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In this study, we examined the expression of an antioxidant defense gene,nkef, in human tissue and isolated populations of rat brain cells using Western and Northern blot analysis. NKEF protein was expressed in human brain, liver, kidney, muscle, and lung. The human endothelial cell line ECV expressed a 25-kDa band in addition to the 22-kDa band normally observed. In the central nervous system, a 22-kDa NKEF band was present in cortical gray and white matter, hippocampus, cerebellum, and spinal cord in roughly similar amounts. Expression of NKEF-A and NKEF-B subtypes was evaluated by Northern analysis of cultured cell types from embryonic rat brain. Astrocyte and microglia expressed both 22- and 25-kDa bands, whereas cortical neurons and oligodendrocytes contained only the 22-kDa protein band. Northern blot analysis of these cell types revealed low levels of NKEF-A message in neurons and oligodendrocytes, and relatively low levels of NKEF-B in microglia. Differential expression of these antioxidant defense genes may contribute to the selective vulnerability of brain cell types to specific kinds of oxidative stress.",{"EN":91},"Expression of the antioxidant geneNKEF in the central nervous system",{"VOID":93},"[\"4356761469389803034\"]",{"VOID":95},"Birnbaum G. (1995) Stress proteins: their role in the normal central nervous system and in disease states, especially multiple sclerosis.Springer Semin. Immunopathol. 17(1), 107–118.\nBoje K. M. and Arora P. K. (1992) Microglial-produced nitric oxide and reactive nitrogen oxides mediate neuronal cell death.Brain Res. 587, 250–256.\nBowling A. C. and Beal M. F. (1995) Bioenergetic and oxidative stress in neurodegenerative diseases.Life Sci. 56, 1151–1171.\nCachianes G., No C., Weber B. F., Williams S. R., Goeddel D. V., and Leung D. W. (1993) Epstein-Barr virus-derived vectors for transient and stable expression of recombinant proteins.Biotechniques 15(2), 255–259.\nChao C. C., Hu S., and Peterson P. K. (1995) Glia, cytokines, and neurotoxicity.Crit. Rev. Neurobiol. 9(2–3), 189–205.\nCole R. and de Vellis J. (1989) Preparation of astrocyte and oligodendrocyte cultures from primary rat glial cultures, inA Dissection and Tissue Culture Manual of the Nervous System (Shahar A., de Vellis J., Vernadakis A., and Haber B., eds.), pp. 121–134, Alan R. Liss, New York.\nDesagher S., Glowinski J., and Premont J. (1996) Astrocytes protect neurons from hydrogen peroxide toxicity.J. Neurosci. 16, 2553–2562.\nGrigorian B., Ling A., Kim A., Shau H., and Sarafian T. (1997) Protection of cellular energy production pathways by human natural killer enhancing factor B.Biochim. Biophys Acta, submitted.\nIchimiya S., Davis J. G., O'Rourke D. M., Katsumata M., and Greene M. I. (1997) Murine thioredoxin peroxidase delays neuronal apoptosis and is expressed in areas of the brain most susceptible to hypoxic and ischemic injury.DNA Cell Biol. 16, 311–321.\nJuurlink B. H. (1997) Response of glial cells to ischemia: roles of reactive oxygen species and glutathione.Neurosci. Biobehav. Rev. 21, 151–166.\nKim A. T., Sarafian T. A., and Shau H. (1997) Characterization of antioxidant properties of natural killer enhancing factor-B and induction of its expression by hydrogen peroxide.Toxicol. Appl. Pharmacol. 147, 135–142.\nKumar S. and de Vellis J. (1981) Induction of lactate dehydrogenase by dibutyryl cAMP in primary cultures of central nervous tissue is an oligodendrocyte marker.Dev. Brain Res. 1, 303–307.\nLazo J. S., Kondo Y., Dellapiazza D., Michalska A. E., Chou K. H., and Pitt B. R. (1995) Enhanced sensitivity to oxidative stress in cultured embryonic cells from transgenic mice deficient in metallothionein I and II genes.J. Biol. Chem. 270, 5506–5510.\nLim Y. S., Cha M. K., Kim H. K., and Kim I. H. (1994) The thiol-specific antioxidant protein from human brain: gene cloning and analysis of conserved cysteine regions.Gene 140, 279–284.\nMcCarthy K. D. and de Vellis J. (1980) Preparation of separate astroglial and oligodendroglial cell cultures from rat cerebral tissue.J. Cell Biol. 85, 890–902.\nMcDuffee A. T., Senisterra G., Huntley S., Lepock J. R., Sekhar K. R., Meredith M. J., et al. (1997) Proteins containing non-native disulfide bonds generated by oxidative stress can act as signals for the induction of the heat shock response.J. Cell Physiol. 171, 143–151.\nMitrovic B., Ignarro L. J., Vinters H. V., Akers M. A., Schmid I., Uittenbogaart C., et al. (1995) Nitric oxide induces necrotic but not apoptotic cell death in oligodendrocytes.Neuroscience 65, 531–539.\nNetto L. E. S., Chae H. Z., Kang S. W., Rhee S. G., and Stadtman E. R. (1996) Removal of hydrogen peroxide by thiol-specific antioxidant enzyme (TSA) is involved with its antioxidant properties. TSA possesses thiol peroxidase activity.J. Biol. Chem. 271, 15,315–15,321.\nPinteaux E., Coplin J. C., Ledig M., and Tholey G. (1996) Modulation of oxygen-radical-scavenging enzymes by oxidative stress in primary cultures of rat astroglial cells.Dev. Neurosci. 18, 397–404.\nRhee S. G., Kim K. H., Chae H. Z., Yim M. B., Uchida K., Netto L. E., et al. (1994) Antioxidant defense mechanisms: a new thiol-specific antioxidant enzyme.Ann. NY Acad. Sci. 738, 86–92.\nSarafian T. A., Vartavarian L., Kane D. J., Bredesen D. E., and Verity M. A. (1994) bcl-2 Expression decreases methyl-induced free-radical generation and cell killing in a neural cell line.Toxicol. Lett. 74, 149–155.\nSarafian T. A., Rajper N., Grigorian B., Kim A., and Shau H. (1996) Cellular antioxidant properties of human natural killer enhancing factor B.Free Radical Res. 26, 281–289.\nSauri H., Butterfield L., Kim A., and Shau H. (1995) Antioxidant function of recombinant human natural killer enhancing factor.Biochem. Biophys. Res. Commun. 208, 964–969.\nShau H., Gupta R., and Golub S. (1993) Identification of a natural killer enhancing factor from human erythroid cells.Cell Immunol. 147, 1–11.\nShau H. and Kim A. (1994) Identification of natural killer enhancing factor as a major antioxidant in human red blood cells.Biochem. Biophys. Res. Commun. 199, 83–88.\nShau H., Butterfield L. H., Chiu R., and Kim A. (1994) Cloning and sequence analysis of candidate human natural killer-enhancing factor genes.Immunogenetics 40, 129–134.\nShau H., Kim A. T., Hedrick C. C., Lusis A. J., Tompkins C., Finney A., et al. (1997) Endogenous natural killer enhancing factor-B increases cellular resistance to oxidative stresses.Free Radical Biol. Med. 22, 497–507.\nSiow R. C., Ishii T., Sato H., Taketani S., Leake D. S., Sweiry J. H., et al. (1995) Induction of the antioxidant stress proteins heme oxygenase-1 and MSP23 by stress agents and oxidized LDL in cultured vascular smooth muscle cells.FEBS Lett. 368, 239–242.\nTartaglia L. A., Storz G., Brodsky M. H., Lai A., and Ames B. N. (1990) Alkyl hydroperoxidase reductase fromSalmonella typhimurium. Sequence and homology to thioredoxin reductase and other flavoprotein disulfide oxidoreductases.J. Biol. Chem. 265, 10,535–10,540.\nWong G. H., Kaspar A. L., and Vehar G. (1996) Tumor necrosis factor and lymphotoxin: protection against oxidative stress through induction of MnSOD.Experientia 77, 321–333.\nYim M. B., Chae H. Z., Rhee S. G., Chock P. B., and Stadtman E. R. (1994) On the protective mechanism of the thiol-specific antioxidant enzyme against the oxidative damage of biomacromolecules.J. Biol. 