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Metab. 279 IssueID2 E314–E322 Occurrence Handle10913031\nS. Rousset M. C. Alves-Guerra J. Mozo B. Miroux A. M. Cassard-Doulcier F. Bouillaud D. Ricquier (2004) ArticleTitleThe biology of mitochondrial uncoupling proteins Diabetes 53 IssueIDSuppl 1: S130-5 S130–S135 Occurrence Handle14749278\nA. Rubio A. Raasmaja A. L. Maia K.-R. Kim J. E. Silva (1995a) ArticleTitleEffects of thyroid hormone on norepinephrine signalling in brown adipose tissue. I: β1- and β2-adrenergic receptors and cyclic adenosine monophosphate generation Endocrinology 136 IssueID8 3267–3276 Occurrence Handle10.1210\u002Fen.136.8.3267\nA. Rubio A. Raasmaja J. E. Silva (1995b) ArticleTitleEffects of thyroid hormone on norepinephrine signalling in brown adipose tissue. I: differential effects of thyroid hormone on β3-adrenergic receptors in brown and white adipose tissue Endocrinology 136 IssueID8 3277–3284 Occurrence Handle10.1210\u002Fen.136.8.3277\nP. A. Schueler H. L. Schwartz K. A. Strait C. N. Mariash J. H. Oppenheimer (1990) ArticleTitleBinding of 3,5,3’-triiodothyronine (T3) and its analogs to the in vitro translational products of c-erbA protooncogenes: differences in the affinity of the α- and [3-forms for the acetic acid analog and failure of the human testis and kidney α-2 products to bind β Mol. Endocrinol. 4 227–234 Occurrence Handle2158622\nJ. E. Silva (2001) ArticleTitleThe multiple contributions of thyroid hormone to heat production J. Clin. Invest. 108 IssueID1 35–37 Occurrence Handle10.1172\u002FJCI200113397 Occurrence Handle11435454\nJ. E. Silva (2003) ArticleTitleThe thermogenic effect of thyroid hormone and its clinical implications Annals Intern. Med. 139 IssueID3 205–213\nJ. E. Silva R. Rabelo (1997) ArticleTitleRegulation of the uncoupling protein gene expression Eur. J. Endocrinol. 136 IssueID3 251–264 Occurrence Handle9100546\nW. S. Sirnonides M. H. Thelen C. G. Linden Particlevan der A. Muller C. Hardeveld Particlevan (2001) ArticleTitleMechanism of thyroid-hormone regulated expression of the SERCA genes in skeletal muscle: implications for thermogenesis Biosci. Rep. 21 IssueID2 139–154 Occurrence Handle10.1023\u002FA:1013692023449 Occurrence Handle11725863\nU. Sundin (1981) ArticleTitleGDP binding to rat brown fat mitochondria: effects of thyroxine at different ambient temperature Am. J. Physiol. 241 C134–C139 Occurrence Handle7282915\nU. Sundin I. Mills J. N. Fain (1984) ArticleTitleThyroid-catecholamine interactions in isolated brown adipocytes Metabolism: Clin. Experiment. 33 1028–1033\nJ. Triandafillou C. Gwilliam J. Himms-Hagen (1982) ArticleTitleRole of thyroid hormone in cold-induced changes in rat brown adipose tissue mitochondria Can. J. Biochem. 60 530–537 Occurrence Handle7104831\nC. R. Vianna T. Hagen C. Y. Zhang E. Bachman O. Boss B. Gereben A. S. Moriscot B. B. Lowell J. E. Bicudo A. C. Bianco (2001) ArticleTitleCloning and functional characterization of an uncoupling protein homolog in hummingbirds Physiol. Genom. 5 IssueID3 137–145\nA. Vidal-Puig G. Solanes D. Grujic J. S. Flier B. B. Lowell (1997) ArticleTitleUCP3: an uncoupling protein homologue expressed preferentially and abundantly in skeletal muscle and brown adipose tissue Biochem. Biophys. Res. Comm. 235 IssueID1 79–82 Occurrence Handle10.1006\u002Fbbrc.1997.6740 Occurrence Handle9196039\nM. Watford (2000) ArticleTitleFunctional glycerol kinase activity and the possibility of a major role for glyceroneogenesis in mammalian skeletal muscle Nutrition. Rev. 58 IssueID5 145–148\nR. T. Weirich H. L. Schwartz J. H. Oppenheimer (1987) ArticleTitleAn analysis of the interrelationship of nuclear and plasma triiodothyronine in the Sea Lamprey, Lake Trout, and Rat: evolutionary considerations Endocrinology 120 664–677 Occurrence Handle3803297\nR.C. Woledge (1989) Energy transformations in living muscle W. Wieser E. Gnaiger (Eds) Energy Transformations in Cells and Organisms Georg Thieme Verlag Stuttgart, New York 36–45\nP. M. Yen (2001) ArticleTitlePhysiological and molecular basis of thyroid hormone action Physiol. Rev. 81 IssueID3 1097–1142 Occurrence Handle11427693",{"EN":228},"Thyroid Hormone and the Energetic Cost of Keeping Body Temperature",{"VOID":230},"10.1007\u002Fs10540-005-2882-9","PUBLICATION","VERIFIED","Auto Verify","https:\u002F\u002Fportlandpress.com\u002Fbioscirep\u002Farticle-abstract\u002F25\u002F3-4\u002F129\u002F54818\u002FThyroid-Hormone-and-the-Energetic-Cost-of-Keeping?redirectedFrom=fulltext",[236],{"id":237,"sortIndex":21,"researcher":20,"roles":238,"affiliations":240,"properties":249},"adc7426d-f26b-4b73-937c-a24b4a9a1afc",[239],"AUTHOR",[241],{"id":20,"sortIndex":21,"affiliation":242,"properties":20},{"id":243,"createTime":244,"updateTime":244,"relativeEntities":245,"slug":20,"properties":246,"entityType":65,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21},"bdabcc5a-2827-493f-acd8-964816e9f4d6","2024-01-20T11:28:58.502+00:00",[],{"title":247},{"VI":248},"Department