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Proc Nat Acad Sci USA 100:1799–1802\nAmdam GV, Simoes ZLP, Guidugli KR, Norberg K, Omholt SW (2003b) Disruption of vitellogenin gene function in adult honeybees by intra-abdominal injection of double stranded RNA. BMC Biotechnol 3:1–8\nAmdam GV, Norberg K, Fondrk MK, Page RE (2004a) Reproductive ground plan may mediate colony-level selection effects on individual foraging behavior in honey bees. Proc Nat Acad Sci USA 101:11350–11355\nAmdam GV, Simoes ZLP, Hagen A, Norberg K, Schroder K, Mikkelsen O, Kirkwood TBL, Omholt SW (2004b) Hormonal control of the yolk precursor vitellogenin regulates immune function and longevity in honeybees. Exp Gerontol 39:767–773\nAmdam GV, Norberg K, Omholt SW, Kryger P, Lourenco AP, Bitondi MMG, Simoes ZLP (2005) Higher vitellogenin concentrations in honey bee workers may be an adaptation to life in temperate climates. Ins Soc 52:316–319\nAmdam GV, Csondes A, Fondrk MK, Page RE (2006a) Complex social behavior derived from maternal reproductive traits. Nature 439:76–78\nAmdam GV, Norberg K, Page RE, Erber J, Scheiner R (2006b) Downregulation of vitellogenin gene activity increases the gustatory responsiveness of honey bee workers (Apis mellifera). Behav Brain Res 169:201–205\nButler CG, Fairey EM (1963) The role of the queen in preventing oogenesis in worker honey bees. J Apic Res 2:14–18\nCapella ICS, Hartfelder K (1998) Juvenile hormone effect on DNA synthesis and apoptosis in caste-specific differentiation of the larval honey bee (Apis mellifera L.) ovary. J Insect Physiol 44:385–391\nCorona M, Velarde RA, Remolina S, Moran-Lauter A, Wang Y, Hughes KA, Robinson GE (2007) Vitellogenin, juvenile hormone, insulin signaling, and queen honey bee longevity. Proc Natl Acad Scie USA 104:7128–7133\nDade HA (1977) Anatomy and dissection of the honeybee. International Bee Research Association, London\nEvans JD, Shearman DCA, Oldroyd BP (2004) Molecular basis of sex determination in haplodiploids. TREE 19:1–3\nFree JB (1987) Pheromones of social bees. Chapman and Hall, London\nGuidugli KR, Nascimento AM, Amdam GV, Barchuk AR, Omholt SW et al (2005) Vitellogenin regulates hormonal dynamics in the worker caste of a eusocial insect. FEBS Lett 579:4961–4965\nHartfelder K, Engels W (1998) Social insect polymorphism: hormonal regulation of plasticity in development and reproduction in the honeybee. Curr Top Dev Biol 40:45–77\nHartfelder K, Steinbruck G (1997) Germ cell cluster formation and cell death are alternatives in caste specific differentiation of the larval honey bee ovary. Invertebr Reprod Dev 31:237–250\nHoover SER, Keeling CI, Winston ML, Slessor KN (2003) The effect of queen pheromones on worker honey bee ovary development. Naturwissenschaften 90:477–480\nJay SC (1968) Factors influencing ovary development of worker honeybees under natural conditions. 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Ann Rev Entomol 47:535–559\nOldroyd BP, Osborne KE (1999) The evolution of worker sterility in honeybees: the genetic basis of failure of worker policing. Proc R Soc Lond Ser B Biol Sci 266:1335–1339\nPage RE, Erickson EH (1988) Reproduction by worker honey bees (Apis mellifera L). Behav Ecol Sociobiol 23:117–126\nRobinson GE, Page RE, Fondrk MK (1990) Intracolonial behavioral variation in worker oviposition, oophagy, and larval care in queenless honey bee colonies. Behav Ecol Sociobiol 26:315–323\nSeehuus S-C, Norberg K, Gimsa U, Krekling T, Amdam GV (2006) Reproductive protein protects functionally sterile honey bee workers from oxidative stress. Proc Natl Acad Sci USA 103:962–967\nSeehuus S-C, Norberg K, Krekling T, Fondrk K, Amdam GV (2007) Immunogold localization of vitellogenin in the ovaries, hypopharyngeal glands and head fat bodies of honeybee workers, Apis mellifera. J Insect Sci 7:52\nTarpy DR, Nielsen DI (2002) Sampling error, effective paternity and estimating the genetic structure of honey bee colonies (Hymenoptera: Apidae). Ann Entomol Soc Am 95:513–528\nThompson GJ, Kucharski R, Maleszka R, Oldroyd BP (2006) Towards a molecular definition of worker sterility: differential gene expression and reproductive plasticity in honey bees. Insect Mol Biol 15(5):637–644\nThompson GJ, Yockey H, Lim J, Oldroyd BP (2007) Experimental manipulation of ovary activation and gene expression in honey bee (Apis mellifera) queens and workers: testing hypotheses of reproductive regulation. J Exp Zool 307A:1–11\nVisscher PK (1989) A quantitative study of worker reproduction in honey bee colonies. Behav Ecol Sociobiol 25:247–254",{"EN":149},"Expression of Vitellogenin and Transferrin in Activated Ovaries of Worker Honey Bees, Apis mellifera",{"VOID":151},"10.1007\u002Fs10528-008-9202-6","PUBLICATION","VERIFIED","Auto Verify","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002Fs10528-008-9202-6",[157,176],{"id":158,"sortIndex":159,"researcher":22,"roles":160,"affiliations":162,"properties":173},"0931e0b3-9611-4be1-971f-4f98382bbeb7",1,[161],"AUTHOR",[163],{"id":22,"sortIndex":23,"affiliation":164,"properties":22},{"id":165,"createTime":166,"updateTime":167,"relativeEntities":168,"slug":169,"properties":170,"entityType":75,"verifyStatus":21,"verifyTime":22,"verifyNote":22,"syncStatus":21,"languages":22,"translateLanguages":22,"viewCount":23},"0a114970-dc54-4d11-afdb-eff1bb834d5d","2024-04-11T09:00:05.876+00:00","2025-06-11T22:59:24.866+00:00",[],"Department-of-Biochemistry-Faculty-of-Science-Chulalongkorn-University-Bangkok-Thailand",{"title":171},{"EN":172},"Department of Biochemistry, Faculty of Science, Chulalongkorn University, Bangkok, Thailand",{"title":174},{"VI":175},"Siriporn Sittipraneed",{"id":177,"sortIndex":23,"researcher":22,"roles":178,"affiliations":179,"properties":185},"ae43c0c9-937b-4dbf-95ed-33f27bc6f6dd",[161],[180],{"id":22,"sortIndex":23,"affiliation":181,"properties":22},{"id":165,"createTime":166,"updateTime":167,"relativeEntities":182,"slug":169,"properties":183,"entityType":75,"verifyStatus":21,"verifyTime":22,"verifyNote":22,"syncStatus":21,"languages":22,"translateLanguages":22,"viewCount":23},[],{"title":184},{"EN":172},{"title":186},{"VI":187},"Preeyada