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(1986) Stimulation of tryptophan uptake into brain microvessels byd-glutamine.Brain Res. 367, 395–397.",{"doi":387},"10.1016\u002F0006-8993(86)91626-4",{"id":18,"text":389,"url":18,"identifiers":390},"Green J. D. (1964) The hippocampus.Physiol. Rev. 44, 561–608.",{"doi":391},"10.1152\u002Fphysrev.1964.44.4.561",{"id":18,"text":393,"url":18,"identifiers":394},"Hargreaves K. M. and Pardridge W. M. (1988) Neutral amino acid transport at the human blood-brain barrier.J. Biol. Chem. 263, 19392–19397.",{"doi":395},"10.1016\u002FS0021-9258(19)77645-5",{"id":18,"text":397,"url":18,"identifiers":398},"Hamberger A. and Nystrom B. (1984) Extra- and intracellular amino acids in the hippocampus during development of hepatic encephalopathy.Neurochem. Res. 9, 1181–1192.",{"doi":399},"10.1007\u002FBF00973033",{"id":18,"text":401,"url":18,"identifiers":402},"Hawkins R. A., Mans A. M., and Biebuyck J. F. (1987) Changes in brain metabolism in hepatic encephalopathy.Neurochem. 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(1988) Changes in the activity of γ-glutamyl transpeptidase in brain microvessels, astroglial cells and synaptosomes derived from rats with hepatic encephalopathy.Neurosci. Lett. 84, 323–328.",{"doi":460},"10.1016\u002F0304-3940(88)90529-0",{"id":18,"text":462,"url":18,"identifiers":463},"Thomas J. W., Banner C., Whitman J., Mullen K. D., and Freese E. (1988) Changes in glutamate-cycle enzyme mRNA levels in a rat model of hepatic encephalopathy.Metabol. Brain Dis. 3, 81–90.",{"doi":464},"10.1007\u002FBF01001011",{"id":18,"text":466,"url":18,"identifiers":467},"Zieve L. (1987) Pathogenesis of hepatic encephalopathy.Metabol. Brain Dis. 2, 147–165.",{"doi":468},"10.1007\u002FBF00999607",{"id":470,"createTime":471,"updateTime":472,"relativeEntities":473,"slug":474,"properties":475,"entityType":98,"verifyStatus":99,"verifyTime":486,"verifyNote":101,"languages":18,"translateLanguages":18,"viewCount":19,"primaryUrl":487,"fullTextUrl":18,"authors":488,"publicationType":202,"publisherRelationship":573,"citationCount":18,"citationInfo":18,"publishDate":598,"publishYear":599,"citationAnalyzeStatus":600,"lastCitationAnalyze":601,"indexDatabases":602,"openAccess":18,"references":18,"isForceReanalyzing":234},"04995e01-21bc-4616-8154-b238ee3a6854","2023-12-22T23:24:20.064+00:00","2026-07-16T22:03:17.893+00:00",[],"In-vivo-and-in-vitro-models-of-medulloblastomas-and-other-primitive-neuroectodermal-brain-tumors-of-childhood",{"abstract":476,"title":478,"gsPaper":480,"references":482,"doi":484},{"EN":477},"Recent advances in understanding the basic biology of the neoplastic cells that populate childhood primitive neuroectodermal tumors (PNET) of the central nervous system (CNS) underline several unique properties of these common pediatric brain neoplasms. For example, studies of posterior fossa cerebellar medulloblastomas (MB), a prototypical group of brain tumors that comprise the largest class of PNET, suggest that the molecular phenotype of subpopulations of neoplastic cells in MB partially recapitulates stages in the acquisition of the neuronal phenotype by normal developing human CNS progenitor cells. However, as reviewed here, it appears that the neoplastic cells in MB exhibit one or more molecular defects in the sequence of normal maturational events that enable CNS progenitor cells to exit the cell cycle, become committed to the neuronal lineage, and undergo terminal differentiation into fully mature, permanently postmitotic CNS neurons. Indeed, since PNET emerge almost exclusively in early childhood, the induction of PNET may result from genetic lesions that arise in developing CNS progenitor cells thereby preventing these neural precursors from executing normal programs of lineage commitment and differentiation in the CNS. Clarification of how lineage commitment and maturation in PNET comprised of neuron-like tumor cells deviate from normal CNS development may clarify how oncogenes and tumor suppressor genes exert their effects in a cell type specific manner at different stages in the normal maturation of CNS cells. Recently, a number of potentially effective in vitro and in vivo model systems of PNET have been developed. Since these model systems could facilitate efforts to elucidate mechanisms of neoplastic transformation and tumor progression in the CNS, we review, the potential utility of several recently described in vitro (e.g., MB cell lines) and in vivo (e.g., transgenic mice) experimental systems as models of authentic childhood CNS neoplasms.",{"EN":479},"In vivo and in vitro models of medulloblastomas and other primitive neuroectodermal brain tumors of childhood",{"VOID":481},"[\"15300438637726589756\"]",{"VOID":483},"Akbasak A., Sunar-Akbasak B. 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Neurol. 42, 1–15.\nRorke L. B., Molenaar W. M., and Trojanowski J. Q. (1992) The impact of monoclonal antibody studies on changing nosology and biological concepts of brain tumors, inNew Trends in Pediatric Neuro-oncology (Bleyer A., Packer R., and Pochedly C., eds.), pp. 8–31, Hardwood, NY.\nRussell D. S. and Rubinstein L. J. (1989)Pathology of Tumors of the Nervous System, 5th ed., Williams & Wilkins, Baltimore, MD.\nSawyers C. L., Denny C. T., and Witte O. N. (1991) Leukemia and the disruption of normal hematopoesis.Cell 64, 337–350.\nSaylors R. L., Sidransky D., Friedman H. S., Bigner S. H., Bigner D. D., Vogelstein B., and Brodeur G. M. (1991) Infrequent p53 gene mutations in medulloblastomas.Cancer Res. 51, 4721–4723.\nSeemayer T. A. and Cavenee W. K. (1990) Molecular mechanisms of oncogenesis.Lab. Invest. 60, 585–599.\nSeizinger B. R. (1992) Antioncogenes and the development of tumors in the human nervous system.Cancer 70, 1782–1787.\nShaw G. 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B., Marvin M., McKay R. D. G., and Trojanowski J. Q. (1992) Nestin expression in embryonic human neuroepithelium and in human neuroepithelial tumors.Lab Invest. 66, 303–313.\nTohyama T., Lee V. M.-Y., Rorke L. B., Marvin M., McKay R. D. G., and Trojanowski J. Q. (1993a) Monoclonal antibodies to a rat nestin fusion protein recognize a 220 kiloDalton polypeptide in subsets of fetal and adult human central nervous system neurons and in primitive neuroectodermal tumor cells.Am. J. Pathol. 143, 258–268.\nTohyama T., Lee V. M.-Y., Rorke L. B., and Trojanowski J. Q. (1991) Molecular milestones that signal axonal maturation and the committment of human spinal cord precursor cells to the neuronal or glial phenotype in development.J. Comp. Neurol. 310, 285–299.\nTohyama T., Lee V. M.-Y., and Trojanowski J. Q. (1993b) Co-expression of low molecular weight neurofilament protein and glial fibrillary acidic protein in established human glioma cell lines.Am. J. Pathol. 142, 883–892.\nTrojanowski J. 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Neurol. 