of Medicine, Division of Endocrinology, Jewish General Hospital, McGill University, Montreal, Canada",{"title":250},{"VI":251},"J. Enrique Silva","ARTICLE",{"url":234,"publisher":254,"properties":282},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":255,"slug":10,"properties":256,"entityType":18,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21,"subjectFields":260,"manageAffiliations":261,"indexDatabases":262,"url":110,"thumbnailPath":20,"statistic":277,"gsStatistic":20,"type":213,"analyzePriority":20},[],{"issn":257,"eissn":258,"title":259},{"VOID":13},{"VOID":15},{"EN":17},[],[],[263,270],{"id":91,"indexDatabase":264,"url":106,"indexYears":20,"academicFieldIds":269,"indexDatabaseRanking":20},{"id":93,"createTime":94,"updateTime":95,"relativeEntities":265,"label":266,"description":267,"key":102,"publicationTags":268,"standard":20},[],{"EN":98,"VI":98},{"VI":100,"EN":101},[104,105],[108,109],{"id":69,"indexDatabase":271,"url":82,"indexYears":83,"academicFieldIds":276,"indexDatabaseRanking":89},{"id":71,"createTime":72,"updateTime":73,"relativeEntities":272,"label":273,"description":274,"key":79,"publicationTags":275,"standard":20},[],{"EN":76,"VI":76},{"EN":76,"VI":78},[81],[85,86,87,88],{"impactFactor":21,"impactFactorByYear":278,"i10Index":121,"i10IndexLast5Year":122,"totalPublication":123,"totalPublicationByYear":279,"totalCitation":148,"totalCitationByYear":280,"totalCitationPerPublication":180,"totalCitationPerPublicationByYear":281,"hindexLast5Year":212,"hindex":212},{"2014":113,"2015":113,"2016":114,"2017":115,"2018":116,"2019":117,"2020":118,"2021":119,"2022":120},{"1981":125,"1982":126,"1983":127,"1984":128,"1985":129,"1986":130,"1987":131,"1988":132,"1989":133,"1990":134,"1991":135,"1992":136,"1993":137,"1994":138,"1995":135,"1996":135,"1997":135,"1998":139,"1999":134,"2000":140,"2001":141,"2002":142,"2003":143,"2004":144,"2005":145,"2006":114,"2007":146,"2008":147,"2013":147,"2015":113,"2016":113,"2017":147,"2018":113,"2019":147,"2020":118},{"1981":150,"1982":151,"1983":152,"1984":153,"1985":154,"1986":155,"1987":156,"1988":157,"1989":158,"1990":159,"1991":160,"1992":159,"1993":161,"1994":162,"1995":140,"1996":150,"1997":163,"1998":164,"1999":165,"2000":166,"2001":167,"2002":168,"2003":169,"2004":170,"2005":171,"2006":172,"2007":173,"2008":125,"2013":174,"2015":175,"2016":176,"2017":177,"2018":178,"2019":138,"2020":179},{"1981":182,"1982":183,"1983":184,"1984":185,"1985":186,"1986":187,"1987":188,"1988":189,"1989":190,"1990":191,"1991":192,"1992":193,"1993":194,"1994":195,"1995":196,"1996":197,"1997":198,"1998":199,"1999":200,"2000":201,"2001":202,"2002":203,"2003":204,"2004":205,"2005":206,"2006":207,"2007":208,"2008":125,"2013":174,"2015":209,"2016":210,"2017":177,"2018":140,"2019":138,"2020":211},{"volume":283,"pages":285},{"VOID":284},"25",{"VOID":286},"129-148","2005-06-01",2005,false,{"id":291,"createTime":292,"updateTime":293,"relativeEntities":294,"slug":295,"properties":296,"entityType":231,"verifyStatus":232,"verifyTime":305,"verifyNote":233,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21,"primaryUrl":306,"fullTextUrl":20,"authors":307,"publicationType":252,"publisherRelationship":323,"citationCount":20,"citationInfo":20,"publishDate":357,"publishYear":358,"citationAnalyzeStatus":19,"lastCitationAnalyze":20,"indexDatabases":20,"openAccess":20,"references":20,"isForceReanalyzing":289},"ea2c189d-4c2a-4ac5-9927-f67d3929c5c9","2024-02-06T07:22:25.810+00:00","2025-01-10T23:57:29.616+00:00",[],"The-Behaviour-of-Ions-in-Narrow-Water-Filled-Pores",{"references":297,"abstract":299,"title":301,"doi":303},{"VOID":298},"Barrer, R. M. and Rees, L. V. C. (1960) Self diffusion of alkali metal ions in analcite. Trans. Faraday Soc. 56:709–721.\nBarrer, R. M., Bartholomew, R. F., and Rees, L. V. C. (1963) Self and exchange diffusion of ions in chabazites. J. Phys. Chem. Solids 242:51–62.\nBerry, R. and Edmonds, D. T. (1993) Correlated ion flux through parallel pores: application to channel subconductance states. J. Mem. Biol. 133:77–84.\nBleaney and Bleaney (1989) Electricity and Magnetism. 3rd. Edn. Oxford: Oxford University Press.\nCooke, A. H., Edmonds, D. T., Finn, C. B. P., and Wolf, W. P. (1962) Demagnetization experiments on substances with large magnetic dipolar interactions. J. Phys. Soc. Japan 17(B1):481–486.