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Kasarda: Structural homology of storage proteins coded by the Hor-1 locus of barley (Hordeum vulgare L.). Planta 153, 246–253 (1981)",{"doi":415},"10.1007\u002FBF00383894",{"id":18,"text":417,"url":18,"identifiers":418},"Nielsen, G., H. Johansen, J. Jensen &J. Hejgaard: Localization in barley chromosome 4 of genes coding for β-amylase (Bmy 1) and protein Z(Paz 1). Barley Genet. Newslett. 13, 55–57 (1983)",{},{"id":18,"text":420,"url":18,"identifiers":421},"Rahman, S., P.R. Shewry, B.G. Forde, M. Kreis &B.J. Miflin: Nutritional control of storage protein synthesis in developing grain of barley (Hordeum vulgare L.). Planta 159, 366–372 (1983)",{"doi":422},"10.1007\u002FBF00393176",{"id":18,"text":424,"url":18,"identifiers":425},"Rasmussen, S.K., H.E. Hopp &A. Brandt: Nucleotide sequences of cDNA clones for B1 hordein polypeptides. Carlsberg Res. Commun. 48, 187–199 (1983)",{"doi":426},"10.1007\u002FBF02907766",{"id":18,"text":428,"url":18,"identifiers":429},"Rasmussen, S.K., H.E. Hopp, A. Brandt, I. Svendsen &J. Hejgaard: Identification of a cDNA clone for protein Z, a major barley endosperm albumin. Carlsberg Res. Commun. 49, 385–390 (1984)",{"doi":430},"10.1007\u002FBF02907781",{"id":18,"text":432,"url":18,"identifiers":433},"Sanger, F., A.R. Coulson, B.G. Barrell, A.J. Smith &B.A. Roe: Cloning in single-stranded bacteriophage as an aid to rapid DNA sequencing. J. Mol. Biol. 143, 161–178 (1980)",{"doi":434},"10.1016\u002F0022-2836(80)90196-5",{"id":18,"text":436,"url":18,"identifiers":437},"Scandalios, J.G. &J.A. Baum: Regulatory gene variation in higher plants. In: Advances in Genetics Vol.21 (Ed. E. W. Caspari) Academic Press, New York pp. 347–366 (1982)",{},{"id":18,"text":439,"url":18,"identifiers":440},"Shewry, P.R., A.J. Faulks, R.A. Pickering, I.T. Jones, R.A. Finch &B.J. Miflin: The genetic analysis of barley storage proteins. Heredity 44, 383–389 (1980)",{"doi":441},"10.1038\u002Fhdy.1980.35",{"id":18,"text":443,"url":18,"identifiers":444},"Shewry, P.R., R.A. Finch, S. Parmar, J. Franklin &B.J. Miflin: Chromosomal location of hor 3, a new locus governing storage proteins in barley. Heredity 50, 179–189 (1983)",{"doi":445},"10.1038\u002Fhdy.1983.19",{"id":18,"text":447,"url":18,"identifiers":448},"Sørensen, S.B. &M. Ottesen: Fractionation and characterization of beer proteins. Carlsberg Res. Commun. 43, 133–144 (1978)",{"doi":449},"10.1007\u002FBF02914237",{"id":18,"text":451,"url":18,"identifiers":452},"Solari, R.M. & E.A. Favret: Polymorphism in endosperm proteins of barley and its genetic control. In: Proc. 2 Int. Barley Genet. Symp. Ed. R. Nilan, Washington State Univ. Press pp. 23–31 (1971)",{},{"id":18,"text":454,"url":18,"identifiers":455},"Wettstein, D. von: Genetic engineering in the adaptation of plants to evolving human needs. Experientia 39, 687–713 (1983)",{"doi":456},"10.1007\u002FBF01990287",{"id":458,"createTime":459,"updateTime":460,"relativeEntities":461,"slug":462,"properties":463,"entityType":92,"verifyStatus":93,"verifyTime":472,"verifyNote":94,"syncStatus":17,"languages":473,"translateLanguages":18,"viewCount":19,"primaryUrl":474,"fullTextUrl":18,"authors":475,"publicationType":136,"publisherRelationship":516,"citationCount":18,"citationInfo":18,"publishDate":530,"publishYear":531,"citationAnalyzeStatus":17,"lastCitationAnalyze":18,"indexDatabases":18,"openAccess":18,"references":532,"isForceReanalyzing":225},"0a9eed2c-156f-477c-87bb-43aaa85fef54","2024-04-09T20:30:12.035+00:00","2024-12-12T23:54:13.960+00:00",[],"Fractionation-of-protein-components-from-beer-by-density-gradient-centrifugation",{"keywords":464,"abstract":466,"title":468,"doi":470},{"EN":465},"",{"EN":467},"A protein-rich beer fraction obtained by alcohol precipitation has been fractionated by cesium chloride density gradient centrifugation into three fractions. One with buoyant density 1.27 g·ml−1 contained essentially pure protein, while a fraction with buoyant density 1.37 g·ml−1 contained protein and some carbohydrate, probably covalently bound to the protein. A large fraction with a buoyant density of 1.60 g·ml−1 consisted of carbohydrate. Preparative isoelectric focusing of the protein-containing fractions revealed in both cases a protein peak with pI=4.7 which for the 1.37 g·ml−1 fraction coincided with a carbohydrate peak.",{"EN":469},"Fractionation of protein components from beer by density gradient centrifugation",{"VOID":471},"10.1007\u002FBF02907874","2024-12-12T23:54:13.959+00:00",[96],"https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002FBF02907874",[476,493,505],{"id":477,"sortIndex":19,"researcher":18,"roles":478,"affiliations":479,"properties":490},"9c0003bf-40a1-4fcb-ab78-17262b39b4ed",[],[480],{"id":18,"sortIndex":19,"affiliation":481,"properties":18},{"id":482,"createTime":483,"updateTime":484,"relativeEntities":485,"slug":486,"properties":487,"entityType":114,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},"0a466496-5722-4d08-a76a-47fe6d94b95a","2024-01-04T19:53:18.148+00:00","2025-06-11T23:11:25.501+00:00",[],"Department-of-Chemistry-Carlsberg-Laboratory-Copenhagen-Valby",{"title":488},{"VI":489},"Department of Chemistry, Carlsberg Laboratory, Copenhagen