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(PXE), an autosomal recessive disease characterized by ectopic calcification of elastic fibers in dermal, ocular and vascular tissues. Similar to other ABC transporters, ABCC6 encloses the core structure of four domains: two transmembrane domains (TMDs) and two nucleotide binding domains (NBDs) but also an additional N-terminal extension, including a transmembrane domain (TMD0) and a cytosolic loop (L0), which is only found in some members of ABCC subfamily, and for which the function remains to be established. To investigate the functional roles of this N-terminal region, we generated several domain deletion constructs of ABCC6, expressed in HEK293 and polarized LLC-PK1 cells. ABCC6 lacking TMD0 displayed full transport activity as the wild type protein. Unlike the wild type protein, ABCC6 without L0 was not targeted to the basolateral membrane. Moreover, homology modeling of L0 suggests that it forms an ATPase regulatory domain. Furthermore, we show that the expression of ABCC6 is linked to a cellular influx of Ca2+. The results suggest that TMD0 is not required for transport function and that L0 maintains ABCC6 in a targeting-competent state for the basolateral membrane and might be involved in regulating the NBDs. 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MF, Ostuni A, Infantino V, et al. (2008) Identification of a new splice variant of the human ABCC6 transporter. Biochem Res Int 2008:912478. doi:10.1155\u002F2008\u002F912478",{"id":22,"text":1230,"url":22,"identifiers":22},"Babenko AP, Bryan J (2002) SUR-dependent modulation of KATP channels by an N-terminal KIR6.2 peptide. defining intersubunit gating interactions. J Biol Chem 277:43997–44004. doi:10.1074\u002Fjbc.M208085200",{"id":22,"text":1232,"url":22,"identifiers":22},"Bakos E, Evers R, Calenda G, et al. (2000) Characterization of the amino-terminal regions in the human multidrug resistance protein (MRP1). J Cell Sci 113(Pt 24):4451–4461",{"id":22,"text":1234,"url":22,"identifiers":22},"Bakos E, Evers R, Szakács G, et al. (1998) Functional multidrug resistance protein (MRP1) lacking the N-terminal transmembrane domain. J Biol Chem 273:32167–32175",{"id":22,"text":1236,"url":22,"identifiers":22},"Belinsky MG, Chen Z-S, Shchaveleva I, et al. (2002) Characterization of the drug resistance and transport properties of multidrug resistance protein 6 (MRP6, ABCC6). Cancer Res 62:6172–6177",{"id":22,"text":1238,"url":22,"identifiers":22},"Biasini M, Bienert S, Waterhouse A, et al. (2014) SWISS-MODEL: modelling protein tertiary and quaternary structure using evolutionary information. Nucleic Acids Res 42:W252–W258. doi:10.1093\u002Fnar\u002Fgku340",{"id":22,"text":1240,"url":22,"identifiers":22},"Birnbaumer L (2009) The TRPC class of ion channels: a critical review of their roles in slow, sustained increases in intracellular Ca(2+) concentrations. Annu Rev Pharmacol Toxicol 49:395–426. doi:10.1146\u002Fannurev.pharmtox.48.113006.094928",{"id":22,"text":1242,"url":22,"identifiers":22},"Boraldi F, Quaglino D, Croce MA, et al. (2003) Multidrug resistance protein-6 (MRP6) in human dermal fibroblasts. comparison between cells from normal subjects and from pseudoxanthoma elasticum patients. Matrix Biol 22:491–500",{"id":22,"text":1244,"url":22,"identifiers":22},"Chan KW, Zhang H, Logothetis DE (2003) N-terminal transmembrane domain of the SUR controls trafficking and gating of Kir6 channel