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The Metabolic Serine Hydrolases and Their Functions in Mammalian Physiology and Disease
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ADVERTISEMENT RETURN TO ISSUEPREVReviewNEXTThe Metabolic Serine Hydrolases and Their Functions in Mammalian Physiology and DiseaseJonathan Z. Long* and Benjamin F. Cravatt*View Author Information The Skaggs Institute for Chemical Biology and Department of Chemical Physiology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037, United StatesE-mail: [email protected] (J.Z.L); [email protected] (B.F.C.).Cite this: Chem. Rev. 2011, 111, 10, 6022–6063Publication Date (Web):June 23, 2011Publication History Received10 March 2011Published online23 June 2011Published inissue 12 October 2011https://pubs.acs.org/doi/10.1021/cr200075yhttps://doi.org/10.1021/cr200075yreview-articleACS PublicationsCopyright © 2011 American Chemical SocietyRequest reuse permissionsArticle Views7111Altmetric-Citations309LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InRedditEmail Other access optionsGet e-Alertsclose SUBJECTS:Anatomy,Inhibitors,Lipids,Peptides and proteins,Rodent models Get e-Alerts
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Items 401–525 of 525
Manya, H., Aoki, J., Kato, H., Ishii, J., Hino, S., Arai, H., & Inoue, K. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.45.31827 · Cited by 69
Lysophospholipase I identified as a ghrelin deacylation enzyme in rat stomach
Shanado, Y., Kometani, M., Uchiyama, H., Koizumi, S., & Teno, N. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.10.193 · Cited by 68
Maes, M., Lambeir, A., Gilany, K., Senten, K., der Veken, P. V., Leiting, B., Augustyns, K., Scharpé, S., & Meester, I. D. (2005) · Biochemical Journal · doi:10.1042/bj20041156 · Cited by 68
Expression of Oncogenic Antigen 519 (OA-519) in Prostate Cancer Is a Potential Prognostic Indicator
Shurbaji, M. S., Kuhajda, F. P., Pasternack, G. R., & Thurmond, T. S. (1992) · American Journal of Clinical Pathology · doi:10.1093/ajcp/97.5.686 · Cited by 67
Role of a serum phospholipase A1in the phosphatidylserine‐induced T cell inhibition
Bellini, F., & Bruni, A. (1993) · FEBS Letters · doi:10.1016/0014-5793(93)81724-e · Cited by 67
Paradis, É., Clavel, S., Julien, P., Murthy, M. R. V., de Bilbao, F., Arsenijevic, D., Giannakopoulos, P., Vallet, P., & Richard, D. (2004) · Neurobiology of Disease · doi:10.1016/j.nbd.2003.09.017 · Cited by 67
Kirby, R. J., Zheng, S., Tso, P., Howles, P. N., & Hui, D. Y. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m107549200 · Cited by 67
Ameis, D., Kobayashi, J., Davis, R. C., Ben-Zeev, O., Malloy, M. J., Kane, J. P., Lee, G., Wong, H., Havel, R. J., & Schotz, M. C. (1991) · Journal of Clinical Investigation · doi:10.1172/jci115114 · Cited by 66
Thioesterase activity and subcellular localization of acylprotein thioesterase 1/lysophospholipase 1
Hirano, T., Kishi, M., Sugimoto, H., Taguchi, R., Obinata, H., Ohshima, N., Tatei, K., & Izumi, T. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2009.05.001 · Cited by 66
Hagen, F. S., Grant, F. J., Kuijper, J. L., Slaughter, C. A., Moomaw, C. R., Orth, K., O’Hara, P. J., & Munford, R. S. (1991) · Biochemistry · doi:10.1021/bi00098a020 · Cited by 66
Svensson, T., ENGBERG, T. S., Aoyama, T., Usuda, N., ALEXSON, E. H. S., & Hashimoto, T. (1998) · Biochemical Journal · doi:10.1042/bj3290601 · Cited by 66
Nagai, Y., Aoki, J., Sato, T., Amano, K., Matsuda, Y., Arai, H., & Inoue, K. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.16.11053 · Cited by 65