Koywiwattrakul","ARTICLE",{"url":155,"publisher":190,"properties":214},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":191,"slug":10,"properties":192,"entityType":20,"verifyStatus":21,"verifyTime":22,"verifyNote":22,"syncStatus":21,"languages":22,"translateLanguages":22,"viewCount":23,"subjectFields":197,"manageAffiliations":198,"indexDatabases":199,"url":22,"thumbnailPath":22,"statistic":22,"gsStatistic":22,"type":134,"analyzePriority":22},[],{"issn":193,"eissn":194,"title":195,"url":196},{"VOID":13},{"VOID":15},{"EN":17},{"VOID":19},[],[],[200,207],{"id":92,"indexDatabase":201,"url":105,"indexYears":106,"academicFieldIds":206,"indexDatabaseRanking":113},{"id":94,"createTime":95,"updateTime":96,"relativeEntities":202,"label":203,"description":204,"key":102,"publicationTags":205,"standard":22},[],{"EN":99,"VI":99},{"EN":99,"VI":101},[104],[108,109,110,111,112],{"id":115,"indexDatabase":208,"url":130,"indexYears":22,"academicFieldIds":213,"indexDatabaseRanking":22},{"id":117,"createTime":118,"updateTime":119,"relativeEntities":209,"label":210,"description":211,"key":126,"publicationTags":212,"standard":22},[],{"EN":122,"VI":122},{"VI":124,"EN":125},[128,129],[132,133],{"volume":215,"pages":217},{"VOID":216},"47",{"VOID":218},"19-26","2008-12-19",2008,false,{"id":223,"createTime":224,"updateTime":224,"relativeEntities":225,"slug":22,"properties":226,"entityType":152,"verifyStatus":21,"verifyTime":22,"verifyNote":22,"syncStatus":21,"languages":22,"translateLanguages":22,"viewCount":23,"primaryUrl":235,"fullTextUrl":22,"authors":236,"publicationType":188,"publisherRelationship":311,"citationCount":22,"citationInfo":22,"publishDate":341,"publishYear":342,"citationAnalyzeStatus":21,"lastCitationAnalyze":22,"indexDatabases":22,"openAccess":22,"references":22,"isForceReanalyzing":221},"3ea711f1-429a-49ef-b647-1cf011f68c21","2024-01-20T23:58:45.044+00:00",[],{"references":227,"abstract":229,"title":231,"doi":233},{"VOID":228},"Azen, E. A., Carlson, D. M., Clements, S., Lalley, P. A., and Vanin, E. (1984). Salivary proline-rich protein genes on chromosome 8 of mouse.Science 226967.\nBarka, T. (1980). Biologically active polypeptides in submandibular glands.J. Histochem. Cytochem. 28836.\nBerger, F. G., Gross, K. W., and Watson, G. (1981). Isolation and characterisation of a DNA sequence complementary to an androgen-inducible messenger RNA from mouse kidney.J. Biol. Chem. 2567006.\nChretien, M. (1977). Action of testosterone on the differentiation and secretory activity of a target organ: The submaxillary gland of the mouse.Int. Rev. Cytol. 50333.\nChu, G., Vollrath, D., and Davis, R. W. (1986). Separation of large DNA molecules by contour-clamped homogeneous electric fields.Science 2341582.\nChurch, G. M., and Gilbert, W. (1984). Genomic sequencing.Proc. Natl. Acad. Sci. USA 811991.\nCox, R. A. (1968). The use of guanidinium hydrochloride in the isolation of nucleic acids.Methods Enzymol. 12B120.\nCraig, A. G., Mullins, J. J., McTurk, P., and Brammar, W. J. (1985). A mouse gene family associated with a major submaxillary-gland glycoprotein.Biochem. J. 225657.\nDickinson, D. P., Gross, K. W., Piccini, N., and Wilson, C. M. (1984). Evolution and variation of renin genes in mice.Genetics 108651.\nDickinson, D. P., Ridall, A. L., and Levine, M. J. (1987). Human submandibular gland statherin and basic histidine-rich peptide are encoded by highly abundant mRNA's derived from a common ancestral sequence.Biochem. Biophys. Res. Commun. 149784.\nDickinson, D. P., Mirels, L., Tabak, L. A., and Gross, K. W. (1989). Rapid evolution of variants in a rodent multigene family encoding salivary proteins.Mol. Biol. Evol. 680.\nFeinberg, A. P., and Vogelstein, B. (1983). A technique for radiolabelling DNA restriction endonuclease fragments to high specific activity.Anal. Biochem. 1326.\nGardiner, K., Laas, W., and Patterson, D. (1986). 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The isolation of a family of cysteine-containing phosphoproteins from human submandibular-sublingual saliva.J. Dent. Res. 61973.\nSouthern, E. M. (1975). Detection of specific sequences among DNA fragments separated by gel electrophoresis.J. Mol. Biol. 98503.\nThomas, P. S. (1980). Hybridisation of denatured RNA and small DNA fragments transferred to nitrocellulose.Proc. Natl. Acad. Sci. USA 775201.\nWindass, J. D., Mullins, J. J., Beecroft, L. J., George, H., Meacock, P. A., Williams, B. R. G., and Brammar, W. J. (1984). Molecular cloning of cDNAs from androgen-independent mRNA species of DBA\u002F2 mouse sub-maxillary glands.Nucleic Acids Res. 121361.\nWong, R. S. C., Madapallimattam, G., and Bennick, A. (1983). The role of glandular kallikrein in the formation of a salivary proline-rich protein A by cleavage of a single band in salivary protein C.Biochem. J. 21135.",{"EN":230},"The murine submandibular gland (SMG) produces a novel class of highly acidic salivary proteins encoded by one or more highly abundant mRNA transcripts. In inbred mice, these transcripts are encoded by members of a multigene family comprising approximately 8–12 homologues. Most, and probably all, of these homologues are clustered at a new locus near belted (bt) on chromosome 15, which we designateSpt (salivary protein). Although physically closely linked,Spt genes differ in their patterns of expression both in strains of mice and in their tissues. One gene,Spt-1, is expressed at high levels in the SMG of all inbred strains examined. This gene is also expressed at significant levels in the lacrimal gland. A second gene,Spt-2, appears to be present as a single copy in some strains and as two copies in others. This gene is expressed at high levels only in the SMG of those strains carrying two copies, andSpt-2 mRNA is not detectable in the SMG of strains carrying only one copy. In contrast toSpt-1, theSpt-2 gene