subunits. EMBO J 22:3833–3843. doi:10.1093\u002Femboj\u002Fcdg376",{"id":22,"text":1246,"url":22,"identifiers":22},"Chassaing N, Martin L, Calvas P, et al. (2005) Pseudoxanthoma elasticum: a clinical, pathophysiological and genetic update including 11 novel ABCC6 mutations. J Med Genet 42:881–892. doi:10.1136\u002Fjmg.2004.030171",{"id":22,"text":1248,"url":22,"identifiers":22},"Cuviello F, Tellgren-Roth Å, Lara P, et al. (2015) Membrane insertion and topology of the amino-terminal domain TMD0 of multidrug-resistance associated protein 6 (MRP6). FEBS Lett. doi:10.1016\u002Fj.febslet.2015.10.030",{"id":22,"text":1250,"url":22,"identifiers":22},"De Boussac H, Ratajewski M, Sachrajda I, et al. (2010) The ERK1\u002F2-hepatocyte nuclear factor 4alpha axis regulates human ABCC6 gene expression in hepatocytes. J Biol Chem 285:22800–22808. doi:10.1074\u002Fjbc.M110.105593",{"id":22,"text":1252,"url":22,"identifiers":22},"Fang K, Csanády L, Chan KW (2006) The N-terminal transmembrane domain (TMD0) and a cytosolic linker (L0) of sulphonylurea receptor define the unique intrinsic gating of KATP channels. J Physiol 576:379–389. doi:10.1113\u002Fjphysiol.2006.112748",{"id":22,"text":1254,"url":22,"identifiers":22},"Finger RP, Charbel Issa P, Ladewig MS, et al. (2009) Pseudoxanthoma elasticum: genetics, clinical manifestations and therapeutic approaches. Surv Ophthalmol 54:272–285. doi:10.1016\u002Fj.survophthal.2008.12.006",{"id":22,"text":1256,"url":22,"identifiers":22},"Fiser A, Sali A (2003) Modeller: generation and refinement of homology-based protein structure models. Methods Enzymol 374:461–491. doi:10.1016\u002FS0076-6879(03)74020-8",{"id":22,"text":1258,"url":22,"identifiers":22},"Hegedus T, Orfi L, Seprodi A, et al. (2002) Interaction of tyrosine kinase inhibitors with the human multidrug transporter proteins, MDR1 and MRP1. Biochim Biophys Acta 1587:318–325",{"id":22,"text":1260,"url":22,"identifiers":22},"Higgins CF (1992) ABC transporters: from microorganisms to man. Annu Rev Cell Biol 8:67–113. doi:10.1146\u002Fannurev.cb.08.110192.000435",{"id":22,"text":1262,"url":22,"identifiers":22},"Jansen RS, Küçükosmanoglu A, de Haas M, et al. (2013) ABCC6 prevents ectopic mineralization seen in pseudoxanthoma elasticum by inducing cellular nucleotide release. Proc Natl Acad Sci U S A 110:20206–20211. doi:10.1073\u002Fpnas.1319582110",{"id":22,"text":1264,"url":22,"identifiers":22},"Kamada K, Miyata M, Hirano T (2013) Molecular basis of SMC ATPase activation: role of internal structural changes of the regulatory subcomplex ScpAB. Structure 21:581–594. doi:10.1016\u002Fj.str.2013.02.016",{"id":22,"text":1266,"url":22,"identifiers":22},"Lee H, Lara P, Ostuni A, et al. (2014) Live-cell topology assessment of URG7, MRP6102 and SP-C using glycosylatable green fluorescent protein in mammalian cells. Biochem Biophys Res Commun 450:1587–1592. doi:10.1016\u002Fj.bbrc.2014.07.046",{"id":22,"text":1268,"url":22,"identifiers":22},"Mason DL, Michaelis S (2002) Requirement of the N-terminal extension for vacuolar trafficking and transport activity of yeast Ycf1p, an ATP-binding cassette transporter. Mol Biol Cell 13:4443–4455. doi:10.1091\u002Fmbc.E02-07-0405",{"id":22,"text":1270,"url":22,"identifiers":22},"Matsuzaki Y, Nakano A, Jiang Q-J, et al. (2005) Tissue-specific expression of the ABCC6 gene. J Invest Dermatol 125:900–905. doi:10.1111\u002Fj.0022-202X.2005.23897.x",{"id":22,"text":1272,"url":22,"identifiers":22},"Miglionico