p125A exists as part of the mammalian Sec13/Sec31 COPII subcomplex to facilitate ER-Golgi transport
Ong, Y. S., Tang, B. L., Loo, L. S., & Hong, W. (2010) · The Journal of Cell Biology · doi:10.1083/jcb.201003005 · Cited by 65
Expanding the Dipeptidyl Peptidase 4-Regulated Peptidome via an Optimized Peptidomics Platform
Tinoco, A. D., Tagore, D. M., & Saghatelian, A. (2010) · Journal of the American Chemical Society · doi:10.1021/ja909524e · Cited by 64
Ebdrup, S., Sørensen, L. G., Olsen, O. H., & Jacobsen, P. (2003) · Journal of Medicinal Chemistry · doi:10.1021/jm031004s · Cited by 64
George, S. T., & Balasubramanian, A. S. (1981) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1981.tb06447.x · Cited by 64
Munford, R. S., & Hunter, J. P. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)50207-1 · Cited by 63
Peptidase substrates via global peptide profiling
Tagore, D. M., Nolte, W. M., Neveu, J. M., Rangel, R., Guzman‐Rojas, L., Pasqualini, R., Arap, W., Lane, W. S., & Saghatelian, A. (2008) · Nature Chemical Biology · doi:10.1038/nchembio.126 · Cited by 63
Plasma PAF-acetylhydrolase: An unfulfilled promise?
Karabina, S., & Ninio, E. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2006.05.008 · Cited by 63
VINOGRADOVA, V. M., MICHAUD, L., MEZENTSEV, V. A., LUKONG, E. K., EL-ALFY, M., MORALES, R. C., POTIER, M., & PSHEZHETSKY, V. A. (1998) · Biochemical Journal · doi:10.1042/bj3300641 · Cited by 63
Trickett, J. I., Patel, D. D., Knight, B. L., SAGGERSON, E. D., Gibbons, G. F., & Pease, R. J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m101764200 · Cited by 63
A retinoblastoma-binding protein that affects cell-cycle control and confers transforming ability
Woitach, J. T., Zhang, M., Niu, C., & Thorgeirsson, S. S. (1998) · Nature Genetics · doi:10.1038/1258 · Cited by 62
S 17092-1, a Highly Potent, Specific and Cell Permeant Inhibitor of Human Proline Endopeptidase
Barelli, H., Petit-Paitel, A., Hirsch, É. C., Wilk, S., Nanteuil, G. D., Morain, P., & Checler, F. (1999) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1999.0366 · Cited by 62
Huggins, K. W., Camarota, L. M., Howles, P. N., & Hui, D. Y. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m303422200 · Cited by 62
Altered Striatal Function and Muscarinic Cholinergic Receptors in Acetylcholinesterase Knockout Mice
Volpicelli‐Daley, L. A., Hrabovská, A., Duysen, E. G., Ferguson, S. M., Blakely, R., Lockridge, O., & Levey, A. I. (2003) · Molecular Pharmacology · doi:10.1124/mol.64.6.1309 · Cited by 62
Long, J. Z., Jin, X., Adibekian, A., Li, W., & Cravatt, B. F. (2010) · Journal of Medicinal Chemistry · doi:10.1021/jm9016976 · Cited by 62
Self-citationMorreau, H., Galjart, N., Willemsen, R., Gillemans, N., Zhou, X., & d’Azzo, A. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)37135-2 · Cited by 61
Cloning and expression of the murine sws/NTE gene
Moser, M., Stempfl, T., Li, Y., Glynn, P., Büttner, R., & Kretzschmar, D. (2000) · Mechanisms of Development · doi:10.1016/s0925-4773(99)00239-7 · Cited by 61
In vitro SAR of (5-(2H)-isoxazolonyl) ureas, potent inhibitors of hormone-sensitive lipase
Lowe, D., Magnuson, S. R., Qi, N. L., et al. (2004) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2004.04.015 · Cited by 61
Mancuso, D. J., Han, X., Jenkins, C. M., Lehman, J. J., Sambandam, N., Sims, H. F., Yang, J., Yan, W., Yang, K., Green, K., et al. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m607307200 · Cited by 60
Bellemère, G., Morain, P., Vaudry, H., & Jégou, S. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.01536.x · Cited by 59
On the question of half- or full-site reactivity of animal fatty acid synthetase.