334, 356–369.",{"VOID":485},"10.1007\u002FBF02815352","2024-06-25T05:45:27.318+00:00","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002FBF02815352",[489,504,517,532,547,560],{"id":490,"sortIndex":19,"researcher":18,"roles":491,"affiliations":492,"properties":501,"displayName":503,"givenName":18,"familyName":18},"8dc74cf7-4f52-4b18-9b5e-bdc22c775350",[107],[493],{"id":494,"sortIndex":19,"affiliation":495,"properties":18},"6d5eff7f-462b-4425-b238-0c26f4a7d989",{"id":494,"createTime":18,"updateTime":18,"relativeEntities":496,"slug":18,"properties":497,"entityType":18,"verifyStatus":18,"verifyTime":18,"verifyNote":18,"languages":18,"translateLanguages":18,"viewCount":18,"url":18,"parentIds":500,"statistic":18},[],{"title":498},{"VI":499},"The Department of Pathology and Laboratory Medicine, Division of Anatomical Pathology, The University of Pennsylvania School of Medicine, Philadelphia",[],{"title":502},{"VI":503},"John Q. Trojanowski",{"id":505,"sortIndex":122,"researcher":18,"roles":506,"affiliations":507,"properties":514,"displayName":516,"givenName":18,"familyName":18},"56b2f37f-d185-4eeb-905e-6b206e22f175",[107],[508],{"id":494,"sortIndex":19,"affiliation":509,"properties":18},{"id":494,"createTime":18,"updateTime":18,"relativeEntities":510,"slug":18,"properties":511,"entityType":18,"verifyStatus":18,"verifyTime":18,"verifyNote":18,"languages":18,"translateLanguages":18,"viewCount":18,"url":18,"parentIds":513,"statistic":18},[],{"title":512},{"VI":499},[],{"title":515},{"VI":516},"Kar-Ming Fung",{"id":518,"sortIndex":147,"researcher":18,"roles":519,"affiliations":520,"properties":529,"displayName":531,"givenName":18,"familyName":18},"abe64924-bdf7-40ea-9476-dee194fcdb24",[107],[521],{"id":522,"sortIndex":19,"affiliation":523,"properties":18},"28dc43d7-d727-4dea-a226-096b05e07414",{"id":522,"createTime":18,"updateTime":18,"relativeEntities":524,"slug":18,"properties":525,"entityType":18,"verifyStatus":18,"verifyTime":18,"verifyNote":18,"languages":18,"translateLanguages":18,"viewCount":18,"url":18,"parentIds":528,"statistic":18},[],{"title":526},{"VI":527},"Children's Hospital of Philadelphia, Philadelphia",[],{"title":530},{"VI":531},"Lucy B. Rorke",{"id":533,"sortIndex":168,"researcher":18,"roles":534,"affiliations":535,"properties":544,"displayName":546,"givenName":18,"familyName":18},"d27b3374-31ce-4cdc-bfa6-75c135b429aa",[107],[536],{"id":537,"sortIndex":19,"affiliation":538,"properties":18},"a4140696-84e2-4b90-9b4a-e792a53f4546",{"id":537,"createTime":18,"updateTime":18,"relativeEntities":539,"slug":18,"properties":540,"entityType":18,"verifyStatus":18,"verifyTime":18,"verifyNote":18,"languages":18,"translateLanguages":18,"viewCount":18,"url":18,"parentIds":543,"statistic":18},[],{"title":541},{"VI":542},"The Department of Neurosurgery, Tokyo Womens Medical School, Tokyo, Japan",[],{"title":545},{"VI":546},"Takashi Tohyama",{"id":548,"sortIndex":44,"researcher":18,"roles":549,"affiliations":550,"properties":557,"displayName":559,"givenName":18,"familyName":18},"e0307595-6eff-41ba-8920-a4a2c0f88efa",[107],[551],{"id":522,"sortIndex":19,"affiliation":552,"properties":18},{"id":522,"createTime":18,"updateTime":18,"relativeEntities":553,"slug":18,"properties":554,"entityType":18,"verifyStatus":18,"verifyTime":18,"verifyNote":18,"languages":18,"translateLanguages":18,"viewCount":18,"url":18,"parentIds":556,"statistic":18},[],{"title":555},{"VI":527},[],{"title":558},{"VI":559},"Anthony T. Yachnis",{"id":561,"sortIndex":351,"researcher":18,"roles":562,"affiliations":563,"properties":570,"displayName":572,"givenName":18,"familyName":18},"b9aa7a02-0f1f-4b53-ba68-3fa4be112092",[107],[564],{"id":494,"sortIndex":19,"affiliation":565,"properties":18},{"id":494,"createTime":18,"updateTime":18,"relativeEntities":566,"slug":18,"properties":567,"entityType":18,"verifyStatus":18,"verifyTime":18,"verifyNote":18,"languages":18,"translateLanguages":18,"viewCount":18,"url":18,"parentIds":569,"statistic":18},[],{"title":568},{"VI":499},[],{"title":571},{"VI":572},"Virginia M. -Y. Lee",{"url":487,"publisher":574,"properties":593},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":575,"slug":10,"properties":576,"entityType":16,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"languages":18,"translateLanguages":18,"viewCount":19,"subjectFields":579,"manageAffiliations":580,"indexDatabases":581,"url":18,"thumbnailPath":18,"statistic":588,"gsStatistic":18,"type":18,"analyzePriority":18},[],{"issn":577,"title":578},{"VOID":13},{"EN":15},[],[],[582],{"id":24,"indexDatabase":583,"url":35,"indexYears":36,"academicFieldIds":18,"indexDatabaseRanking":37},{"id":26,"createTime":18,"updateTime":18,"relativeEntities":584,"label":585,"description":586,"key":32,"publicationTags":587,"standard":18},[],{"EN":29,"VI":29},{"EN":29,"VI":31},[34],{"impactFactor":19,"impactFactorByYear":589,"i10Index":40,"i10IndexLast5Year":19,"totalPublication":41,"totalPublicationByYear":590,"totalCitation":55,"totalCitationByYear":591,"totalCitationPerPublication":64,"totalCitationPerPublicationByYear":592,"hindexLast5Year":76,"hindex":76},{},{"1986":43,"1987":44,"1988":45,"1989":46,"1990":40,"1991":47,"1992":48,"1993":49,"1994":50,"1995":51,"1996":52,"1997":53,"1998":54},{"1989":43,"1990":57,"1991":54,"1992":58,"1993":59,"1994":60,"1995":61,"1996":62,"1997":63,"1998":43},{"1989":66,"1990":67,"1991":68,"1992":69,"1993":70,"1994":71,"1995":72,"1996":73,"1997":74,"1998":75},{"pages":594,"volume":596},{"VOID":595},"219-239",{"VOID":597},"21","1994-02-01",1994,"ERROR_IN_ANALYZE_CITATION","2026-07-16T22:03:17.892+00:00",[37],{"id":604,"createTime":605,"updateTime":606,"relativeEntities":607,"slug":608,"properties":609,"entityType":98,"verifyStatus":99,"verifyTime":620,"verifyNote":101,"languages":18,"translateLanguages":18,"viewCount":19,"primaryUrl":621,"fullTextUrl":18,"authors":622,"publicationType":202,"publisherRelationship":640,"citationCount":19,"citationInfo":665,"publishDate":668,"publishYear":666,"citationAnalyzeStatus":353,"lastCitationAnalyze":669,"indexDatabases":670,"openAccess":18,"references":18,"isForceReanalyzing":234},"739cb161-9cf8-43ab-810f-4f28b9cb5dc8","2024-01-04T03:54:45.101+00:00","2026-07-11T08:34:38.823+00:00",[],"Plasma-membrane-Ca2-pump-functional-specialization-in-the-brain",{"abstract":610,"title":612,"gsPaper":614,"references":616,"doi":618},{"EN":611},"The plasma membrane Ca2+-pump (PMCA) is a key element in the removal of intracellular Ca2+. A number of PMCA pumps, encoded by a multigenic family and differing in their regulatory domains, also exist in the neuronal cells. We discuss here an idea regarding a new, higher level of specialization of PMCA protein isoforms with different sensitivities toward phospholipids and calmodulin. The idea is based on the kinetic data from PMCA stimulation by acidic phospholipids, with a combination of results describing an alternative RNA splicing at site A and C coding of regulatory domains of protein. The resulting complex modulation of the Ca2+-pump underlies the specific cellular requirements for Ca2+ homeostasis in a tissue-selective manner and is regulated by the level and spatial distribution of enzyme isoforms as well as by the level of their regulatory factors. The possible role of PMCA protein in the neuronal injury is also discussed.",{"EN":613},"Plasma membrane Ca2+-pump functional specialization in the brain",{"VOID":615},"[\"9624942368967287322\"]",{"VOID":617},"Adamo H. 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Biol.120, 1–15.\nTalamoni N. T., Smith C. A. Wasserman R. H., Beltramino C., Fullmer C. S., and Penniston J. T. (1993) Immunocytochemical localization of the plasma membrane calcium pump, calbindin-D28k, and parvalbumin in Purkinje cells of avian and mammalian cerebellum.Proc. Natl. Acad. Sci. USA 90, 11949–11953.