Valby",{"title":491},{"EN":492},"Steen Bech Sørensen",{"id":494,"sortIndex":101,"researcher":18,"roles":495,"affiliations":496,"properties":502},"65acffbf-cfb2-4a69-961a-dd36c69fd492",[],[497],{"id":18,"sortIndex":19,"affiliation":498,"properties":18},{"id":482,"createTime":483,"updateTime":484,"relativeEntities":499,"slug":486,"properties":500,"entityType":114,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":501},{"VI":489},{"title":503},{"EN":504},"Torben Graves Pedersen",{"id":506,"sortIndex":153,"researcher":18,"roles":507,"affiliations":508,"properties":514},"77f3d930-4564-4182-876b-742ec746723b",[],[509],{"id":18,"sortIndex":19,"affiliation":510,"properties":18},{"id":482,"createTime":483,"updateTime":484,"relativeEntities":511,"slug":486,"properties":512,"entityType":114,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":513},{"VI":489},{"title":515},{"EN":121},{"url":18,"publisher":517,"properties":18},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":518,"slug":10,"properties":519,"entityType":16,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19,"subjectFields":522,"manageAffiliations":523,"indexDatabases":524,"url":18,"thumbnailPath":18,"statistic":525,"gsStatistic":18,"type":18,"analyzePriority":18},[],{"issn":520,"title":521},{"VOID":13},{"EN":15},[],[],[],{"impactFactor":19,"impactFactorByYear":526,"i10Index":25,"i10IndexLast5Year":19,"totalPublication":26,"totalPublicationByYear":527,"totalCitation":39,"totalCitationByYear":528,"totalCitationPerPublication":55,"totalCitationPerPublicationByYear":529,"hindexLast5Year":30,"hindex":30},{},{"1976":28,"1977":29,"1978":30,"1979":31,"1980":32,"1981":33,"1982":34,"1983":35,"1984":36,"1985":33,"1986":37,"1987":29,"1988":31,"1989":38},{"1976":41,"1977":42,"1978":43,"1979":44,"1980":45,"1981":46,"1982":47,"1983":48,"1984":49,"1985":50,"1986":51,"1987":52,"1988":53,"1989":54},{"1976":57,"1977":58,"1978":59,"1979":60,"1980":61,"1981":62,"1982":63,"1983":64,"1984":65,"1985":66,"1986":67,"1987":68,"1988":69,"1989":70},"1982-07-01",1982,[533,535,537,539,541,543,545,546,548,550,552,554,556,558,560,562,564,566],{"id":18,"text":534,"url":18,"identifiers":18},"Asano, K. &N. Hashimoto: Isolation and characterization of foaming proteins of beer. J. Amer. Soc. Brew. Chem. 38, 129–137 (1980)",{"id":18,"text":536,"url":18,"identifiers":18},"Ashwell, G.: New colorimetric methods of sugar analysis. In: Meth. Enzymol., E. F. Neufeld & V. Ginsberg, eds., Academic Press Vol. 8, 85–95 (1966)",{"id":18,"text":538,"url":18,"identifiers":18},"Bishop, L. R.: Haze- and foam-forming substances in beer. J. Inst. Brew. 81, 444–449 (1975)",{"id":18,"text":540,"url":18,"identifiers":18},"Brandt, A.: Endosperm protein formation during kernel development of wild type and a high-lysine barley mutant. Cereal Chem. 53, 890–901 (1976)",{"id":18,"text":542,"url":18,"identifiers":18},"Dobson, N. &U. Melcher: Density comparisons of heavy chains of membrane and secreted immunoglobulins of mouse. Biochem. J. 183, 395–403 (1978)",{"id":18,"text":544,"url":18,"identifiers":18},"Hebert, J. P.: Contribution á l'étude de la mousse de bière. Procédés de fractionnement d'une entité mousse positive. Thése. Lille (1972)",{"id":18,"text":367,"url":18,"identifiers":18},{"id":18,"text":547,"url":18,"identifiers":18},"Hejgaard, J. &S. B. Sørensen: Characterization of a protein-rich beer fraction by two-dimensional immunoelectrophoretic techniques. Compt. Rend. Trav. Lab. Carlsberg 40, 187–204 (1975)",{"id":18,"text":549,"url":18,"identifiers":18},"Honda, A., Y. Kanke &Y. Mori: Proteoglycans and glycoproteins from bovine heart valve. Density-gradient ultracentrifugal and gel chromatographic behaviour of the valvular matrix macromolecules under dissociative and associative conditions. J. Biochem. 81, 1595–1603 (1977)",{"id":18,"text":551,"url":18,"identifiers":18},"Ifft, J. B., W. R. Martin III &K. Kinzie: Density gradient proportionality constants for a number of aqueous binary solutions. Biopolymers 9, 597–614 (1970)",{"id":18,"text":553,"url":18,"identifiers":18},"Kaersgaard, P. &J. Hejgaard: Antigenic beer macromolecules. An experimental survey of purification methods. J. Inst. Brew. 85, 103–111 (1979)",{"id":18,"text":555,"url":18,"identifiers":18},"Marshall, T. &A. Allen: The isolation and characterization of the high-molecular-weight glycoprotein from pig colonic mucus. Biochem. J. 173, 569–578 (1978)",{"id":18,"text":557,"url":18,"identifiers":18},"Nadzeyka, A., U. Altenhofen &H. Zahn: Isolierung und Charakterisierung von Protein-fraktionen aus Bier. Brauwissenschaft 32, 85–93 (1979)",{"id":18,"text":559,"url":18,"identifiers":18},"Pedersen, T. G. &J. B. Ifft: Buoyant titration of ovalbumin in four alkali halides. Hydration and ion binding. Carlsberg Res. Commun. 43, 65–76 (1978)",{"id":18,"text":561,"url":18,"identifiers":18},"Périn, J.-P., F. Bonnet &P. Jollès: Comparative studies on human and bovine nasal cartilage proteoglycan complex components. Mol. Cel. Biochem. 21, 71–82 (1978)",{"id":18,"text":563,"url":18,"identifiers":18},"Spee-Brand, R., G. J. A. M. Strous &M. F. Kramer: Isolation and partial characterization of rat gastric mucous glycoprotein. Biochim. Biophys. Acta 621, 104–116 (1980)",{"id":18,"text":565,"url":18,"identifiers":18},"Sørensen, S. B. &M. Ottesen: Fractionation and characterization of beer proteins. Carlsberg Res. Commun. 