensen, O. N. (2006) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1939 · Cited by 502
Metadata
- Authors
- Posewitz, M. C., & Tempst, P.
- Venue
- Analytical Chemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 1999-06-10
- Volume
- 71
- Issue
- 14
- Pages
- 2883-2892
- ISSN
- 0003-2700 (ISSN-L)
- 1520-6882
- OpenAlex
- W1996693787
- Cited by
- 832
- References
- 30
- FWCI
- 14.50
- 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.
