Reviews

  1. Azuma, M., C. Fukiage, L. L. David, and T. R. Shearer. 1997. Activation of calpain in lens: a review and proposed mechanism. Exp. Eye Res. 64:529-538.

    2.

  2. Bachs, O., N. Agell, and E. Carafoli. 1994. Calmodulin and calmodulin-binding proteins in the nucleus. Cell Calcium. 16:289-296.

    3.

  3. Barrett, A. W. and C. Scully. 1994. S100 protein in oral biology and pathology. J. Oral. Pathol. Med. 23:433-440.

    4.

  4. Berthelot, J. M., Y. Maugars, A. Prost, and P. Youinou. 1995. Rheumatoid arthritis and filaggrin. A review. Rev. Rhum. Engl. Ed. 62:127-138.

    5.

  5. Carafoli, E. and M. Molinari. 1998. Calpain: a protease in search of a function? [published erratum appears in Biochem Biophys Res Commun 1998 Aug 19;249(2):572]. Biochem. Biophys. Res. Commun. 247:193-203.

    6.

  6. Coudrey, L. 1998. The troponins. Arch. Intern. Med. 158:1173-1180.

    7.

  7. Crivici, A. and M. Ikura. 1995. Molecular and structural basis of target recognition by calmodulin. Annu. Rev. Biophys. Biomol. Struct. 24:85-116.

    8.

  8. Dear, N., K. Matena, M. Vingron, and T. Boehm. 1997. A new subfamily of vertebrate calpains lacking a calmodulin-like domain: implications for calpain regulation and evolution. Genomics. 45:175-184.

    9.

  9. Emori, Y. 1997. [Calpain: an approach using Drosophila melanogaster]. Tanpakushitsu. Kakusan. Koso. 42:2175-2180.

    10.

  10. Fano, G., S. Biocca, S. Fulle, M. A. Mariggio, S. Belia, and P. Calissano. 1995. The S-100: a protein family in search of a function. Prog. Neurobiol. 46:71-82.

    11.

  11. Filipek, A., U. Wojda, W. Lesniak, and J. Kuznicki. 1996. [Calcyclin--calcium binding protein of the S-100 protein]. Postepy. Biochem. 42:213-217.

    12.

  12. Finn, B. E. and S. Forsen. 1995. The evolving model of calmodulin structure, function and activation. Structure. 3:7-11.

    13.

  13. Gnegy, M. E. 1995. Calmodulin: effects of cell stimuli and drugs on cellular activation. Prog. Drug. Res. 45:33-65.

    14.

  14. Goll, D. E., V. F. Thompson, R. G. Taylor, and T. Zalewska. 1992. Is calpain activity regulated by membranes and autolysis or by calcium and calpastatin? Bioessays 14:549-556.

    15.

  15. Guerini, D. 1997. Calcineurin: not just a simple protein phosphatase. Biochem. Biophys. Res. Commun. 235:271-275.

    16.

  16. Hermann, A. and J. A. Cox. 1995. Sarcoplasmic calcium-binding protein. Comp. Biochem. Physiol. Biochem. Mol. Biol. 111:337-345.

    17.

  17. Ikura, M. 1996. Calcium binding and conformational response in EF-hand proteins. Trends. Biochem. Sci. 21:14-17.

    18.

  18. Izumo, S. and H. Aoki. 1998. Calcineurin--the missing link in cardiac hypertrophy [news]. Nat. Med. 4:661-662.

    19.

  19. James, P., T. Vorherr, and E. Carafoli. 1995. Calmodulin-binding domains: just two faced or multi-faceted? Trends. Biochem. Sci. 20:38-42.

    20.

  20. Jin, S., L. Yin, D. S. Wang, and H. T. Liu. 1995. [The regulation of calmodulin in the cell cycle]. Shih. Yen. Sheng. Wu. Hsueh. Pao. 28:121-129.

    21.

  21. Johnson, K. A. and F. A. Quiocho. 1996. Protein kinases. Twitching worms catch S100 [news; comment]. Nature 380:585-587.

    22.

  22. Keltner, J. L. and C. E. Thirkill. 1998. Cancer-associated retinopathy vs recoverin-associated retinopathy [editorial]. Am. J. Ophthalmol. 126:296-302.

    23.

  23. Klee, C. B., H. Ren, and X. Wang. 1998. Regulation of the calmodulin-stimulated protein phosphatase, calcineurin. J. Biol. Chem. 273:13367-13370.