\nDoyle, D. A., et al. (1998) The structure of the potassium channel: molecular basis of K+ conduction and selectivity. Science 280:69–77.\nDu, Q., Freysz, E., and Shen, Y. R. (1994) Surface vibrational studies of hydrogen bonding and hydrophobicity. Science 264:826–828.\nEdmonds, D. T. (1979) A reversible electrostatic channel for ion transport. Chem. Phys. Lett. 65:429–433.\nEdmonds, D. T. (1980) Membrane ion channels and ionic hydration energies. Proc. R. Soc. Lond. B211:61–62.\nEdmonds, D. T. (1981) A physicist's view of membrane ion channels. TIBS 6:92–94.\nEdmonds, D. T. (1984) The ordered water model of membrane ion channels. In Biological Membranes, vol. 5 (D. Chapman, ed.), London: Academic Press, pp. 349–387.\nEdmonds, D. T. and Berry, R. (1991) The proton ladder, a static mechanism for ion\u002Fproton coports and counterports. Eur. Biophys. J. 20:241–245.\nEdmonds, D. T. (1994) Enhanced ionic interaction in narrow pores and ion pair formation. Eur. Biophys. J. 23:133–138.\nEnderby, J. E. and Neilson, G. W. (1979) X-ray and neutron scattering by aqueous solutions of electrolytes. In Water a Comprehensive Treatise. (F. Franks, ed.), London: Plenum Press, pp 1–46.\nHille, B. (1992) Ionic Channels in Excitable Membranes, 2nd Edn. Sunderland, Massachusetts: Sinauer Associates.\nIsraelachvli, I. and Pashley, R. (1982) The hydrophobic interaction is long range, decaying exponentially with distance. Nature 300:341–342.\nIsraelachvili, J. (1992) Intermolecular and Surface Forces, 2nd Edn. London: Academic Press.\nKim, K. S., Nguyen, P. K., Swaminathan, P. K., and Clement, E. (1985) Na+ and K+ transport through a solvated Gramicidin A transmembrane channel: Molecular dynamics studies using parallel processors. J. Phys. Chem. 89:2870–2876.\nKorchev, Y. E. et al. (1997) A novel explanation for fluctuations of ion current through narrow pores. FASB 11:600–608.\nLee, C. Y. and McCammon, J. A. (1984) The structure of liquid water at an extended hydrophobic surface. J. Chem. Phys. 80:4448–4455.\nLev, A. A., Korchev, Y. E., Rostovtseva, T. A., Bashford, C. L., Edmonds, D. T., and Pasternak, C. A. (1993) Rapid switching of ion current in narrow pores: implications for biological ion channels. Proc. R. Soc. Lond. B252:187–192.\nMackay, D. H. J., Berens, P. H., and Wilson, K. R. (1984) Structure and dynamics of ion transport through Gramicidin A. Biophys. J. 46:229–248.\nParsegian, A. (1969) Energy of an ion crossing a low dielectric membrane: solutions of four relevant problems. Nature 221:844–846.\nPasternak, C. A. et al. (1995) Nuclear track-etched filters as model pores for biological membranes. Radiation Meas. 25:675–683.\nRostovtseva, T. K. et al. (1996) Diffusion through narrow pores: Movement of ions, water and nonelectrolytes through track-etched PETP membranes. J. Mem. Biol. 151:29–43.\nSachs, F. and Quin, F. (1993) Gated, ion-selective channels observed with patch pipettes in the absence of membranes: Novel properties of a gigaseal. Biophys. J. 65:1101–1107.\nToney, M. F. et al. (1994) Voltage-dependent ordering of water molecules at an electrode-electrolyte interface. Nature 368:444–446.\nWarshel, A. and Russell, S. T. (1984) Electrostatic interactions in biological systems and in solution. Q. Rev. Biophys. 17:283–422.\nZhu, S. B. and Robinson, G. W. (1991) Structure and dynamics of liquid water between plates. J. Chem. Phys. 42(2):1403–1410.",{"EN":300},"Today, the equilibrium behavior of ions in solution may be predicted with some confidence, essentially because rapid ionic diffusion over small distances ensures homogeneity throughout the solution. Equilibrium concepts such as ionic strength and pH apply. However, when attempting to understand the behavior of ions passing rapidly through narrow pores such as ion channels, no such equilibrium state may be assumed. The passing solution may have been in equilibrium with conditions at the mouth of the pore but will not be in equilibrium with charged molecules on the pore wall. In addition, the water in narrow pores will be partially ordered by contact with the pore walls and will not behave like bulk water. To illustrate this difference, a simple equilibrium calculation of the ion concentrations near a plastic sheet penetrated by narrow pores and containing in its surface partially ionized carboxyl groups is shown to be in good agreement with experiment. However, to predict the non-equilibrium behavior within the narrow pores is much more difficult. To illustrate the difficulty, a Monte Carlo computer model is described which attempts to predict the rapid switching of ion current observed experimentally with these narrow pores.",{"EN":302},"The Behaviour of Ions in Narrow