R, Armentano MF, Carmosino M, Salvia AM, Cuviello F, Bisaccia FOA (2014) Dysregulation of gene expression in ABCC6 knockdown HepG2 cells. Cell Mol Biol Lett 19:517–526",{"id":22,"text":1274,"url":22,"identifiers":22},"Mikhailov MV, Campbell JD, de Wet H, et al. (2005) 3-D structural and functional characterization of the purified KATP channel complex Kir6.2-SUR1. EMBO J 24:4166–4175. doi:10.1038\u002Fsj.emboj.7600877",{"id":22,"text":1276,"url":22,"identifiers":22},"Mikhailov MV, Mikhailova EA, Ashcroft SJ (2001) Molecular structure of the glibenclamide binding site of the beta-cell K(ATP) channel. FEBS Lett 499:154–160",{"id":22,"text":1278,"url":22,"identifiers":22},"Ostuni A, Lara P, Armentano MF, et al. (2013) The hepatitis B x antigen anti-apoptotic effector URG7 is localized to the endoplasmic reticulum membrane. FEBS Lett 587:3058–3062. doi:10.1016\u002Fj.febslet.2013.07.042",{"id":22,"text":1280,"url":22,"identifiers":22},"Ostuni A, Miglionico R, Monné M, et al. (2011) The nucleotide-binding domain 2 of the human transporter protein MRP6. J Bioenerg Biomembr 43:465–471",{"id":22,"text":1282,"url":22,"identifiers":22},"Paumi CM, Chuk M, Chevelev I, et al. (2008) Negative regulation of the yeast ABC transporter Ycf1p by phosphorylation within its N-terminal extension. J Biol Chem 283:27079–27088. doi:10.1074\u002Fjbc.M802569200",{"id":22,"text":1284,"url":22,"identifiers":22},"Sinkó E, Iliás A, Ujhelly O, et al. (2003) Subcellular localization and N-glycosylation of human ABCC6, expressed in MDCKII cells. Biochem Biophys Res Commun 308:263–269",{"id":22,"text":1286,"url":22,"identifiers":22},"Slot AJ, Molinski SV, Cole SPC (2011) Mammalian multidrug-resistance proteins (MRPs). Essays Biochem 50:179–207. doi:10.1042\u002Fbse0500179",{"id":22,"text":1288,"url":22,"identifiers":22},"Ter Beek J, Guskov A, Slotboom DJ (2014) Structural diversity of ABC transporters. J Gen Physiol 143:419–435. doi:10.1085\u002Fjgp.201411164",{"id":22,"text":1290,"url":22,"identifiers":22},"Uitto J, Pulkkinen L, Ringpfeil F (2001) Molecular genetics of pseudoxanthoma elasticum: a metabolic disorder at the environment-genome interface? Trends Mol Med 7:13–17",{"id":22,"text":1292,"url":22,"identifiers":22},"Volkov A, Mascarenhas J, Andrei-Selmer C, et al. (2003) A prokaryotic condensin\u002Fcohesin-like complex can actively compact chromosomes from a single position on the nucleoid and binds to DNA as a ring-like structure. Mol Cell Biol 23:5638–5650",{"id":22,"text":1294,"url":22,"identifiers":22},"Westlake CJ, Cole SPC, Deeley RG (2005) Role of the NH2-terminal membrane spanning domain of multidrug resistance protein 1\u002FABCC1 in protein processing and trafficking. Mol Biol Cell 16:2483–2492. doi:10.1091\u002Fmbc.E04-12-1113",{"id":22,"text":1296,"url":22,"identifiers":22},"Winkler M, Kühner P, Russ U, et al. (2012) Role of the amino-terminal transmembrane domain of sulfonylurea receptor SUR2B for coupling to K(IR)6.2, ligand binding, and oligomerization. Naunyn Schmiedeberg's Arch Pharmacol 385:287–298. doi:10.1007\u002Fs00210-011-0708-9",{"id":22,"text":1298,"url":22,"identifiers":22},"Xue P, Crum CM, Thibodeau PH (2014) Regulation of ABCC6 trafficking and stability by a conserved C-terminal PDZ-like sequence. PLoS one 