    24.

  24. Krieg, P., M. Schuppler, R. Koesters, A. Mincheva, P. Lichter, and F. Marks. 1997. Repetin (Rptn), a new member of the "fused gene" subgroup within the S100 gene family encoding a murine epidermal differentiation protein. Genomics. 43:339-348.

    25.

  25. Maki, M. 1998. [A family of the intracellular calcium-binding proteins with five EF-hand motifs]. Seikagaku. 70:202-207.

    26.

  26. Maki, M., S. V. Narayana, and K. Hitomi. 1997. A growing family of the Ca2+-binding proteins with five EF-hand motifs [letter]. Biochem. J. 328:718-720.

    27.

  27. Matsui, H., Y. F. Lu, and A. Moriwaki. 1998. [Physiological role of calcineurin in central nervous system]. Tanpakushitsu. Kakusan. Koso. 43:1039-1046.

    28.

  28. Nakayama, S. 1995. [Evolution of EF-hand proteins]. Seikagaku. 67:131-137.

    29.

  29. Nishimura, H. and Y. Yazaki. 1995. [Myosin light chain]. Nippon. Rinsho. 53 Su Pt 1:243-245.

    30.

  30. Nixon, R. A., K. I. Saito, F. Grynspan, W. R. Griffin, S. Katayama, T. Honda, P. S. Mohan, T. B. Shea, and M. Beermann. 1994. Calcium-activated neutral proteinase (calpain) system in aging and Alzheimer's disease. Ann. N. Y. Acad. Sci. 747:77-91.

    31.

  31. Omori, N. and F. Shibasaki. 1998. [The role of calcineurin in the regulation of transcription factors]. Tanpakushitsu. Kakusan. Koso. 43:1047-1054.

    32.

  32. Ono, Y., H. Sorimachi, and K. Suzuki. 1998. Structure and physiology of calpain, an enigmatic protease. Biochem. Biophys. Res. Commun. 245:289-294.

    33.

  33. Reed, M. J. and E. H. Sage. 1996. SPARC and the extracellular matrix: implications for cancer and wound repair. Curr. Top. Microbiol. Immunol. 213:81-94.

    34.

  34. Salisbury, J. L. 1995. Centrin, centrosomes, and mitotic spindle poles. Curr. Opin. Cell Biol. 7:39-45.

    35.

  35. Schafer, B. W. and C. W. Heizmann. 1996. The S100 family of EF-hand calcium-binding proteins: functions and pathology. Trends. Biochem. Sci. 21:134-140.

    36.

  36. Shimomura, O. 1995. A short story of aequorin. Biol. Bull. 189:1-5.

    37.

  37. Shuntoh, H., R. Sugiura, and T. Kuno. 1998. [The structure and regulation of calcineurin]. Tanpakushitsu. Kakusan. Koso. 43:952-958.

    38.

  38. Sugiura, R., T. Kuno, and H. Shuntoh. 1998. [Calcineurin-mediated signal transduction pathways in yeast]. Tanpakushitsu. Kakusan. Koso. 43:1021-1028.

    39.

  39. Suzuki, K. and H. Sorimachi. 1998. A novel aspect of calpain activation. FEBS Lett. 433:1-4.

    40.

  40. Suzuki, K., H. Sorimachi, T. Yoshizawa, K. Kinbara, and S. Ishiura. 1995. Calpain: novel family members, activation, and physiologic function. Biol. Chem. Hoppe. Seyler. 376:523-529.

    41.

  41. Tagawa, K., H. Sorimachi, S. Ishiura, K. Suzuki, and Y. Seyama. 1997. [Calpain super family and its interacting-proteins]. Tanpakushitsu. Kakusan. Koso. 42:2165-2174.

    42.

  42. Takano, E. and M. Maki. 1997. [Calpastatin: molecular mechanism of calpain inhibition]. Tanpakushitsu. Kakusan. Koso. 42:2181-2188.

    43.

  43. Takuwa, N., W. Zhou, and Y. Takuwa. 1995. Calcium, calmodulin and cell cycle progression. Cell Signal. 7:93-104.

    44.

  44. Tamura, K. 1998. [Multiple actions of tacrolimus and cyclosporin A as specific inhibitors of calcineurin]. Tanpakushitsu. Kakusan. Koso. 43:1118-1130.