\nVerbist J., Gadella Jr. T. W., Raeymaekers L., Wuytack F., Wirtz K. W. A., and Casteels R. (1991) Phosphoinositide-protein interactions of the plasma membrane Ca2+ transport ATPase as revealed by fluorescence energy transfer.Biochim. Biophys. Acta 1063, 1–6.\nWang K. K. W., Villalobo A., Roufagalis B. G. (1992) The plasma membrane calcium pump: a multiregulated transporter.Trends Cell Biol.2, 46–52.\nWrzosek A., Famulski K., Lehotsky J., and Pikula S. (1989) Conformational changes of the Ca2+, Mg2+-ATPase of erythrocyte plasma membrane caused by calmodulin and phosphatidylserine as revealed by circular dichroism and fluorescence study.Biochim. Biophys. Acta 986, 263–270.\nWuytack F. and Raeymaekers L. (1992) The Ca2+-transport ATPases from plasma membrane.J. Bioenerg. Biomembr.24, 285–300.\nWuytack F., Raeymaekers L., De Smedt H., Eggermont J. A., Missiaen L., van den Bosch L., De Jaegere S., Verboomen H., Plessers L., and Casteels R. (1992) Ca2+-transport ATPases and their regulation in muscle and brain.Ann. NY Acad. Sci.671, 82–91.\nZvaritch E., James P., Vorherr T., Falchetto R., Modyanov N., and Carafoli E. (1990) Mapping of functional domains in the plasma membrane Ca2+ pump using trypsin proteolysis.Biochemistry 29, 8070–8076.",{"VOID":619},"10.1007\u002FBF02960911","2024-06-24T14:16:55.757+00:00","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002FBF02960911",[623],{"id":624,"sortIndex":19,"researcher":18,"roles":625,"affiliations":626,"properties":635,"displayName":637,"givenName":18,"familyName":18},"845c190f-995f-4a8d-858d-2a2aa0ab46ef",[107],[627],{"id":628,"sortIndex":19,"affiliation":629,"properties":18},"ae75e5cd-a523-4117-bb84-2a415d8b65e1",{"id":628,"createTime":18,"updateTime":18,"relativeEntities":630,"slug":18,"properties":631,"entityType":18,"verifyStatus":18,"verifyTime":18,"verifyNote":18,"languages":18,"translateLanguages":18,"viewCount":18,"url":18,"parentIds":634,"statistic":18},[],{"title":632},{"VI":633},"Jessenius Medical Faculty, Department of Biochemistry, Comenius University, Martin, Slovak Republic",[],{"title":636,"gsAuthor":638},{"VI":637},"Ján Lehotský",{"VOID":639},"[\"rXl9hY0AAAAJ\"]",{"url":621,"publisher":641,"properties":660},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":642,"slug":10,"properties":643,"entityType":16,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"languages":18,"translateLanguages":18,"viewCount":19,"subjectFields":646,"manageAffiliations":647,"indexDatabases":648,"url":18,"thumbnailPath":18,"statistic":655,"gsStatistic":18,"type":18,"analyzePriority":18},[],{"issn":644,"title":645},{"VOID":13},{"EN":15},[],[],[649],{"id":24,"indexDatabase":650,"url":35,"indexYears":36,"academicFieldIds":18,"indexDatabaseRanking":37},{"id":26,"createTime":18,"updateTime":18,"relativeEntities":651,"label":652,"description":653,"key":32,"publicationTags":654,"standard":18},[],{"EN":29,"VI":29},{"EN":29,"VI":31},[34],{"impactFactor":19,"impactFactorByYear":656,"i10Index":40,"i10IndexLast5Year":19,"totalPublication":41,"totalPublicationByYear":657,"totalCitation":55,"totalCitationByYear":658,"totalCitationPerPublication":64,"totalCitationPerPublicationByYear":659,"hindexLast5Year":76,"hindex":76},{},{"1986":43,"1987":44,"1988":45,"1989":46,"1990":40,"1991":47,"1992":48,"1993":49,"1994":50,"1995":51,"1996":52,"1997":53,"1998":54},{"1989":43,"1990":57,"1991":54,"1992":58,"1993":59,"1994":60,"1995":61,"1996":62,"1997":63,"1998":43},{"1989":66,"1990":67,"1991":68,"1992":69,"1993":70,"1994":71,"1995":72,"1996":73,"1997":74,"1998":75},{"pages":661,"volume":663},{"VOID":662},"175-187",{"VOID":664},"25",{"total":19,"publishYear":666,"statisticByYear":667},1995,{},"1995-06-01","2026-07-11T08:34:38.822+00:00",[37],{"id":672,"createTime":673,"updateTime":674,"relativeEntities":675,"slug":676,"properties":677,"entityType":98,"verifyStatus":99,"verifyTime":686,"verifyNote":101,"languages":18,"translateLanguages":18,"viewCount":19,"primaryUrl":687,"fullTextUrl":18,"authors":688,"publicationType":202,"publisherRelationship":730,"citationCount":19,"citationInfo":755,"publishDate":758,"publishYear":756,"citationAnalyzeStatus":17,"lastCitationAnalyze":759,"indexDatabases":760,"openAccess":18,"references":761,"isForceReanalyzing":234},"b7846d92-42cb-40b1-807e-63cce0998254","2024-02-11T23:02:17.516+00:00","2026-05-20T10:58:46.923+00:00",[],"Myelin-proteins-in-aging-human-brain",{"abstract":678,"title":680,"gsPaper":682,"doi":684},{"EN":679},"Autopsy material of 13 persons who died between 70 and 89 yrs old and of patients who died between 27 and 44 yrs old was studied. White matter of temporal, parietal, and occipital lobes was investigated using histological and biochemical methods. According to results of neuropathological studies, the material of aged patients was divided into two subgroups: (a) brains with vascular changes only and (b) patients with senile atrophy of Alzheimer type. Chemical changes found in all studied brain lobes included a mild decrease in Wolfgram protein content with reciprocal increase in large basic protein content, together with a marked decrease in myelin yield. The abovementioned chemical changes were almost identical whether they were only vascular changes or whether senile atrophy of Alzheimer type was also present. It seems, therefore, that the degeneration of vessels is the decisive factor in the pathogenetic mechanism of myelin lesions in the aged brain.",{"EN":681},"Myelin proteins in aging human brain",{"VOID":683},"[\"14634571783051245466\"]",{"VOID":685},"10.1007\u002FBF03160993","2024-05-03T19:06:32.867+00:00","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002FBF03160993",[689,704,717],{"id":690,"sortIndex":19,"researcher":18,"roles":691,"affiliations":692,"properties":701,"displayName":703,"givenName":18,"familyName":18},"d8515b47-467d-4af0-8b06-00b36d796b9b",[107],[693],{"id":694,"sortIndex":19,"affiliation":695,"properties":18},"3230b8b5-8792-4f47-912c-d7192d1db6c6",{"id":694,"createTime":18,"updateTime":18,"relativeEntities":696,"slug":18,"properties":697,"entityType":18,"verifyStatus":18,"verifyTime":18,"verifyNote":18,"languages":18,"translateLanguages":18,"viewCount":18,"url":18,"parentIds":700,"statistic":18},[],{"title":698},{"VI":699},"Department of Neurology, School of Medicine, Poznań, Poland",[],{"title":702},{"VI":703},"Mieczysław Wender",{"id":705,"sortIndex":122,"researcher":18,"roles":706,"affiliations":707,"properties":714,"displayName":716,"givenName":18,"familyName":18},"fcb3e8e5-210b-4285-b0de-d1987476a865",[107],[708],{"id":694,"sortIndex":19,"affiliation":709,"properties":18},{"id":694,"createTime":18,"updateTime":18,"relativeEntities":710,"slug":18,"properties":711,"entityType":18,"verifyStatus":18,"verifyTime":18,"verifyNote":18,"languages":18,"translateLanguages":18,"viewCount":18,"url":18,"parentIds":713,"statistic":18},[],{"title":712},{"VI":699},[],{"title":715},{"VI":716},"Zofia Adamczewska-Goncerzewicz",{"id":718,"sortIndex":147,"researcher":18,"roles":719,"affiliations":720,"properties":727,"displayName":729,"givenName":18,"familyName":18},"20aa052b-c578-4cde-ac0f-bb15d3f65349",[107],[721],{"id":694,"sortIndex":19,"affiliation":722,"properties":18},{"id":694,"createTime":18,"updateTime":18,"relativeEntities":723,"slug":18,"properties":724,"entityType":18,"verifyStatus":18,"verifyTime":18,"verifyNote":18,"languages":18,"translateLanguages":18,"viewCount":18,"url":18,"parentIds":726,"statistic":18},[],{"title":725},{"VI":699},[],{"title":728},{"VI":729},"Jolanta