Water-Filled Pores",{"VOID":304},"10.1023\u002FA:1020209332415","2025-01-10T23:57:29.615+00:00","https:\u002F\u002Fportlandpress.com\u002Fbioscirep\u002Farticle-abstract\u002F18\u002F6\u002F313\u002F54161\u002FThe-Behaviour-of-Ions-in-Narrow-Water-Filled-Pores?redirectedFrom=fulltext",[308],{"id":309,"sortIndex":21,"researcher":20,"roles":310,"affiliations":311,"properties":320},"44bd8116-8acc-4497-9e51-26cead8906c2",[239],[312],{"id":20,"sortIndex":21,"affiliation":313,"properties":20},{"id":314,"createTime":315,"updateTime":315,"relativeEntities":316,"slug":20,"properties":317,"entityType":65,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21},"3c44d197-1af2-4b36-969d-4bfb84d4efe7","2024-02-06T07:22:25.828+00:00",[],{"title":318},{"VI":319},"The Clarendon Laboratory, The University of Oxford, Oxford, UK",{"title":321},{"VI":322},"D. 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Per the hypothesis that plasma miRNA is valuable for this purpose, we performed complete transcriptional profiling of an miRNA discovery-set in 14 samples: three patients with ST-elevated acute myocardial infarction (STEMI) at baseline and after three months of follow-up, four with stable ischaemic heart disease (stable-IHD) and four healthy age-matched volunteers. Our aim was to determine whether we could distinguish patients with unstable plaques from stable patients following a STEMI event. After analysing miRNA profiles, we conducted a validation study comparing three-month STEMI (n=40) with stable-IHD (n=35), which confirmed that miR-486-3P differentiates patients with three-month STEMI from those with stable-IHD (P=0.019).\u003C\u002Fjats:p>",{"EN":375},"MicroRNA 486-3P as a stability marker in acute coronary 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Karolinska University Hospital, Stockholm, Sweden",{"openalex":402,"orcid":404,"title":406},{"VOID":403},"A5026153766",{"VOID":405},"https:\u002F\u002Forcid.org\u002F0009-0003-8838-3463",{"EN":407},"Anders Gabrielsen",{"id":409,"sortIndex":113,"researcher":20,"roles":410,"affiliations":411,"properties":422},"6a546c30-bb68-4849-bbae-7bd2aa9114de",[],[412],{"id":413,"sortIndex":21,"affiliation":414,"properties":20},"d95ca338-d43f-42d5-bb46-f9ad03b11828",{"id":415,"createTime":416,"updateTime":416,"relativeEntities":417,"slug":418,"properties":419,"entityType":65,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21},"ec710c1c-ee8a-4c03-9741-0ea98d338966","2024-09-17T23:57:17.983+00:00",[],"Atherosclerosis-Research-Unit-Department-of-Medicine-Center-for-Molecular-Medicine-Karolinska-University-Hospital-Stockholm-Sweden",{"title":420},{"EN":421},"Atherosclerosis Research Unit, Department of Medicine, Center for Molecular Medicine, Karolinska University Hospital, Stockholm, Sweden",{"openalex":423,"orcid":425,"title":427},{"VOID":424},"A5017225831",{"VOID":426},"https:\u002F\u002Forcid.org\u002F0000-0003-1993-2468",{"EN":428},"Ewa Ehrenborg",{"id":430,"sortIndex":147,"researcher":20,"roles":431,"affiliations":432,"properties":444},"42d15669-fad4-4ca6-b6ec-ce970b35760e",[],[433],{"id":434,"sortIndex":21,"affiliation":435,"properties":20},"f883f8e4-a6b4-4738-a933-bf37a945b73d",{"id":436,"createTime":437,"updateTime":438,"relativeEntities":439,"slug":440,"properties":441,"entityType":65,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21},"bafe534f-c078-4ce7-87ce-73b76a6a10e0","2024-01-18T21:25:16.096+00:00","2024-10-05T06:26:30.184+00:00",[],"Department-of-Systems-Biology-Technical-University-of-Denmark-Lyngby-Denmark",{"title":442},{"VI":443},"Department of Systems Biology, Technical University of Denmark, Lyngby, 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2013, Cardiac biomarkers in acute myocardial infarction, Int. J. Cardiol., 164, 282, 10.1016\u002Fj.ijcard.2012.01.081",{"doi":515},"10.1016\u002Fj.ijcard.2012.01.081",{"id":20,"text":517,"url":20,"identifiers":518},"Chen, 2008, Characterization of microRNAs in serum: a novel class of biomarkers for diagnosis of cancer and other diseases, Cell Res., 18, 997, 10.1038\u002Fcr.2008.282",{"doi":519},"10.1038\u002Fcr.2008.282",{"id":20,"text":521,"url":20,"identifiers":522},"Corsten, 2010, Circulating microRNA-208b and microRNA-499 reflect myocardial damage in cardiovascular disease, Circ. Cardiovasc. Genet., 3, 499, 10.1161\u002FCIRCGENETICS.110.957415",{"doi":523},"10.1161\u002FCIRCGENETICS.110.957415",{"id":20,"text":525,"url":20,"identifiers":526},"Creemers, 2012, Circulating microRNAs: novel biomarkers and extracellular communicators in cardiovascular disease?, Circ. Res., 110, 483, 10.1161\u002FCIRCRESAHA.111.247452",{"doi":527},"10.1161\u002FCIRCRESAHA.111.247452",{"id":20,"text":529,"url":20,"identifiers":530},"Zhang, 