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Journal articles on the topic 'Calcium-binding proteins'

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Published: 4 June 2021
Last updated: 29 July 2024

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1

Kerkut, G. A. "Calcium and calcium binding proteins." Comparative Biochemistry and Physiology Part A: Physiology 92, no. 1 (January 1989): 152. http://dx.doi.org/10.1016/0300-9629(89)90768-8.

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2

Mochida, Sumiko. "Calcium Channels and Calcium-Binding Proteins." International Journal of Molecular Sciences 24, no. 18 (September 19, 2023): 14257. http://dx.doi.org/10.3390/ijms241814257.

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Signals of nerve impulses are transmitted to excitatory cells to induce the action of organs via the activation of Ca2+ entry through voltage-gated Ca2+ channels (VGCC), which are classified based on their activation threshold into high- and low-voltage activated channels, expressed specifically for each organ [...]
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3

Heizmann, Claus W. "Intracellular Calcium-Binding Proteins." Journal of Cardiovascular Pharmacology 8 (1986): S7—S12. http://dx.doi.org/10.1097/00005344-198600088-00003.

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4

Maurer, Patrik, Erhard Hohenester, and Jürgen Engel. "Extracellular calcium-binding proteins." Current Opinion in Cell Biology 8, no. 5 (October 1996): 609–17. http://dx.doi.org/10.1016/s0955-0674(96)80101-3.

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5

Williams, R. J. P. "The calcium-binding proteins." Trends in Biochemical Sciences 16 (January 1991): 206. http://dx.doi.org/10.1016/0968-0004(91)90084-9.

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6

Michetti, Fabrizio. "The calcium-binding proteins." Giornale botanico italiano 127, no. 3 (January 1993): 470–73. http://dx.doi.org/10.1080/11263509309431029.

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7

Sohar, Istvan, John W. C. Bird, and Pamela B. Moore. "Calcium-dependent proteolysis of calcium-binding proteins." Biochemical and Biophysical Research Communications 134, no. 3 (February 1986): 1269–75. http://dx.doi.org/10.1016/0006-291x(86)90387-6.

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8

Lewit-Bentley, Anita, and Stéphane Réty. "EF-hand calcium-binding proteins." Current Opinion in Structural Biology 10, no. 6 (December 2000): 637–43. http://dx.doi.org/10.1016/s0959-440x(00)00142-1.

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9

Hutton, J. C. "Calcium-binding proteins and secretion." Cell Calcium 7, no. 5-6 (December 1986): 339–52. http://dx.doi.org/10.1016/0143-4160(86)90037-0.

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10

Hermann, A., T. L. Pauls, and C. W. Heizmann. "Calcium-binding proteins inAplysia neurons." Cellular and Molecular Neurobiology 11, no. 4 (August 1991): 371–86. http://dx.doi.org/10.1007/bf00711419.

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11

Fuhrman, J. A. "Calcium binding proteins in schistosomes." Parasitology Today 6, no. 6 (June 1990): 172–73. http://dx.doi.org/10.1016/0169-4758(90)90347-7.

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12

Van Den Eijnden-Van Raaij, A. J. M., A. L. M. De Leeuw, and R. M. Broekhuyse. "Calcium-binding lens membrane proteins." Documenta Ophthalmologica 61, no. 3-4 (January 1986): 255–65. http://dx.doi.org/10.1007/bf00142351.

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13

Tang, Shen, Xiaonan Deng, Jie Jiang, Michael Kirberger, and Jenny J. Yang. "Design of Calcium-Binding Proteins to Sense Calcium." Molecules 25, no. 9 (May 4, 2020): 2148. http://dx.doi.org/10.3390/molecules25092148.

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Calcium controls numerous biological processes by interacting with different classes of calcium binding proteins (CaBP’s), with different affinities, metal selectivities, kinetics, and calcium dependent conformational changes. Due to the diverse coordination chemistry of calcium, and complexity associated with protein folding and binding cooperativity, the rational design of CaBP’s was anticipated to present multiple challenges. In this paper we will first discuss applications of statistical analysis of calcium binding sites in proteins and subsequent development of algorithms to predict and identify calcium binding proteins. Next, we report efforts to identify key determinants for calcium binding affinity, cooperativity and calcium dependent conformational changes using grafting and protein design. Finally, we report recent advances in designing protein calcium sensors to capture calcium dynamics in various cellular environments.
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14

Gilchrist, James S. C., Michael P. Czubryt, and Grant N. Pierce. "Calcium and calcium-binding proteins in the nucleus." Molecular and Cellular Biochemistry 135, no. 1 (1994): 79–88. http://dx.doi.org/10.1007/bf00925963.