43, 133–144 (1978)",{"id":18,"text":567,"url":18,"identifiers":18},"Traube, J.: Über den Raum der Atome. Samm. Chem.-Tech. Vorträge 4, 255–332 (1899)",{"id":569,"createTime":570,"updateTime":570,"relativeEntities":571,"slug":18,"properties":572,"entityType":92,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19,"primaryUrl":581,"fullTextUrl":18,"authors":582,"publicationType":136,"publisherRelationship":645,"citationCount":18,"citationInfo":18,"publishDate":664,"publishYear":665,"citationAnalyzeStatus":17,"lastCitationAnalyze":18,"indexDatabases":18,"openAccess":18,"references":18,"isForceReanalyzing":225},"f37513a3-de8a-4938-bc4d-ddf467959b66","2024-01-20T23:51:50.616+00:00",[],{"references":573,"abstract":575,"title":577,"doi":579},{"VOID":574},"Ambler, A. P.: Enzymatic hydrolysis with carboxypeptidase. Methods Enzymol. 25, 143–154 (1972)\nBarra, D., F. Martini, F. Bossa, G. Rotilio, J. V. Bannister &W. H. Bannister: Primary structure of human Cu,Zn superoxide dismutase. Cysteine and tryptophan containing peptides. Biochem. Biophys. Res. Comm. 81, 1195–1200 (1978)\nBegg, G. &F. J. Morgan: A non-volatile buffer with improved performance in automated protein sequencing. Febs Lett. 66, 243–245 (1976)\nBenzon, J. R. &P. E. Hare: O-phthalaldehyde: Fluorogenic detection of primary amines in the picomole range. Comparison with fluorescamine and ninhydrin. Proc. Nat. Acad. Sci. U.S.A., 72, 619–622 (1975)\nButler, P. J. G. &B. S. Hartley: Maleylation of amino groups. Methods Enzymol. 25, 191–199 (1972)\nCass, A. E. G., H. A. O. Hill, V. Hasemann &J. T. Johansen:1H nuclear magnetic resonance spectroscopy of yeast copper- zinc superoxide dismutase. Structural homology with the bovine enzyme. Carlsberg Res. Commun. 43, 439–449 (1978)\nCass, A. E. G., H. A. O. Hill, J. V. Bannister, W. H. Bannister, V. Hasemann & J. T. Johansen: The exchange of histidine C2 protons in superoxide dismutase. A novel method for assigning metal ligands in proteins. Biochem. J. (1979) in the press.\nDayhoff, M. O., ed.: Atlas of protein sequence and structure 1972. Volume 5. National Biomedical Research Foundation, Washington, D.C. (1972)\nDixon, H. B. F. &R. N. Perham: Reversible blocking of amino groups with citraconic anhydride. Biochem. J. 109, 312–314 (1968)\nEdman, P. &G. Begg: A protein sequenator. Eur. J. Biochem. 1, 80–91 (1967)\nEdman, P. &A. Henschen: Sequence determination. In: Protein Sequence Determination. Molecular Biology Biochemistry and Biophysics 8. 2nd edition, S. B. Needleman, ed., Springer-Verlag, Berlin, Heidelberg & New York, pp. 232–279 (1975)\nFridovich, I.: Superoxide dismutases. Adv. Enzymol. 41, 35–97 (1974)\nFridovich, I.: Superoxide dismutases. Ann. Rev. Biochem. 44, 147–159 (1975)\nGold, A. M. &D. F. Fahrney: Sulfonyl fluorides as inhibitors of esterases. II. Formation and reactions of phenylmethanesulfonyl-chymotrypsin. Biochemistry 3, 783–791 (1964)\nHarris, J. I. &H. M. Steinman: Amino acid sequence homologies among superoxide dismutases. In: Superoxide and Superoxide dismutases, A. M. Michelson, J. M. McCord and I. Fridovich, eds., Academic Press, London, New York and San Francisco, pp. 225–230 (1977)\nHermodson, M. A., L. H. Ericsson, K. Titani, H. Neurath &K. A. Walsh: Application of sequenator analysis to the study of proteins. Biochemistry 11, 4493–4502 (1972)\nHirs, C. H. W., S. Moore &W. H. Stein: Peptides obtained by tryptic hydrolysis of performic acid-oxidized ribonuclease. J. Biol. Chem. 219, 623–642 (1956)\nHirs, C. H. W.: Performic acid oxidation. Methods Enzymol. 11, 197–199 (1967)\nHounard, J. &G. R. Drapeau: Staphylococcal protease. A proteolytic enzyme specific for glutamoyl bonds. Proc. Nat. Acad. Sci. U.S.A. 69, 3506–3509 (1972)\nKasper, C. B.: Fragmentation of proteins for sequence studies and separation of peptide mixtures. In: Protein Sequence Determination. Molecular Biology and Biophysics 8, 2nd edition. S. B. Needleman, ed., Springer-Verlag, Berlin, Heidelberg and New York, pp. 114–161 (1975)\nKulbe, K. D.: Micropolyamide thin-layer chromatography of phenylthiohydantoin amino acids (PTH) at subnanomolar level. A rapid microtechnique for simultaneous multisample identification after automated Edman degradations. Anal. Biochem. 59, 564–573 (1974)\nMendez, E. &C. Y. Lai: Regeneration of amino acids from thiazolinones. Anal. Biochem. 68, 47–53 (1975)\nMichelson, A. M., J. M. McCord &I. Fridovich, eds.: Superoxide and superoxide dismutases. Academic Press, London, New York and San Francisco (1977)\nPetersen, C., V. Hasemann, B. Martin, J. T. Johansen, I. Svendsen &M. Ottosen: The amino terminal sequence of superoxide dismutase from Saccharomyces cerevisiae. Carlsberg Res. Commun. 