is not expressed at detectable levels in the lacrimal gland.",{"EN":232},"Genetic and tissue-specific variation in the expression of a closely linked murine multigene family on chromosome 15 that encodes salivary and lacrimal proteins",{"VOID":234},"10.1007\u002FBF00553636","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002FBF02396156",[237,253,269,281,293],{"id":238,"sortIndex":239,"researcher":22,"roles":240,"affiliations":241,"properties":250},"89cc9c31-8967-43a2-8b02-8fb01e932dfe",4,[161],[242],{"id":22,"sortIndex":23,"affiliation":243,"properties":22},{"id":244,"createTime":245,"updateTime":245,"relativeEntities":246,"slug":22,"properties":247,"entityType":75,"verifyStatus":21,"verifyTime":22,"verifyNote":22,"syncStatus":21,"languages":22,"translateLanguages":22,"viewCount":23},"889e36df-0ab4-4cb6-a023-8e8295ec9cc4","2024-01-09T05:02:18.259+00:00",[],{"title":248},{"VI":249},"Department of Molecular and Cellular Biology, Roswell Park Memorial Institute, Buffalo",{"title":251},{"VI":252},"K. W. Gross",{"id":254,"sortIndex":255,"researcher":22,"roles":256,"affiliations":257,"properties":266},"89ced010-d76d-4a36-b27d-310eabd0119b",2,[161],[258],{"id":22,"sortIndex":23,"affiliation":259,"properties":22},{"id":260,"createTime":261,"updateTime":261,"relativeEntities":262,"slug":22,"properties":263,"entityType":75,"verifyStatus":21,"verifyTime":22,"verifyNote":22,"syncStatus":21,"languages":22,"translateLanguages":22,"viewCount":23},"a1a36af6-513d-4aaa-ad98-7ac123ab51ff","2024-01-20T23:58:45.161+00:00",[],{"title":264},{"VI":265},"Department of Biology, State University College at Buffalo, Buffalo",{"title":267},{"VI":268},"J. Near",{"id":270,"sortIndex":159,"researcher":22,"roles":271,"affiliations":272,"properties":278},"9c6629a7-0e16-45a9-a461-ccaec5f75de3",[161],[273],{"id":22,"sortIndex":23,"affiliation":274,"properties":22},{"id":244,"createTime":245,"updateTime":245,"relativeEntities":275,"slug":22,"properties":276,"entityType":75,"verifyStatus":21,"verifyTime":22,"verifyNote":22,"syncStatus":21,"languages":22,"translateLanguages":22,"viewCount":23},[],{"title":277},{"VI":249},{"title":279},{"VI":280},"K. Abel",{"id":282,"sortIndex":23,"researcher":22,"roles":283,"affiliations":284,"properties":290},"f01c42c0-d13a-441a-b308-b089c488cb62",[161],[285],{"id":22,"sortIndex":23,"affiliation":286,"properties":22},{"id":244,"createTime":245,"updateTime":245,"relativeEntities":287,"slug":22,"properties":288,"entityType":75,"verifyStatus":21,"verifyTime":22,"verifyNote":22,"syncStatus":21,"languages":22,"translateLanguages":22,"viewCount":23},[],{"title":289},{"VI":249},{"title":291},{"VI":292},"D. P. Dickinson",{"id":294,"sortIndex":295,"researcher":22,"roles":296,"affiliations":297,"properties":308},"7a8c2bfb-a2f8-4ddf-a6cc-e9472a820164",3,[161],[298],{"id":22,"sortIndex":23,"affiliation":299,"properties":22},{"id":300,"createTime":301,"updateTime":302,"relativeEntities":303,"slug":304,"properties":305,"entityType":75,"verifyStatus":21,"verifyTime":22,"verifyNote":22,"syncStatus":21,"languages":22,"translateLanguages":22,"viewCount":23},"0c900360-9439-4408-a181-72e8329ab37d","2024-01-21T04:32:40.936+00:00","2025-06-12T01:22:39.827+00:00",[],"The-Jackson-Laboratory-Bar-Harbor",{"title":306},{"VI":307},"The Jackson Laboratory, Bar Harbor",{"title":309},{"VI":310},"B. A. Taylor",{"url":235,"publisher":312,"properties":336},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":313,"slug":10,"properties":314,"entityType":20,"verifyStatus":21,"verifyTime":22,"verifyNote":22,"syncStatus":21,"languages":22,"translateLanguages":22,"viewCount":23,"subjectFields":319,"manageAffiliations":320,"indexDatabases":321,"url":22,"thumbnailPath":22,"statistic":22,"gsStatistic":22,"type":134,"analyzePriority":22},[],{"issn":315,"eissn":316,"title":317,"url":318},{"VOID":13},{"VOID":15},{"EN":17},{"VOID":19},[],[],[322,329],{"id":92,"indexDatabase":323,"url":105,"indexYears":106,"academicFieldIds":328,"indexDatabaseRanking":113},{"id":94,"createTime":95,"updateTime":96,"relativeEntities":324,"label":325,"description":326,"key":102,"publicationTags":327,"standard":22},[],{"EN":99,"VI":99},{"EN":99,"VI":101},[104],[108,109,110,111,112],{"id":115,"indexDatabase":330,"url":130,"indexYears":22,"academicFieldIds":335,"indexDatabaseRanking":22},{"id":117,"createTime":118,"updateTime":119,"relativeEntities":331,"label":332,"description":333,"key":126,"publicationTags":334,"standard":22},[],{"EN":122,"VI":122},{"VI":124,"EN":125},[128,129],[132,133],{"volume":337,"pages":339},{"VOID":338},"27",{"VOID":340},"613-637","1989-10-01",1989,{"id":344,"createTime":345,"updateTime":346,"relativeEntities":347,"slug":348,"properties":349,"entityType":152,"verifyStatus":153,"verifyTime":346,"verifyNote":154,"syncStatus":21,"languages":22,"translateLanguages":22,"viewCount":23,"primaryUrl":359,"fullTextUrl":22,"authors":360,"publicationType":188,"publisherRelationship":413,"citationCount":22,"citationInfo":22,"publishDate":438,"publishYear":439,"citationAnalyzeStatus":21,"lastCitationAnalyze":22,"indexDatabases":22,"openAccess":22,"references":22,"isForceReanalyzing":221},"ee39afe1-cfd7-49fd-b548-d1a115de77cd","2024-04-09T06:01:57.552+00:00","2025-02-26T23:58:44.893+00:00",[],"There-are-two-distinct-arylsulfatase-activities-inDrosophila",{"references":350,"keywords":352,"abstract":354,"title":355,"doi":357},{"VOID":351},"Dinan, L., Glasener, G., and Emmerich, H. (1983). Characterization of the acid phosphatase and arylsulfatase activities in a tumorous blood cell line ofDrosophila melanogaster.Insect Biochem. 13411.\nDubendorfer, A., and Maroy, P. (1986). Ecdysteroid conjugation by tissues of adult females ofDrosophila melanogaster.Insect Biochem. 16109.\nGateff, E., Gissman, L., Shrestha, R., Plus, N., Pfister, H., Schroder, J., and Zur Hausen, H. (1980). Characterization of two tumorous blood cell lines ofDrosophila melanogaster and the viruses they contain. In Kurstak, E., Maramorosch, K., and Dubendorfer, A. (eds.),Invertebrate Systems in Vitro Elsevier\u002FNorth-Holland, Amsterdam, p. 517.