Dorszewska",{"url":687,"publisher":731,"properties":750},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":732,"slug":10,"properties":733,"entityType":16,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"languages":18,"translateLanguages":18,"viewCount":19,"subjectFields":736,"manageAffiliations":737,"indexDatabases":738,"url":18,"thumbnailPath":18,"statistic":745,"gsStatistic":18,"type":18,"analyzePriority":18},[],{"issn":734,"title":735},{"VOID":13},{"EN":15},[],[],[739],{"id":24,"indexDatabase":740,"url":35,"indexYears":36,"academicFieldIds":18,"indexDatabaseRanking":37},{"id":26,"createTime":18,"updateTime":18,"relativeEntities":741,"label":742,"description":743,"key":32,"publicationTags":744,"standard":18},[],{"EN":29,"VI":29},{"EN":29,"VI":31},[34],{"impactFactor":19,"impactFactorByYear":746,"i10Index":40,"i10IndexLast5Year":19,"totalPublication":41,"totalPublicationByYear":747,"totalCitation":55,"totalCitationByYear":748,"totalCitationPerPublication":64,"totalCitationPerPublicationByYear":749,"hindexLast5Year":76,"hindex":76},{},{"1986":43,"1987":44,"1988":45,"1989":46,"1990":40,"1991":47,"1992":48,"1993":49,"1994":50,"1995":51,"1996":52,"1997":53,"1998":54},{"1989":43,"1990":57,"1991":54,"1992":58,"1993":59,"1994":60,"1995":61,"1996":62,"1997":63,"1998":43},{"1989":66,"1990":67,"1991":68,"1992":69,"1993":70,"1994":71,"1995":72,"1996":73,"1997":74,"1998":75},{"pages":751,"volume":753},{"VOID":752},"1-10",{"VOID":754},"14",{"total":19,"publishYear":756,"statisticByYear":757},1991,{},"1991-02-01","2026-05-20T10:58:46.922+00:00",[37],[762,765,771,774,777,783,786,789,792,795,798,801,804,807,810,816],{"id":18,"text":763,"url":18,"identifiers":764},"Agrawal H. (1974) Analysis of membrane proteins by sodium dodecyl-sulfate-polyacrylamide gel electrophoresis, inFundamentals of Lipids Chemistry, (Burton R.M. and Guerro BL.F., eds.), pp. 511–543, Science Publ. Div., Webster Groves, MO.",{},{"id":766,"text":767,"url":768,"identifiers":769},"4c68646b-0035-4279-8000-0006b275d4fa","Buee L., Laine A., Delacourte A., Flament S., and Kia-Ki Han (1989) Qualitative and quantitative comparison of brain proteins in Alzheimer’s disease.Biol. Chem. Hoppe-Seyler 370, 1229–1234.","https:\u002F\u002Flink.springer.com\u002F10.1007\u002Fs10440-022-00541-7",{"doi":770},"10.1007\u002Fs10440-022-00541-7",{"id":766,"text":772,"url":768,"identifiers":773},"Drummond R. and Dean G. (1980) Comparison of 2′,3′-cyclic nucleotide 3′-phosphodiesterase and the major component of Wolfgram protein W1.J. Neurochem. 35, 1155–1165.",{"doi":770},{"id":18,"text":775,"url":18,"identifiers":776},"England E. and Brun A. (1986) The white matter changes in senile dementia of Alzheimer type: Neuropathological and biochemical correlates.X Intern. Congr. Neuropathol. Abstracts, Stockholm, p. 291.",{},{"id":778,"text":779,"url":780,"identifiers":781},"5ad81604-a87b-4214-bfee-3e1526849509","Horrocks L. (1967) Composition of myelin from peripheral and central nervous system of the squirrel monkey.J. Lipid. Res. 8, 569–576.","https:\u002F\u002Fwww.sciencedirect.com\u002Fscience\u002Farticle\u002Fpii\u002FS0022227520388775",{"doi":782},"10.1016\u002Fs0022-2275(20)38877-5",{"id":18,"text":784,"url":18,"identifiers":785},"Horrocks L. (1973) Composition and metabolism of myelin phosphoglycerides during maturation and aging, inNeurobiological Aspects of Maturation and Aging, pp. 383–395, Elsevier, Amsterdam.",{},{"id":766,"text":787,"url":768,"identifiers":788},"Horrocks L. (1978) Pathway for hydrolysis of plasmalogens in brain.Adv. Exp. Med. Biol. 101, 393–406.",{"doi":770},{"id":18,"text":790,"url":18,"identifiers":791},"Horrocks L., Sun G., and D’Amato R. (1979) Changes of brain lipids during aging, inNeurobiology of Aging, (Ordy J. and K. Brizzee, eds.), pp. 359–368, Plenum, New York, London.",{},{"id":18,"text":793,"url":18,"identifiers":794},"Lees M. and Brostoff S. (1984) Proteins of myelin, inMyelin (Morell P., ed.), pp. 197–224, Plenum, New York, London.",{},{"id":18,"text":796,"url":18,"identifiers":797},"Mann D. and Yates P. (1986) Neurotransmitter deficits in Alzheimer’s disease and in other dementing disorders.Human Neurobiol. 5, 147–158.",{},{"id":18,"text":799,"url":18,"identifiers":800},"Norton W. and Cammer W. (1984) Proteins of myelin, inMyelin (Morell P, ed.), pp. 147–195, Plenum, New York, London.",{},{"id":18,"text":802,"url":18,"identifiers":803},"Norton W. and Poduslo S. (1973) Myelination in rat brains: Method of myelin isolation.J. Neurochem. 21, 749–758.",{},{"id":18,"text":805,"url":18,"identifiers":806},"Rossor M. and Iversen L. (1986) Non-cholinergic abnormalities in Alzheimer’s disease.Br. Med. Bull. 42, 70–74.",{},{"id":766,"text":808,"url":768,"identifiers":809},"Sprinkle T., Wells M., Garver F., and Smith D. (1980) Studies on the Wolfgram high molecular weight CNS myelin proteins. Relationship to 2′,3′-cyclic nucleotide 3′phosphodiesterase.J. Neurochem. 35 1200–1208.",{"doi":770},{"id":811,"text":812,"url":813,"identifiers":814},"56f52aa2-d212-4b63-b030-add35988dd85","Wender M., Adamczewska-Goncerzewicz Z., Szoczech J., and Godlewski A. (1988) Myelin lipids in aging human brain.Neurochem. Pathol. 8, 121–130.","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002FBF03160140",{"doi":815},"10.1007\u002FBF03160140",{"id":817,"text":818,"url":819,"identifiers":820},"7d52a701-081d-486c-83b7-04064b9e7886","Wiśniewski H. (1990) Alzheimer disease: A brain specific form of amyloidosis.Conference of Pol. Neuropathol. Soc. Kraków, p. 5.","http:\u002F\u002Flink.springer.com\u002F10.1007\u002FBF02312187",{"doi":821},"10.1007\u002Fbf02312187",{"id":823,"createTime":824,"updateTime":825,"relativeEntities":826,"slug":827,"properties":828,"entityType":98,"verifyStatus":99,"verifyTime":839,"verifyNote":101,"languages":18,"translateLanguages":18,"viewCount":19,"primaryUrl":840,"fullTextUrl":18,"authors":841,"publicationType":202,"publisherRelationship":870,"citationCount":18,"citationInfo":18,"publishDate":895,"publishYear":896,"citationAnalyzeStatus":897,"lastCitationAnalyze":898,"indexDatabases":899,"openAccess":18,"references":18,"isForceReanalyzing":234},"90d93862-ad90-4b84-80db-4ef1dd4c896d","2024-01-11T09:44:17.395+00:00","2026-03-09T15:56:56.208+00:00",[],"Prevention-of-delayed-neuronal-death-in-gerbil-hippocampus-by-a-novel-vinca-alkaloid-derivative-Vinconate-",{"abstract":829,"title":831,"gsPaper":833,"references":835,"doi":837},{"EN":830},"We investigated the effect of vinconate, a novel vinca alkaloid derivative, on delayed neuronal death using Mongolian gerbils. The animals were allowed to survive for 7 d after 3 or 5 min of forebrain ischemia induced by bilateral occlusion of the common carotid arteries. Morphological changes and calcium (45Ca) accumulation were evaluated in the CA1 sector of the hippocampus after ischemia. Vinconate (50, 100, and 300 mg\u002Fkg) showed protective effects against neuronal death in a dose-dependent manner when administered intraperitoneally (ip) 10 min before 5 min of ischemia. However, the administration of vinconate (100 and 300 mg\u002Fkg, ip) immediately after 5 min of ischemia showed no therapeutic effect, whereas a marked therapeutic effect of vinconate (50 and 100 mg\u002Fkg, ip) was observed when administered immediately after 3 min of ischemia. An anesthetic dose of pentobarbital (40 mg\u002Fkg, ip) also produced significant protection against neuronal death. Furthermore, a45Ca autoradiographic study indicated that a marked calcium accumulation was found in the CA1 sector at 7 d after 5 min of ischemia, which was consistent with the extent of histological neuronal damage. When vinconate (100 and 300 mg\u002Fkg, ip) was administered 10 min before 5 min of ischemia, the abnormal calcium accumulation was not detected in the CA1 sector. These data indicate that suppression of abnormal neuronal activity may be owing to the antagonistic action of vinconate on calcium accumulation.",{"EN":832},"Prevention of delayed neuronal death in gerbil hippocampus by a novel vinca alkaloid derivative (Vinconate)",{"VOID":834},"[]",{"VOID":836},"Alps B. J., Calder C., Hass W. K., and Wilson A. D. (1988) Comparative protective effects of nicardipine, flunarizine, lidoflazine and nimodipine against ischaemic injury in the hippocampus of the Mongolian gerbils.Br. J. Pharmacol. 