2015, Circulating miR-499 are novel and sensitive biomarker of acute myocardial infarction, J. Thorac. Dis., 7, 303",{},{"id":20,"text":532,"url":20,"identifiers":533},"Livak, 2001, Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) method, Methods, 25, 402, 10.1006\u002Fmeth.2001.1262",{"doi":534},"10.1006\u002Fmeth.2001.1262",{"id":20,"text":536,"url":20,"identifiers":537},"Hsu, 2014, Systemic approach to identify serum microRNAs as potential biomarkers for acute myocardial infarction, BioMed Res. Int., 2014, 418628, 10.1155\u002F2014\u002F418628",{"doi":538},"10.1155\u002F2014\u002F418628",{"id":540,"createTime":541,"updateTime":541,"relativeEntities":542,"slug":20,"properties":543,"entityType":231,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21,"primaryUrl":552,"fullTextUrl":20,"authors":553,"publicationType":252,"publisherRelationship":617,"citationCount":20,"citationInfo":20,"publishDate":651,"publishYear":652,"citationAnalyzeStatus":19,"lastCitationAnalyze":20,"indexDatabases":20,"openAccess":20,"references":20,"isForceReanalyzing":289},"df8b0d1b-1e83-4e05-b98d-b14293990230","2023-12-08T23:57:00.164+00:00",[],{"references":544,"abstract":546,"title":548,"doi":550},{"VOID":545},"Bergstrom, J. D., Wong, G. A., Edwards, P. A. and Edmond, J. (1984).J. Biol. Chem. 259:14548–14553.\nBergstrom, J. D., Robbins, K. A. and Edmond, J. (1982).Biochem. Biophys. Res. Comm. 106:856–862.\nEndemann, G., Goetz, P. G., Edmond, J. and Brunengraben, H. (1982).J. Biol. Chem. 257:3434–3440.\nBuckley, B. M. and Williamson, D. H. (1975).FEBS Lett. 60:7–10.\nGeelen, M. J. H., Lopes-Cardozo, M. and Edmond, J. (1983).FEBS Lett. 163:269–273.\nBreslow, J. L., Lothrop, D. A., Spaulding, D. R. and Kandutsch, A. A. (1975).Biochim. Biophys. Acta 398:10–17.\nBrown, M. S. and Goldstein, J. L. (1974).J. Biol. Chem. 249:7306–7314.\nEdwards, P. A. (1975).Biochim. Biophys. Acta 409:39–50.\nEdwards, P. A., Lan, S-F. and Fogelman, A. M. (1984).J. Biol. Chem. 259:8190–8194.\nFogelman, A. M., Shechter, I., Seager, J., Hokom, M., Child, J. S. and Edwards, P. A. (1980).Proc. Natl. Acad. Sci. USA 77:2214–2218.\nBerry, M. N. and Friend, D. S. (1969).J. Cell Biol. 43:506–520.\nEdwards, P. A. (1975).Arch. Biochem. Biophys. 170:188–203.\nBergstrom, J. D. and Edmond, J. (1985).Methods in Enzymology 110:3–9.\nEdwards, P. A., Lemongello, D. and Fogelman, A. M. (1979).J. Lipid Res. 20:40–46.\nBradford, M. M. (1976).Anal. Biochem. 72:248–254.\nWebber, R. J. and Edmond, J. (1979).J. Biol. Chem. 254:3912–3920.\nPopjak, G. (1969).Methods in Enzymology 15:393–454.\nPullinger, C. R. and Gibbons, G. F. (1983).J. Lipid Research 724:1321–1328.\nKandutsch, A. A., Chen, H. W. and Heiniger, H. J. (1978).Science 201:498–501.\nPullinger, C. R. and Gibbons, G. F. (1983).Biochem. J. 210:625–632.\nCavenee, W. K. and Melnykovych, G. (1977).J. Biol. Chem. 252:3272–3276.\nRamachandran, C. K., Gray, S. L. and Melnykovych, G. (1978).Arch. Biochem. 189:205–211.\nJohnston, D., Cavenee, W. K., Ramachandran, C. K. and Melnykovych, G. (1979).Biochim. Biophys. Acta 572:188–192.\nCavenee, W. K., Johnston, D. and Melnykovych, G. (1978).Proc. Natl. Acad. Sci. USA 75:2103–2107.\nRamachandran, C. K., Gray, S. L. and Melnykovych, G. (1980).Biochim. Biophys. Acta 618:439–448.\nVolpe, J. J. and Obert, K. A. (1981).Arch. Biochem. Biophys. 212:88–97.\nRaulston, D. L., Miller, L. R. and Schroepfer, G. J. (1980).J. Biol. Chem. 255:4706–4709.\nNervi, F. O., Carrella, M. and Dietschy, J. M. (1976).J. Biol. Chem. 251:3831–3833.\nHenze, K., Kudchodkar, B. J., Chait, A., Albers, J. J. and Bierman, E. L. (1981).Biochim. Biophys. Acta 666:199–204.\nGibbons, G. F., Pullinger, C. R., Munday, M. R. and Williamson, D. H. (1983).Biochem. J. 212:843–848.",{"EN":547},"The activity of acetoacetyl-CoA (AcAc-CoA) ligase (E.C.6.2.1.16) in hepatocytes from rats was shown to be the same as the activity in homogenates of their livers. In hepatocytes treated with 25-hydroxycholesterol, AcAc-CoA ligase, 3-hydroxy-3-methyl-glutaryl-CoA (HMG-CoA) reductase and rates of sterol synthesis were substantially decreased. Hepatocytes treated with high density lipoprotein (HDL) exhibited a 2 to 4 fold induction of HMG-CoA reductase activity; however an accompanying increase in AcAc-CoA ligase activity and the rate of cholesterol synthesis was not observed. We conclude (a) that increases in the activity of HMG-CoA reductase when mediated by HDL in hepatocytes do not result in a corresponding change in the capacity for sterol synthesis and (b) that changes in the activity state of HMG-CoA reductase can be dissociated from that of AcAc-CoA ligase.",{"EN":549},"Acetoacetyl-CoA