42, 391–395 (1977)\nRichardson, J. S., K. A. Thomas, B. H. Rubin &D. C. Richardson: Crystal structure of bovine Cu,Zn superoxide dismutase at 3Å resolution: Chain tracing and metal ligands. Proc. Nat. Acad. Sci., U.S.A., 72, 1349–1353 (1975)\nSteinman, H. M.: The amino acid sequence of mangano superoxide dismutase from Escherichia coli B. J. Biol. Chem. 253, 8708–8720 (1978)\nSteinman, H. M. &R. L. Hill: Sequence homologies among bacterial and mitochondrial superoxide dismutases. Proc. Nat. Sci. U.S.A. 70, 3725–3729 (1973)\nSteinman, H. M., V. R. Naik, J. L. Abernethy &R. L. Hill: Bovine erythrocyte superoxide dismutase. Complete amino acid sequence. J. Biol. Chem. 249, 7326–7338 (1974)\nTarr, G. E., J. F. Beecher, M. Bell &D. J. McKean: Polyquarternary amines prevent peptide loss from sequenators. Anal. Biochem. 84, 622–627 (1978)\nWaxdal, M. J., W. H. Konigsberg, W. L. Henley &G. M. Edelman: The covalent structure of a human γ-G-immunoglobulin. II. Isolation and characterization of the cyanogen bromide fragments. Biochemistry 7, 1959–1966 (1968)\nWoods, K. R. &K. T. Wang: Separation of dansyl amino acids by polyamide layer chromatography. Biochim. Biophys. Acta. 133, 369–730 (1967)",{"EN":576},"The amino acid sequence of the copper zinc superoxide dismutase from Saccharomyces cerevisiae has been determined by automated Edman degradation. Peptides were obtained from cyanogen bromide cleavage, Staphylococcus aureus V8 protease digestion, tryptic and chymotryptic digests of the citraconylated reduced and carboxymethylated enzyme, and by further fragmentation of selected peptides with trypsin. From the alignment of these peptides and the previously published sequence of the first 54 amino terminal residues (24) the complete sequence was deduced by direct sequence identification of all 153 amino acid residues and of all peptide overlaps. The amino acid sequence corresponds to a molecular weight of 15,950 for each of the two identical subunits in the native enzyme. The primary structure of yeast copper, zinc superoxide dismutase is 55% identical with the sequence of the copper, zinc enzyme from bovine erythrocytes. Importantly, all the copper and zinc ligands, six histidine residues and one aspartate residue from the bovine enzyme, are conserved in the yeast enzyme. The high overall sequence homology and conservation of important metal binding active site amino acid residues suggest that the three-dimensional structure and in particular the active site geometry is virtually the same for the bovine and yeast enzyme. In contrast no sequence homology is apparent by comparison with the manganese or iron class of superoxide dismutases indicating that the two classes have not evolved from a common ancestor.",{"EN":578},"The complete amino acid sequence of copper, zinc superoxide dismutase from Saccharomyces cerevisiae",{"VOID":580},"10.1007\u002FBF02906155","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002FBF02906155",[583,596,608,621,633],{"id":584,"sortIndex":19,"researcher":18,"roles":585,"affiliations":587,"properties":593},"0386b6a9-c9f7-4947-a43a-358cc430abce",[586],"AUTHOR",[588],{"id":18,"sortIndex":19,"affiliation":589,"properties":18},{"id":482,"createTime":483,"updateTime":484,"relativeEntities":590,"slug":486,"properties":591,"entityType":114,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":592},{"VI":489},{"title":594},{"VI":595},"Jack T. Johansen",{"id":597,"sortIndex":101,"researcher":18,"roles":598,"affiliations":599,"properties":605},"8a6e20b4-43fc-4a53-8772-7586309942ee",[586],[600],{"id":18,"sortIndex":19,"affiliation":601,"properties":18},{"id":482,"createTime":483,"updateTime":484,"relativeEntities":602,"slug":486,"properties":603,"entityType":114,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":604},{"VI":489},{"title":606},{"VI":607},"Carsten Overballe-Petersen",{"id":609,"sortIndex":610,"researcher":18,"roles":611,"affiliations":612,"properties":618},"963d67e6-8bdb-42f4-afb3-b2eac2d3fa03",4,[586],[613],{"id":18,"sortIndex":19,"affiliation":614,"properties":18},{"id":482,"createTime":483,"updateTime":484,"relativeEntities":615,"slug":486,"properties":616,"entityType":114,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":617},{"VI":489},{"title":619},{"VI":620},"Ib Svendsen",{"id":622,"sortIndex":153,"researcher":18,"roles":623,"affiliations":624,"properties":630},"7c4bd1ed-8d15-4237-a9a8-66efe6e23f56",[586],[625],{"id":18,"sortIndex":19,"affiliation":626,"properties":18},{"id":482,"createTime":483,"updateTime":484,"relativeEntities":627,"slug":486,"properties":628,"entityType":114,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":629},{"VI":489},{"title":631},{"VI":632},"Brian Martin",{"id":634,"sortIndex":58,"researcher":18,"roles":635,"affiliations":636,"properties":642},"7082c51e-869d-4733-9936-ba3921839134",[586],[637],{"id":18,"sortIndex":19,"affiliation":638,"properties":18},{"id":482,"createTime":483,"updateTime":484,"relativeEntities":639,"slug":486,"properties":640,"entityType":114,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":641},{"VI":489},{"title":643},{"VI":644},"Villy