\nHagedorn, H. H. (1983). The role of ecdysteroid in the adult insect. In Downer, R. G. H., and Laufer, H. (eds.),Endocrinology of Insects Alan R. Liss, New York, p. 271.\nIsaac, R. E., and Rees, H. H. (1985). Metabolism of maternal ecdysteroid-22-phosphates in developing embryos of the desert locust,Schistocerca gregaria.Insect Biochem. 1565.\nKoolman, J., Hoffmann, J. A., and Karlson, P. (1973). Sulphate esters as inactivation products of ecdysone inLocusta migratoria.Hoppe-Seyler Z. Physiol. Chem. Bd. 3541043.\nMilsom, D. W., Rose, F., and Dodgson, K. (1972). The specific assay of arylsulfatase C from rat liver microsomes.Biochem. J. 128331.\nRees, H. H., and Isaac, R. E. (1985). Biosynthesis and metabolism of ecdysteroids and methods of isolation and identification of the free and conjugated compounds.Methods Enzymol. 111 (Part B):377.\nRoy, A. B. (1960). The sulfatase of ox liver.Biochem. J. 77380.\nRussell, G. B., and Price, G. M. (1977). Metabolism of β-ecdysone during the larval and white puparial stage of the blowfly,Calliphora erythrocephala.Insect Biochem. 7197.\nSmith, S. L., and Bollenbacher, W. E. (1985). Ovarian ecdysteroids and their secretion in late-pharate adults ofGalleria mellonella.J. Insect Physiol. 31419.\nYang, R. S. H., Pelliccia, J. G., and Wilkinson, C. F. (1973). Age-dependent arylsulfatase and sulfotransferase activities in the southern armyworm: A possible insect endocrine regulatory mechanism?Biochem. J. 136817.",{"EN":353},"",{"EN":353},{"EN":356},"There are two distinct arylsulfatase activities inDrosophila",{"VOID":358},"10.1007\u002FBF00554348","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002FBF00554348",[361,377,389,401],{"id":362,"sortIndex":159,"researcher":22,"roles":363,"affiliations":364,"properties":374},"7249ccb0-a27c-4710-9d2e-9074e965c91a",[161],[365],{"id":22,"sortIndex":23,"affiliation":366,"properties":22},{"id":367,"createTime":368,"updateTime":368,"relativeEntities":369,"slug":370,"properties":371,"entityType":75,"verifyStatus":21,"verifyTime":22,"verifyNote":22,"syncStatus":21,"languages":22,"translateLanguages":22,"viewCount":23},"8350f2e4-6fa8-451c-afda-61f06896192c","2024-04-09T03:33:11.756+00:00",[],"Department-of-Biology-Bates-College-Lewiston",{"title":372},{"VI":373},"Department of Biology, Bates College, Lewiston",{"title":375},{"VI":376},"Andrea Freshler",{"id":378,"sortIndex":255,"researcher":22,"roles":379,"affiliations":380,"properties":386},"78116a1e-3e53-44b8-94ea-4d566aa52d30",[161],[381],{"id":22,"sortIndex":23,"affiliation":382,"properties":22},{"id":367,"createTime":368,"updateTime":368,"relativeEntities":383,"slug":370,"properties":384,"entityType":75,"verifyStatus":21,"verifyTime":22,"verifyNote":22,"syncStatus":21,"languages":22,"translateLanguages":22,"viewCount":23},[],{"title":385},{"VI":373},{"title":387},{"VI":388},"Carll Ladd",{"id":390,"sortIndex":295,"researcher":22,"roles":391,"affiliations":392,"properties":398},"9e5394a5-8ec7-4ada-8ec7-8b5fd4a80edf",[161],[393],{"id":22,"sortIndex":23,"affiliation":394,"properties":22},{"id":367,"createTime":368,"updateTime":368,"relativeEntities":395,"slug":370,"properties":396,"entityType":75,"verifyStatus":21,"verifyTime":22,"verifyNote":22,"syncStatus":21,"languages":22,"translateLanguages":22,"viewCount":23},[],{"title":397},{"VI":373},{"title":399},{"VI":400},"Stephanie Richards",{"id":402,"sortIndex":23,"researcher":22,"roles":403,"affiliations":404,"properties":410},"721d3acb-cbc8-413e-82cc-b0471b5bf2e9",[161],[405],{"id":22,"sortIndex":23,"affiliation":406,"properties":22},{"id":367,"createTime":368,"updateTime":368,"relativeEntities":407,"slug":370,"properties":408,"entityType":75,"verifyStatus":21,"verifyTime":22,"verifyNote":22,"syncStatus":21,"languages":22,"translateLanguages":22,"viewCount":23},[],{"title":409},{"VI":373},{"title":411},{"VI":412},"Joseph G. Pelliccia",{"url":22,"publisher":414,"properties":22},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":415,"slug":10,"properties":416,"entityType":20,"verifyStatus":21,"verifyTime":22,"verifyNote":22,"syncStatus":21,"languages":22,"translateLanguages":22,"viewCount":23,"subjectFields":421,"manageAffiliations":422,"indexDatabases":423,"url":22,"thumbnailPath":22,"statistic":22,"gsStatistic":22,"type":134,"analyzePriority":22},[],{"issn":417,"eissn":418,"title":419,"url":420},{"VOID":13},{"VOID":15},{"EN":17},{"VOID":19},[],[],[424,431],{"id":92,"indexDatabase":425,"url":105,"indexYears":106,"academicFieldIds":430,"indexDatabaseRanking":113},{"id":94,"createTime":95,"updateTime":96,"relativeEntities":426,"label":427,"description":428,"key":102,"publicationTags":429,"standard":22},[],{"EN":99,"VI":99},{"EN":99,"VI":101},[104],[108,109,110,111,112],{"id":115,"indexDatabase":432,"url":130,"indexYears":22,"academicFieldIds":437,"indexDatabaseRanking":22},{"id":117,"createTime":118,"updateTime":119,"relativeEntities":433,"label":434,"description":435,"key":126,"publicationTags":436,"standard":22},[],{"EN":122,"VI":122},{"VI":124,"EN":125},[128,129],[132,133],"1987-08-01",1987,{"id":441,"createTime":442,"updateTime":443,"relativeEntities":444,"slug":445,"properties":446,"entityType":152,"verifyStatus":153,"verifyTime":443,"verifyNote":154,"syncStatus":21,"languages":22,"translateLanguages":22,"viewCount":23,"primaryUrl":455,"fullTextUrl":22,"authors":456,"publicationType":188,"publisherRelationship":578,"citationCount":22,"citationInfo":22,"publishDate":608,"publishYear":609,"citationAnalyzeStatus":21,"lastCitationAnalyze":22,"indexDatabases":22,"openAccess":22,"references":22,"isForceReanalyzing":221},"10b02cd0-d323-4d4a-8b4f-1409c191ddb6","2024-01-19T15:40:36.810+00:00","2024-12-18T23:58:15.373+00:00",[],"Human-stomach-alcohol-and-aldehyde-dehydrogenases-ALDH-A-genetic-model-proposed-for-ALDH-III-isozymes",{"references":447,"abstract":449,"title":451,"doi":453},{"VOID":448},"Azevedo, E. S., Silva, M. C. B. O., and Tavares-Neto, J. (1975). Human alcohol dehydrogenaseADH 1,ADH 2 andADH 3 loci in a mixed population of Bahia, Brazil.Ann. Hum. Genet. London. 