93, 877–883.\nBenveniste H., Drejer J., Schousboe A., and Diemer N. H. (1984) Elevation of the extracellular concentrations of glutamate and aspartate in rat hippocampus during transient cerebral ischemia monitored by intracerebral microdialysis.J. Neurochem. 43, 1369–1374.\nCaravaggi A. M., Sardi A., Baldoli E., Di Francesco G. F., and Luca C. (1977) Hemodynamic profile of a new cerebral vasodilator, vincamine and of one of its derivatives, apovincaminic acid ethylester (RGH-4405)(1).Arch. Int. Pharmacodyn. 226, 139–148.\nCotman C. W., Monaghan D. T., Ottersen O. P., and Storm-Mathisen J (1987) Anatomical organization of excitatory amino acid receptors and their pathways.Trend. Neurosci. 10, 273–280.\nDeshpande J. K. and Wieloch T. (1985) Amelioration of ischaemic brain damage by postischaemic treatment with flunarizine.Neurol. Res. 7, 27–29.\nDeshpande J. K., Siesjö B. K., and Wieloch T. (1987) Calcium accumulation and neuronal damage in the rat hippocampus following cerebral ischemia.J. Cereb. Blood Flow Metab. 7, 89–95.\nDienel G. A. (1984) Regional accumulation of calcium in postischemic rat brain.J. Neurochem. 43, 913–925.\nGill R., Foster A. C., and Woodruff G. N. (1988) MK-801 is neuroprotective in gerbils when administered during the post-ischaemic period.Neuroscience 25, 847–855.\nIzumiyama K. and Kogure K. (1988) Prevention of delayed neuronal death in gerbil hippocampus by ion channel blockers.Stroke 19, 1003–1007.\nJohansen F. F., Jorgensen M. B., and Diemer N. H. (1986) Ischemic CA-1 pyramidal cell loss is prevented by preischemic colchicine destruction of dentate gyrus granule cells.Brain Res. 377, 344–347.\nJorgensen M. B., Johansen, F. F., and Diemer N. H. (1987) Removal of the entorhinal cortex protects hippocampal CA-1 neurons from ischemic damage.Acta Neuropathol. (Berlin)73, 189–194.\nKárpáti E. and Szporny L. (1976) General and cerebral haemodynamic activity of ethyl apovicaminate.Arzneim-Forsch 26, 1908–1912.\nKatsuragi T., Ohba M., Mori R., Kushiku K., and Furukawa T. (1984) Calcium antagonistic action involved in vasodilation by brovincamine.Gen. Pharmac. 15, 43–45.\nKing G. A. (1987) Protective effects of vinpocetine and structurally related drugs on the lethal consequences of hypoxia in mice.Arch. Int. Pharmacodyn. 286, 299–307.\nKirino T. (1982) Delayed neuronal death in the gerbil hippocampus following ischemia.Brain Res. 239, 57–69.\nKirino T. and Sano K. (1984a) Sefective vulnerability in the gerbil hippocampus following transient ischemia.Acta Neuropathol. (Berlin)62, 201–208.\nKirino T., Tamura A., and Sano K. (1986) A reversible type of neuronal injury following ischemia in the gerbil hippocampus.Stroke 17, 455–459.\nMayo B. C., Biggs S. R., Hawkins D. R., Chasseaud L. F., Darragh A., Baldock G. A., and Whitby B. R. (1982) The metabolic fate of 11-bromo-[15-3H] vincamine in rats, dogs and humans.J. Pharm. Dyn. 5, 951–964.\nMizon J. P., Gentit T., and Billecocq G. (1971) Les anemies refractaires sideroblastiques.Lille Med. 16, 1427–1429.\nNedergaard M. (1988) Mechanisms of brain damage in focal cerebral ischemia.Acta Neurol. Scand. 77, 81–101.\nOnodera H., Sato G., and Kogure K. (1986) Lesions to Schaffer collaterals prevent ischemic death of CA1 pyramidal cells.Neurosci. Lett. 68, 169–174.\nOlpe H. R., Barrionuevo G., and Lynch G. (1982) Vincamine: A psychogeriatric agent blocking synaptic potentiation in hippocampus.Life Science 31, 1947–1953.\nPulsinelli W. A., Brierley J. B., and Plum F. (1982) Temporal profile of neuronal damage in a model of transient forebrain ischemia.Ann. Neurol. 11, 491–498.\nRothman S. M. and Olney J. W. (1986) Glutamate and the pathophysiology of hypoxic-ischemic brain damage.Ann. Neurol. 19, 105–111.\nRudolphi K. A., Keil M., and Hinze H. J. (1987) Effect of theophylline on ischemically induced hippocampal damage in mongolian gerbils. A behavioral and histopathological study.J. Cereb. Blood Flow Metab. 7, 74–81.\nSaletu B., Grunberger J., Linzmayer L., and Wittek, R. (1984) Classification and determination of pharmacodynamics of a new antihypoxidotic drug, vinconate, by pharmaco-EEG and psychometry.Arch. Gerontol. Geriatr. 3, 127–146.\nSakamoto N., Kogure K., Kato H., and Ohtomo H. (1985) Disturbed Ca2+ homeostasis in the gerbil hippocampus following brief transient ischemia.Brain Res. 364, 372–376.\nSiesjö B. K. (1981) Cell damage in the brain: a speculative synthesis.J. Cereb. Blood Flow Metab. 1, 155–185.\nSimon R. P., Swan J. H., Griffiths T., and Meldrum B. S. (1984) Blockade ofN-methyl-D-aspartate receptor may protect against ischemic damage in the brain.Science 226, 850–852.\nSuzuki R., Yamaguchi T., Li C.-L., and Klatzo, I. (1983) The effects of 5-min ischemia in mongolian gerbils. Changes of spontaneous neuronal activity in cerebral cortex and CA1 sector of hippocampus.Acta Neuropathol. (Berlin)60, 217–222.\nSzobor A. and Klein M. (1976) Ethyl apovincaminate therapy in neurovascular diseases.Arzneim-Forsch 26, 1984–1989.\nThiebauld C., Van Mullem J., Lintermans J., and Sprumont P. (1983) Testing in a hypobaric chamber drugs claimed to improve impaired brain functions.Lancet 2, 225, 226.\nVereczkey L., Zolyomi G., and Szporny L. (1976) Pharmacokinetic data on tritium labelled ethyl apovincaminate.Arzneim-Forsch 26, 1929–1933.\nWieloch T., Lindvall O., Blomqvist P., and Gage F. (1985) Evidence for amelioration of ischemic damage in the hippocampal formation by lesions of the perforant path.Neurol. Res. 7, 24–26.\nZola-Morgan S., Squire L. R., and Amaral G. (1986) Human amnesia and the medial temporal region: enduring memory impairment following a bilateral lesion limited to field CA1 sector of the hippocampus.J. 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USA 73, 2043–2046.",{"doi":1157},"10.1073\u002Fpnas.73.6.2043",{"id":18,"text":1159,"url":18,"identifiers":1160},"Litwin J. A. and Beier K. (1988) Immunogold localization of peroxisomal enzymes in Epon-embedded liver tissue.Histochemistry 88, 193–196.",{"doi":1161},"10.1007\u002FBF00493304",{"id":18,"text":1163,"url":18,"identifiers":1164},"Litwin J. A., Völkl A., Müller-Höcker J., Hashimoto T., and Fahimi H. D. (1987) Immunohistochemical localization of peroxisomal enzymes in human liver biopsies.Am. J. Pathol. 