Hasemann",{"url":581,"publisher":646,"properties":659},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":647,"slug":10,"properties":648,"entityType":16,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19,"subjectFields":651,"manageAffiliations":652,"indexDatabases":653,"url":18,"thumbnailPath":18,"statistic":654,"gsStatistic":18,"type":18,"analyzePriority":18},[],{"issn":649,"title":650},{"VOID":13},{"EN":15},[],[],[],{"impactFactor":19,"impactFactorByYear":655,"i10Index":25,"i10IndexLast5Year":19,"totalPublication":26,"totalPublicationByYear":656,"totalCitation":39,"totalCitationByYear":657,"totalCitationPerPublication":55,"totalCitationPerPublicationByYear":658,"hindexLast5Year":30,"hindex":30},{},{"1976":28,"1977":29,"1978":30,"1979":31,"1980":32,"1981":33,"1982":34,"1983":35,"1984":36,"1985":33,"1986":37,"1987":29,"1988":31,"1989":38},{"1976":41,"1977":42,"1978":43,"1979":44,"1980":45,"1981":46,"1982":47,"1983":48,"1984":49,"1985":50,"1986":51,"1987":52,"1988":53,"1989":54},{"1976":57,"1977":58,"1978":59,"1979":60,"1980":61,"1981":62,"1982":63,"1983":64,"1984":65,"1985":66,"1986":67,"1987":68,"1988":69,"1989":70},{"volume":660,"pages":662},{"VOID":661},"44",{"VOID":663},"201-217","1979-07-01",1979,{"id":667,"createTime":668,"updateTime":669,"relativeEntities":670,"slug":671,"properties":672,"entityType":92,"verifyStatus":93,"verifyTime":681,"verifyNote":94,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19,"primaryUrl":682,"fullTextUrl":18,"authors":683,"publicationType":136,"publisherRelationship":743,"citationCount":18,"citationInfo":18,"publishDate":762,"publishYear":155,"citationAnalyzeStatus":17,"lastCitationAnalyze":18,"indexDatabases":18,"openAccess":18,"references":18,"isForceReanalyzing":225},"f058a76b-9968-4543-a21f-28198bc121b7","2024-02-10T23:52:04.999+00:00","2025-01-25T23:48:55.035+00:00",[],"%CE%94-aminolevulinic-acid-formation-in-the-archaebacterium-Methanobacterium-thermoautotrophicum-requires-tRNAGlu",{"references":673,"abstract":675,"title":677,"doi":679},{"VOID":674},"Bokranz, M., G.Baumner, R. Allmansberger, D. Ankel-Fuchs &A. Klein: Cloning and characterization of the methyl coenzyme M reductase genes from Methanobacterium thermoautotrophicum. Submitted to J. Bacteriol.\nCastelfranco, P. A. &S. I. Beale: Chlorophyll biosynthesis: Recent advances and areas of current interest. Ann. Rev. Plant Physiol. 34, 241–278 (1983)\nChibbar, R. N. &R. B. van Huystee: Glutamic acid is the haem precursor for peroxidase synthesised by pea nut cells in suspension culture. Phytochemistry 22, 1721–1723 (1983)\nDörnemann, D. &H. Senger: The synthesis and properties of 4,5-dioxovaleric acid, a possible intermediate in the biosynthesis of 5-aminolaevulinic acid, and its in vivo formation in Scenedesmus obliquus. Biochim. Biophys. Acta 628, 35–45 (1980)\nDörnemann, D. &H. Senger: Organism dependent pathways of tetrapyrrole biosynthesis. In: Optical Properties and Structure of tetrapyrroles. Eds. G. Blauer & H. Sund. Walter de Gruyter, Berlin, pp. 43–60 (1985)\nFord, S. H. &H. C. Friedmann: Formation of δ-aminolevulinic acid from glutamic acid by a partially purified enzyme system from wheat leaves. Biochim. Biophys. Acta 569, 153–158 (1979)\nFriedmann, H. C. &R. K. Thauer: Ribonuclease-sensitive δ-aminolevulinic acid formation from glutamate in cell extracts of Methanobacterium thermoautotrophicum. FEBS Letters 207, 84–88 (1986)\nGilles, H., R. Jaenchen &R. K. Thauer: Biosynthesis of 5-aminolevulinic acid in Methanobacterium thermoautotrophicum. Arch. Microbiol. 135, 237–240 (1983)\nHarel, E., E. Ne’eman &E. Meller: Alternative routes for the synthesis of 5-aminolevulinic acid in maize leaves. Plant Physiol. 72, 1056–1061 (1983)\nHöllriegl, V., L. Lamm, J. Rowold, J. Hörig &P. Renz: Biosynthesis of vitamin B12. Different pathways in some aerobic and anaerobic microorganisms. Arch. Microbiol. 132, 155–158 (1982)\nHuang, D. -D., W. -Y. Wang, S. P. Gough &C. G. Kannangara: δ-Aminolevulinic acid-synthesising enzymes need an RNA moiety for activity. Science 225, 1482–1484 (1984)\nJordan, P. M. &D. Shemin: δ-Aminolevulinic acid synthatase. In: Enzymes. Ed. P. D. Boyer, Academic Press, New York, vol 7, pp. 339–356 (1972)\nKah, A. &D. Dörnemann: Glutamic acid-1-semialdehyde, a hypothetical intermediate in the biosynthesis of 5-aminolevulinic acid. Z. Naturforsch. 42c, 209–214 (1987)\nKannangara, C. G. &A. Schouboe: Biosynthesis of δ-aminolevulinate in greening barley leaves VII. Glutamate 1-semialdehyde accumulation in gabaculine treated leaves. Carlsberg Res. Commun. 50, 179–191 (1985)\nKannangara, C. G., S. P. Gough &D. von Wettstein: The biosynthesis of Δ-aminolevulinate and chlorophyll and its genetic regulation. In: Development in Plant Biology. vol 2. Chloroplast development. Eds. G. Akoyunoglou & J. H. Akoyunoglou, Elsevier, Amsterdam. pp. 147–160 (1978)\nKannangara, C. G., S. P. Gough, R. P. Oliver &S. K. Rasmussen: Biosynthesis of δ-aminolevulinate in greening barley VI. Activation of glutamate by ligation to RNA. Carlsberg Res. Commun. 49, 417–437 (1984)\nMauzerall, D. &S. Granick: The occurence and determination of δ-aminolevulinic acid and porphobilinogen in urine. J. Biol. Chem. 219, 435–446 (1956)\nMeisch, H. -U. &R. Maus: Untersuchungen zur Synthese und biologischen Bedeutung von Glutaminsäure-1-semialdehyd als Vorstufe der Chlorophylle. Z. Naturforsch. 38c, 563–570 (1983)\nOh-hama, T., H. Seto &S. Miyachi:13C-NMR evidence of bacteriochlorophyll a formation by the C5 pathway in Chromatium. Arch. Biochem. Biophys. 