9:e97360. doi:10.1371\u002Fjournal.pone.0097360",{"id":1300,"createTime":1301,"updateTime":1302,"relativeEntities":1303,"slug":1304,"properties":1305,"entityType":241,"verifyStatus":242,"verifyTime":1316,"verifyNote":244,"languages":22,"translateLanguages":22,"viewCount":172,"primaryUrl":1317,"fullTextUrl":22,"authors":1318,"publicationType":409,"publisherRelationship":1361,"citationCount":22,"citationInfo":22,"publishDate":1413,"publishYear":1414,"citationAnalyzeStatus":1415,"lastCitationAnalyze":1416,"indexDatabases":1417,"openAccess":22,"references":22,"isForceReanalyzing":697},"6ca89da0-e815-495a-815c-a6f75ab4dc98","2024-02-13T18:21:58.018+00:00","2026-07-22T16:58:02.805+00:00",[],"Effect-of-ATP-ADP-phosphate-potential-on-the-maximal-steady-state-uptake-of-Ca2-by-skeletal-sarcoplasmic-reticulum",{"abstract":1306,"title":1308,"gsPaper":1310,"references":1312,"doi":1314},{"EN":1307},"The ability of the Ca2+-Mg2+ ATPase pump of skeletal SR to produce and maintain a Ca2+ gradient was studied as a function of the ATP\u002FADP\u002FPi ratio. The internal free Ca2+ concentration [Ca2+]i was monitored by changes in fluorescence of CTC. Increasing ADP concentrations in the medium reduce the maximal [Ca2+]i concentration achieved. The inclusion or the omission of 4×10−4 M Pi or doubling the absolute ATP and ADP concentrations at a constant ATP\u002FADP ratio does not affect the level obtained. The level depends primarily on the ATP\u002FADP ratio. The [Ca2+] concentration shows a 1.5 power dependence on the ATP\u002FADP ratio. Further, [Ca2+]i achieved at steady state does not depend on whether the pump had been working in the forward or the reverse direction prior to testing. Analysis shows that the levels of Ca2+ achieved are much lower than the levels predicted thermodynamically under the assumption of ideal coupling between Ca2+ transport and ATP hydrolysis with a stoichiometry of 2:1. Under this condition the “osmotic” energy of the [Ca2+]i\u002F[Ca2+]o ratio was shown to be 48% as large as the free energy of hydrolysis of ATP, giving an overall thermodynamic efficiency of 48%. Analysis shows that maximal steady-state uptake is determined by the balance between the rates of uptake by the pump and rates of leak processes (intrinsic or extrinsic to the pump). Comparison with other studies shows that the [Ca2+]i achieved results in trans-inhibition of the pump by tying up the Ca2+ translocator in the inwardly oriented phosphorylated form. The absence of an effect of Pi can be taken as evidence that the dissociation of Ca2+ from the inwardly oriented translocator on the phosphoylated enzyme must precede the dephosphorylation of the enzyme.",{"EN":1309},"Effect of ATP\u002FADP\u002Fphosphate potential on the maximal steady-state uptake of Ca2+ by skeletal sarcoplasmic reticulum",{"VOID":1311},"[]",{"VOID":1313},"Alberty, R. A. (1968).J. Biol. Chem. 243 1337–1348.\nCaswell, A. H., and Hutchison, J. D. (1971).Biochem. Biophys. Res. Commun. 42 43–49.\nChiu, V. C. K., and Haynes, D. H. (1980).J. Membr. Biol. 56 219–239.\nChiu, V. C. K., Mouring, D., Watson, B. W., and Haynes, D. H. (1980).J. Membr. Biol. 56 121–132.\nde Meis, L., and Masuda, H. (1974).Biochemistry 13 2057–2062.\nde Meis, L., and Vianna, A. L. (1979).Annu. Rev. Biochem. 48 275–292.\nFabiato, A., and Fabiato, F. (1978).J. Physiol. 276 233–255.\nFroehlich, J. P., and Taylor, E. W. (1975).J. Biol. Chem. 250 2013–2021.\nFroehlich, J. P., and Taylor, E. W. (1976).J. Biol. Chem. 251 2307–2315.\nHasselbach, W. (1978).Biochim. Biophys. Acta 463 23–53.\nHasselbach, W., and Makinose, M. (1963).Biochem. Z. 339 94–111.\nInesi, G. (1972).Annu. Rev. Biophys. Bioeng. 