The DOI matches its Crossref record; 37 of the 37 references it cites were found in a registry or an index.
The Concise Guide to PHARMACOLOGY 2013/14: Enzymes
Open accessAbstract
The Concise Guide to PHARMACOLOGY 2013/14 provides concise overviews of the key properties of over 2000 human drug targets with their pharmacology, plus links to an open access knowledgebase of drug targets and their ligands (www.guidetopharmacology.org), which provides more detailed views of target and ligand properties. The full contents can be found at http://onlinelibrary.wiley.com/doi/10.1111/bph.12444/full. Enzymes are one of the seven major pharmacological targets into which the Guide is divided, with the others being G protein‐coupled receptors, ligand‐gated ion channels, ion channels, nuclear hormone receptors, catalytic receptors and transporters. These are presented with nomenclature guidance and summary information on the best available pharmacological tools, alongside key references and suggestions for further reading. A new landscape format has easy to use tables comparing related targets. It is a condensed version of material contemporary to late 2013, which is presented in greater detail and constantly updated on the website www.guidetopharmacology.org, superseding data presented in previous Guides to Receptors and Channels. It is produced in conjunction with NC‐IUPHAR and provides the official IUPHAR classification and nomenclature for human drug targets, where appropriate. It consolidates information previously curated and displayed separately in IUPHAR‐DB and the Guide to Receptors and Channels, providing a permanent, citable, point‐in‐time record that will survive database updates.
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
Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex
Sarbassov, D. D., Guertin, D. A., Ali, S. M., & Sabatini, D. M. (2005) · Science · doi:10.1126/science.1106148 · Cited by 6,216
Role of AMP-Activated Protein Kinase in Mechanism of Metformin Action
Zhou, G., Myers, R., Li, Y., Chen, Y., Shen, X., Fenyk-Melody, J., Wu, M., Ventre, J., Doebber, T., Fujii, N., et al. (2001) · Journal of Clinical Investigation · doi:10.1172/jci13505 · Cited by 5,652
AMPK: a nutrient and energy sensor that maintains energy homeostasis
Hardie, D. G., Ross, F. A., & Hawley, S. A. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3311 · Cited by 4,602
How many drug targets are there?
Overington, J. P., Al-Lazikani, B., & Hopkins, A. L. (2006) · Nature Reviews Drug Discovery · doi:10.1038/nrd2199 · Cited by 3,505
SP600125, an anthrapyrazolone inhibitor of Jun N-terminal kinase
Bennett, B. L., Sasaki, D. T., Murray, B. W., O'Leary, E. C., Sakata, S. T., Xu, W., Leisten, J. C., Motiwala, A., Pierce, S., Satoh, Y., et al. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.251194298 · Cited by 2,558
The Molecular Biology, Biochemistry, and Physiology of Human Steroidogenesis and Its Disorders
Miller, W. L., & Auchus, R. J. (2011) · Endocrine Reviews · doi:10.1210/er.2010-0013 · Cited by 2,458
The functions and regulation of the PTEN tumour suppressor
Song, M. S., Salmena, L., & Pandolfi, P. P. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3330 · Cited by 1,926
The emerging mechanisms of isoform-specific PI3K signalling
Vanhaesebroeck, B., Guillermet-Guibert, J., Graupera, M., & Bilanges, B. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2882 · Cited by 1,767
Structural mechanism for statin inhibition of HMG-CoA reductase
Istvan, E. S., & Deisenhofer, J. (2001) · Science · doi:10.1126/science.1059344 · Cited by 1,644
The nuts and bolts of AGC protein kinases
Pearce, L. R., Komander, D., & Alessi, D. R. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2822 · Cited by 1,294
Mechanisms of Cell Protection by Heme Oxygenase-1
Gozzelino, R., Jeney, V., & Soares, M. P. (2010) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.010909.105600 · Cited by 1,241
García-Martínez, J. M., & Alessi, D. R. (2008) · Biochemical Journal · doi:10.1042/bj20081668 · Cited by 907
Sutherland, C., Leighton, I. A., & Cohen, P. (1993) · Biochemical Journal · doi:10.1042/bj2960015 · Cited by 903
Cellular and Molecular Basis of Deiodinase-Regulated Thyroid Hormone Signaling1
Gereben, B., Zavacki, A. M., Ribich, S., Kim, B. W., Huang, S. A., Simonides, W. S., Zeöld, A., & Bianco, A. C. (2008) · Endocrine Reviews · doi:10.1210/er.2008-0019 · Cited by 891
Lipoxygenase and leukotriene pathways: biochemistry, biology, and roles in disease
Haeggström, J. Z., & Funk, C. D. (2011) · Chemical Reviews · doi:10.1021/cr200246d · Cited by 875
Soluble Adenylyl Cyclase as an Evolutionarily Conserved Bicarbonate Sensor
Chen, Y., Cann, M. J., Litvin, T. N., Iourgenko, V., Sinclair, M. L., Levin, L. R., & Buck, J. (2000) · Science · doi:10.1126/science.289.5479.625 · Cited by 846
Levy, M., & Futerman, A. H. (2010) · IUBMB Life · doi:10.1002/iub.319 · Cited by 632
Matrix metalloproteinases and their multiple roles in neurodegenerative diseases
Rosenberg, G. A. (2009) · The Lancet Neurology · doi:10.1016/s1474-4422(09)70016-x · Cited by 594
