The DOI matches its Crossref record; 33 of the 33 references it cites were found in a registry or an index.
Autophosphorylation reversibly regulates the Ca2+/calmodulin-dependence of Ca2+/calmodulin-dependent protein kinase II.
Open accessAbstract
Ca2+/calmodulin-dependent protein kinase II contains two subunits, alpha (Mr 50,000) and beta (Mr 60,000/58,000), both of which undergo Ca2+/calmodulin-dependent autophosphorylation. In the present study, we have studied the mechanism of this autophosphorylation reaction and its effect on the activity of the enzyme. Both subunits are autophosphorylated through an intramolecular mechanism. Using synapsin I as substrate, Ca2+/calmodulin-dependent protein kinase II, in its unphosphorylated form, was totally dependent on Ca2+ and calmodulin for its activity. Preincubation of the enzyme with Ca2+, calmodulin, and ATP, under conditions where autophosphorylation of both subunits occurred, converted the enzyme to one that was only partially dependent on Ca2+ and calmodulin for its activity. No change in the total activity, measured in the presence of Ca2+ and calmodulin, was observed. The nonhydrolyzable ATP analog adenosine 5'-[beta, gamma-imido] triphosphate did not substitute for ATP in the preincubation. Moreover, dephosphorylation of autophosphorylated Ca2+/calmodulin-dependent protein kinase II with protein phosphatase 2A resulted in an enzyme that was again totally dependent on Ca2+ and calmodulin for its activity. We propose that autophosphorylation and dephosphorylation reversibly regulate the Ca2+ and calmodulin requirement of Ca2+/calmodulin-dependent protein kinase II.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“it was not until the discovery of a Ca2+/calmodulin-dependent protein kinase, now referred to as CaMKII (9, 10), which became independent of Ca2+ (autonomous) after autophosphorylation (11–15)”
From Synaptic memory and CaMKII (2023) · cites this paper as [13]
In the citing paper
“Fourth, CaMKII has the intriguing property that once activated by Ca2+ the enzymatic activity toward substrates remains after Ca2+ removal (11–15).”
From Synaptic memory and CaMKII (2023) · cites this paper as [13]
In the citing paper
“A further complication for either of these possibilities is that it appears that the subunit being phosphorylated apparently would need to have Ca2+/CaM bound, i.e., it does not significantly occur on inactive subunits (13, 15, 82, 83, 406).”
From Synaptic memory and CaMKII (2023) · cites this paper as [13]
Citations
Cites
A simplification of the protein assay method of Lowry et al. which is more generally applicable
Peterson, G. L. (1977) · Analytical Biochemistry · doi:10.1016/0003-2697(77)90043-4 · Cited by 8,531
Calmodulin Plays a Pivotal Role in Cellular Regulation
Cheung, W. Y. (1980) · Science · doi:10.1126/science.6243188 · Cited by 2,434
Miller, S. (1986) · Cell · doi:10.1016/0092-8674(86)90008-5 · Cited by 864
Llinas, R. H., McGuinness, T. L., Leonard, C. S., Sugimori, M., & Greengard, P. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.9.3035 · Cited by 641
Self-citationNaira, A. C., Hemmings, H. C., & Greengard, P. (1985) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.54.070185.004435 · Cited by 551
Self-citationPhosphorylation activates the insulin receptor tyrosine protein kinase.