1 191–210.\nKanazawa, T., Yamada, S., Yamamoto, T. and Tonomura, Y. (1971).J. Biochem. 70 95–123.\nMacLennan, D. H., and Holland, P. C. (1975).Annu. Rev. Biophys. Bioeng. 4 377–404.\nMakinose, M., and Boll, W. (1979). InCation Flux across Biomembranes Mukohata (Mukohata, Y., and Packer, L., eds.), Academic Press, New York, p. 89.\nMakinose, M., and Hasselbach, W. (1971).FEBS Lett. 12 271–272.\nMasuda, H., and de Meis, L. (1973).Biochemistry 12 4581–4585.\nMeissner, G. (1973).Biochim. Biophys. Acta 298 906–929.\nMeissner, G. (1975).Biochim. Biophys. Acta 389 51–68.\nMillman, M. S., Caswell, A. H., and Haynes, D. H. (1980).Membr. Biochem. 3 129–315.\nSakamoto, J., and Tonomura, Y. (1980).J. Biochem. (Tokyo) 87 1721–1727.\nShikama, K., and Nakamura, K-I (1973).Arch. Biochem. Biophys. 157 457–463.\nTada, M., Yamamoto, T., and Tonomura, Y. (1978).Physiol. Rev. 58 1–79.\nWeber, A., Herz, R., and Reiss, I. (1966).Biochem. Z. 345 329–369.\nYamada, S., and Ikemoto, N., (1980).,J. Biol. Chem. 255 3108.",{"VOID":1315},"10.1007\u002FBF00745022","2024-06-25T16:45:59.252+00:00","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002FBF00745022",[1319,1335,1348],{"id":1320,"sortIndex":23,"researcher":22,"roles":1321,"affiliations":1323,"properties":1332,"displayName":1334,"givenName":22,"familyName":22},"d5e87586-eb41-4f73-97e6-41140fa09748",[1322],"AUTHOR",[1324],{"id":1325,"sortIndex":23,"affiliation":1326,"properties":22},"c4044ee4-1679-4772-9ea1-439385823371",{"id":1325,"createTime":22,"updateTime":22,"relativeEntities":1327,"slug":22,"properties":1328,"entityType":22,"verifyStatus":22,"verifyTime":22,"verifyNote":22,"languages":22,"translateLanguages":22,"viewCount":22,"url":22,"parentIds":1331,"statistic":22},[],{"title":1329},{"VI":1330},"Department of Pharmacology, University of Miami School of Medicine, Miami",[],{"title":1333},{"VI":1334},"Deborah Dixon",{"id":1336,"sortIndex":172,"researcher":22,"roles":1337,"affiliations":1338,"properties":1345,"displayName":1347,"givenName":22,"familyName":22},"e666e192-b845-40ff-b15a-525287232e6c",[1322],[1339],{"id":1325,"sortIndex":23,"affiliation":1340,"properties":22},{"id":1325,"createTime":22,"updateTime":22,"relativeEntities":1341,"slug":22,"properties":1342,"entityType":22,"verifyStatus":22,"verifyTime":22,"verifyNote":22,"languages":22,"translateLanguages":22,"viewCount":22,"url":22,"parentIds":1344,"statistic":22},[],{"title":1343},{"VI":1330},[],{"title":1346},{"VI":1347},"Adrian Corbett",{"id":1349,"sortIndex":285,"researcher":22,"roles":1350,"affiliations":1351,"properties":1358,"displayName":1360,"givenName":22,"familyName":22},"2495d8d0-e8c4-43fb-ac88-aa35a839ec37",[1322],[1352],{"id":1325,"sortIndex":23,"affiliation":1353,"properties":22},{"id":1325,"createTime":22,"updateTime":22,"relativeEntities":1354,"slug":22,"properties":1355,"entityType":22,"verifyStatus":22,"verifyTime":22,"verifyNote":22,"languages":22,"translateLanguages":22,"viewCount":22,"url":22,"parentIds":1357,"statistic":22},[],{"title":1356},{"VI":1330},[],{"title":1359},{"VI":1360},"Duncan H. 