ligase activity in the isolated rat hepatocyte: Effects of 25-hydroxycholesterol and high density lipoprotein",{"VOID":551},"10.1007\u002FBF01124792","https:\u002F\u002Fportlandpress.com\u002Fbioscirep\u002Farticle\u002F7\u002F3\u002F217\u002F56421\u002FAcetoacetyl-CoA-ligase-activity-in-the-isolated",[554,579,598],{"id":555,"sortIndex":113,"researcher":20,"roles":556,"affiliations":557,"properties":576},"70ba0258-d9ce-4cba-8955-a1221b3c3f44",[239],[558,566],{"id":20,"sortIndex":21,"affiliation":559,"properties":20},{"id":560,"createTime":561,"updateTime":561,"relativeEntities":562,"slug":20,"properties":563,"entityType":65,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21},"8e8a591e-df20-4ce2-b7d6-720b3d9c5f33","2023-12-08T23:57:00.175+00:00",[],{"title":564},{"VI":565},"Department of Biological Chemistry, 33-257 CHS, UCLA School of Medicine, Los Angeles",{"id":567,"sortIndex":147,"affiliation":568,"properties":575},"dd3c6bd3-5f70-49be-a7af-3265ef61f48a",{"id":569,"createTime":570,"updateTime":570,"relativeEntities":571,"slug":20,"properties":572,"entityType":65,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21},"5f58356c-b7de-4715-8e62-7e1979cc9522","2023-12-08T23:57:00.194+00:00",[],{"title":573},{"VI":574},"Mental Retardation Research Center, UCLA School of Medicine, Los Angeles",{},{"title":577},{"VI":578},"John Edmond",{"id":580,"sortIndex":21,"researcher":20,"roles":581,"affiliations":582,"properties":595},"2a11e69a-4ea2-4059-a3c7-aee9317f2cb2",[239],[583,590],{"id":584,"sortIndex":147,"affiliation":585,"properties":589},"451a54da-a4e1-4183-94a1-ce84b0636a0f",{"id":569,"createTime":570,"updateTime":570,"relativeEntities":586,"slug":20,"properties":587,"entityType":65,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21},[],{"title":588},{"VI":574},{},{"id":20,"sortIndex":21,"affiliation":591,"properties":20},{"id":560,"createTime":561,"updateTime":561,"relativeEntities":592,"slug":20,"properties":593,"entityType":65,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21},[],{"title":594},{"VI":565},{"title":596},{"VI":597},"Gail A. 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J.119, 129–138.\nBrighton CT & Hunt RM (1974) Clin. Orthop.100, 406–416.\nMatthews JL, Martin JV, Sampson HW, Kunin AS & Roan JH (1970) Calc. Tiss. Res.5, 91–99.\nZanetti M, Camerotto R, Romeo D, DeBernard B (1982) Biochem. J.202, 303–307.\nBoyde A & Shapiro IM (1980) Histochem.69, 85–94.\nKrefting ER, Libner G & Hohling HJ (1981) Direktabb. Oberfl.14, 373–384.\nBrighton CT & Heppenstall RB (1971) J. Bone Joint Surg.53A, 719–728.\nShapiro IM, Golub EE, Kakuta S, Haselgrove J, Havery J, Chance B & Frasca P (1982) Science217, 950–952.\nMeyer WL & Kunin AS (1972) Arch. Biochem. Biophys.156, 122–133.\nArsenis C, Eisenstein R, Soble LW & Kuettner KE (1971) J. Cell Biol.49, 459–467.\nRabinowtiz JL, Staeffen J, Aumonier P, Ballan P, Ferrer J, Terme R, Series C & Myerson RM (1977) Clin. Chem.23\u002F12, 2202–2206.\nLowry OH, Rosebrough NJ, Farr AL & Randall RJ (1951) J. Biol. Chem.193, 265–275.\nShanfeld J, Jones J & Davidovitch Z (1981) Anal. Biochem.113, 256–263.\nHartwick RA & Brown PR (1975) J. Chromatogr.112, 651–652.\nShapiro IM (1971) Arch. Oral Biol.16, 411–421.\nMarsh JB & Weinstein DB (1966) J. Lipid Res.7, 574–576.\nAtkinson DE (1968) Biochemistry7, 4030–4034.\nWuthier RE (1968) J. Lipid Res.9, 68–78.\nErecinska M, Stubbs M, Miyata Y, Ditre CM & Wilson DF (1977) Biochim. Biophys. Acta462, 20–35.\nShapiro IM & Lee NH (1975) Arch. Biochem. Biophys.170, 627–633.\nLee NH & Shapiro IM (1978) J. Membrane Biol.41, 349–360.\nShapiro IM & Lee NH (1978) Metab. Bone Dis. Related Res.1, 173–177.",{"EN":663},"The objective of this study was to examine the nucleotides of chick growth-plate cartilage and to measure the concentration of adenine nucleotides in the pre-mineralizing and mineralizing zones. Nucleotides were isolated from the two regions using a rapid-freezing technique and the concentration of individual components was ascertained by HPLC. The actual values of ATP, ADP, and other nucleotides in cartilage was low. The lowest values were recorded in the mineralized zone. In this latter zone the energy charge ratio and the ATP\u002FADP ratio were depressed. This was probably due to 02-related inhibition of mitochondrial oxidative activity . Additionally, the percentage of octanoate, a short-chain fatty acid that accumulates when aerobic metabolism is disturbed, was found to have increased in the calcifying zone. These findings suggest that calcification of cartilage is associated with hypoxia-related modulation of chondrocyte metabolism.",{"EN":665},"Studies of nucleotides of growth-plate