    45.

  45. Vogel, H. J. 1994. The Merck Frosst Award Lecture 1994. Calmodulin: a versatile calcium mediator protein. Biochem. Cell Biol. 72:357-376.

    46.

  46. Wang, K. K. and P. W. Yuen. 1994. Calpain inhibition: an overview of its therapeutic potential. Trends. Pharmacol. Sci. 15:412-419.

    47.

  47. Yakel, J. L. 1997. Calcineurin regulation of synaptic function: from ion channels to transmitter release and gene transcription. Trends. Pharmacol. Sci. 18:124-134.

    48.

  48. Yazawa, M. 1994. [Calmodulin--Ca2+ binding and enzyme activation]. Seikagaku. 66:1145-1149.

    49.

  49. Yoshino, H. and Y. Izumi. 1994. [How does calmodulin express Ca(2+)-signals--recent progress by solution X-ray scattering]. Seikagaku. 66:1523-1528.

    50.

  50. Zimmer, D. B., E. H. Cornwall, A. Landar, and W. Song. 1995. The S100 protein family: history, function, and expression. Brain Res. Bull. 37:417-429.

Binding

  1. Afshar, M., L. S. Caves, L. Guimard, R. E. Hubbard, B. Calas, G. Grassy, and J. Haiech. 1994. Investigating the high affinity and low sequence specificity of calmodulin binding to its targets. J. Mol. Biol. 244:554-571.

    2.

  2. al Hillawi, E., D. G. Bhandari, H. R. Trayer, and I. P. Trayer. 1995. The effects of phosphorylation of cardiac troponin-I on its interactions with actin and cardiac troponin-C. Eur. J. Biochem. 228:962-970.

    3.

  3. Alcazar, A., M. E. Martin, E. Soria, S. Rodriguez, J. L. Fando, and M. Salinas. 1995. Purification and characterization of guanine nucleotide-exchange factor, eIF-2B, and p37 calmodulin-binding protein from calf brain. J. Neurochem. 65:754-761.

    4.

  4. Anagli, J., F. Hofmann, M. Quadroni, T. Vorherr, and E. Carafoli. 1995. The calmodulin-binding domain of the inducible (macrophage) nitric oxide synthase. Eur. J. Biochem. 233:701-708.

    5.

  5. Anderson, J. T., R. P. Rogers, and H. W. Jarrett. 1996. Ca2+-calmodulin binds to the carboxyl-terminal domain of dystrophin. J. Biol. Chem. 271:6605-6610.

    6.

  6. Anglister, J., H. Ren, C. B. Klee, and A. Bax. 1995. NMR identification of calcineurin B residues affected by binding of a calcineurin A peptide. FEBS Lett. 375:108-112.

    7.

  7. Arazi, T., G. Baum, W. A. Snedden, B. J. Shelp, and H. Fromm. 1995. Molecular and biochemical analysis of calmodulin interactions with the calmodulin-binding domain of plant glutamate decarboxylase. Plant. Physiol. 108:551-561.

    8.

  8. Arbuzova, A., J. Wang, D. Murray, J. Jacob, D. S. Cafiso, and S. McLaughlin. 1997. Kinetics of interaction of the myristoylated alanine-rich C kinase substrate, membranes, and calmodulin. J. Biol. Chem. 272:27167-27177.

    9.

  9. Arthur, J. S. and C. Crawford. 1996. Investigation of the interaction of m-calpain with phospholipids: calpain-phospholipid interactions. Biochim. Biophys. Acta 1293:201-206.

    10.

  10. Auerswald, E. A., D. K. Nagler, S. Gross, I. Assfalg Machleidt, M. T. Stubbs, C. Eckerskorn, W. Machleidt, and H. Fritz. 1996. Hybrids of chicken cystatin with human kininogen domain 2 sequences exhibit novel inhibition of calpain, improved inhibition of actinidin and impaired inhibition of papain, cathepsin L and cathepsin B. Eur. J. Biochem. 235:534-542.

    11.

  11. Babiychuk, E. B. and A. Sobieszek. 1997. Oligomerization of smooth muscle myosin light chain kinase and its modifications by melittin and calmodulin. Biopolymers. 42:673-686.

    12.