128, 141–150.",{},{"id":18,"text":1166,"url":18,"identifiers":1167},"Litwin J. A., Völk A., Stachura J., and Fahimi H. D. (1988) Detection of peroxisomes in human liver and kidney fixed in formalin and embedded in paraffin: the use of catalase and lipid β-oxidation enzymes as immunocytochemical markers.Histochem. J. 20, 165–173.",{"doi":1168},"10.1007\u002FBF01746680",{"id":18,"text":1170,"url":18,"identifiers":1171},"Master C. and Holmes R. (1977) Peroxisomes: new aspects of cell physiology and biochemistry.Physiol. Rev. 57, 816–882.",{"doi":1172},"10.1152\u002Fphysrev.1977.57.4.816",{"id":18,"text":1174,"url":18,"identifiers":1175},"Miyazawa S., Osumi T., and Hashimoto T. (1980) The presence of a new 3-ketoacyl-CoA thiolase in rat liver peroxisomes.Eur. J. Biochem. 103, 589–596.",{"doi":1176},"10.1111\u002Fj.1432-1033.1980.tb05984.x",{"id":18,"text":1178,"url":18,"identifiers":1179},"Moser H. W. (1988) The peroxisome: Nervous system role of a previously underrated organelle, the 1987 Robert Wartenberg Lecture.Neurology 38, 1617–1627.",{"doi":1180},"10.1212\u002FWNL.38.10.1617",{"id":18,"text":1182,"url":18,"identifiers":1183},"Novikoff A. B. and Goldfischer S. (1969) Visualization of peroxisomes (microbodies) and mitochondria with diaminobenzidine.J. Histochem. Cytochem. 17, 675–680.",{"doi":1184},"10.1177\u002F17.10.675",{"id":18,"text":1186,"url":18,"identifiers":1187},"Novikoff A. B., Novikoff P. M., Davis C., and Quintana N. (1972) Studies on microperoxisomes II. A cytochemical method for light and electron microscopy.J. Histochem. Cytochem. 20, 1006–1023.",{"doi":1188},"10.1177\u002F20.12.1006",{"id":18,"text":1190,"url":18,"identifiers":1191},"Osumi T. and Hashimoto T. (1980) Acyl-CoA oxidase for rat liver: a new enzyme for fatty acid oxidation.J. Biochem. 87, 1735–1746.",{"doi":1192},"10.1093\u002Foxfordjournals.jbchem.a132918",{"id":18,"text":1194,"url":18,"identifiers":1195},"Poll-The B. T., Roels F., Ogier H., Scott J., Vamecq J., Schutgens R. B. H., Wanders R. J. A., van Roermund C. W. T., van Wijland M. J. A., Schram A. W., Tager J. M., and Saudubray J. M. (1988) A new peroxisomal disorder with enlarged peroxisomes and a specific deficiency of acyl-CoA oxidase (pseudo-neonatal adrenoleukodystrophy).Am. J. Hum. Genet. 42, 422–434.",{},{"id":18,"text":1197,"url":18,"identifiers":1198},"Rhodin J. (1954) Correlation of ultrastructural organization and function in normal and experimentally changed proximal convoluted tubule cells of the human kidney, Ph. D thesis.Aktiebolaget Godvil, Stockholm. p. 76.",{},{"id":18,"text":1200,"url":18,"identifiers":1201},"Roels F., Cornelis A., Poll-The B. T., Aubourg P., Ogier H., Scott J., and Saudubray J. M. (1986) Hepatic peroxisomes are deficient in infantile Refsum disease: a cytochemical study of 4 cases.Amer. J. Med. Genet. 25, 257–271.",{"doi":1202},"10.1002\u002Fajmg.1320250210",{"id":18,"text":1204,"url":18,"identifiers":1205},"Schram A. W., Goldfischer S., van Roermund C. W. T., Brouwer-Kelder E. M., Collins J., Hashimoto T., Heymans, H. S. A, van den Bosch H., Schutgens R. B. H., Tager J. M., and Wanders R. J. A. (1987) Human peroxisomal 3-oxoacyl-CoA thiolase deficiency.Proc. Natl. Acad. Sci. USA 84, 2494–2496.",{"doi":1206},"10.1073\u002Fpnas.84.8.2494",{"id":18,"text":1208,"url":18,"identifiers":1209},"Shimozawa N., Suzuki Y., Orii T., Yokota S., and Hashimoto T. (1988) Biochemical and morphologic aspects of peroxisomes in the human rectal mucosa: diagnosis of Zellweger syndrome simplified by rectal biopsy.Pediatr. Res. 24, 723–727.",{"doi":1210},"10.1203\u002F00006450-198812000-00015",{"id":18,"text":1212,"url":18,"identifiers":1213},"Takashima S. and Becker L. E. (1983) Developmental changes of glial fibrillary acidic protein in cerebral white matter.Arch. Neurol. 40, 14–18.",{"doi":1214},"10.1001\u002Farchneur.1983.04050010034008",{"id":18,"text":1216,"url":18,"identifiers":1217},"Takashima S., Chan F., Becker L. E., Houdou S., and Suzuki Y. (1991) Cortical cytoarchitectural and immunohistochemical studies on Zellweger syndrome.Brain Dev. 13, 158–162.",{"doi":1218},"10.1016\u002FS0387-7604(12)80022-2",{"id":18,"text":1220,"url":18,"identifiers":1221},"Volpe J. J. and Adamus R. D. (1972) Cerebro-hepatorenal syndrome of Zellweger: an inherited disorder of neuronal migration.Acta Neuropathol. 20, 175–198.",{"doi":1222},"10.1007\u002FBF00686900",{"id":1224,"createTime":1225,"updateTime":1226,"relativeEntities":1227,"slug":1228,"properties":1229,"entityType":98,"verifyStatus":99,"verifyTime":1226,"verifyNote":101,"languages":18,"translateLanguages":18,"viewCount":19,"primaryUrl":1238,"fullTextUrl":18,"authors":1239,"publicationType":202,"publisherRelationship":1270,"citationCount":18,"citationInfo":18,"publishDate":1295,"publishYear":349,"citationAnalyzeStatus":17,"lastCitationAnalyze":18,"indexDatabases":1296,"openAccess":18,"references":18,"isForceReanalyzing":234},"62bfd944-b029-4596-b525-6b847631985b","2024-01-11T05:46:46.405+00:00","2025-02-26T17:18:27.814+00:00",[],"Laser-doppler-flowmetry",{"abstract":1230,"title":1232,"references":1234,"doi":1236},{"EN":1231},"Laser-Doppler flowmetry is a new technique for noninvasive and continuous measurement of local microcirculatory cerebral and spinal-cord blood flow. The flow estimate by this technique is based on the assessment of the Doppler shift of low-power laser light, which is scattered by moving red blood cells. Laser-Doppler flowmetry has been validated for various organs, including the central nervous system. These studies revealed a linear relationship between relative changes of the Doppler signal and blood flow over a wide range of pharmacological as well as pathological flow alterations, including cerebral ischemia. The usefulness of laser-Doppler flowmetry in experimental as well as clinical applications has received growing attention. The superiority of the technique lies in its high spatial and temporal resolution. Disadvantages are the difficulty of obtaining absolute flow values and the sensitivity to artifacts. The versatility and on-line capacity of laser-Doppler flowmetry might allow new insights into the pathophysiology of alterations of the cerebral and spinal-cord microcirculation.",{"EN":1233},"Laser-doppler flowmetry",{"VOID":1235},"Ahn H., Lindhagen J., Nilsson G. E., Salerud E. G., Jodal M., and Lundgren O. (1985) Evaluation of laser Doppler flowmetry in the assessment of intestinal blood flow in cat.Gastroenterology 88, 951–957.\nArbit E., DiResta G. R., Bedford R. F., Shah N. K., and Galicich J. H. (1989) Intraoperative measurement of cerebral and tumor blood flow with laser-Dopper flowmetry.Neurosurgery 24, 166–170.\nBonner R. and Nossal R. (1988) Model for laser Doppler measurements of blood flow in tissue. Appl. Optics20, 2097–2107.\nBonner R. F., Clem T. R., Bowen P. D., and Bowman R. L. (1988) Laser-Doppler continuous real-time monitor of pulsatile and mean blood flow in tissue microcirculation,Scattering Techniques Applied to Supramolecular and Non Equilibrium Systems (Chen S. H., Chu B., and Nossal R., eds.) pp. 685–702, Plenum, New York.\nChen R. Y. Z., Fan F.-C., Schuessler G. B., Usami S., and Chien S. (1983) Effects of sphere size and injection site on regional cerebral blood flow measurements.Stroke 14, 769–776.\nChen S. T., Hsu C. Y., Hogan E. L., Mariq H., and Balentine J. D. (1986) A model of focal ischemic stroke in the rat: Reproducible extensive cortical infarction.Stroke 17, 738–743.\nDiResta G. R., Kiel J. W., Riedel G. L., Kaplan P., and Sheperd A. P. (1987) Hybrid blood flow probe for simultaneous H2 clearance and laser-Doppler velocimetry.Am. J. Physiol. 