Rosen, O. M., Herrera, R., Olowe, Y., Petruzzelli, L., & Cobb, M. H. (1983) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.80.11.3237 · Cited by 545
Bennett, M. K., Erondu, N. E., & Kennedy, M. B. (1983) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)44239-6 · Cited by 481
Ueda, T., & Greengard, P. (1977) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)40170-0 · Cited by 407
Self-citationGoldenring, J. R., Gonzalez, B. I., McGuire, J. S., & DeLorenzo, R. J. (1983) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)44223-2 · Cited by 339
Miller, S. G., & Kennedy, M. B. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)39454-1 · Cited by 304
Flagged first, then by citations
Cited by
Sorted by citations
Items 201–292 of 292
Weinberger, R. P., & Rostas, J. A. P. (1988) · Developmental Brain Research · doi:10.1016/0165-3806(88)90104-6 · Cited by 25
Kojundžić, S. L., Puljak, L., Hogan, Q. H., & Sapunar, D. (2009) · The Journal of Comparative Neurology · doi:10.1002/cne.22209 · Cited by 24
Kameshita, I., Ishida, A., Okuno, S., & Fujisawa, H. (1997) · Analytical Biochemistry · doi:10.1006/abio.1996.9945 · Cited by 24
Mishra-Gorur, K., Singer, H. A., & Castellot, J. J. (2002) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)64465-3 · Cited by 24
Dudai, Y. (1987) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238709101484 · Cited by 24
Modulation of mammalian cardiac AMP deaminase by protein kinase C-mediated phosphorylation
Thakkar, J. K., Janero, D. R., Yarwood, C., & Sharif, H. M. (1993) · Biochemical Journal · doi:10.1042/bj2910523 · Cited by 24
Siekevitz, P. (1991) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.88.12.5374 · Cited by 23
Ardestani, G., West, M. C., Maresca, T. J., Fissore, R. A., & Stratton, M. M. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.009235 · Cited by 23
CaMKII Inhibition is a Novel Therapeutic Strategy to Prevent Diabetic Cardiomyopathy
Veitch, C. R., Power, A., & Erickson, J. R. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.695401 · Cited by 23
Imaging single CaMKII holoenzymes at work by high-speed atomic force microscopy
Tsujioka, S., Sumino, A., Nagasawa, Y., Sumikama, T., Flechsig, H., Puppulin, L., Tomita, T., Baba, Y., Kakuta, T., Ogoshi, T., et al. (2023) · Science Advances · doi:10.1126/sciadv.adh1069 · Cited by 22
Matlhagela, K., Borsick, M., Rajkhowa, T., & Taub, M. L. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m411415200 · Cited by 23
Mahadev, K., Chetty, C., & Vemuri, M. (2001) · Alcohol · doi:10.1016/s0741-8329(01)00133-1 · Cited by 22
Calcium/calmodulin-dependent protein kinase II: role in learning and memory
Soderling, T. R. (1993) · Springer eBooks · doi:10.1007/978-1-4615-2600-1_8 · Cited by 22
Characterization of a Novel Calcium/Calmodulin-Dependent Protein Kinase from Tobacco
Ma, L., Liang, S., Jones, R. L., & Lu, Y. (2004) · PLANT PHYSIOLOGY · doi:10.1104/pp.104.041970 · Cited by 22
Zhang, G. Y., Wang, J. H.-C., & Sharma, R. K. (1993) · Molecular and Cellular Biochemistry · doi:10.1007/bf01076100 · Cited by 22
The cardiac CaMKII-Nav1.5 relationship: From physiology to pathology
Takla, M., Huang, C. L.-H., & Jeevaratnam, K. (2020) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2019.12.014 · Cited by 21
Cui, X., Li, J., Li, T., Ji, F., Bu, X., Zhang, N., & Zhang, B. (2009) · Journal of Neurosurgical Anesthesiology · doi:10.1097/ana.0b013e31819ac2c0 · Cited by 21
Miyamoto, E., & Fukunaga, K. (1996) · Neurosciences research · doi:10.1016/0168-0102(95)00991-4 · Cited by 22
EASOM, A. R., TARPLEY, L. J., FILLER, R. N., & Bhatt, H. S. (1998) · Biochemical Journal · doi:10.1042/bj3290283 · Cited by 21
Modeling CaMKII in cardiac physiology: from molecule to tissue
Önal, B., Unudurthi, S. D., & Hund, T. J. (2014) · Frontiers in Pharmacology · doi:10.3389/fphar.2014.00009 · Cited by 23
Kameshita, I., Ishida, A., & Fujisawa, H. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)00958-8 · Cited by 20
Autophosphorylation of neuronal calcium/calmodulin-stimulated protein kinase II
Dunkley, P. (2008) · Molecular Neurobiology · doi:10.1007/bf02935545 · Cited by 5
Regulation of Ca2+/calmodulin-dependent protein kinase from Trypanosoma cruzi