Singh, N., Wakil, S. J., & Stoops, J. K. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)43136-x · Cited by 59
Spatial control of protein phosphatase 2A (de)methylation
Longin, S., Zwaenepoel, K., Martens, E., Louis, J. V., Rondelez, E., Goris, J., & Janssens, V. (2007) · Experimental Cell Research · doi:10.1016/j.yexcr.2007.07.030 · Cited by 59
Lysosomal Protective Protein/Cathepsin A
Bonten, E. J., Galjart, N. J., Willemsen, R., Usmany, M., Vlak, J. M., & d'Azzo, A. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.44.26441 · Cited by 59
Structure of the human fatty acid synthase KS-MAT didomain as a framework for inhibitor design.
Pappenberger, G., Benz, J., Gsell, B., Hennig, M., Ruf, A., Stihle, M., Thoma, R., & Rudolph, M. (2010) · Journal of Molecular Biology · doi:10.1016/j.jmb.2010.01.066 · Cited by 59
Wada, H., Yasuda, T., Miura, I., Watabe, K., Sawa, C., Kamijuku, H., Kojo, S., Taniguchi, M., Nishino, I., Wakana, S., et al. (2009) · American Journal Of Pathology · doi:10.2353/ajpath.2009.090343 · Cited by 58
Mice deficient for cytosolic thymidine kinase gene develop fatal kidney disease
Dobrovolsky, V. N., Bucci, T. J., Heflich, R. H., Desjardins, J. P., & Richardson, F. C. (2003) · Molecular Genetics and Metabolism · doi:10.1016/s1096-7192(02)00224-x · Cited by 58
Sontag, J., Nunbhakdi‐Craig, V., Mitterhuber, M., Ogris, E., & Sontag, E. (2010) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2010.07049.x · Cited by 57
Yoda, E., Hachisu, K., Taketomi, Y., Yoshida, K., Nakamura, M., Ikeda, K., Taguchi, R., Nakatani, Y., Kuwata, H., Murakami, M., et al. (2010) · Journal of Lipid Research · doi:10.1194/jlr.m008060 · Cited by 57
Soisson, S. M., Patel, S. B., Abeywickrema, P. D., Bryne, N. J., Diehl, R. E., Hall, D. L., Ford, R. E., Reid, J. C., Rickert, K. W., Shipman, J. M., et al. (2010) · BMC Structural Biology · doi:10.1186/1472-6807-10-16 · Cited by 57
Jm, H., Demosky, S. J., Pescovitz, O. H., & Brewer, H. B. (1984) · Europe PMC (PubMed Central) · Cited by 56
Huhtinen, K., O'Byrne, J., Lindquist, P. J. G., Contreras, J. A., & Alexson, S. E. H. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m109040200 · Cited by 56
Esterification of Oxysterols by Human Plasma Lecithin-Cholesterol Acyltransferase
Szedlacsek, S. E., Wa̧sowicz, E., Hulea, S. A., Nishida, H. I., Kummerow, F. A., & Nishida, T. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.20.11812 · Cited by 56
A brain detoxifying enzyme for organophosphorus nerve poisons
Nomura, D. K., Leung, D., Chiang, K. P., Quistad, G. B., Cravatt, B. F., & Casida, J. E. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0501915102 · Cited by 56
Self-citationCloning and Sequence Analysis of a Rat Liver cDNA Encoding Acyl-peptide Hydrolase
Kobayashi, K., Lin, L. H., Yeadon, J. E., Klickstein, L. B., & Smith, J. A. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)81877-4 · Cited by 54
Jennens, M. L., & Lowe, M. E. (1995) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)39718-2 · Cited by 54
Tumorigenicity of cell lines with altered lipid composition.