253, G573-G581.\nDirnagl U., Kaplan B., Jacewicz M., and Pulsinelli W. (1989) Continuous measurement of cerebral cortical blood flow by laser-doppler flowmetry in a rat stroke model.J. Cereb. Blood Flow Metab. 9, 589–596.\nEyre J. A., Essex T. J. H., Flecknell P. A., Bartholomew P. H., and Sinclair J. I. (1988) A comparison of measurements of cerebral blood flow in the rabbit using laser Doppler spectroscopy and radionuclide labelled microspheres.Clin. Phys. Physiol. Meas. 9, 65–74.\nFasano V. A., Urciuoli R., Bolognese P., and Mostert M. (1988) Intraoperative use of laser-Doppler in the study of cerebral microvascular circulation.Acta Neurochir. 95, 40–48.\nFrerichs K. U., Lindsberg P. J., Hallenbeck J. M., and Feuerstein G. Z. Platelet-activating factor and progressive brain damage following focal brain injury.J. Neurosurg. (in press).\nHaberl R. L., Heizer M. L., Marmarou A., and Ellis E. F. (1989a) Laser-Doppler assessment of brain microcirculation: Effect of systemic alterations.Am. J. Physiol. 256, H1247-H1254.\nHaberl R. L., Heizer M. L., and Ellis E. F. (1989b) Laser-Doppler assessment of brain microcirculation: Effect of local alterations.Am. J. Physiol. 256, H1255-H1260.\nHalsey J. H., Capra N. F., and McFarland R. S. (1977) Use of hydrogen for measurement of regional cerebral blood flow. Problem of intercompartmental diffusion.Stroke 8, 351–357.\nHolloway G. A. and Watkins D. W. (1977) Laser-Doppler measurement of cutaneous blood flow.J. Invest. Dermatol. 69, 306–309.\nLacombe P., Meric P., and Seylaz J. (1980) Validity of cerebral blood flow measurements obtained with quantitative tracer technique.Brain Res. Rev. 2, 105–169.\nLindsberg P. J., O’Neill J. T., Paakkari I. A., Hallenbeck J. M., and Feuerstein G. (1989) Validation of laser-Doppler flowmetry in measurement of spinal cord blood flow.Am. J. Physiol. 257, H674-H680.\nNilsson G. E., Tenland T., and Oberg P. A. (1980) Evaluation of a laser Doppler flowmeter for measurement of tissue blood flow.IEEE Trans. Biomed. Eng. BME-27, 597–604.\nRiva C., Ross B., and Benedek G. B. (1972) Laser Doppler measurements of blood flow in capillary tubes and retinal arteries.Invest. Opthalmol. 11, 936–944.\nRosenblum B. R., Bonner R. F., and Oldfield E. H. (1987) Intraoperative measurement of cortical blood flow adjacent to cerebral AVM using laser Doppler velocimetry.J. Neurosurg. 66, 369–399.\nSakurada O., Kennedy C., Jehle J., Brown J. D., Carbin G. L. and Sokoloff L. (1978) Measurement of local cerebral blood flow with iodo[14C]antipyrine.Am. J. Physiol. 234, H59-H66.\nSheperd A. P. and Riedel G. L. (1982) Continuous measurement of intestinal mucosal blood flow by laser-Doppler velocimetry.Am. J. Physiol. 242, G668-G672.\nSkarphedinsson J. O., Hårding H., and Thoreń P. (1988) Repeated measurements of cerebral blood flow in rats. Comparisons between the hydrogen clearance method and laser Doppler flowmetry.Acta Physiol. Scand. 134, 133–142.\nSkarphedinsson J. O., Sandberg M., Hagberg H., Carlsson S., and Thoreń P. (1989a) Relative cerebral ischemia in SHR due to hypotensive hemorrhage: Cerebral function, blood flow and extracellular levels of lactate and purine catabolites.J. Cereb. Blood Flow Metab. 9, 364–372.\nSkarphedinsson J. O., Delle M., Hoffmann P., and Thoreń P. (1989b) The effects of naloxone on cerebral blood flow and cerebral function during relative cerebral ischemia.J. Cereb. Blood Flow Metab. 9, 515–522.\nStern M. D., Lappe D. L., Bowen P. D., Chimosky J. E., Holloway G. A., Keiser H. R., and Bowman R. L. (1977) Continuous measurement of tissue blood flow by laser-Doppler spectroscopy.Am. J. Physiol. 232, H441-H448.\nTamura A., Graham D. I., McGulloch J., and Teasdale G. M. (1981) Focal cerebral ischaemia in the rat: 2. Regional cerebral blood flow determined by [14C]iodoantipyrine autoradiography following middle cerebral artery occlusion.J. Cereb. Blood Flow Metab. 1, 61–69.\nTomida S., Wagner H. G., Klatzo I., and Nowak T. S. (1989) Effect of acute electrode placement on regional CBF in the gerbil: A comparison of blood flow measured by hydrogen clearance, [3H]nicotine, and [14C]iodoantipyrine techniques.J. Cereb. Blood Flow Metab. 9, 79–86.\nYoung W. (1980) H2 clearance measurement of blood flow: A review of techniques and polarographic principles.Stroke 11, 552–564.",{"VOID":1237},"10.1007\u002FBF03160057","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002FBF03160057",[1240,1255],{"id":1241,"sortIndex":19,"researcher":18,"roles":1242,"affiliations":1243,"properties":1252,"displayName":1254,"givenName":18,"familyName":18},"7a067ea5-6660-4253-ab8b-da686551984b",[107],[1244],{"id":1245,"sortIndex":19,"affiliation":1246,"properties":18},"9e44be5d-3c7a-468e-92ac-3a3c66adc015",{"id":1245,"createTime":18,"updateTime":18,"relativeEntities":1247,"slug":18,"properties":1248,"entityType":18,"verifyStatus":18,"verifyTime":18,"verifyNote":18,"languages":18,"translateLanguages":18,"viewCount":18,"url":18,"parentIds":1251,"statistic":18},[],{"title":1249},{"VI":1250},"Department of Neurology, USUHS, F. Edward Hébert School of Medicine, Bethesda",[],{"title":1253},{"VI":1254},"Kai U. Frerichs",{"id":1256,"sortIndex":122,"researcher":18,"roles":1257,"affiliations":1258,"properties":1267,"displayName":1269,"givenName":18,"familyName":18},"8cfa3ca7-cd00-4106-8bda-94eed1b3d21e",[107],[1259],{"id":1260,"sortIndex":19,"affiliation":1261,"properties":18},"17e1fd39-4d59-48f8-a301-55924d126c61",{"id":1260,"createTime":18,"updateTime":18,"relativeEntities":1262,"slug":18,"properties":1263,"entityType":18,"verifyStatus":18,"verifyTime":18,"verifyNote":18,"languages":18,"translateLanguages":18,"viewCount":18,"url":18,"parentIds":1266,"statistic":18},[],{"title":1264},{"VI":1265},"Department of Pharmacology, Smith, Kline and French Research and Development, King of Prussia",[],{"title":1268},{"VI":1269},"Giora Z. Feuerstein",{"url":1238,"publisher":1271,"properties":1290},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":1272,"slug":10,"properties":1273,"entityType":16,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"languages":18,"translateLanguages":18,"viewCount":19,"subjectFields":1276,"manageAffiliations":1277,"indexDatabases":1278,"url":18,"thumbnailPath":18,"statistic":1285,"gsStatistic":18,"type":18,"analyzePriority":18},[],{"issn":1274,"title":1275},{"VOID":13},{"EN":15},[],[],[1279],{"id":24,"indexDatabase":1280,"url":35,"indexYears":36,"academicFieldIds":18,"indexDatabaseRanking":37},{"id":26,"createTime":18,"updateTime":18,"relativeEntities":1281,"label":1282,"description":1283,"key":32,"publicationTags":1284,"standard":18},[],{"EN":29,"VI":29},{"EN":29,"VI":31},[34],{"impactFactor":19,"impactFactorByYear":1286,"i10Index":40,"i10IndexLast5Year":19,"totalPublication":41,"totalPublicationByYear":1287,"totalCitation":55,"totalCitationByYear":1288,"totalCitationPerPublication":64,"totalCitationPerPublicationByYear":1289,"hindexLast5Year":76,"hindex":76},{},{"1986":43,"1987":44,"1988":45,"1989":46,"1990":40,"1991":47,"1992":48,"1993":49,"1994":50,"1995":51,"1996":52,"1997":53,"1998":54},{"1989":43,"1990":57,"1991":54,"1992":58,"1993":59,"1994":60,"1995":61,"1996":62,"1997":63,"1998":43},{"1989":66,"1990":67,"1991":68,"1992":69,"1993":70,"1994":71,"1995":72,"1996":73,"1997":74,"1998":75},{"pages":1291,"volume":1293},{"VOID":1292},"55-70",{"VOID":1294},"12","1990-01-01",[37]]