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-Ca2-gradients-with-a-thermodynamic-efficiency-of-100-",{"abstract":1425,"title":1427,"gsPaper":1429,"references":1431,"doi":1433},{"EN":1426},"The thermodynamic efficiency of the calmodulin-activated form of the Ca2+-pumping ATPase of the bovine cardiac sarcolemma (SL) was evaluated in sealed vesicles under reversible conditions. The free internal Ca2+ concentration ([Ca2+]i) established in the SL vesicle lumen by action of the ATPase was determined as a function of the [ATP]\u002F([ADP][Pi]) ratio for the following experimental conditions: 250mM sucrose, 100mM KCI, 0.1mM Mg2+, 25mM HEPES, 25mM Tris, pH 7.40, at 37°C, [Ca2+]o=50nM (1mM Ca\u002FEGTA buffer), 0.75mM Mg-ATP, 0.1mM Pi, variable [ADP]. Under these conditions, with the pump working near itsK\n\n                  m\n                 of 64nM, the [Ca2+]i achieved was ≤18mM, decreasing with increasing [ADP] for [ADP] ≥0.84mM. A plot of the square of the [Ca2+]i\u002F[Ca2+]o ratio against [ATP]\u002F([ADP][Pi]) gave a straight line with a slope of 1.5×107M. This was in agreement, within the experimental error, with the equilibrium constant for ATP hydrolysis under these conditions (1.09×107M). These results demonstrate (1) tight coupling between Ca2+ transport and ATP hydrolysis with a stoichiometry of 2 Ca2+ moved per ATP split and (2) a low degree of passive leakage. Analysis at low [ADP] (\u003C0.83mM) showed the unexpected result that ADP increases the rate of theforward reaction of the pump. The maximal effect on the initial rate is a 96±5% increase, with an EC50 of approximately 0.4mM (ADP). Similar but lesser stimulation was observed with CDP. The implications of the above results for the energetics of the pump and for its physiological function in the beating heart are discussed.",{"EN":1428},"The calmodulin-activated form of the Ca2+-pumping ATPase of the cardiac sarcolemmal membrane produces Ca2+ gradients with a thermodynamic efficiency of 100%",{"VOID":1430},"[\"12362151558197386906\"]",{"VOID":1432},"Alberty, R. A. (1968)J. Biol. Chem. 243, 1337–1348.\nBrandt, N. (1985).Arch. Biochem. Biophys. 242, 306–319.\nCarafoli, E. (1984). InEpithelial Calcium and Phosphate Transport: Molecular and Cellular Aspects. (Bronner, F., and Paterlile, M., eds.), Alan R. Liss, Inc., New York, pp. 13–17.\nCaroni, P., and Carafoli, E. (1981).J. Biol. Chem. 256, 3263–3270; 9371–9373.\nCaroni, P., and Carafoli, E. (1981a).J. Biol. Chem. 256, 3263–3270.\nCaroni, P., and Carafoli, E. (1981b)J. Biol. Chem. 256, 9371–9373.\nCaroni, P., and Carafoli, E. (1983).Eur. J. Biochem. 132 451–460.\nCaroni, P., Zurini, M., Clark, A., and Carafoli, E. (1983).J. Biol. Chem. 258, 7305–7310.\nCaswell, A. H. (1972).J. Membrane. Biol. 7, 345–364.\nCaswell, A. H., and Hutchinson, J. D. (1971).Biochem. Biophys. Res. Commun. 42, 43–49.\nCaswell, A. H., and Warren, S. (1972).Biochem. Biophys. Res. Commun. 46, 1757–1763.\nDixon, D., Corbett, A., and Haynes, D. H. (1982).J. Bioenerg. Biomembr. 14, 87–96.\nDixon, D., Brandt, N., and Haynes, D. H. (1984).J. Biol. Chem. 259, 13737–13741.\nDixon, D. A., and Haynes, D. H. (1989a).J. Biol. Chem.,264, 13612–13622.\nDixon, D. A., and Haynes, D. H. (1989b).J. Membr. Biol. 112, 169–183.\nFagan, M. H., and Dewey, T. G. (1985).J. Biol. Chem. 260, 6147–6152.\nFroehlich, J. P., and Taylor, E. W. (1975).J. Biol. Chem. 250, 2013–2021.\nFroehlich, J. P., and Taylor, E. W. (1976).J. Biol. Chem. 251, 2307–2315.\nHasselbach, W., and Makinose, M. (1963).Biochem. Z. 339, 94–111.\nHaynes, D. H. (1982).Arch. Biochem. Biophys. 215, 444–461.\nHaynes, D. H. (1983).Am. J. Physiol. 244, G3-G12.\nHaynes, D. H., and Mandveno, A. (1983).J. Membr. Biol. 74, 25–40.\nHaynes, D. H., and Mandveno, A. (1987).Physiol. Rev. 67, 244–284.\nInesi, G. (1972).Annu. Rev. Biophys. Bioenerg. 