246, 192–198 (1986)\nPorra, R. J. &H. -U. Meisch: The biosynthesis of chlorophyll. Trends Biochem. Sci. 9, 99–104 (1984)\nPorra, R. J., R. Barnes &O. T. G. Jones: The level and sub-cellular distribution of δ-aminolaevulinate synthase activity in semi-anaerobic and aerobic yeast. Hoppe-Seyler’s Z. Physiol. Chem. 353, 1365–1368 (1972)\nSchön, A., G. Krupp, S. P. Gough, S. Berry-Lowe, C. G. Kannangara &D. Söll: The RNA required in the first step of chlorophyll biosynthesis is a chloroplast glutamate tRNA. Nature 322, 281–284 (1986)\nSchön, A., C. G. Kannangara, S. P. Gough &D. Söll: Transfer RNA mischarging and a transamidase reaction are required for normal protein biosynthesis in orgenelles: A tRNA-dependent amidotransferase synthesizes GLN-tRNAGln from GLU-tRNAGln. In: Abstracts of Papers Presented at the 1987 Meeting on Molecular Biology of Mitochondria and Chloroplasts. Cold Spring Harbor Laboratory, Cold Spring Harbor, New York. p. 130 (1987)\nSmith, K. M. &M. S. Huster: Bacteriochlorophyllc formation via glutamate C-5 pathway in Chlorobium bacteria. J. Chem. Soc. Chem. Commun. 14–16 (1987)\nSoper, T. S. &J. M. Manning: Inactivation of pyridoxal phosphate enzymes by gabaculine. Correlation with enzymic exchange of β-protons. J. Biol. Chem. 257, 13930–13936 (1982)\nWang, W. -Y., S. P. Gough &C. G. Kannangara: Biosynthesis of δ-aminolevulinate in greening barley leaves IV. Isolation of three soluble enzymes required for the conversion of glutamate to δ-aminolevulinate. Carlsberg Res. Commun. 46, 243–257 (1981)\nWeinstein, J. D. &S. I. Beale: Enzymatic conversion of glutamate to δ-aminolevulinate in soluble extracts of the unicellular green alga,Chlorella vulgaris. Arch. Biochem. Biophys. 237, 454–464 (1985)\nWilcox, M. &M. Nirenberg: Transfer RNA as a cofactor coupling amino acid synthesis with that of protein. Proc. Natl. Acad. Sci., USA 61, 229–236 (1968)",{"EN":676},"By combining three fractions separated from cell extracts of Methanobacterium thermoautotrophicum (strain Marburg) synthesis of δ-aminolevulinic acid from glutamate was obtained. One of the required fractions contained two tRNAs which could be charged with glutamate and separated by high pressure liquid chromatography. Both supported the synthesis of δ-aminolevulinate. The formation of δ-aminolevulinate from glutamate or from glutamate 1-semialdehyde was inhibited by gabaculine. The conversion of glutamate to δ-aminolevulinate in Methanobacterium thus displays the same features as found in the chloroplasts of plants.",{"EN":678},"Δ-aminolevulinic acid formation in the archaebacterium Methanobacterium thermoautotrophicum requires tRNAGlu",{"VOID":680},"10.1007\u002FBF02933528","2025-01-25T23:48:55.034+00:00","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002FBF02933528",[684,701,716,728],{"id":685,"sortIndex":19,"researcher":18,"roles":686,"affiliations":687,"properties":698},"77566eb7-0996-448c-91ae-7a2d5dbcaae7",[586],[688],{"id":18,"sortIndex":19,"affiliation":689,"properties":18},{"id":690,"createTime":691,"updateTime":692,"relativeEntities":693,"slug":694,"properties":695,"entityType":114,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},"866df726-ae5f-4940-a3df-f30daa34b057","2024-04-13T08:31:24.799+00:00","2025-01-29T21:53:08.686+00:00",[],"Department-of-Biochemistry-and-Molecular-Biology-The-University-of-Chicago-Chicago-USA",{"title":696},{"EN":697},"Department of Biochemistry and Molecular Biology, The University of Chicago, Chicago, USA",{"title":699},{"VI":700},"Herbert C. Friedmann",{"id":702,"sortIndex":153,"researcher":18,"roles":703,"affiliations":704,"properties":713},"8d5dee4e-9c30-4e57-ac99-eb3f1dab9f7f",[586],[705],{"id":18,"sortIndex":19,"affiliation":706,"properties":18},{"id":707,"createTime":708,"updateTime":708,"relativeEntities":709,"slug":18,"properties":710,"entityType":114,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},"3fafc6c5-082d-420d-a787-2f45044818b2","2023-12-11T04:16:27.933+00:00",[],{"title":711},{"VI":712},"Department of Physiology, Carlsberg Laboratory, Copenhagen Valby, Denmark",{"title":714},{"VI":715},"Simon P. Gough",{"id":717,"sortIndex":58,"researcher":18,"roles":718,"affiliations":719,"properties":725},"2c177779-498f-40a0-81c1-34435b052706",[586],[720],{"id":18,"sortIndex":19,"affiliation":721,"properties":18},{"id":707,"createTime":708,"updateTime":708,"relativeEntities":722,"slug":18,"properties":723,"entityType":114,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":724},{"VI":712},{"title":726},{"VI":727},"C. Gamini Kannangara",{"id":729,"sortIndex":101,"researcher":18,"roles":730,"affiliations":731,"properties":740},"9919118e-7a95-4cdf-9d7e-b83eda89d0ef",[586],[732],{"id":18,"sortIndex":19,"affiliation":733,"properties":18},{"id":734,"createTime":735,"updateTime":735,"relativeEntities":736,"slug":18,"properties":737,"entityType":114,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},"31b42b33-4127-4023-8139-3eb525cf9f0c","2023-12-07T20:16:35.333+00:00",[],{"title":738},{"VI":739},"Fachbereich Biologie, Philipps-Universität, Marburg, Germany",{"title":741},{"VI":742},"Rudolf