Roos, D. S., & Choppin, P. W. (1984) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.81.23.7622 · Cited by 54
Function, Activity, and Membrane Targeting of Cytosolic Phospholipase A2ζ in Mouse Lung Fibroblasts
Ghosh, M., Loper, R., Ghomashchi, F., Tucker, D. E., Bonventre, J. V., Gelb, M. H., & Leslie, C. C. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m608458200 · Cited by 54
Identification of the Expressed Form of Human Cytosolic Phospholipase A2β (cPLA2β)
Ghosh, M., Loper, R., Gelb, M. H., & Leslie, C. C. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m601770200 · Cited by 53
Discovery of potent, selective sulfonylfuran urea endothelial lipase inhibitors
Goodman, K. B., Bury, M. J., Cheung, M., Cichy-Knight, M. A., Dowdell, S. E., Dunn, A. K., Lee, D. M., Lieby, J. A., Moore, M. L., Scherzer, D. A., et al. (2008) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2008.11.033 · Cited by 53
Buchebner, M., Pfeifer, T., Rathke, N., Chandak, P. G., Lass, A., Schreiber, R., Kratzer, A., Zimmermann, R., Sattler, W., Köfeler, H. C., et al. (2010) · Journal of Lipid Research · doi:10.1194/jlr.m004259 · Cited by 52
Self-citationHunt, M. C., Lindquist, P. J. G., Peters, J. M., Gonzalez, F. J., Diczfalusy, U., & Alexson, S. E. H. (2000) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)32390-7 · Cited by 52
Chiravuri, M., Agarraberes, F. A., Mathieu, S. L., Lee, H., & Huber, B. T. (2000) · The Journal of Immunology · doi:10.4049/jimmunol.165.10.5695 · Cited by 51
Stimulus-dependent Deacylation of Bacterial Lipopolysaccharide by Dendritic Cells
Lu, M., Zhang, M., Kitchens, R. L., Fosmire, S. P., Takashima, A., & Munford, R. S. (2003) · The Journal of Experimental Medicine · doi:10.1084/jem.20030420 · Cited by 51
Dobrovolsky, V. N., Bowyer, J. F., Pabarcus, M. K., Heflich, R. H., Williams, L. D., Doerge, D. R., Arvidsson, B., Bergquist, J., & Casida, J. E. (2005) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2005.03.010 · Cited by 51
Khan, W. A. (2000) · Toxicological Sciences · doi:10.1093/toxsci/57.1.112 · Cited by 51
Ortega-Gutiérrez, S., Leung, D., Ficarro, S., Peters, E. C., & Cravatt, B. F. (2008) · PLoS ONE · doi:10.1371/journal.pone.0002486 · Cited by 50
Self-citationLo, V., Erickson, B., Thomason-Hughes, M., Ko, K. W. S., Dolinsky, V. W., Nelson, R. C., & Lehner, R. S. (2009) · Journal of Lipid Research · doi:10.1194/jlr.m000596 · Cited by 50
Pillai, S., Cariappa, A., & Pirnie, S. P. (2009) · Trends in immunology · doi:10.1016/j.it.2009.07.006 · Cited by 49
Harris, J., Schwinn, N., Mahoney, J. A., Lin, H., Shaw, M. K., Howard, C. J., SILVA, R. P. D., & Gordon, S. (2006) · International Journal of Experimental Pathology · doi:10.1111/j.0959-9673.2006.00450.x · Cited by 49
Identification of Functional Domains of Rat Intestinal Phospholipase B/Lipase
Takemori, H., Zolotaryov, F. N., Lü, T., Tchoua, U., Komatsubara, T., Hatano, O., Okamoto, M., & Tojo, H. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.4.2222 · Cited by 48
Smith, T. S., Southan, C., Ellington, K., Campbell, D. S., Tew, D. G., & Debouck, C. M. (2001) · Genomics · doi:10.1006/geno.2001.6643 · Cited by 47
Westin, M., Alexson, S. E. H., & Hunt, M. C. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m313863200 · Cited by 47