1, 191–210.\nInesi, G., Kurzmack, M., Coan, C., and Lewis, D. E. (1980).J. Biol. Chem. 255, 3025–3031.\nJones, L. R., Maddock, S. W., and Besch, H. R. (1980).J. Biol. Chem. 255, 9971–9980.\nKanazawa, T., Yamada, S., Yamamoto, T., and Tonomura, Y. J. (1971).J. Biochem. 70, 95–123.\nMacLennan, D. H., and Holland, P. C. (1975).Annu. Rev. Biophys. Bioenerg. 4, 377–404.\nMartell, A. E., and Smith, R. M. (1974).Critical Stability Constants. Vol. F. Plenum Publishing Corp., New York.\nMasuda, H., and de Meis, L. (1973).Biochemistry 12, 4581–4585.\nMeis, L. de, and Vianna, A. L. (1979).Annu. Rev. Biochem. 48, 275–292.\nNiggli, V., Adunya, E. S., Penniston, T., and Carafoli, E. (1981).J. Biol. Chem. 256, 295–401.\nPhilipson, K. D., Bersohn, M. M., and Nishimoto, A. (1982).Circ. Res. 50, 287–293.\nPhillips, R. C., George, P., and Rtuman, R. J. (1969).J. Biol. Chem. 244, 3330–3342.\nPitts, B. J. R. (1979).J. Biol. Chem. 254, 6232–6235.\nReeves, J. P., and Sutko, J. L. (1979).Proc. Natl. Acad. Sci. USA 76, 590–594.\nRiviero, J. M. C., and Vianna, A. L. (1978).J. Biol. Chem. 253, 3133–3157.\nShikama, K., and Nakamura, K. (1973).Arch. Biochem. Biophys. 157, 457–463.\nTrevorrow, K., and Haynes, D. H. (1984).J. Bioenerg. Biomembr. 16, 53–59.\nWang, T., Tsai, L. I., Solaro, R. J., Grasside-Gende, A. U., and Schwartz, A. (1979).Biochem. Biophys. Res. Commun. 91, 356–361.\nWeber, A., Hertz, R., and Reiss, I. (1966).Biochem. Z. 345, 329–369.\nYamada, S., and Tonomura, Y. (1972).J. Biochem. (Tokyo)72, 417–425.",{"VOID":1434},"10.1007\u002FBF00762945","2024-05-12T05:03:58.828+00:00","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002FBF00762945",[1438,1451],{"id":1439,"sortIndex":23,"researcher":22,"roles":1440,"affiliations":1441,"properties":1448,"displayName":1450,"givenName":22,"familyName":22},"6a37fcee-2985-4b25-bd51-52324cfe3c82",[1322],[1442],{"id":1325,"sortIndex":23,"affiliation":1443,"properties":22},{"id":1325,"createTime":22,"updateTime":22,"relativeEntities":1444,"slug":22,"properties":1445,"entityType":22,"verifyStatus":22,"verifyTime":22,"verifyNote":22,"languages":22,"translateLanguages":22,"viewCount":22,"url":22,"parentIds":1447,"statistic":22},[],{"title":1446},{"VI":1330},[],{"title":1449},{"VI":1450},"Deborah A. 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disease (HD) is an autosomal dominant neurodegenerative disease which is characterized by psychiatric symptoms, involuntary choreiform movements and dementia with maximum degeneration occurring in striatum and cerebral cortex. Several studies implicate mitochondrial dysfunction to the selective neurodegeneration happening in this disorder. Calcium buffering imbalance and oxidative stress in the mitochondria, critically impaired movement across axons and abnormal fission or fusion of this organelle in the cells are some of the salient features that results in the loss of mitochondrial electron transport chain (ETC) complex function in HD. Although several models involving mutant huntingtin, excitotoxins and mitochondrial complex-II inhibitors have been used to explore the disease, it is not clear how disturbances in mitochondrial functioning is associated with such selective neurodegeneration, or in the expression of huntingtonian phenotypes in animals or man. We have carefully assessed various mitochondrial abnormalities observed in human patient samples, postmortem HD brains, cellular, vertebrate and invertebrate models of the disease, to