39321.\nBahr-Lindström, H. v., Höög, J.-O., Hedén, L.-O., Kaiser, R., Fleetwood, L., Larsson, K., Lake, M., Holmquist, B., Holmgren, A., Hempel, J., Vallee, B. L., and Jornvall, H. (1986). cDNA and protein structure for the subunit of human liver alcohol dehydrogenase.Biochemistry 252465.\nBosron, W. F., and Li, T.-K. (1981). Genetic determinants of alcohol and aldehyde dehydrogenases and alcohol metabolism.Semin. Liver Dis. 1179.\nBosron, W. F., and Li, T.-K. (1986). Genetic polymorphism of human liver alcohol and aldehyde dehydrogenases, and their relationship to alcohol metabolism and alcoholism.Hepatology 6502.\nBosron, W. F., Magnes, L. J., and Li, T.-K. (1983). Human liver alcohol dehydrogenase: ADHIndianapolis results from genetic polymorphism at theADH 2 gene locus.Biochem. Genet. 21735.\nChao, T.-J., Chang, C.-P., Chang, M.-C., Liu, H.-C., Wang, J., and Yin, S.-J. (1987). Liver alcohol and aldehyde dehydrogenase isoenzymes in Chinese.Proc. Natl. Sci. Counc. R.O.C. 11B260.\nCleland, W. W. (1979). Statistical analysis of enzyme kinetic data.Methods Enzymol. 63103.\nDuester, G., Smith, M., Bilanchone, V., and Hatfield, G. W. (1986). Molecular analysis of the human class I alcohol dehydrogenase gene family and nucleotide sequence of the gene encoding the β subuuit.J. Biol. Chem. 2612027.\nDuley, J. A., Harris, O., and Holmes, R. S. (1985). Analysis of human alcohol- and aldehydemetabolizing isozymes by electrophoresis and isoelectric focusing.Alcohol. Clin. Exp. Res. 9263.\nForte-McRobbie, C. M., and Pietruszko, R. (1986). Purification and characterization of human liver “high Km” aldehyde dehydrogenase and its identification as glutamic γ-semialdehyde dehydrogenase.J. Biol. Chem. 2612154.\nGoedde, H. W., Agarwal, D. P., and Harada, S. (1979). Alcohol metabolizing enzymes: Studies of isozymes in human biopsies and cultured fibroblasts.Clin. Genet. 1629.\nGoedde, H. W., Agarwal, D. P., and Harada, S. (1980). Genetic studies on alcohol-metabolizing enzymes: Detection of isozymes in human hair roots.Enzyme 25281.\nGoedde, H. W., Agarwal, D. P., and Harada, S. (1983a). The role of alcohol dehydrogenase and aldehyde dehydrogenase isozymes in alcohol metabolism, alcohol sensitivity and alcoholism. In Scandalios, J. G., Rattazzi, M. C., and Whitt, G. S. (eds.),Isozymes: Current Topics in Biological and Medical Research, Vol. 8 Alan R. Liss, New York, p. 175.\nGoedde, H. W., Agarwal, D. P., Harada, S., Meier-Tackmann, D., Ruofu, D., Bienzle, U., Kroeger, A., and Hussein, L. (1983b). Population genetic studies on aldehyde dehydrogenase isozyme deficiency and alcohol sensitivity.Am. J. Hum. Genet. 35769.\nGreenfield, N. J., and Pietruszko, R. (1977). Two aldehyde dehydrogenases from human liver. Isolation via affinity chromatography and characterization of the isozymes.Biochim. Biophys. Acta 48335.\nHarada, S., Agarwal, D. P., and Goedde, H. W. (1978a). Isozyme variations in acetaldehyde dehydrogenase (E.C.1.2.1.3) in human tissues.Hum. Genet. 44181.\nHarada, S., Agarwal, D. P., and Goedde, H. W. (1978b). Human liver alcohol dehydrogenase isoenzyme variations. Improved separation methods using prolonged high voltage starch-gel electrophoresis and isoelectric focusing.Hum. Genet. 40215.\nHarada, S., Agarwal, D. P., and Goedde, H. W. (1980a). Electrophoretic and biochemical studies of human aldehyde dehydrogenase isozymes in various tissues.Life Sci. 261773.\nHarada, S., Misawa, S., Agarwal, D. P., and Goedde, H. W. (1980b). Liver alcohol dehydrogenase and aldehyde dehydrogenase in the Japanese: Isozyme variation and its possible role in alcohol intoxication.Am. J. Hum. Genet. 328.\nHempel, J., Bahr-Lindström, H. v., and Jörnvall, H. (1984). Aldehyde dehydrogenase from human liver. Primary Structure of the cytoplasmic isoenzyme.Eur. J. Biochem. 14121.\nHempel, J., Holmquist, B., Fleetwood, L., Kaiser, R., Barros-Söderling, J., Bühler, R., Vallee, B. L., and Jörnvall, H. (1985a). Structural relationships among class I isozymes of human liver alcohol dehydrogenase.Biochemistry 245303.\nHempel, J., Kaiser, R., and Jörnvall, H. (1985b). Mitochondrial aldehyde dehydrogenase from human liver. Primary structure, differences in relation to the cytosolic enzyme, and functional correlations.Eur. J. Biochem. 15313.\nHolmes, R. S., and Vandeberg, J. L. (1986). Aldehyde dehydrogenases, aldehyde oxidase and xanthine oxidase from baboon tissues: Phenotypic variability and subcellular distribution in liver and brain.Alcohol 3205.\nHöög, J.-O., Hedén, L.-O., Larsson, K., Jörnvall, H., and Bahr-Lindström, H. v. (1986). The γ1 and γ2 subunits of human liver alcohol dehydrogenase. cDNA structures, two amino acid replacements, and compatibility with changes in the enzymatic properties.Eur. J. Biochem. 159215.\nHöög, J.-O., Bahr-Lindström, H. v., Hedén, L.-O., Holmquist, B., Larsson, K., Hempel, J., Vallee, B. L., and Jörnvall, H. (1987). Structure of the class II enzyme of human liver alcohol dehydrogenase: Combined cDNA and protein sequence determination of the π subunit.Biochemistry 261926.\nHopkinson, D. A., Santisteban, I., Povey, S., and Smith, M. (1985). Biochemical genetic analysis of human and rodent aldehyde dehydrogenase.Alcohol 273.\nHsu, L. C., Tani, K., Fujiyoshi, T., Kurachi, K., and Yoshida, A. (1985). Cloning of cDNAs for human aldehyde dehydrogenases 1 and 2.Proc. Natl. Acad. Sci. USA 823771.\nIkuta, T., Szeto, S., and Yoshida, A. (1986). Three human alcohol dehydrogenase subunits: cDNA structure and molecular and evolutionary divergence.Proc. Natl. Acad. Sci. USA 83634.\nJones, G. L., and Teng, Y.-S. (1983). A chemical and enzymological account of the multiple forms of human liver aldehyde dehydrogenase. Implications for ethnic differences in alcohol metabolism.Biochim. Biophys. Acta 745162.\nJörnvall, H., Hempel, J., Vallee, B. L., Bosron, W. F., and Li, T.