The Ste20-like kinase Mst2 activates the human large tumor suppressor kinase Lats1
Chan, E. H. Y., Nousiainen, M., Chalamalasetty, R. B., Schäfer, A., Nigg, E. A., & Silljé, H. H. W. (2005) · Oncogene · doi:10.1038/sj.onc.1208445 · Cited by 584
Cytosolic adenylyl cyclase defines a unique signaling molecule in mammals
Buck, J., Sinclair, M. L., Schapal, L., Cann, M. J., & Levin, L. R. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.1.79 · Cited by 527
Structure and Regulation of Soluble Guanylate Cyclase
Derbyshire, E. R., & Marletta, M. A. (2012) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-050410-100030 · Cited by 466
Duncia, J. V., Santella, J. B., Higley, C. A., Pitts, W. J., Wityak, J., Frietze, W. E., Rankin, F. W., Sun, J.-H., Earl, R. A., Tabaka, A. C., et al. (1998) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/s0960-894x(98)00522-8 · Cited by 401
Potter, G. A., Barrie, S. E., Jarman, M., & Rowlands, M. G. (1995) · Journal of Medicinal Chemistry · doi:10.1021/jm00013a022 · Cited by 379
Cali, J. J., Zwaagstra, J. C., Mons, N., Cooper, D. M., & Krupinski, J. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)32700-x · Cited by 363
Activation of Phospholipase C-γ by Phosphatidylinositol 3,4,5-Trisphosphate
Bae, Y. S., Cantley, L. G., Chen, C.-S., Kim, S.-R., Kwon, K.-S., & Rhee, S. G. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.8.4465 · Cited by 330
Cholesterol 24-Hydroxylase: an enzyme of cholesterol turnover in the brain
Russell, D. W., Halford, R. W., Ramirez, D. M. O., Shah, R., & Kotti, T. (2009) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.78.072407.103859 · Cited by 317
Cytochrome P450s in the Regulation of Cellular Retinoic Acid Metabolism
Catharine Ross, A., & Zolfaghari, R. (2011) · Annual Review of Nutrition · doi:10.1146/annurev-nutr-072610-145127 · Cited by 296
Neural circuitry engaged by prostaglandins during the sickness syndrome
Saper, C. B., Romanovsky, A. A., & Scammell, T. E. (2012) · Nature Neuroscience · doi:10.1038/nn.3159 · Cited by 285
Rask-Andersen, M., Masuram, S., & Schiöth, H. B. (2014) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-011613-135943 · Cited by 282
Cloning and expression of a Ca(2+)-inhibitable adenylyl cyclase from NCB-20 cells.
Yoshimura, M., & Cooper, D. M. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.15.6716 · Cited by 268
Iodothyronine deiodinase structure and function: from ascidians to humans
Darras, V. M., & Van Herck, S. L. J. (2012) · Journal of Endocrinology · doi:10.1530/joe-12-0204 · Cited by 162
Local impact of thyroid hormone inactivation
Dentice, M., & Salvatore, D. (2011) · Journal of Endocrinology · doi:10.1530/joe-11-0002 · Cited by 143
Protein Kinase C Alters the Responsiveness of Adenylyl Cyclases to G Protein α and βγ Subunits
Zimmermann, G., & Taussig, R. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.43.27161 · Cited by 142
Chen, J., & Iyengar, R. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)31381-4 · Cited by 109
Schindler, U., Strobel, H., Schönafinger, K., Linz, W., Löhn, M., Martorana, P. A., Rütten, H., Schindler, P. W., Busch, A. E., Sohn, M., et al. (2006) · Molecular Pharmacology · doi:10.1124/mol.105.018747 · Cited by 100
Isozyme-specific stimulation of phospholipase C-γ2 by Rac GTPases
Piechulek, T., Rehlen, T., Walliser, C., Vatter, P., Moepps, B., & Gierschik, P. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m509396200 · Cited by 80
Walliser, C., Retlich, M., Harris, R., Everett, K. L., Josephs, M. B., Vatter, P., Esposito, D., Driscoll, P. C., Katan, M., Gierschik, P., et al. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m803316200 · Cited by 56
Cited by
Microglial M1/M2 polarization and metabolic states
Orihuela, R., McPherson, C. A., & Harry, G. J. (2016) · British Journal of Pharmacology · doi:10.1111/bph.13139 · Cited by 2,070
Update on leukotriene, lipoxin and oxoeicosanoid receptors: IUPHAR Review 7
Bäck, M., Powell, W. S., Dahlén, S., Drazen, J. M., Evans, J. F., Serhan, C. N., Shimizu, T., Yokomizo, T., & Rovati, G. E. (2014) · British Journal of Pharmacology · doi:10.1111/bph.12665 · Cited by 217
Chen, J., Lai, J., Yang, L., Ruan, G., Chaugai, S., Ning, Q., Chen, C., & Wang, D. W. (2016) · British Journal of Pharmacology · doi:10.1111/bph.13386 · Cited by 120
Analgesic efficacy of opioids in chronic pain: recent meta‐analyses
Reinecke, H., Weber, C., Lange, K., Simon, M., Stein, C., & Sorgatz, H. (2015) · British Journal of Pharmacology · doi:10.1111/bph.12634 · Cited by 120
Zhu, G., Li, J., He, L., Wang, X., & Hong, X. (2015) · British Journal of Pharmacology · doi:10.1111/bph.13061 · Cited by 118
Metadata
- Authors
- Alexander, S. P. H., Benson, H. E., Faccenda, E., Pawson, A. J., Sharman, J. L., Spedding, M., Peters, J. A., Harmar, A. J., & Collaborators, C.
- Venue
- British Journal of Pharmacology
- Publisher
- Wiley
- Published
- 2013-12
- Volume
- 170
- Issue
- 8
- Pages
- 1797-1867
- ISSN
- 0007-1188 (ISSN-L)
- 1476-5381
- OpenAlex
- W1529023379
- Cited by
- 425
- References
- 37
- FWCI
- 132.49
- Type
- journal article
- Language
- en
- Open access
- hybrid
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.