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15

Domínguez, Delfina C., Manita Guragain, and Marianna Patrauchan. "Calcium binding proteins and calcium signaling in prokaryotes." Cell Calcium 57, no. 3 (March 2015): 151–65. http://dx.doi.org/10.1016/j.ceca.2014.12.006.

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16

Fullmer, C. S., S. Edelstein, and R. H. Wasserman. "Lead-binding properties of intestinal calcium-binding proteins." Journal of Biological Chemistry 260, no. 11 (June 1985): 6816–19. http://dx.doi.org/10.1016/s0021-9258(18)88853-6.

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17

Randall, Stephen K. "Characterization of Vacuolar Calcium-Binding Proteins." Plant Physiology 100, no. 2 (October 1, 1992): 859–67. http://dx.doi.org/10.1104/pp.100.2.859.

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18

Krausz, Yodphat, Ludmilla Eylon, and Erol Cerasi. "Calcium-binding proteins and insulin release." Acta Endocrinologica 116, no. 2 (October 1987): 241–46. http://dx.doi.org/10.1530/acta.0.1160241.

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Abstract. Calcium and cAMP are interdependent regulators of glucose-induced insulin release. In the present study we investigated the importance of cAMP and calcium-binding proteins for biphasic insulin secretion by assessing the effects of two phenothiazines known to block such proteins, trifluoroperazine (TFP) and promethazine (PMZ). In isolated rat islets, during 60-min incubations with 16.7 mmol/l glucose both agents inhibited the insulin response with ID50 values of 15 μmol/l for TFP and 5 μmol/l for PMZ. Both agents decreased the maximal insulin response without gross changes in the islet sensitivity to glucose. TFP (15 μmol/l), whereas inducing 50% inhibition of second-phase insulin release, totally suppressed the cAMP response to glucose and the accompanying first-phase insulin secretion (5-min incubations); these effects of TFP could be partially reversed by isobutyl methylxanthine (IBMX). In contrast, 5 μmol/l PMZ, which produced 60% inhibition of second-phase insulin release, had no effect on first-phase insulin and cAMP responses to glucose. Furthermore, IBMX did not modify the inhibitory effect of PMZ on second-phase insulin secretion. The following is concluded: 1. TFP acts preferentially on first-phase insulin release and inhibits cAMP formation; this suggests that calmodulin plays a major role in mediating the initial glucose effect on secretion via stimulation of cAMP. 2. The islet probably contains calcium-sensitive proteins other than calmodulin, since the low concentrations of PMZ shown to inhibit second-phase insulin release lack effects on calmodulin. Synexin could be such a protein. 3. PMZ had no effect on cAMP generation and first-phase insulin release; it is speculated that synexin-like proteins may mediate the glucose effect on second-phase release by increasing the responsiveness of the islet to calcium/cAMP.
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19

COX, JOS A., and AMOS BAIROCH. "Sequence similarities in calcium-binding proteins." Nature 331, no. 6156 (February 1988): 491. http://dx.doi.org/10.1038/331491a0.

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20

Eyles, D. W., J. J. McGrath, and G. P. Reynolds. "Neuronal calcium-binding proteins and schizophrenia." Schizophrenia Research 57, no. 1 (September 2002): 27–34. http://dx.doi.org/10.1016/s0920-9964(01)00299-7.

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21

Babitch, Joseph A. "On calcium binding to channel proteins." Journal of Theoretical Biology 133, no. 4 (August 1988): 525–28. http://dx.doi.org/10.1016/s0022-5193(88)80339-4.

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22

Schelling, Claude P., Liliane Didierjean, Marthe Rizk, Jana H. Pavlovitch, Takashi Takagi, and Claus W. Heizmann. "Calcium-binding proteins in rat skin." FEBS Letters 214, no. 1 (April 6, 1987): 21–27. http://dx.doi.org/10.1016/0014-5793(87)80006-6.

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23

Fortin, Michel, Raymond Marchand, and André Parent. "Calcium-binding proteins in primate cerebellum." Neuroscience Research 30, no. 2 (February 1998): 155–68. http://dx.doi.org/10.1016/s0168-0102(97)00124-7.

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24

Penfold, Robert, James Warwicker, and Bo Jönsson. "Electrostatic Models for Calcium Binding Proteins." Journal of Physical Chemistry B 102, no. 43 (October 1998): 8599–610. http://dx.doi.org/10.1021/jp973420s.

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25

Bak, Ji Hyun, and William Bialek. "Information Flow through Calcium Binding Proteins." Biophysical Journal 106, no. 2 (January 2014): 380a. http://dx.doi.org/10.1016/j.bpj.2013.11.2151.