-K. (1984). Human liver alcohol dehydrogenase: Amino acid substitution in the β2β2 Oriental isozyme explains functional properties, establishes an active site structure, and parallels mutational exchanges in the yeast enzyme.Proc. Natl. Acad. Sci. USA 813024.\nLi, T.-K. (1977). Enzymology of human alcohol metabolism.Adv. Enzymol. 45427.\nLowry, O. H., Rosebrough, N. J., Farr, A. L., and Randall, R. J. (1951). Protein measurement with the Folin phenol reagent.J. Biol. Chem. 193265.\nMather, P. B., and Holmes, R. S. (1984). Biochemical genetics of aldehyde dehydrogenase isozymes in the mouse: Evidence for stomach- and testis-specific isozymes.Biochem. Genet. 22981.\nMeier-Tackmann, D., Agarwal, D. P., Saha, N., and Goedde, H. W. (1984). Aldehyde dehydrogenase isozymes in stomach autopsy specimens from Germans and Chinese.Enzyme 32170.\nPestalozzi, D. M., Bühler, R., Wartburg, J. P. v., and Hess, M. (1983). Immunohistochemical localization of alcohol dehydrogenase in the human gastrointestinal tract.Gastroenterology 851011.\nPietruszko, R. (1983). Aldehyde dehydrogenase isozymes. In Scandalios, J. G., Rattazzi, M. C., and Whitt, G. S. (eds.),Isozymes: Current Topics in Biological and Medical Research, Vol. 8 Alan R. Liss, New York, p. 195.\nRex, D. K., Bosron, W. F., Smialek, J. E., and Li, T.-K. (1985). Alcohol and aldehyde dehydrogenase isoenzymes in North American Indians.Alcohol. Clin. Exp. Res. 9147.\nRicciardi, B. R., Saunders, J. B., Williams, R., and Hopkinson, D. A. (1983). Identification of alcohol dehydrogenase and aldehyde dehydrogenase isoenzymes in human liver biopsy specimens.Clin. Chim. Acta 13085.\nSantisteban, I., Povey, S., West, L. F., Parrington, J. M., and Hopkinson, D. A. (1985). Chromosome assignment, biochemical and immunological studies on a human aldehyde dehydrogenase, ALDH3.Ann. Hum. Genet. Lond. 4987.\nSmith, M. (1986). Genetics of human alcohol and aldehyde dehydrogenases.Adv. Hum. Genet. 15249.\nSmith, M., Hopkinson, D. A., and Harris, H. (1971). Developmental changes and polymorphism in human alcohol dehydrogenase.Ann. Hum. Genet. Lond. 34251.\nSmith, M., Hopkinson, D. A., and Harris, H. (1972). Alcohol dehydrogenase isozymes in adult human stomach and liver: Evidence for activity of theADH 3 locus.Ann. Hum. Genet. Lond. 35243.\nTeng, Y.-S. (1981a). Human liver aldehyde dehydrogenase in Chinese and Asiatic Indians: Gene deletion and its possible implications in alcohol metabolism.Biochem. Genet. 19107.\nTeng, Y.-S. (1981b). Stomach aldehyde dehydrogenase: Report of a new locus.Hum. Hered. 3174.\nTeng, Y.-S., Jehan, S., and Lie-Injo, L. E. (1979). Human alcohol dehydrogenaseADH 2 andADH 3 polymorphisms in ethnic Chinese and Indians of West Malaysia.Hum. Genet. 5387.\nVallee, B. L., and Bazzone, T. J. (1983). Isozymes of human liver alcohol dehydrogenase. In Scandalios, J. G., Rattazzi, M. C., and Whitt, G. S. (eds.),Isozymes: Current Topics in Biological and Medical Research, Vol. 8 Alan R. Liss, New York, p. 219.\nYin, S.-J., Bosron, W. F., Li, T.-K., Ohnishi, K., Okuda, K., Ishii, H., and Tsuchiya, M. (1984a). Polymorphism of human liver alcohol dehydrogenase: Identification of ADH22-1 and ADH22-2 phenotypes in the Japanese by isoelectric focusing.Biochem. Genet. 22169.\nYin, S.-J., Bosron, W. F., Magnes, L. J., and Li, T.-K. (1984b). Human liver alcohol dehydrogenase: Purification and kinetic characterization of the β2β2, β2β1, αβ2 and β2γ1 “Oriental” isoenzymes.Biochemistry 235847.\nYoshida, A., Huang, I.-Y., and Ikawa, M. (1984). Molecular abnormality of an inactive aldehyde dehydrogenase variant commonly found in Orientals.Proc. Natl. Acad. Sci. USA 81258.",{"EN":450},"Isozyme phenotypes of alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) from human gastroendoscopic as well as surgical gastric biopsies were determined by starch gel electrophoresis and agarose isoelectric focusing. γγ ADH isozymes were expressed predominantly in the mucosal layer of the stomach, whereas ββ isozymes were in the muscular layer. In the 56 gastroendoscopic mucosal biopsies examined, the homozygous ADH3 1-1 phenotype was found in 75% of the samples, and the heterozygous ADH3 2-1 phenotype in 25%. Accordingly, the gene frequencies of the allelesADH\n\n                  3\n                  1\n                 andADH\n\n                  3\n                  2\n                 were calculated to be 0.88 and 0.12, respectively. Using a modified agarose isoelectric focusing procedure, gastric ALDH I, ALDH II, and up to five ALDH III forms could be clearly resolved. The ALDH III isozymes accounted for more than 80% of the total ALDH activities in gastric mucosa and exhibitedK\nm values in the millimolar range for propionaldehyde atpH 9.0. Forty-five percent of the 55 gastroendoscopic biopsies studied lacked ALDH I isozyme. The complex gastric ALDH III isozyme phenotypes seen in these biopsies fall into three patterns. They can be interpreted by a genetic hypothesis, based on a dimeric molecule, in which there are two separate genes,ALDH\n3a andALDH\n3b, with theALDH\n3b locus exhibiting polymorphism. The homozygous phenotypes ALDH3b 1-1 and ALDH3b 2-2 were found to be 4 and 76%, respectively, and the heterozygous ALDH3b 2-1 phenotype 20%, of the total. Therefore, the allele frequencies forALDH\n\n                  3b\n                  1\n                 andALDH\n\n                  3b\n                  2\n                 were calculated to be 0.14 and 0.86, respectively. Several lines of biochemical evidence consistent with this genetic model are discussed.",{"EN":452},"Human stomach alcohol and aldehyde dehydrogenases (ALDH): A genetic model proposed for ALDH III isozymes",{"VOID":454},"10.1007\u002FBF00554070","https:\u002F\u002Fidp.springer.com\u002Fauthorize?response_type=cookie&client_id=springerlink&redirect_uri=https%3A%2F%2Flink.springer.com%2Farticle%2F10.1007%2FBF02401788",[457,473,488,510,525,537,550,566],{"id":458,"sortIndex":459,"researcher":22,"roles":460,"affiliations":461,"properties":470},"9a0c83e5-4141-4dcc-8a01-7a3bdb998a0f",6,[161],[462],{"id":22,"sortIndex":23,"affiliation":463,"properties":22},{"id":464,"createTime":465,"updateTime":465,"relativeEntities":466,"slug":22,"properties":467,"entityType":75,"verifyStatus":21,"verifyTime":22,"verifyNote":22,"syncStatus":21,"languages":22,"translateLanguages":22,"viewCount":23},"43581e1a-4b3d-4f2f-80aa-4b082ca80b19","2024-01-19T15:40:36.909+00:00",[],{"title":468},{"VI":469},"Department of Surgery, Tri-Service General Hospital, National Defense Medical Center, Taipei, Taiwan, Republic of China",{"title":471},{"VI":472},"T. -M. 