  12. Bao, J., A. H. Sharp, M. V. Wagster, M. Becher, G. Schilling, C. A. Ross, V. L. Dawson, and T. M. Dawson. 1996. Expansion of polyglutamine repeat in huntingtin leads to abnormal protein interactions involving calmodulin. Proc. Natl. Acad. Sci. U. S. A. 93:5037-5042.

    13.

  13. Barth, A., S. R. Martin, and P. M. Bayley. 1998. Specificity and symmetry in the interaction of calmodulin domains with the skeletal muscle myosin light chain kinase target sequence. J. Biol. Chem. 273:2174-2183.

    14.

  14. Bartoli, M., A. Monneron, and D. Ladant. 1998. Interaction of calmodulin with striatin, a WD-repeat protein present in neuronal dendritic spines. J. Biol. Chem. 273:22248-22253.

    15.

  15. Baudier, J., E. Bergeret, N. Bertacchi, H. Weintraub, J. Gagnon, and J. Garin. 1995. Interactions of myogenic bHLH transcription factors with calcium-binding calmodulin and S100a (alpha alpha) proteins. Biochemistry 34:7834-7846.

    16.

  16. Baum, G., S. Lev Yadun, Y. Fridmann, T. Arazi, H. Katsnelson, M. Zik, and H. Fromm. 1996. Calmodulin binding to glutamate decarboxylase is required for regulation of glutamate and GABA metabolism and normal development in plants. EMBO J. 15:2988-2996.

    17.

  17. Benguria, A., J. Martin Nieto, G. Benaim, and A. Villalobo. 1995. Regulatory interaction between calmodulin and the epidermal growth factor receptor. Ann. N. Y. Acad. Sci. 766:472-476.

    18.

  18. Bing, W., I. D. Fraser, and S. B. Marston. 1997. Troponin I and troponin T interact with troponin C to produce different Ca2+-dependent effects on actin-tropomyosin filament motility. Biochem. J. 327:335-340.

    19.

  19. Bjork, J., S. Lundberg, and L. Backman. 1995. Characterization of the binding of calmodulin to non-erythroid spectrin. Eur. J. Cell Biol. 66:200-204.

    20.

  20. Bouhoute, A. and G. Leclercq. 1995. Modulation of estradiol and DNA binding to estrogen receptor upon association with calmodulin. Biochem. Biophys. Res. Commun. 208:748-755.

    21.

  21. Bouhss, A., M. Vincent, H. Munier, A. M. Gilles, M. Takahashi, O. Barzu, A. Danchin, and J. Gallay. 1996. Conformational transitions within the calmodulin-binding site of Bordetella pertussis adenylate cyclase studied by time-resolved fluorescence of Trp242 and circular dichroism. Eur. J. Biochem. 237:619-628.

    22.

  22. Bowser, J. and A. S. Reddy. 1997. Localization of a kinesin-like calmodulin-binding protein in dividing cells of Arabidopsis and tobacco. Plant. J. 12:1429-1437.

    23.

  23. Brill, S., S. Li, C. W. Lyman, D. M. Church, J. J. Wasmuth, L. Weissbach, A. Bernards, and A. J. Snijders. 1996. The Ras GTPase-activating-protein-related human protein IQGAP2 harbors a potential actin binding domain and interacts with calmodulin and Rho family GTPases. Mol. Cell Biol. 16:4869-4878.

    24.

  24. Brown, S. E., S. R. Martin, and P. M. Bayley. 1997. Kinetic control of the dissociation pathway of calmodulin-peptide complexes. J. Biol. Chem. 272:3389-3397.

    25.

  25. Brownawell, A. M. and C. E. Creutz. 1997. Calcium-dependent binding of sorcin to the N-terminal domain of synexin (annexin VII). J. Biol. Chem. 272:22182-22190.

    26.

  26. Browne, J. P., M. Strom, S. R. Martin, and P. M. Bayley. 1997. The role of beta-sheet interactions in domain stability, folding, and target recognition reactions of calmodulin. Biochemistry 36:9550-9561.

    27.

  27. Buku, A., W. C. Probst, K. R. Weiss, and J. Heierhorst. 1996. Studies of the calmodulin-binding site of twitchin with synthetic peptides using fluorescence and CD spectroscopy. Biochem. Biophys. Res. Commun. 218:854-859.

    28.

  28. Camoni, L., J. F. Harper, and M. G. Palmgren. 1998. 14-3-3 proteins activate a plant calcium-dependent protein kinase (CDPK). FEBS Lett. 430:381-384.