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26

Kreimer, Georg, Barbara Surek, Ian E. Woodrow, and Erwin Latzko. "Calcium binding by spinach stromal proteins." Planta 171, no. 2 (June 1987): 259–65. http://dx.doi.org/10.1007/bf00391103.

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27

Bhattacharya, Alok, Narendra Padhan, Ruchi Jain, and Sudha Bhattacharya. "Calcium-Binding Proteins of Entamoeba histolytica." Archives of Medical Research 37, no. 2 (February 2006): 221–25. http://dx.doi.org/10.1016/j.arcmed.2005.10.002.

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28

Winsky, L., and J. Kuźnicki. "Antibody Recognition of Calcium-Binding Proteins Depends on Their Calcium-Binding Status." Journal of Neurochemistry 66, no. 2 (November 23, 2002): 764–71. http://dx.doi.org/10.1046/j.1471-4159.1996.66020764.x.

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29

Iacopino, Anthony M. "Calcium regulation by calcium binding proteins in neurodegenerative disorders." Journal of Chemical Neuroanatomy 11, no. 4 (October 1996): 283–84. http://dx.doi.org/10.1016/s0891-0618(96)00168-8.

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30

Rothwell, Nancy J. "Calcium regulation by calcium binding proteins in neurodegenerative disorders." Cell Calcium 18, no. 6 (December 1995): 569–70. http://dx.doi.org/10.1016/0143-4160(95)90018-7.

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31

Santamaria-Kisiel, Liliana, and Gary S. Shaw. "Identification of regions responsible for the open conformation of S100A10 using chimaeric S100A11–S100A10 proteins." Biochemical Journal 434, no. 1 (January 27, 2011): 37–48. http://dx.doi.org/10.1042/bj20100887.

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S100A11 is a dimeric EF-hand calcium-binding protein. Calcium binding to S100A11 results in a large conformational change that uncovers a broad hydrophobic surface used to interact with phospholipid-binding proteins (annexins A1 and A2) and facilitate membrane vesiculation events. In contrast with other S100 proteins, S100A10 is unable to bind calcium due to deletion and substitution of calcium-ligating residues. Despite this, calcium-free S100A10 assumes an ‘open’ conformation that is very similar to S100A11 in its calcium-bound state. To understand how S100A10 is able to adopt an open conformation in the absence of calcium, seven chimaeric proteins were constructed where regions from calcium-binding sites I and II, and helices II–IV in S100A11 were replaced with the corresponding regions of S100A10. The chimaeric proteins having substitutions in calcium-binding site II displayed increased hydrophobic surface exposure as assessed by bis-ANS (4,4′-dianilino-1,1′-binaphthyl-5,5′disulfonic acid, dipotassium salt) fluorescence and phenyl-Sepharose binding in the absence of calcium. This response is similar to that observed for Ca2+–S100A11 and calcium-free S100A10. Further, this substitution resulted in calcium-insensitive binding to annexin A2 for one chimaeric protein. The results indicate that residues within site II are important in stabilizing the open conformation of S100A10 and presentation of its target binding site. In contrast, S100A11 chimaeric proteins with helical substitutions displayed poorer hydrophobic surface exposure and, consequently, unobservable annexin A2 binding. The present study represents a first attempt to systematically understand the molecular basis for the calcium-insensitive open conformation of S100A10.
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32

Yang, Tianbao, Liqun Du, and B. W. Poovaiah. "Viewpoint: Concept of redesigning proteins by manipulating calcium/calmodulin-binding domains to engineer plants with altered traits." Functional Plant Biology 34, no. 4 (2007): 343. http://dx.doi.org/10.1071/fp06293.

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The importance of calcium and calcium-binding proteins such as calmodulin in plant growth and development as well as plant response to environmental stimuli has been recognised for some time. However, it is only recently that the underlying mechanisms have begun to be unravelled. A variety of intracellular calcium signatures have been observed in response to various stimuli. However, how these changes induce downstream actions and how one can manipulate these events to alter plant response is an area of major interest. Here we discuss the recent advances on three intriguing calcium/calmodulin-regulated proteins: a calcium/calmodulin-regulated metabolic enzyme (DWF1); a chimeric calcium/calmodulin-dependent protein kinase (CCaMK); and a family of calcium/calmodulin-regulated transcription factors (AtSRs or CAMTAs). These proteins play critical roles in plant growth, plant : microbe interactions and plant response to multiple environmental signals. The identification and manipulation of calcium-binding and calmodulin-binding sites in these proteins have provided direct evidence for the role of calcium-binding and calmodulin-binding to the proteins, as well as providing new ways to rebuild the proteins and engineer plants to obtain desired traits.
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33

Bandorowicz, J., and S. Pikuła. "Annexins--multifunctional, calcium-dependent, phospholipid-binding proteins." Acta Biochimica Polonica 40, no. 3 (September 30, 1993): 281–93. http://dx.doi.org/10.18388/abp.1993_4801.