Toide, K., Fujiwara, T., Iwamoto, Y., Shinoda, M., Okamiya, K., & Kato, T. (1996) · Naunyn-Schmiedeberg s Archives of Pharmacology · doi:10.1007/bf00168640 · Cited by 47
A specific human lysophospholipase: cDNA cloning, tissue distribution and kinetic characterization
Wang, A., Yang, H., Friedman, P., Johnson, C., & Dennis, E. A. (1999) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/s1388-1981(99)00012-8 · Cited by 47
Tissue and cellular specific expression of murine lysosomal acid lipase mRNA and protein
Du, H., Witte, D. P., & Grabowski, G. A. (1996) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)42005-x · Cited by 47
Hui, D. Y., Hayakawa, K., & Oizumi, J. (1993) · Biochemical Journal · doi:10.1042/bj2910065 · Cited by 46
Mailly, F., Palmen, J., Muller, D. P. R., Gibbs, T., Lloyd, J. K., Brunzell, J. D., Durrington, P. N., Mitropoulos, K., Betteridge, J. D., Watts, G. F., et al. (1997) · Human Mutation · doi:10.1002/(sici)1098-1004(1997)10:6<465::aid-humu8>3.0.co;2-c · Cited by 46
Getting a chemical handle on proteinpost-translational modification
Heal, W. P., & Tate, E. W. (2009) · Organic & Biomolecular Chemistry · doi:10.1039/b917894e · Cited by 46
Yamashita, A., Tanaka, K., Kamata, R., 司紗, 熊., Suzuki, N., Koga, H., Waku, K., & Sugiura, T. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2009.05.008 · Cited by 45
Evidence for Hormone-Sensitive Lipase mRNA Expression in Human Monocyte/Macrophages
Reue, K., Cohen, R. D., & Schotz, M. C. (1997) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.17.12.3428 · Cited by 45
Scanu, A. M. (1966) · Science · doi:10.1126/science.153.3736.640 · Cited by 44
Peptidomics of Prolyl Endopeptidase in the Central Nervous System
Nolte, W. M., Tagore, D. M., Lane, W. S., & Saghatelian, A. (2009) · Biochemistry · doi:10.1021/bi901637c · Cited by 43
Pabarcus, M. K., & Casida, J. E. (2002) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/s0167-4838(02)00232-7 · Cited by 42
Sato, S., Inoue, H., Kogure, T., Tagaya, M., & Tani, K. (2010) · FEBS Letters · doi:10.1016/j.febslet.2010.09.047 · Cited by 42
Ultrastructural localization of dipeptidylpeptidase IV in the glomerulum of the rat kidney
Kettmann, U., Humbel, B. M., & Holzhausen, H.-J. (1992) · Acta Histochemica · doi:10.1016/s0065-1281(11)80085-1 · Cited by 41
Yamin, R., Bagchi, S., Hildebrant, R., Scaloni, A., Widom, R. L., & Abraham, C. R. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04251.x · Cited by 41
Production of the Butyrylcholinesterase Knockout Mouse
Li, B., Duysen, E. G., Saunders, T. L., et al. (2006) · Journal of Molecular Neuroscience · doi:10.1385/jmn:30:1:193 · Cited by 41
Overexpression of Lysosomal Acid Lipase and Other Proteins in Atherosclerosis
Zschenker, O., Illies, T., & Ameis, D. (2006) · The Journal of Biochemistry · doi:10.1093/jb/mvj137 · Cited by 40
Senten, K., der Veken, P. V., Meester, I. D., Lambeir, A., Scharpé, S., Haemers, A., & Augustyns, K. (2004) · Journal of Medicinal Chemistry · doi:10.1021/jm031122f · Cited by 40
Takematsu, H., Diaz, S. L., Stoddart, A., Zhang, Y., & Varki, A. P. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.36.25623 · Cited by 40