    29.

  29. Cao, Q. P., C. A. McGrath, E. F. Baril, P. J. Quesenberry, and G. P. Reddy. 1995. The 68 kDa calmodulin-binding protein is tightly associated with the multiprotein DNA polymerase alpha-primase complex in HeLa cells. Biochemistry 34:3878-3883.

    30.

  30. Capelli, N., F. Barja, D. Van Tuinen, J. Monnat, G. Turian, and R. Ortega Perez. 1997. Purification of a 47-kDa calmodulin-binding polypeptide as an actin-binding protein from Neurospora crassa [published erratum appears in FEMS Microbiol Lett 1997 May 1;150(1);173]. FEMS. Microbiol. Lett. 147:215-220.

    31.

  31. Castets, F., M. Bartoli, J. V. Barnier, G. Baillat, P. Salin, A. Moqrich, J. P. Bourgeois, F. Denizot, G. Rougon, G. Calothy, and A. Monneron. 1996. A novel calmodulin-binding protein, belonging to the WD-repeat family, is localized in dendrites of a subset of CNS neurons. J. Cell Biol. 134:1051-1062.

    32.

  32. Chabbert, M., E. Piemont, F. G. Prendergast, and H. Lami. 1995. Fluorescence of a tryptophan bearing peptide from smooth muscle myosin light chain kinase upon binding to two closely related calmodulins. Arch. Biochem. Biophys. 322:429-436.

    33.

  33. Chapin, S. J., C. Enrich, B. Aroeti, R. J. Havel, and K. E. Mostov. 1996. Calmodulin binds to the basolateral targeting signal of the polymeric immunoglobulin receptor. J. Biol. Chem. 271:1336-1342.

    34.

  34. Chen, C. K., J. Inglese, R. J. Lefkowitz, and J. B. Hurley. 1995. Ca(2+)-dependent interaction of recoverin with rhodopsin kinase. J. Biol. Chem. 270:18060-18066.

    35.

  35. Cohen, O., E. Feinstein, and A. Kimchi. 1997. DAP-kinase is a Ca2+/calmodulin-dependent, cytoskeletal-associated protein kinase, with cell death-inducing functions that depend on its catalytic activity. EMBO J. 16:998-1008.

    36.

  36. Coluccio, L. M. 1994. Differential calmodulin binding to three myosin-1 isoforms from liver. J. Cell Sci. 107:2279-2284.

    37.

  37. Craescu, C. T., A. Bouhss, J. Mispelter, E. Diesis, A. Popescu, M. Chiriac, and O. Barzu. 1995. Calmodulin binding of a peptide derived from the regulatory domain of Bordetella pertussis adenylate cyclase. J. Biol. Chem. 270:7088-7096.

    38.

  38. Craven, C. J., B. Whitehead, S. K. Jones, E. Thulin, G. M. Blackburn, and J. P. Waltho. 1996. Complexes formed between calmodulin and the antagonists J-8 and TFP in solution. Biochemistry 35:10287-10299.

    39.

  39. Croall, D. E. and K. S. McGrody. 1994. Domain structure of calpain: mapping the binding site for calpastatin. Biochemistry 33:13223-13230.

    40.

  40. Dash, S., W. Niemaczura, and H. M. Harrington. 1997. Characterization of the basic amphiphilic alpha-helix calmodulin-binding domain of a 61.5 kDa tobacco calmodulin-binding protein. Biochemistry 36:2025-2029.

    41.

  41. Deloulme, J. C., L. Prichard, O. Delattre, and D. R. Storm. 1997. The prooncoprotein EWS binds calmodulin and is phosphorylated by protein kinase C through an IQ domain. J. Biol. Chem. 272:27369-27377.

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  42. Dingley, A. J., J. P. Mackay, B. E. Chapman, M. B. Morris, P. W. Kuchel, B. D. Hambly, and G. F. King. 1995. Measuring protein self-association using pulsed-field-gradient NMR spectroscopy: application to myosin light chain 2. J. Biomol. NMR. 6:321-328.

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    45.

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    46.

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    49.

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    50.

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    51.

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Derivatisation

  1. Ames, J. B., T. Porumb, T. Tanaka, M. Ikura, and L. Stryer. 1995. Amino-terminal myristoylation induces cooperative calcium binding to recoverin. J. Biol. Chem. 270:4526-4533.

    2.

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    4.