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34

Burgoyne, Robert D., and Alan Morgan. "Phospholipid-binding proteins in calcium-dependent exocytosis." Biochemical Society Transactions 20, no. 4 (November 1, 1992): 834–36. http://dx.doi.org/10.1042/bst0200834.

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35

Benjamins, René, Carlos S. Galván Ampudia, Paul J. J. Hooykaas, and Remko Offringa. "PINOID-Mediated Signaling Involves Calcium-Binding Proteins." Plant Physiology 132, no. 3 (June 12, 2003): 1623–30. http://dx.doi.org/10.1104/pp.103.019943.

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36

Hiraoki, Toshifumi, and Hans J. Vogel. "Structure and Function of Calcium-Binding Proteins." Journal of Cardiovascular Pharmacology 10 (1987): S14—S31. http://dx.doi.org/10.1097/00005344-198710001-00004.

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37

Heizmann, Claus W. "Calcium-Binding Proteins of the EF-Type." Journal of Cardiovascular Pharmacology 12, Supplement (1988): 30–37. http://dx.doi.org/10.1097/00005344-198800125-00006.

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38

Heizmann, Claus W. "Calcium-Binding Proteins of the EF-Type." Journal of Cardiovascular Pharmacology 12 (1988): 30–37. http://dx.doi.org/10.1097/00005344-198806125-00006.

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39

Mooibroek, M. J., D. F. Michiel, and J. H. Wang. "Clathrin light chains are calcium-binding proteins." Journal of Biological Chemistry 262, no. 1 (January 1987): 25–28. http://dx.doi.org/10.1016/s0021-9258(19)75879-7.

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40

Klee, Claude B. "Calcium-dependent phospholipid- (and membrane-) binding proteins." Biochemistry 27, no. 18 (September 6, 1988): 6645–53. http://dx.doi.org/10.1021/bi00418a001.

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41

Leiser, M., and L. M. Sherwood. "Calcium-binding proteins in the parathyroid gland." Journal of Biological Chemistry 264, no. 5 (February 1989): 2792–800. http://dx.doi.org/10.1016/s0021-9258(19)81683-6.

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42

Maruyama, Kei, and Yoshiaki Nonomura. "CALCIUM BINDING PROTEINS OF CEREBRUM AND CEREBELLUM." Japanese Journal of Pharmacology 39 (1985): 81. http://dx.doi.org/10.1016/s0021-5198(19)63330-5.

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43

Selvam, Ramasamy, and Periandavan Kalaiselvi. "Oxalate binding proteins in calcium oxalate nephrolithiasis." Urological Research 31, no. 4 (August 1, 2003): 242–56. http://dx.doi.org/10.1007/s00240-003-0316-3.

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44

Tokuda, Masaaki, Navin C. Khanna, and David M. Waisman. "Identification of bovine brain calcium binding proteins." Cell Calcium 8, no. 3 (June 1987): 229–39. http://dx.doi.org/10.1016/0143-4160(87)90021-2.

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45

Burgoyne, R. D., and M. J. Geisow. "The annexin family of calcium-binding proteins." Cell Calcium 10, no. 1 (January 1989): 1–10. http://dx.doi.org/10.1016/0143-4160(89)90038-9.

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46

Baimbridge, K. G., M. R. Celio, and J. H. Rogers. "Calcium-binding proteins in the nervous system." Trends in Neurosciences 15, no. 8 (August 1992): 303–8. http://dx.doi.org/10.1016/0166-2236(92)90081-i.

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47

Moore, Blake W. "Identification of calcium binding proteins from brain." Neurochemical Research 13, no. 8 (August 1988): 693–97. http://dx.doi.org/10.1007/bf00971590.

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48

Zhuang, O., and A. Stracher. "Study on the platelet calcium binding proteins." Thrombosis Research 63, no. 2 (July 1991): 277. http://dx.doi.org/10.1016/0049-3848(91)90318-q.

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49

Israelson, Adrian, Laetitia Arzoine, Salah Abu-hamad, Vladimir Khodorkovsky, and Varda Shoshan-Barmatz. "A Photoactivable Probe for Calcium Binding Proteins." Chemistry & Biology 12, no. 11 (November 2005): 1169–78. http://dx.doi.org/10.1016/j.chembiol.2005.08.006.

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50

Parent, A., M. Fortin, P. Y. Côté, and F. Cicchetti. "Calcium-binding proteins in primate basal ganglia." Neuroscience Research 25, no. 4 (August 1996): 309–34. http://dx.doi.org/10.1016/0168-0102(96)01065-6.

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