K. Thauer",{"url":682,"publisher":744,"properties":757},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":745,"slug":10,"properties":746,"entityType":16,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19,"subjectFields":749,"manageAffiliations":750,"indexDatabases":751,"url":18,"thumbnailPath":18,"statistic":752,"gsStatistic":18,"type":18,"analyzePriority":18},[],{"issn":747,"title":748},{"VOID":13},{"EN":15},[],[],[],{"impactFactor":19,"impactFactorByYear":753,"i10Index":25,"i10IndexLast5Year":19,"totalPublication":26,"totalPublicationByYear":754,"totalCitation":39,"totalCitationByYear":755,"totalCitationPerPublication":55,"totalCitationPerPublicationByYear":756,"hindexLast5Year":30,"hindex":30},{},{"1976":28,"1977":29,"1978":30,"1979":31,"1980":32,"1981":33,"1982":34,"1983":35,"1984":36,"1985":33,"1986":37,"1987":29,"1988":31,"1989":38},{"1976":41,"1977":42,"1978":43,"1979":44,"1980":45,"1981":46,"1982":47,"1983":48,"1984":49,"1985":50,"1986":51,"1987":52,"1988":53,"1989":54},{"1976":57,"1977":58,"1978":59,"1979":60,"1980":61,"1981":62,"1982":63,"1983":64,"1984":65,"1985":66,"1986":67,"1987":68,"1988":69,"1989":70},{"volume":758,"pages":760},{"VOID":759},"52",{"VOID":761},"363-371","1987-09-01",{"id":764,"createTime":765,"updateTime":766,"relativeEntities":767,"slug":768,"properties":769,"entityType":92,"verifyStatus":93,"verifyTime":780,"verifyNote":94,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19,"primaryUrl":781,"fullTextUrl":18,"authors":782,"publicationType":136,"publisherRelationship":798,"citationCount":18,"citationInfo":18,"publishDate":817,"publishYear":818,"citationAnalyzeStatus":17,"lastCitationAnalyze":766,"indexDatabases":18,"openAccess":18,"references":18,"isForceReanalyzing":225},"75bf6b94-f6ef-485e-80a2-bea3bc52f291","2024-02-07T11:42:47.647+00:00","2026-04-15T23:48:07.747+00:00",[],"In-situ-crosslinking-of-chlorophyll-to-protein-Use-of-specific-heterobifunctional-photoactivated-reagents",{"references":770,"abstract":772,"title":774,"doi":776,"gsPaper":778},{"VOID":771},"Anderson, J.M. &D.J. Goodchild: Lateral heterogeneity of thylakoid complexes and the transverse arrangement of the light-harvesting chlorophyll a\u002Fb protein of photosystem II of thylakoid membranes. Chem. Scr. 27B, 181–188 (1987)\nDeisenhofer, J., O. Epp, K. Miki, R. Huber &H. Michel: X-ray structure analysis of a membrane protein complex. Electron density map at 3 Å resolution and a model of the chromophores of the photosynthetic reaction center from Rhodopseudomonas viridis. J. Mol. Biol. 180, 385–398 (1984)\nFish, L.E., U. Kück &L. Bogorad: Two partially homologous adjacent light-inducible maize chloroplast polypeptides of the P700 Chl-a-protein complex of photosystem I. J. Biol. Chem. 260, 1413–1421 (1985a)\nFish, L.E., U. Kück & L. Bogorad: Analysis of the two partially homologous P700 chlorophylla proteins of maize photosystem I: prediction based on the primary sequences and features shared by other chlorophyll proteins. In: Molecular Biology of the Photosynthetic Apparatus (Stainback, K.E., S. Bonitz, C.J. Arntzen & L. Bogorad eds.) Publ.: Cold Spring Harbor Laboratory. pp. 111–120 (1985b)\nFord, R.C., D. Picot &R.M. Garavito: Crystallization of the photosystem I reaction centre. EMBO J. 6, 1581–1586 (1987)\nFujimori, E.: Chlorophyll-photosensitized reduction of triphenyltetrazolium chloride by hydrazine hydrate. J. Am. Chem. Soc. 77, 6495–6498 (1955)\nHenry, L.E.A., J.D. Mikkelsen &B.L. Møller: Pigment and acyl lipid composition of photosystem I and II vesicles and of photosynthetic mutants in barley. Carlsberg Res. Commun. 48, 131–148 (1983)\nHinz, U.G.: Isolation of the photosystem II reaction center complex from barley. Characterization by circular dichroism spectroscopy and amino acid sequencing. Carlsberg Res. Commun. 50, 285–298 (1985)\nHinz, U.G. &K.G. Welinder: The light-harvesting complex of photosystem II in barley. Structure and chlorophyll organization. Carlsberg Res. Commun. 52, 39–54 (1987)\nKarlin-Neumann, G.A., B.D. Kohorn, J.P. Thornber &E.M. Tobin: A chlorophyll a\u002Fb-protein encoded by a gene containing an intron with characteristics of a transposable element. J. Mol. Appl. Genetics 3, 45–61 (1985)\nMachold, O., D.J. Simpson &B.L. Møller: Chlorophyll proteins of thylakoids from wild type and mutants of barley (Hordeum vulgare). Carlsberg Res. Commun. 44, 235–254 (1979)\nMøller, B.L. &P.B. Høj: A thylakoid polypeptide involved in the reconstitution of photosynthetic oxygen evolution. Carlsberg Res. Commun. 48, 161–185 (1983)\nNabedryk, E., P. Biaudet, S. Darr, C.J. Arntzen &J. Breton: Conformation and orientation of Chl-proteins in photosystem I by circular dichroism and polarized infrared spectroscopies. Biochim. Biophys. Acta 767, 640–647 (1984)\nNabedryk, E., S. Andrianambinintsoa &J. Breton: Transmembrane orientation of α-helices in the thylakoid membrane and in the light-harvesting complex. A polarized infrared spectroscopy study. Biochim. Biophys. Acta 765, 380–387 (1984)\nNanba, O. &K. Satoh: Isolation of a photosystem II reaction center constisting of D1 and D2 polypeptides and cytochrome b559. Proc. Natl. Acad. Sci. USA 84, 109–112 (1987)\nPiccioni, R.G., P. Bennoun &N.-H. Chua: A nuclear mutant of Chlamydomonas reinhardii defective in photosynthetic photophosphorylation. Characterization of the alga coupling factor ATPase. Eur. J. Biochem. 