Ogueta, S. B., Intosh, G. M., & Téllez-Iñón, M. T. (1996) · Molecular and Biochemical Parasitology · doi:10.1016/s0166-6851(96)02622-9 · Cited by 19
Mapping of the adenosine 5'-triphosphate binding site of type II calmodulin-dependent protein kinase
Kwiatkowski, A. P., & King, M. M. (1987) · Biochemistry · doi:10.1021/bi00398a016 · Cited by 19
Pandey, S., & Sopory, S. K. (2001) · Journal of Experimental Botany · doi:10.1093/jexbot/52.357.691 · Cited by 18
Distribution of Calmodulin‐ and Cyclic AMP‐Stimulated Protein Kinases in Synaptosomes
Dunkley, P. R., Jarvie, P. E., & Rostas, J. A. P. (1988) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1988.tb04835.x · Cited by 18
The Insulin Receptor Tyrosine Kinase
Rothenberg, P., White, M. F., & Kahn, C. R. (1990) · Handbook of experimental pharmacology · doi:10.1007/978-3-642-74098-5_11 · Cited by 18
Altfelder, K., Müller, U., & Menzel, R. (1991) · Insect Biochemistry · doi:10.1016/0020-1790(91)90101-j · Cited by 18
A Ca2+‐Dependent Protein Kinase Activity Associated with Serotonin Binding Protein
Adlersberg, M., Liu, K., Hsiung, S., Ehrlich, Y. H., & Tamir, H. (1987) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1987.tb10000.x · Cited by 18
Suzuki, T., Okumura-Noji, K., Ogura, A., Kudo, Y., & Tanaka, R. (1992) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.89.1.109 · Cited by 20
Sathyanarayanan, P. V., & Poovaiah, B. W. (2002) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2002.02904.x · Cited by 16
Matsumura, F., Clark, J. M., & Matsumura, F. M. (1989) · Comparative Biochemistry and Physiology Part C Comparative Pharmacology · doi:10.1016/0742-8413(89)90086-8 · Cited by 16
Matsushita, T., Moriyama, S., & Fukai, T. (1995) · Biological Cybernetics · doi:10.1007/bf00199892 · Cited by 15
Calcium/Calmodulin‐Dependent Protein Kinase II in Squid Synaptosomes
Bass, M., Pant, H. C., Gainer, H., & Soderling, T. R. (1987) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1987.tb10001.x · Cited by 15
Koszka, C., Brent, V. A., & Rostas, J. A. P. (1991) · Neurochemical Research · doi:10.1007/bf00965549 · Cited by 14
Ogueta, S. B., MacIntosh, G. C., & Téllez‐No̊n, M. T. (1998) · Journal of Eukaryotic Microbiology · doi:10.1111/j.1550-7408.1998.tb05089.x · Cited by 14
Rieker, J. P., Swanljung-Collins, H., Montibeller, J. A., & Collins, J. H. (1987) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(87)39078-0 · Cited by 14
Ca2+/Calmodulin-Dependent Cyclic Nucleotide Phosphodiesterase (PDE1)
Sharma, R. K., & Hickie, R. A. (1996) · Elsevier eBooks · doi:10.1016/b978-012210720-7/50006-x · Cited by 13
Pharmacological profiling of a berbamine derivative for lymphoma treatment
Xu, S., Wu, S., Zhang, M., Xie, J., Lin, M., Jin, L., Zhang, J., Wang, Y., Fan, M., Fang, Z., et al. (2023) · Blood Advances · doi:10.1182/bloodadvances.2023010873 · Cited by 12
Tao-Cheng, J.-H., Vinade, L., Winters, C. A., Reese, T. S., & Dosemeci, A. (2005) · Neuroscience · doi:10.1016/j.neuroscience.2004.10.008 · Cited by 12
Rieker, J. P., Swanljung-Collins, H., & Collins, J. H. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)48169-0 · Cited by 12
Characterization of Ca2+/calmodulin-dependent protein kinase II from smooth muscle
Zhou, Z., Ando, S., Furutsuka, D., & Ikebe, M. (1995) · Biochemical Journal · doi:10.1042/bj3100517 · Cited by 11
Coomber, C. J. (1998) · Computers and Chemistry · doi:10.1016/s0097-8485(97)00002-8 · Cited by 12
Suzuki, T., Fujii, T., & Tanaka, R. (1987) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1987.tb05728.x · Cited by 10
Rostas, J. A. P., Brent, V. A., Seccombe, M. A., Weinberger, R. P., & Dunkley, P. R. (1989) · Journal of Molecular Neuroscience · doi:10.1007/bf02896893 · Cited by 10
Yamauchi, T., Sekihara, S.-I., & Ohsako, S. (1991) · Brain Research · doi:10.1016/0006-8993(91)91019-w · Cited by 9
Food Protein–Derived Peptides as Calmodulin Inhibitors
Aluko, R. E. (2010) · doi:10.1002/9780813811048.ch5 · Cited by 9
Kato, K.-I., Iwamoto, T., & Kida, S. (2013) · Molecular Brain · doi:10.1186/1756-6606-6-37 · Cited by 8
Identification of Pin1-Binding Phosphorylated Proteins in the Mouse Brain
Tatara, Y., Terakawa, T., & Uchida, T. (2010) · Bioscience Biotechnology and Biochemistry · doi:10.1271/bbb.100580 · Cited by 8
Second messenger systems and adaptation.