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    6.

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    7.

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    8.

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    9.

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    10.

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    11.

  11. Fukuda, K., Y. Ozaki, K. Satoh, S. Kume, M. Tawata, T. Onaya, K. Sakurada, M. Seto, and Y. Sasaki. 1997. Phosphorylation of myosin light chain in resting platelets from NIDDM patients is enhanced: correlation with spontaneous aggregation. Diabetes. 46:488-493.

    12.

  12. Gagnon, A. and J. Welsh. 1997. Modulation and phosphorylation of calbindin-D28K correlates with protein kinase C activation1. Biochem. Cell Biol. 75:33-40.

    13.

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    14.

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    15.

  15. Harada, T., M. Seto, Y. Sasaki, S. London, Z. Luo, and M. Mayberg. 1995. The time course of myosin light-chain phosphorylation in blood-induced vasospasm. Neurosurgery. 36:1178-1182.

    16.

  16. Heierhorst, J., W. C. Probst, R. A. Kohanski, A. Buku, and K. R. Weiss. 1995. Phosphorylation of myosin regulatory light chains by the molluscan twitchin kinase. Eur. J. Biochem. 233:426-431.

    17.

  17. Helms, M. K., D. A. Malencik, and S. R. Anderson. 1998. Flexibility involving the intermolecular dityrosyl cross-links of enzymatically polymerized calmodulin. Biochemistry 37:8378-8384.

    18.

  18. Hohenadl, C., K. Mann, U. Mayer, R. Timpl, M. Paulsson, and D. Aeschlimann. 1995. Two adjacent N-terminal glutamines of BM-40 (osteonectin, SPARC) act as amine acceptor sites in transglutaminaseC-catalyzed modification. J. Biol. Chem. 270:23415-23420.

    19.

  19. Ishibashi, S., K. Kawasaki, Y. Tate, T. Ihara, and K. Shimada. 1995. Nitroglycerin inhibits the phosphorylation of intermediate filament proteins rather than myosin light chain on porcine coronary artery sustained contraction. Experientia. 51:980-985.

    20.

  20. Jha, P. K., C. Mao, and S. Sarkar. 1996. Photo-cross-linking of rabbit skeletal troponin I deletion mutants with troponin C and its thiol mutants: the inhibitory region enhances binding of troponin I fragments to troponin C. Biochemistry 35:11026-11035.

    21.

  21. Joyal, J. L., D. L. Crimmins, R. S. Thoma, and D. B. Sacks. 1996. Identification of insulin-stimulated phosphorylation sites on calmodulin. Biochemistry 35:6267-6275.

    22.

  22. Kuo, W. N., U. Ganesan, D. L. Davis, and D. L. Walbey. 1994. Regulation of the phosphorylation of calpain II and its inhibitor. Mol. Cell Biochem. 136:157-161.

    23.

  23. Kureishi, Y., S. Kobayashi, M. Amano, K. Kimura, H. Kanaide, T. Nakano, K. Kaibuchi, and M. Ito. 1997. Rho-associated kinase directly induces smooth muscle contraction through myosin light chain phosphorylation. J. Biol. Chem. 272:12257-12260.

    24.

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    25.

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    26.

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    27.

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    28.

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    29.

  29. Lucius, C., A. Arner, A. Steusloff, M. Troschka, F. Hofmann, K. Aktories, and G. Pfitzer. 1998. Clostridium difficile toxin B inhibits carbachol-induced force and myosin light chain phosphorylation in guinea-pig smooth muscle: role of Rho proteins. J. Physiol. Lond. 506:83-93.

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    35.

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    36.

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    37.

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    38.

  38. Rao, A. S. and A. S. Balasubramanian. 1994. Phosphorylation of casein, fibrinogen and calmodulin by a glycoprotein protein kinase from monkey cerebellum: a casein kinase II-like enzyme. Indian J. Biochem. Biophys. 31:392-397.

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    53.

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Expression

  1. Abbott, L. C. and D. M. Jacobowitz. 1995. Development of calretinin-immunoreactive unipolar brush-like cells and an afferent pathway to the embryonic and early postnatal mouse cerebellum. Anat. Embryol. Berl. 191:541-559.

    2.

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    3.

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    18.

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Nucleotide

Sequence

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    2.

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    3.

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    4.

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    5.

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    6.

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    7.

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    8.

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    9.

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    10.

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    11.