Tojo, H., Ichida, T., & Okamoto, M. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.4.2214 · Cited by 39
Taniyama, Y., Shibata, S., Kita, S., Horikoshi, K., Fuse, H., Shirafuji, H., Sumino, Y., & Fujino, M. (1999) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1999.0411 · Cited by 39
The 2p21 deletion syndrome: Characterization of the transcription content
Parvari, R., GONEN, Y., Alshafee, I., Buriakovsky, S., Regev, K., & Hershkovitz, E. (2005) · Genomics · doi:10.1016/j.ygeno.2005.04.001 · Cited by 36
Ghomashchi, F., Naika, G. S., Bollinger, J. G., Aloulou, A., Lehr, M., Leslie, C. C., & Gelb, M. H. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.165647 · Cited by 36
Pyrrolopyrazinedione-Based Inhibitors of Human Hormone-Sensitive Lipase
Slee, D. H., Bhat, A., Nguyen, T. N., Kish, M., Lundeen, K., Newman, M. J., & McConnell, S. J. (2003) · Journal of Medicinal Chemistry · doi:10.1021/jm020460y · Cited by 36
Bunkòczi, G., Misquitta, S. A., Wu, X., Lee, W. H., Рожкова, А. М., Kochan, G. T., Kavanagh, K. L., Oppermann, U. C. T., & Smith, S. (2009) · Chemistry & Biology · doi:10.1016/j.chembiol.2009.04.011 · Cited by 35
Miyata, K., Oike, Y., Hoshii, T., Maekawa, H., Ogawa, H., Suda, T., Araki, K., & Yamamura, K. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.01.127 · Cited by 35
PREPL: a putative novel oligopeptidase propelled into the limelight
Martens, K., Derua, R., Meulemans, S. M. P., Waelkens, E., Jaeken, J., Matthijs, G., & Creemers, J. W. M. (2006) · Biological Chemistry · doi:10.1515/bc.2006.111 · Cited by 34
Age-related pulmonary emphysema in mice lacking α/β hydrolase domain containing 2 gene
Jin, S., Zhao, G., Li, Z., Nishimoto, Y., Isohama, Y., Shen, J., Ito, T., Takeya, M., Araki, K., He, P., et al. (2009) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2009.01.098 · Cited by 34
Determination of Functional Regions of p125, a Novel Mammalian Sec23p-Interacting Protein
Mizoguchi, T., Nakajima, K., Hatsuzawa, K., Nagahama, M., Hauri, H., Tagaya, M., & Tani, K. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.3846 · Cited by 34
Hartmann, J., Kiewert, C., Duysen, E. G., Lockridge, O., & Klein, J. (2007) · Neurochemistry International · doi:10.1016/j.neuint.2007.10.008 · Cited by 33
Development of potent and selective dipeptidyl peptidase II inhibitors
Senten, K., der Veken, P. V., Bal, G., et al. (2002) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/s0960-894x(02)00603-0 · Cited by 33
Jessani, N., Young, J. A., Diaz, S. L., Patricelli, M. P., Varki, A. P., & Cravatt, B. F. (2005) · Angewandte Chemie International Edition · doi:10.1002/anie.200463098 · Cited by 33
Self-citationOjogun, N., Kuang, T., Shao, B., Greaves, D. R., Munford, R. S., & Varley, A. W. (2009) · The Journal of Infectious Diseases · doi:10.1086/646616 · Cited by 33
Schuettengruber, B., Doetzlhofer, A., Kroboth, K., Wintersberger, E., & Seiser, C. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m204843200 · Cited by 32
Pancreatic lipase-related protein type I: a specialized lipase or an inactive enzyme
Crenon, I., Foglizzo, E., Kerfélec, B., Vérine, A., Pignol, D., Hermoso, J. A., BONICEL, J. J., & Chapus, C. (1998) · Protein Engineering Design and Selection · doi:10.1093/protein/11.2.135 · Cited by 32