Gorelick, F. S. (1987) · Gut · doi:10.1136/gut.28.suppl.79 · Cited by 8
Activation is only the beginning: mechanisms that tune kinase substrate specificity
Clark, L. K., & Cullati, S. N. (2025) · Biochemical Society Transactions · doi:10.1042/bst20241420 · Cited by 7
Yamauchi, T. (2007) · YAKUGAKU ZASSHI · doi:10.1248/yakushi.127.1173 · Cited by 7
Benfenati, F., Fuxe, K., & Agnati, L. (1991) · Neurochemistry International · doi:10.1016/0197-0186(91)90011-2 · Cited by 5
Lee, D.-S., Kim, T. H., Park, H., & Kim, J.-E. (2023) · Scientific Reports · doi:10.1038/s41598-023-41014-7 · Cited by 6
Action of deltamethrin on the calcium/calmodulin‐dependent protein kinase from the rat brain
Enan, E. E., & Matsumura, F. (1993) · Pesticide Science · doi:10.1002/ps.2780370105 · Cited by 6
Calmodulin and calmodulin-binding proteins of Rhodosporidium toruloides, a basidiomycetous yeast
Liu, Y., Ohki, O., Azuma, Y., Tachikawa, T., Tsuchiya, E., Fukui, S., & Miyakawa, T. (1990) · Journal of General Microbiology · doi:10.1099/00221287-136-1-131 · Cited by 6
Serine/threonine‐specific protein kinase activity associated with viral pp60src protein
David-Pfeuty, T., & Nouvian-Dooghe, Y. (1990) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1990.tb19194.x · Cited by 5
Clark, J. M., & Matsumura, F. (1991) · Pesticide Science · doi:10.1002/ps.2780310109 · Cited by 5
Assay and Purification of Calmodulin-Dependent Protein Kinase
Sharma, R. K. (2005) · Humana Press eBooks · doi:10.1385/1-59259-949-4:305 · Cited by 5
Kakkar, R., Raju, R. V. S., & Sharma, R. K. (1996) · Cell Calcium · doi:10.1016/s0143-4160(96)90040-8 · Cited by 4
Phosphorylation of Amyloid Precursor Protein (APP) Family Proteins
Suzuki, T., Ando, K., Iijima, K., Oguchi, S., & Takeda, S. (2003) · Humana Press eBooks · doi:10.1385/1-59259-195-7:271 · Cited by 3
Serine/Threonine Protein Phosphatases in Apoptosis
Gausdal, G., Krakstad, C., Herfindal, L., & Døskeland, S. O. (2007) · Humana Press eBooks · doi:10.1007/978-1-59745-199-4_7 · Cited by 3
Yasugawa, S., Fukunaga, K., Yamamoto, H., Miyakawa, T., & Miyamoto, E. (1991) · The Japanese Journal of Pharmacology · doi:10.1016/s0021-5198(19)39958-5 · Cited by 3
Palmelund, L. B., van Woerden, G. M., Bräuner‐Osborne, H., & Wellendorph, P. (2022) · Journal of Pharmacological and Toxicological Methods · doi:10.1016/j.vascn.2022.107226 · Cited by 2
A Novel Histone-stimulated Protein Kinase in Normal and Psoriatic Epidermis
Takematsu, H., Fisher, G. J., & Voorhees, J. J. (1989) · Journal of Investigative Dermatology · doi:10.1111/1523-1747.ep12277226 · Cited by 2
TASUGAWA, S., Fukunaga, K., Yamamoto, H., Miyakawa, T., & Miyamoto, E. (1988) · Biomedical Research · doi:10.2220/biomedres.9.497 · Cited by 2
Wellendorph, P., Gauger, S. J., Andersen, J. V., Kornum, B. R., Solbak, S. M. Ø., & Frølund, B. (2025) · Pharmacological Reviews · doi:10.1016/j.pharmr.2025.100064 · Cited by 2
CaMKIIα holoenzymes self-organize into chain-like mesoscale clusters
Suzuki, T., Sumikama, T., Matsushima, K., Hasegawa, K., Sumino, A., Umeda, K., Kodera, N., Das, T., Beta, C., Murakoshi, H., et al. (2026) · Science Advances · doi:10.1126/sciadv.aeg0958 · Cited by 1
CDPKs in Plant Signaling Networks
Gupta, M. D., & Chaudhuri, S. (2001) · Springer eBooks · doi:10.1007/978-1-4615-1365-0_15 · Cited by 1