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Phytochemistry 56(6):543–549\nChang CS, Kim H, Park TY (2003) Patterns of allozyme diversity in several selected rare species in Korea and implications for conservation. Biodivers Conserv 12:529–544\nChen LQ, Gao KD, Chen M, Xu CJ (2005) The use of RAPD markers for detecting genetic diversity, relationship and molecular identification of Chinese elite tea genetic resources [Camellia sinensis (L.) O. Kuntze] preserved in a tea germplasm repository. Biodivers Conserv 14:1433–1444\nCheres MT, Miller JF, Crane JM (2000) Genetic distance as a predictor of heterosis and hybrid performance within and between heterotic groups in sunflower. Theor Appl Genet 100:889–894\nDuan SH, Lu B, Li Z, Tong JP, Kong J, Yao W, Li SQ, Zhu YG (2007) Phylogenetic analysis of AA-genome Oryza species (Poaceae) based on chloroplast, mitochondrial, and nuclear DNA sequences. Biochem Genet 45:113–129\nGeng RQ, Chang H, Wang LP, Tsunoda K, Yang ZP, Sun W, Ji DJ, Li YH (2007) Genetic differentiation of native sheep populations in East and South Asia. Biochem Genet 45:263–279\nHsieh MT, Wu CR, Chen CF (1997) Gastrodin and p-hydroxybenzyl alcohol facilitate memory consolidation and retrieval, but not acquisition, on the passive avoidance task in rats. J Ethnopharmacol 56:45–54\nKim HJ, Moon KD, Oh SY, Kim SP, Lee SR (2001) Ether fraction of methanol extracts of Gastrodia tuber, a traditional medicinal herb protects against kainie acid-induced neuronal damage in the mouse hippocampus. Neurosci Lett 314:65–68\nLi K, Fan B, Zhao S (2000) Analysis of diversity and genetic relation between four Chinese indigenous pig breeds and one Australian commercial pig breed. Anim Genet 5:322–325\nLi LY, Zhong GY, Wei YF (2002) DNA markers and their applications in Chinese traditional medicine. Chin J Tradit Med Sci Technol 9:315–320\nLi XB, Tu PF (2003) Fingerprint system of Chinese medicinal materials. Chin Tradit Herbal Drugs 34(5):385–387\nLiang MS, Zeng Y, Zhou X, Hou LJ, Li X (2001) Genetic markers and their applications in identifying crop cultivars. Chin Bull Bot 18:257–265\nLiu YP, Luo JP, Feng YF, Guo H (2002) DNA profiling of Pogostemon cablin chemotypes differing in essential oil composition. Acta Pharm Sin 37:304–308\nLiu ZH, Hu HT, Feng GF, Zhao ZY, Mao NY (2005) Protective effects gastrodin on the cellular model of Alzheimer’s disease induced by Abeta 25–35. Sichuan Da Xue Xue Bao (Yi Xue Ban) 36:537–540\nMachon N, Bardin P, Mazer SJ, Moret J, Godelle B, Austerlitz F (2003) Relationship between genetic structure and seed and pollen dispersal in the endangered orchid Spiranthes spiralis. New Phytol 157:677–687\nMeng A, Gong G, Chen D (1996) DNA fingerprint variability within and among parental lines and its correlation with performance of F1 laying hens. Theor Appl Genet 92:769–776\nMoriuchi KS, Winn AA (2005) Relationships among growth, development and plastic response to environment quality in a perennial plant. New Phytol 166:149–158\nNei M (1978) Estimation of average heterozygosity and genetic distance from a small number of individuals. Genetics 89:583–590\nSangwan RS, Sangwan NS, Jain DC, Kumar S, Ranade SA (1999) RAPD profile based genetic characterization of chemotypic variants of Artemisia annua L. Biochem Mol Biol Int 47(6):935–944\nSun ZQ, Xu YY (2002) Medical statistics, 1st edn. People’s Medical Publishing House, Beijing, pp 33–36\nTao J, Luo ZY, Liu SP, Wen L, Tao Y, Hu WX (2005) Optimizing of RAPD amplifying condition and analysis of genomic DNA polymorphism of Gastrodia tuber Blume. Life Sci Res 9:150–155\nTao J, Fu TX, Luo ZY, Wen L, Wang ZC, Shu XS, Liu SP, Tao Y, Hu WX (2006) Cloning of distinguishing DNA sequences of Gastrodia elata Blume and application of them in identifying Gastrodia tuber. Chin J Biotechnol 22:587–591\nTao J, Qin ZQ, Tao Y, Wen L, Shu XS, Wang ZC, Liu XW, Li WJ, Hu WX (2007) Genetic relationships among Chinese pigs and other pig populations from Hunan Province, China. Anim Genet 38:417–420\nWei Y, Ding MY, Li HX (2001) Determination of gastrodin in Gastrodia elata Blume by HPLC with ELSD and DAD. Chem Res Chin Univ 22:563–566\nWilliams JG, Kubelik AR, Livak KJ, Rafalski JA (1990) DNA polymorphisms amplified by arbitrary primers are useful as genetic markers. Nucleic Acids Res 18:6531–6535\nXu YQ, Wang Y, Li ZZ, Bao ZX, Zao JF, Huang HW (2006) Characterization of polymorphic microsatellite loci in a traditional Chinese medicinal plant Gastrodia elata. Mol Ecol Notes 6:316–318\nYan BQ, Li ZZ, Huang HW, Qin L (2007) Genetic diversity and population differentiation of chestnut blight fungus, Cryphonectria parasitica, in China as revealed by RAPD. Biochem Genet 45:487–506\nZhang YW, Chen YJ, Shen FR, Yang YX, Yang DR, Zhang YP (1999) Study of genetic divergence in Cordyceps sinetic and C. crassispora from northwest of Yunnan by using RAPD. Mycosystema 18:176–183",{"EN":620},"\n                        Gastrodia tuber and its component gastrodin have many pharmacological effects. The chemical fingerprints and gastrodin contents of eight Gastrodia populations were determined, and the genomic DNA polymorphism of the populations was investigated. Genetic distance coefficients among the populations were calculated using the DNA polymorphism data. A dendrogram of the genetic similarities between the populations was constructed using the genetic distance coefficients. The results indicated that