Kirincich, S. J., Xiang, J. S., Green, N., Tam, S., Yang, H., Shim, J., Shen, M. W. H., Clark, J. D., & McKew, J. C. (2009) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2009.05.027 · Cited by 31
Westin, M. A. K., Hunt, M. C., & Alexson, S. E. H. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m703718200 · Cited by 30
Bachovchin, D. A., Wolfe, M. R., Masuda, K. R., Brown, S. J., Spicer, T., Fernández-Vega, V., Chase, P. S., Hodder, P., Rosen, H., & Cravatt, B. F. (2010) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2010.02.011 · Cited by 30
Self-citationCloning of a Novel Retinoid-inducible Serine Carboxypeptidase from Vascular Smooth Muscle Cells
Chen, J., Streb, J. W., Maltby, K. M., Kitchen, C. M., & Miano, J. M. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m104162200 · Cited by 29
Nomura, D. K., Fujioka, K., Issa, R. S., Ward, A. M., Cravatt, B. F., & Casida, J. E. (2007) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2007.11.021 · Cited by 28
Self-citationTsoukatos, D. C., Liapikos, T. A., Tselepis, A. D., et al. (2001) · Biochemical Journal · doi:10.1042/0264-6021:3570457 · Cited by 28
Miller, R., & Lowe, M. E. (2008) · Journal of Nutrition · doi:10.1093/jn/138.5.927 · Cited by 25
van Groningen, J. J. M., Egmond, M. R., Bloemers, H. P. J., & Swart, G. W. M. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)00098-7 · Cited by 25
Histochemistry of proteases in ependyma, choroid plexus and leptomeninges
Mitro, A., & Lojda, Z. (1988) · Histochemistry · doi:10.1007/bf00570337 · Cited by 24
Lavallée, B., Provost, P. R., & Bélanger, A. (1996) · Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism · doi:10.1016/0005-2760(95)00222-7 · Cited by 24
Cloning, expression, and catalytic triad of recombinant arylformamidase
Pabarcus, M. K., & Casida, J. E. (2005) · Protein Expression and Purification · doi:10.1016/j.pep.2005.04.013 · Cited by 24
Stoddart, A. (1996) · Nucleic Acids Research · doi:10.1093/nar/24.20.4003 · Cited by 23
Molecular characterization and gene disruption of mouse lysosomal putative serine carboxypeptidase 1
Kollmann, K., Daμμe, M., Deuschl, F. G., Kahle, J., D’Hooge, R., Lüllmann‐Rauch, R., & Lübke, T. (2009) · FEBS Journal · doi:10.1111/j.1742-4658.2009.06877.x · Cited by 23
Signalling mechanism in the lysophosphatidylserine-induced activation of mouse mast cells
Bellini, F., Viola, G., Menegus, A. M., Toffano, G., & Bruni, A. (1990) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/0167-4889(90)90079-s · Cited by 21
Infantile galactosialidosis presenting with congenital adrenal hyperplasia and renal hypertension
Kyllerman, M., Månsson, J., Westphal, O., CONRADI, N. G., & Nellström, H. (1993) · Pediatric Neurology · doi:10.1016/0887-8994(93)90073-l · Cited by 21
Perroud, B., Alvarado, R., Espinal, G. M., Morado, A. R., Phinney, B. S., & Warden, C. H. (2009) · Molecular Brain · doi:10.1186/1756-6606-2-14 · Cited by 21
The Crystal Structure of CCG1/TAFII250-interacting Factor B (CIB)
Padmanabhan, B., Kuzuhara, T., Adachi, N., & Horikoshi, M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m312165200 · Cited by 19