Effects of nicotine on DARPP-32 and CaMKII signaling relevant to addiction
Lee, A. M., & Picciotto, M. R. (2020) · Advances in pharmacology · doi:10.1016/bs.apha.2020.09.002 · Cited by 1
Autophosphorylation: a salient feature of protein kinases
Smith, J. A., Francis, S. H., & Corbin, J. D. (1993) · Springer eBooks · doi:10.1007/978-1-4615-2600-1_5 · Cited by 1
Various cases of rapid-equilibrium ordered bireactant mechanisms - their bases and differentiation
Huang, C. (1990) · Biochemistry · doi:10.1021/bi00453a020 · Cited by 1
(2009) · Chemical industries · doi:10.1201/9781420059656-p8 · Cited by 1
Analysis of Protein Phosphorylation in Intact Cells and Extracts
Walaas, S. I., & Østvold, A. C. (2003) · Humana Press eBooks · doi:10.1385/0-89603-415-1:1 · Cited by 1
Regulation of Ca2+/Calmodulin-Dependent Protein Kinase II By Autophosphorylation/Dephosphorylation
Kelly, P. T., Licktelg, R., & Shenolikar, S. (1987) · Calcium-Binding Proteins in Health and Disease · doi:10.1016/b978-0-12-521040-9.50035-8 · Cited by 1
Ca2+/calmodulin‐dependent protein kinase and neuronal function
Mayford, M. R. (1996) · doi:10.1002/9783527615032.ch5
Phosphoproteins and the Regulation of Vesicular Neurotransmitter Release
Hens, J. J. H., Hoogland, G., Gispen, W. H., & Graan, P. N. E. D. (1997) · Springer eBooks · doi:10.1007/978-3-642-60704-2_11
Dong, Y. (2003) · OhioLink ETD Center (Ohio Library and Information Network)
Miyamoto, E., Fukunaga, K., Ohta, Y., Yamamoto, H., Yasugawa, S., Goto, S., & Ohba, T. (1989) · Elsevier eBooks · doi:10.1016/b978-0-12-375655-8.50010-x
Mechanisms of Action of Drugs Which Alter Aqueous Humour Formation
Shahidullah (1994) · Enlighten: Theses (The University of Glasgow)
Investigation of CaMKII activation: a model of self-regulation
Hoffman, L. (2011)
Ohtsuka, S., Chen, Y., Magari, M., Ishikawa, T., Sakagami, H., Suizu, F., & Tokumitsu, H. (2025) · Biochemistry · doi:10.1021/acs.biochem.5c00477
CaMKII-RNMT axis directs activity-dependent control of RNA dynamics in neuronsPreprint
Almohammed, R., Liang, S., Bage, M., Hepburn, L. A., Davidson, L., Haward, F., Prescott, A. R., Yoshikawa, H., Lamond, A. I., Pisliakov, A. V., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.10.30.685591
Metadata
- Authors
- Lai, Y., Nairn, A. C., & Greengard, P.
- Affiliations
- Rockefeller University (US)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 1986-06
- Volume
- 83
- Issue
- 12
- Pages
- 4253-4257
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC323710
- OpenAlex
- W2011962611
- Cited by
- 292
- References
- 33
- Citations by year
- 2026: 1 · 2025: 5 · 2023: 4 · 2022: 2 · 2021: 4 · 2020: 4 · 2019: 5 · 2018: 1 · 2017: 2 · 2016: 2 · 2015: 2 · 2014: 2 · 2013: 5 · 2012: 6
- FWCI
- 10.93
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Signaling Pathways in Disease
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Keywords
- calcium/calmodulin-dependent protein kinase II, autophosphorylation, kinase regulation, synapsin I, protein phosphatase 2A, dephosphorylation, ATP requirement, enzyme activation
- MeSH terms
- Adenosine Triphosphate, Animals, Calcium, Calmodulin, Enzyme Activation, Hot Temperature, Kinetics, Phosphoprotein Phosphatases, Phosphorylation, Protein Kinases, Structure-Activity Relationship, Rats, Protein Phosphatase 2
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