The DOI matches its Crossref record; 13 of the 13 references it cites were found in a registry or an index.
Profiling Serine Hydrolase Activities in Complex Proteomes
Abstract
Serine hydrolases represent one of the largest and most diverse families of enzymes in higher eukaryotes, comprising numerous proteases, lipases, esterases, and amidases. The activities of many serine hydrolases are tightly regulated by posttranslational mechanisms, limiting the suitability of standard genomics and proteomics methods for the functional characterization of these enzymes. To facilitate the global analysis of serine hydrolase activities in complex proteomes, a biotinylated fluorophosphonate (FP-biotin) was recently synthesized and shown to serve as an activity-based probe for several members of this enzyme family. However, the extent to which FP-biotin reacts with the complete repertoire of active serine hydrolases present in a given proteome remains largely unexplored. Herein, we describe the synthesis and utility of a variant of FP-biotin in which the agent's hydrophobic alkyl chain linker was replaced by a more hydrophilic poly(ethylene glycol) moiety (FP-peg-biotin). When incubated with both soluble and membrane proteomes for extended reaction times, FP-biotin and FP-peg-biotin generated similar "maximal coverage" serine hydrolase activity profiles. However, kinetic analyses revealed that several serine hydrolases reacted at different rates with each FP agent. These rate differences were exploited in studies that used the biotinylated FPs to examine the target selectivity of reversible serine hydrolase inhibitors directly in complex proteomes. Finally, a general method for the avidin-based affinity isolation of FP-biotinylated proteins was developed, permitting the rapid and simultaneous identification of multiple serine peptidases, lipases, and esterases. Collectively, these studies demonstrate that chemical probes such as the biotinylated FPs can greatly accelerate both the functional characterization and molecular identification of active enzymes in complex proteomes.
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
Proteins: Structures and Molecular Properties
Creighton, T. E. (1986) · Medical Entomology and Zoology · Cited by 2,645
Molecular characterization of an enzyme that degrades neuromodulatory fatty-acid amides
Cravatt, B. F., Giang, D. K., Mayfield, S. P., Boger, D. L., Lerner, R. A., & Gilula, N. B. (1996) · Nature · doi:10.1038/384083a0 · Cited by 2,125
Self-citationProtease Inhibitors: Current Status and Future Prospects
Leung, D., Abbenante, G., & Fairlie, D. P. (2000) · Journal of Medicinal Chemistry · doi:10.1021/jm990412m · Cited by 883
Steiner, D. F. (1998) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(98)80033-1 · Cited by 650
A nucleotide-flipping mechanism from the structure of human uracil–DNA glycosylase bound to DNA
Slupphaug, G., Mol, C. D., Kavli, B., Arvai, A. S., Krokan, H. E., & Tainer, J. A. (1996) · Nature · doi:10.1038/384087a0 · Cited by 581
Multiple species of CPP32 and Mch2 are the major active caspases present in apoptotic cells
Faleiro, L., Kobayashi, R., Fearnhead, H., & Lazebnik, Y. (1997) · The EMBO Journal · doi:10.1093/emboj/16.9.2271 · Cited by 357
Ueda, N., Kurahashi, Y., Yamamoto, S., & Tokunaga, T. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.40.23823 · Cited by 303
Maurelli, S., Bisogno, T., De Petrocellis, L., Di Luccia, A., Marino, G., & Di Marzo, V. (1995) · FEBS Letters · doi:10.1016/0014-5793(95)01311-3 · Cited by 199
An atlas of serpin conformations
Whisstock, J., Skinner, R., & Lesk, A. M. (1998) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(97)01172-9 · Cited by 192
The Regulation of Clotting Factors
Kalafatis, M., Egan, J. O., Veer, C. V., Cawthern, K. M., & Mann, K. G. (1997) · Critical Reviews in Eukaryotic Gene Expression · doi:10.1615/critreveukargeneexpr.v7.i3.40 · Cited by 138
Patterson, J. E., Ollmann, I. R., Cravatt, B. F., Boger, D. L., Wong, C. H., & Lerner, R. A. (1996) · Journal of the American Chemical Society · doi:10.1021/ja954064z · Cited by 116
Self-citationRegulation and Regulatory Role of Proteinase Inhibitors
Roberts, R. M., Mathialagan, N., Duffy, J. Y., & Smith, G. W. (1995) · Critical Reviews in Eukaryotic Gene Expression · doi:10.1615/critreveukargeneexpr.v5.i3-4.80 · Cited by 90
Peptidomimetic Inhibitors of the Human Cytomegalovirus Protease
Ogilvie, W. W., Bailey, M. D., Poupart, M., et al. (1997) · Journal of Medicinal Chemistry · doi:10.1021/jm970104t · Cited by 85
Cited by
Activity-Based Protein Profiling: From Enzyme Chemistry to Proteomic Chemistry
Cravatt, B. F., Wright, A. T., & Kozarich, J. W. (2008) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.75.101304.124125 · Cited by 1,270
Self-citationMonoacylglycerol lipase regulates a fatty acid network that promotes cancer pathogenesis
Nomura, D. K., Long, J. Z., Niessen, S., Hoover, H. S., Ng, S.-W., & Cravatt, B. F. (2010) · Cell · doi:10.1016/j.cell.2009.11.027 · Cited by 1,002
Self-citationProteomics: the first decade and beyond
Patterson, S. D., & Aebersold, R. H. (2003) · Nature Genetics · doi:10.1038/ng1106 · Cited by 745
Structure and function of fatty acid amide hydrolase
McKinney, M. K., & Cravatt, B. F. (2005) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.74.082803.133450 · Cited by 680
Self-citationProtein analysis on a proteomic scale
Phizicky, E., Bastiaens, P. I. H., Zhu, H., Snyder, M., & Fields, S. (2003) · Nature · doi:10.1038/nature01512 · Cited by 629
Metadata
- Authors
- Kidd, D., Liu, Y., & Cravatt, B. F.
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 2001-03-08
- Volume
- 40
- Issue
- 13
- Pages
- 4005-4015
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W2028185344
- Cited by
- 368
- References
- 13
- FWCI
- 11.20
- 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.