Danilova, O. V., Tai, A., Mele, D. A., Beinborn, M., Leiter, A. B., Greenberg, A. S., Perfield, J. W., DeFuria, J., Singru, P. S., Lechan, R. M., et al. (2009) · Endocrinology · doi:10.1210/en.2009-0386 · Cited by 19
Functional Characterization of a Putative Serine Carboxypeptidase in Vascular Smooth Muscle Cells
Lee, T.-H., Chen, J., & Miano, J. M. (2009) · Circulation Research · doi:10.1161/circresaha.109.199869 · Cited by 18
Stölting, M., Geyer, M., Reuter, S., Reichelt, R., Bek, M. J., & Pavenstädt, H. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.12.008 · Cited by 17
Crystal structure of human retinoblastoma binding protein 9
Vorobiev, S. M., Su, M., Seetharaman, J., Huang, Y. J., Chen, C. X., Maglaqui, M., Janjua, H., Proudfoot, M., Yakunin, A. F., Xiao, R., et al. (2008) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.22278 · Cited by 17
Blank, M. L., Smith, Z. L., Cress, E. A., & Snyder, F. F. C. (1990) · Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism · doi:10.1016/0005-2760(90)90001-e · Cited by 16
Angiotensin carboxypeptidase activity in urine from normal subjects and patients with kidney damage
Miller, J. J., Changaris, D. G., & Levy, R. S. (1991) · Life Sciences · doi:10.1016/0024-3205(91)90277-i · Cited by 15
Tissue Expression of the Novel Serine Carboxypeptidase Scpep1
Lee, T.-H. D., Streb, J. W., Georger, M. A., & Miano, J. M. (2006) · Journal of Histochemistry & Cytochemistry · doi:10.1369/jhc.5a6894.2006 · Cited by 15
Zhao, X., Southwick, K., Cardasis, H. L., Du, Y., Lassman, M. E., Xie, D., El-Sherbeini, M., Geissler, W. M., Pryor, K. D., Verras, A., et al. (2010) · PROTEOMICS · doi:10.1002/pmic.201000145 · Cited by 15
Processing of pro-colipase and trypsinogen by pancreatic dipeptidyl peptidase IV.
Heymann, E., Mentlein, R., Nausch, I., et al. (1986) · PubMed · Cited by 14
Expression of Phosphatidylserine-Specific Phospholipase A 1 mRNA in Human THP-1-Derived Macrophages
Hosono, H., Homma, M., Ogasawara, Y., Makide, K., Aoki, J., Niwata, H., Watanabe, M., Inoue, K., Ohkohchi, N., & Kohda, Y. (2010) · Cell Transplantation · doi:10.3727/096368910x508861 · Cited by 10
Wen, X. (1998) · Human Molecular Genetics · doi:10.1093/hmg/7.4.743 · Cited by 8
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Hsu, K.-L., Tsuboi, K., Adibekian, A., Pugh, H., Masuda, K., & Cravatt, B. F. (2012) · Nature Chemical Biology · doi:10.1038/nchembio.1105 · Cited by 222
“22) and then performed lipid and cytokine measurements.”
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Moellering, R. E., & Cravatt, B. F. (2012) · Chemistry & Biology · doi:10.1016/j.chembiol.2012.01.001 · Cited by 182
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Metadata
- Authors
- Long, J. Z., & Cravatt, B. F.
- Venue
- Chemical Reviews
- Publisher
- American Chemical Society (ACS)
- Published
- 2011-06-23
- Volume
- 111
- Issue
- 10
- Pages
- 6022-6063
- ISSN
- 0009-2665 (ISSN-L)
- 1520-6890
- OpenAlex
- W2019387110
- Cited by
- 425
- References
- 525
- FWCI
- 1.35
- Type
- journal article
- Language
- en
- Open access
- green
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.
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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.