conclude that ETC dysfunction is an integral part of the disease and justify a causal role of mitochondrial ETC dysfunction for the genesis of this disorder",{"EN":1532},"Mitochondrial functional alterations in relation to pathophysiology of Huntington’s disease",{"VOID":1534},"[\"18026877390852649908\"]",{"EN":1064},{"VOID":1537},"10.1007\u002Fs10863-010-9288-5","2024-05-15T19:38:35.629+00:00",[246],"https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002Fs10863-010-9288-5",[1542,1567,1582],{"id":1543,"sortIndex":23,"researcher":22,"roles":1544,"affiliations":1545,"properties":1562,"displayName":1564,"givenName":22,"familyName":22},"81dc276e-c420-4fac-b708-82a3ff790e30",[],[1546,1554],{"id":1547,"sortIndex":23,"affiliation":1548,"properties":22},"111bbdfc-3556-4f34-b77c-1a2a752b9b92",{"id":1547,"createTime":22,"updateTime":22,"relativeEntities":1549,"slug":22,"properties":1550,"entityType":22,"verifyStatus":22,"verifyTime":22,"verifyNote":22,"languages":22,"translateLanguages":22,"viewCount":22,"url":22,"parentIds":1553,"statistic":22},[],{"title":1551},{"VI":1552},"Division of Cell Biology & Physiology, Laboratory of Clinical & Experimental Neuroscience, Indian Institute of Chemical Biology (CSIR), Kolkata, India",[],{"id":1555,"sortIndex":23,"affiliation":1556,"properties":22},"58e8ff42-28a3-4f65-b326-dd237cfb510c",{"id":1555,"createTime":22,"updateTime":22,"relativeEntities":1557,"slug":22,"properties":1558,"entityType":22,"verifyStatus":22,"verifyTime":22,"verifyNote":22,"languages":22,"translateLanguages":22,"viewCount":22,"url":22,"parentIds":1561,"statistic":22},[],{"title":1559},{"EN":1560},"Manovikas Biomedical Research and Diagnostic Centre, Manovikas Kendra Rehabilitation & Research Institute for the Handicapped, Kolkata, India",[],{"title":1563,"gsAuthor":1565},{"EN":1564},"Mritunjay Pandey",{"VOID":1566},"[\"f9PylScAAAAJ\"]",{"id":1568,"sortIndex":172,"researcher":22,"roles":1569,"affiliations":1570,"properties":1577,"displayName":1579,"givenName":22,"familyName":22},"382f379c-5189-4490-b581-78c25d6d02da",[],[1571],{"id":1547,"sortIndex":23,"affiliation":1572,"properties":22},{"id":1547,"createTime":22,"updateTime":22,"relativeEntities":1573,"slug":22,"properties":1574,"entityType":22,"verifyStatus":22,"verifyTime":22,"verifyNote":22,"languages":22,"translateLanguages":22,"viewCount":22,"url":22,"parentIds":1576,"statistic":22},[],{"title":1575},{"VI":1552},[],{"title":1578,"gsAuthor":1580},{"EN":1579},"Kochupurackal P. 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453:921–924",{"id":1877,"createTime":1878,"updateTime":1879,"relativeEntities":1880,"slug":1881,"properties":1882,"entityType":241,"verifyStatus":242,"verifyTime":1893,"verifyNote":244,"languages":22,"translateLanguages":22,"viewCount":23,"primaryUrl":1894,"fullTextUrl":22,"authors":1895,"publicationType":409,"publisherRelationship":1911,"citationCount":124,"citationInfo":1963,"publishDate":1966,"publishYear":1964,"citationAnalyzeStatus":1519,"lastCitationAnalyze":1879,"indexDatabases":1967,"openAccess":22,"references":22,"isForceReanalyzing":697},"843dccbd-2eb5-417e-80fd-36af8d8d9d93","2023-12-06T01:50:01.954+00:00","2026-07-18T16:13:49.508+00:00",[],"Natural-electrical-RF-oscillation-from-cells",{"abstract":1883,"title":1885,"gsPaper":1887,"references":1889,"doi":1891},{"EN":1884},"Electrical oscillatory rf phenomena are present during the division of cells. 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