cartilage: evidence linking changes in cellular metabolism with cartilage calcification",{"VOID":667},"10.1007\u002FBF01122899","https:\u002F\u002Fportlandpress.com\u002Fbioscirep\u002Farticle-abstract\u002F3\u002F4\u002F345\u002F55251\u002FStudies-of-nucleotides-of-growth-plate-cartilage?redirectedFrom=fulltext",[670,685,697,709],{"id":671,"sortIndex":147,"researcher":20,"roles":672,"affiliations":673,"properties":682},"7a355049-bb60-4c71-a683-f6d0ce316fc6",[239],[674],{"id":20,"sortIndex":21,"affiliation":675,"properties":20},{"id":676,"createTime":677,"updateTime":677,"relativeEntities":678,"slug":20,"properties":679,"entityType":65,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21},"8e81cef9-4621-4942-91bf-80a460bec257","2024-01-16T04:53:05.580+00:00",[],{"title":680},{"VI":681},"Department of Biochemistry, School of Dental Medicine, University of Pennsylvania, Philadelphia, USA",{"title":683},{"VI":684},"Ellis E. 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Several models have been presented for the effects of ligand-induced receptor conformation and aggregation on signal transduction but little is known about the direct effects on receptor diffusion. This study concerns the lateral mobility of PDGF receptors in fibroblasts. It was assessed with fluorescence recovery after photobleaching (FRAP), using rhodaminated receptor antibodies or Fab-fragments of the antibody as ligands. The aims of the investigation were: (a) to compare the lateral mobility of membrane receptors of human fibroblasts labelled with either antibodies against the PDGF receptor or Fab-fragments of the same antibodies, and (b) to study the effects of serum or PDGF on the mobility of the receptors. Human foreskin fibroblasts (AG 1523) were grown on coverslips either under standard or under serum-free conditions yielding “normal” and “starved” cells, respectively. Two parameters of the diffusion were evaluated; the diffusion coefficient (D) and the mobile fraction (R) of the receptors. We found that normal fibroblasts had a smaller diffusion coefficient and a lower mobile fraction compared to starved cells using antibodies for receptor labelling. The addition of PDGF, just before the measurement, increased the D and R for normal cells, while starved cells, showing higher initial values, displayed slightly reduced values of D and R. After the addition of serum, D increased and R remained low for normal cells, whereas for starved cells both D and R increased to upper limits of 11.0×10−10 cm2s−1 and >90% respectively. In general, the D and R values, both in normal and starved cells, were higher for cells labelled with Fab-fragments than for antibody-labelled cells. 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(1985) Surface marker characterization of EBV target cells in normal blood and tonsil B lymphocyte populations.J. Immunol. 135:2362?2367.",{"doi":1146},"10.4049\u002Fjimmunol.135.4.2362",{"id":20,"text":1148,"url":20,"identifiers":1149},"Dennis, G., et al. (1987) Glucocorticoids suppress calcium mobilization and phospholipid hydrolysis in anti-Ig antibody stimulated B-cells.J. Immunol. 139:2516?2523.",{"doi":1150},"10.4049\u002Fjimmunol.139.8.2516",{"id":20,"text":1152,"url":20,"identifiers":1153},"Dröge, W. (1986) Protein kinase C In T cell regulation.Immun. Today 7:340?343.",{"doi":1154},"10.1016\u002F0167-5699(86)90141-6",{"id":20,"text":1156,"url":20,"identifiers":1157},"Fassio, A., Cofano, F., Cavallo, G. and Landolfo, S. (1987) Activation protein kinase C down regulates IFN-gamma receptors.Biochem. Biophy. Res. Com. 144:337?344.",{"doi":1158},"10.1016\u002FS0006-291X(87)80515-6",{"id":20,"text":1160,"url":20,"identifiers":1161},"Gillis, S. -Crabtree, G. R. and Smith, K. A. (1979) Glucocorticoid induced inhibition of T-cell growth factor production. I. The effect of mitogen-induced lymphocyte proliferation.J. Immunol. 123:1624?1631.",{"doi":1162},"10.4049\u002Fjimmunol.123.4.1624",{"id":20,"text":1164,"url":20,"identifiers":1165},"Hadden, J. W. (1988) Transmembrane signals in the activation of T lymphocytes by mitogenic antigens.Immunol. Today 9:235?239.",{"doi":1166},"10.1016\u002F0167-5699(88)91222-4",{"id":20,"text":1168,"url":20,"identifiers":1169},"Lacroix, A., Bonnard, G. D. and Lippman, M. E. (1984) Modulation of glucocorticoid receptors by mitogenic stimuli, glucocorticoids and retinoids in normal human cultured T cells.J. Steroid Bio-chem. 21:73?80.",{"doi":1170},"10.1016\u002F0022-4731(84)90062-1",{"id":20,"text":1172,"url":20,"identifiers":1173},"Larsson, E. L. (1980) Cyclosporin A and dexamethasone suppress T cell responses by selectively acting at distinct sites of the triggering process.J. 