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    12.

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    13.

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    14.

  14. Chatterjee, A., T. Tanaka, J. E. Parrish, and G. E. Herman. 1995. Refined mapping of caltractin in human Xq28 and in the homologous region of the mouse X chromosome places the gene within the bare patches (Bpa) and striated (Str) critical regions. Mamm. Genome. 6:802-804.

    15.

  15. Chen, J. J., C. E. Reid, V. Band, and E. J. Androphy. 1995. Interaction of papillomavirus E6 oncoproteins with a putative calcium-binding protein. Science 269:529-531.

    16.

  16. Chye, M. L., C. M. Liu, and C. T. Tan. 1995. A cDNA clone encoding Brassica calmodulin. Plant. Mol. Biol. 27:419-423.

    17.

  17. DeAngelis, M. M., J. P. Doucet, S. Drury, S. T. Sherry, M. B. Robichaux, Z. Den, M. Z. Pelias, G. M. Ditta, B. J. Keats, P. L. Deininger, and M. A. Batzer. 1998. Assembly of a high-resolution map of the Acadian Usher syndrome region and localization of the nuclear EF-hand acidic gene. Biochim. Biophys. Acta 1407:84-91.

    18.

  18. Dell'Angelica, E. C., C. H. Schleicher, and J. A. Santome. 1994. Primary structure and binding properties of calgranulin C, a novel S100-like calcium-binding protein from pig granulocytes. J. Biol. Chem. 269:28929-28936.

    19.

  19. Drayer, A. L., M. E. Meima, M. W. Derks, R. Tuik, and P. J. van Haastert. 1995. Mutation of an EF-hand Ca(2+)-binding motif in phospholipase C of Dictyostelium discoideum: inhibition of activity but no effect on Ca(2+)-dependence. Biochem. J. 311:505-510.

    20.

  20. Dyer, J. R., W. S. Sossin, and M. Klein. 1996. Cloning and characterization of aplycalcin and Aplysia neurocalcin, two new members of the calmodulin superfamily of small calcium-binding proteins. J. Neurochem. 67:932-942.

    21.

  21. Ebenbichler, C. F., H. Stoiber, R. Schneider, J. R. Patsch, and M. P. Dierich. 1996. The human immunodeficiency virus type 1 transmembrane gp41 protein is a calcium-binding protein and interacts with the putative second-receptor molecules in a calcium-dependent manner. J. Virol. 70:1723-1728.

    22.

  22. Eschenlauer, S. C., N. R. McEwan, R. E. Calza, R. J. Wallace, R. Onodera, and C. J. Newbold. 1998. Phylogenetic position and codon usage of two centrin genes from the rumen ciliate protozoan, Entodinium caudatum. FEMS. Microbiol. Lett. 166:147-154.

    23.

  23. Farber, P. M., R. Graeser, R. M. Franklin, and B. Kappes. 1997. Molecular cloning and characterization of a second calcium-dependent protein kinase of Plasmodium falciparum. Mol. Biochem. Parasitol. 87:211-216.

    24.

  24. Fischer, R., J. Julsgart, and M. W. Berchtold. 1998. High affinity calmodulin target sequence in the signalling molecule PI 3-kinase. FEBS Lett. 425:175-177.

    25.

  25. Fulton, C., E. Y. Lai, and S. P. Remillard. 1995. A flagellar calmodulin gene of Naegleria, coexpressed during differentiation with flagellar tubulin genes, shares DNA, RNA, and encoded protein sequence elements. J. Biol. Chem. 270:5839-5848.

    26.

  26. Fyrberg, C., H. Parker, B. Hutchison, and E. Fyrberg. 1994. Drosophila melanogaster genes encoding three troponin-C isoforms and a calmodulin-related protein. Biochem. Genet. 32:119-135.

    27.

  27. Galaud, J. P., V. Laval, M. Carriere, A. Barre, H. Canut, P. Rouge, and R. Pont Lezica. 1997. Osmotic stress activated expression of an Arabidopsis plasma membrane-associated protein: sequence and predicted secondary structure. Biochim. Biophys. Acta 1341:79-86.

    28.

  28. Gill, R. K. and S. Christakos. 1995. Regulation by estrogen through the 5'-flanking region of the mouse calbindin-D28k gene. Mol. Endocrinol. 9:319-326.

    29.

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    30.

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    2.

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    3.

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    7.

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