the genomic DNA of Gastrodia tubers was highly polymorphic; the eight populations clustered into three major groups, and the gastrodin content varied greatly among these groups. There were obvious correlations among genetic makeup, gastrodin content, and place of origin. The ecological environments in Guizhou and Shanxi may be conducive to evolution and to gastrodin biosynthesis, and more suitable for cultivation of Gastrodia tubers. These findings may provide a scientific basis for overall genetic resource management and for the selection of locations for cultivating Gastrodia tubers.",{"EN":622},"Relationships Among Genetic Makeup, Active Ingredient Content, and Place of Origin of the Medicinal Plant Gastrodia Tuber",{"VOID":624},"10.1007\u002Fs10528-008-9201-7","2025-01-12T23:57:45.126+00:00","http:\u002F\u002Flink.springer.com\u002F10.1007\u002Fs10528-008-9201-7",[628,643,658,670,685,697,716,728,740],{"id":629,"sortIndex":239,"researcher":22,"roles":630,"affiliations":631,"properties":640},"4a0bc993-9470-450f-87e2-cce8cca44883",[161],[632],{"id":22,"sortIndex":23,"affiliation":633,"properties":22},{"id":634,"createTime":635,"updateTime":635,"relativeEntities":636,"slug":22,"properties":637,"entityType":75,"verifyStatus":21,"verifyTime":22,"verifyNote":22,"syncStatus":21,"languages":22,"translateLanguages":22,"viewCount":23},"f2f4e4bb-1dc0-4a16-957f-fb345542147d","2023-12-01T11:53:13.327+00:00",[],{"title":638},{"VI":639},"School of Biology and Food Engineering, Changsha University of Science and Technology, Changsha, P.R. 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W., Christiansen, F. B., Eanes, W. F., and Frydenberg, O. (1978). Homozygosity in the polar bear. Science (submitted).\nBonnell, M. L., and Selander, R. K. (1974). Elephant seals: Genetic variation and near extinction. Science 184908.\nGillespie, J. H., and Kojima, K. (1968). The degree of polymorphism in enzymes involved in energy production compared to that in nonspecific enzymes in two Drosophila ananassae populations. Proc. Natl. Acad. Sci. 61582.\nHouston, D. (1974). The northern Yellowstone elk. Parts I and II. History and demography. Yellowstone National Park Report. 182 pp.\nKing, J. L., and Jukes, T. H. (1969). Non-Darwinian evolution: Random fixation for selectively neutral alleles. Science 164788.\nKojima, K., Gillespie, J. H., and Tobari, Y. N. (1970). A profile of Drosophila species' enzymes assayed by electrophoresis. I. Number of alleles, heterozygosities and linkage disequilibrium in glucose-metabolizing systems and some other enzymes. Biochem. Genet. 4627.\nManlove, M. N., Avise, J. C., Hillestad, H. O., Ramsey, P. R., Smith, M. H., and Straney, D. O. (1976). Starch gel electrophoresis for the study of population genetics in white-tailed deer. Proc. 29th Ann. Conf. S.E. Game and Fish Comm. 29392.\nManlove, M. N., Baccus, R., Pelton, M. R., Smith, M. H., and Gruber, D. (1978). Genetic variability in black bear populations. In Martinka, C. J. (ed.), Proceedings of the 4th International Conference on Bear Research and Management, Wildlife Management Institute, in press.\nMcDermid, E. M., Ananthakirshnan, R., and Agar, N. S. (1972). Electrophoretic investigation of plasma and red cell proteins and enzymes of Macquarie Island elephant seals. Anim. Blood Groups Biochem. Genet. 383.\nNei, M., and Roychoudhury, A. K. (1974a). Sampling variances of heterozygosity and genetic distance. Genetics 76379.\nNei, M., and Roychoudhury, A. K. (1974b). Genetic variation within and between the three major races of man, Caucasoids, Negroids and Mongoloids. Am. J. Hum. Genet. 26421.\nNei, M., Maruyama, T., and Chakraborty, R. (1975). The bottleneck effect and genetic variability in populations. Evolution 291.\nPowell, J. R. (1975). Protein variation in natural populations of animals. Evol. Biol. 879.\nRyman, N., Beckman, G., Bruun-Petersen, G., and Reuterwall, C. (1977). Variability of red cell enzymes and genetic implications of management policies in Scandinavian moose (Alces alces). Hereditas 85157.\nSelander, R. K. (1976). Genic variation in natural populations. In Ayala, F. J. (ed.), Molecular Evolution Sinauer Associates, Sunderland, Mass., pp. 21–45.\nSelander, R. K., and Kaufman, D. W. (1973). Genic variability and strategies of adaptation in animals. Proc. Natl. Acad. Sci. 701875.\nSelander, R. K., Smith, M. H., Yang, S. Y., Johnson, W. E., and Gentry, J. B. (1971). IV. Biochemical polymorphism and systematics in the genus Peromyscus. I. Variation in the old-field mouse (Peromyscus polionotus). Stud. Genet. VI: Univ. Texas Publ. 710349.\nSoule, M. (1976). Allozyme variation: Its determinants in space and time. In Ayala, F. J. (ed.), Molecular Evolution Sinauer Associates, Sunderland, Mass., pp. 60–77.\nValentine, J. W. (1976). Genic strategies of adaptation. In Ayala, F. J. (ed.), Molecular Evolution Sinauer Associates, Sunderland, Mass., pp. 78–94.\nWard, R. D. (1977). Relationships between enzyme heterozygosity and quaternary structure. Biochem. Genet. 15123.",{"EN":792},"Protein products of 24 loci from the genomes of Yellowstone Park elk were analyzed by electrophoresis. Heterozygosity was detected in only one system, making elk much less polymorphic than eastern whitetailed deer. Data for several other large mammals are compared with those for elk and reveal similarly low levels of isozymic variation. 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Meera Khan",{"id":1344,"sortIndex":159,"researcher":22,"roles":1345,"affiliations":1346,"properties":1352},"043c5a88-3686-4834-b08e-b77e9695e86c",[161],[1347],{"id":22,"sortIndex":23,"affiliation":1348,"properties":22},{"id":1332,"createTime":1333,"updateTime":1334,"relativeEntities":1349,"slug":1336,"properties":1350,"entityType":75,"verifyStatus":21,"verifyTime":22,"verifyNote":22,"syncStatus":21,"languages":22,"translateLanguages":22,"viewCount":23},[],{"title":1351},{"VI":1339},{"title":1353},{"VI":1354},"M. C. 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