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Natl. Acad. Sci. U.S.A. 74, 5260–5264.\nCarson SD & Konigsberg WH (1980)Science 208, 307–309.\nCarson SD & Konigsberg WH (1980)Thrombos. Haemostas. 44, 12–15.\nNemerson Y (1968)J. Clin. Invest. 47, 72–80.\nHvatum M & Prydz, H (1969)Thrombos. Diathes. Haemorrh. 21, 217–222.\nNemerson Y (1969)J. Clin. Invest. 48, 322–331.\nWijngaards G, van Deenen LLM, & Hemker HC (1977)Biochim. Biophys. Acta 488, 161–171.\nNemerson Y, Zur M, Bach R, & Gentry R (1980) inRegulation of Coagulation (Mann KB and Taylor FB, eds), pp 193–202, Elsevier, New York.\nPitlick FA & Nemerson Y (1978)Meth. Enzymol. 45, 37–48.\nChen PS Jr, Toribara TY, & Warner H (1956)Anal. Chem. 28, 1756–1758.\nBartlett GR (1959)J. Biol. Chem. 234, 466–469.\nGodson GN, Fiddles JC, Barrel BG, & Sanger F (1978) inThe Single-Stranded DNA Phages (Denhardt DT, Dressler D, & Ray DS, eds), pp 51–86, Cold Spring Harbor.\nGodson GN (1978) inThe Single-Stranded DNA Phages (Denhardt DT, Dressler D, and Ray DS, eds), pp 103–112, Cold Spring Harbor.\nHuang C-H (1969)Biochemistry 8, 344–352.\nLiao M-J & Prestegard JH (1979)Biochim. Biophys. Acta 550, 157–173.\nHolz RW & Stratford CA (1979)J. Membrane Biol. 46, 331–358.\nPapahadjopoulos D, Vail WJ, Pangborn WA, & Poste G (1976)Biochim. Biophys. Acta 448, 265–283.\nNelsestuen GL, Kisiel W, & DiScipio RG (1978)Biochemistry 17, 2134–2138.\nTanford C (1980)The Hydrophobic Effect, 2nd ed, pp 114–117, John Wiley and Sons, New York.",{"EN":1463},"Coagulation factor III (tissue factor) is a membrane glycoprotein which serves as a cofactor in the proteolytic activation of factor X and factor IX by factor VIIa. Mixing of human placental factor III apoprotein with vesicles of bovine brain phospholipids does not produce significant reconstitution of factor III activity, but, when the mixture of apoprotein and vesicles is made 5 mM with CdCI2, the apoprotein is incorporated into the vesicles. Ultracentrifugation on sucrose density gradients demonstrated that the active factor III-lipid complex formed by reconstitution with vesicles had a density indistinguishable from that of the complex formed by detergent dialysis. Vesicles isolated after centrifugation were shown to range in diameter from 20 nm to over 100 nm using the electron microscope. Gel filtration showed that factor-III activity was associated with all size-classes of vesicles. 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P., Hammerstedt, R. H. and Veeramachanen, D. N. R. (1993)Reprod. Fertil. Dev. 5:361–381.\nHammerstedt, R. H., Graham, J. K. and Nolan, J. P. (1990)J. Androl. 11:73–88.\nBredderman, P. J. and Foote, R. H. (1971)Exp. Cell. Res. 66:458–464.\nBredderman, P. J. and Foote, R. H. (1971)Exp. Cell Res. 66:190–196.\nCartwright, E. J., Cowin, A. and Sharpe, P. T. (1991)Bioscience Rep. 11:265–273.\nCartwright, E. J., Harrington, P., Norbury, L., Leeming, G. and Sharpe, P. T. (1992)Bioscience Rep. 12:57–67.\nHarrison, R. A. P., Jacques, M. L., Pascual, M. L. and Miller, N. G. A. (1992)J. Cell Sci. 102:123–132.\nPascual, M. L., Muiño-Blanco, T., Cebrián-Pérez, J. A. and López-Pérez, M. J. (1992)J. Biochem Biophys. Methods 24:275–284.\nPascual, M. L., Muiño-Blanco, T., Cebrián-Pérez, J. A. and López-Pérez, M. J. (1993)J. Chromatogr. 617:51–57.\nPascual, M. L., Muiño-Blanco, T., Cebrián-Pérez, J. A. and López-Perez, M. J. (1994)Biology Cell 82:75–78.\nOllero, M., Pascual, M. L., Muiño-Blanco, T., Cebrián-Pérez, J. A. and López-Pérez, M. J. (1994)J. Chromatogr. 668:173–178.\nAkerlund, H. E. (1984)J. Biochem Biophys. Methods 9:133–141.\nHarrison, R. A. P. and Vickers, S. E. (1990)J. Reprod. Fert. 88:343–352.\nCummins, J. M., Jequier, A. M. and Kan, R. (1994)Mol. Reprod. Dev. 37:345–262.\nKao, S. H., Chao, H. T. and Wei, Y. H. (1995)Biol. Reprod. 52:729–736.\nShams-Borham, G. and Harrison, R. A. P. (1981)Gamete Res. 4:407–432.",{"EN":1544},"Centrifugal countercurrent distribution (CCCD) in aqueous two-phase systems has been proven to be a useful method to study subtle surface properties of spermatozoa. The present work shows that a short-term inhibition of the energy metabolism of sperm cells effected by incubating bovine sperm cells with KCN or ouabain, did not account for changes in the cell surface properties, as assessed either by estimation of the cell viability or by CCCD analysis. However, the short-term inhibition of energy metabolism provoked a clear decrease of cell motility, suggesting that a drop of cellular ATP levels brings about a rapid decrease of motility followed by a very delayed effect on cell surface properties. 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