117, 93–102 (1981)\nPlumley, F.G. &G.W. Schmidt: Reconstitution of chlorophyll a\u002Fb light-harvesting complexes: Xanthophyll-dependent assembly and energy transfer. Proc. Natl. Acad. Sci. USA 84, 146–150 (1987)\nOrtiz, W., E. Lam, S. Chollar, D. Munt &R. Malkin: Topography of the protein complexes of the chloroplast thylakoid membrane. Studies of photosystem I using a chemical probe and proteolytic digestion. Plant Physiol. 77, 387–397 (1985)\nSatoh, K.: Protein-pigments and photosystem II reaction center. Photochem. Photobiol. 42, 845–853 (1985)\nSiefermann-Harms, D. &H. Ninneman: Pigment organization in the light-harvesting chlorophyll-a\u002Fb protein complex of lettuce chloroplasts. Evidence obtained from protection of the chlorophylls against proton attack and from excitation engergy transfer. Photochem. Photobiol. 35, 719–731 (1982)\nWeller, A. &R. Livingston: The reaction of chlorophyll in amines. J. Am. Chem. Soc. 76, 1575–1578 (1954)\nZuber, H.: Structure and function of light-harvesting complexes and their polypeptides. Photochem. Photobiol. 42, 821–844 (1985)",{"EN":773},"It is shown that reagents containing one reactive amino group and one azide group crosslink chlorophyll to protein in situ. Using the light-harvesting complex of photosystem II as model system a small fraction of the chlorophylla, but no chlorophyllb was covalently bound to the protein. This confirms that chlorophylla is more accessible from the medium. 4-Azidoaniline, 4-azido-2-nitroaniline and 2-azido-4-chloroaniline are equally effective crosslinkers and are recommended as probes for the chlorophyll organization in native or reconstituted chlorophyll-protein complexes.",{"EN":775},"In situ crosslinking of chlorophyll to protein. Use of specific heterobifunctional photoactivated reagents",{"VOID":777},"10.1007\u002FBF02908304",{"VOID":779},"[\"6400730942547589809\"]","2024-05-07T12:59:39.452+00:00","http:\u002F\u002Flink.springer.com\u002F10.1007\u002FBF02908304",[783],{"id":784,"sortIndex":19,"researcher":18,"roles":785,"affiliations":786,"properties":795},"e9d94e2b-5de4-4e48-8e65-757b19904ad3",[586],[787],{"id":18,"sortIndex":19,"affiliation":788,"properties":18},{"id":789,"createTime":790,"updateTime":790,"relativeEntities":791,"slug":18,"properties":792,"entityType":114,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},"16e313fa-c717-4d4c-83bf-a273a3b47eb2","2023-12-19T20:09:34.733+00:00",[],{"title":793},{"VI":794},"Department of Physiology, Carlsberg Laboratory, Copenhagen Valby",{"title":796},{"VI":797},"Ursula G. Hinz",{"url":781,"publisher":799,"properties":812},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":800,"slug":10,"properties":801,"entityType":16,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19,"subjectFields":804,"manageAffiliations":805,"indexDatabases":806,"url":18,"thumbnailPath":18,"statistic":807,"gsStatistic":18,"type":18,"analyzePriority":18},[],{"issn":802,"title":803},{"VOID":13},{"EN":15},[],[],[],{"impactFactor":19,"impactFactorByYear":808,"i10Index":25,"i10IndexLast5Year":19,"totalPublication":26,"totalPublicationByYear":809,"totalCitation":39,"totalCitationByYear":810,"totalCitationPerPublication":55,"totalCitationPerPublicationByYear":811,"hindexLast5Year":30,"hindex":30},{},{"1976":28,"1977":29,"1978":30,"1979":31,"1980":32,"1981":33,"1982":34,"1983":35,"1984":36,"1985":33,"1986":37,"1987":29,"1988":31,"1989":38},{"1976":41,"1977":42,"1978":43,"1979":44,"1980":45,"1981":46,"1982":47,"1983":48,"1984":49,"1985":50,"1986":51,"1987":52,"1988":53,"1989":54},{"1976":57,"1977":58,"1978":59,"1979":60,"1980":61,"1981":62,"1982":63,"1983":64,"1984":65,"1985":66,"1986":67,"1987":68,"1988":69,"1989":70},{"volume":813,"pages":815},{"VOID":814},"54",{"VOID":816},"121-129","1989-05-01",1989,{"id":820,"createTime":821,"updateTime":822,"relativeEntities":823,"slug":824,"properties":825,"entityType":92,"verifyStatus":93,"verifyTime":822,"verifyNote":94,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19,"primaryUrl":834,"fullTextUrl":18,"authors":835,"publicationType":136,"publisherRelationship":863,"citationCount":18,"citationInfo":18,"publishDate":882,"publishYear":883,"citationAnalyzeStatus":17,"lastCitationAnalyze":18,"indexDatabases":18,"openAccess":18,"references":18,"isForceReanalyzing":225},"b5c6a43a-6848-46c9-a2b6-5a686f961c3c","2024-02-11T16:54:37.346+00:00","2025-01-26T23:35:51.962+00:00",[],"Dual-capacity-for-nutrient-uptake-in-tetrahymena-importance-of-the-oral-uptake-system-for-Fe-and-Cu-uptake",{"references":826,"abstract":828,"title":830,"doi":832},{"VOID":827},"Albert, A.: Selective Toxicity. London: Methuen and Co. Ltd.: New York: John Wiley and Sons, Inc. (1960)\nAngelici, R. J.: Stability of coordination compounds. In G. L. Eichorn (ed.) Inorganic Biochemistry, 63–101, Elsevier Scientific Publishing Company, Amsterdam-London-New York (1973)\nByers, B. R.: Iron transport in gram-positive and acid-fast Bacilli. In J. B. Neilands (ed.) Microbial Iron Metabolism, 83–105. Academic Press, New York (1974)\nConner R. L., &S. G. Cline: Iron deficiency and the metabolism ofTetrahymena pyriformis.J. Protozool. 11: 486–491 (1964)\nGaribaldi, J. A.: Influence of temperature on the biosynthesis of iron transport compounds bySalmonella typhimurium. J. Bact. 110: 262–265 (1972)\nHutner, S. H.: Inorganic nutrition. Ann. Rev. Microbiol. 26: 313–346 (1972)\nKitchings, J. A.: Food vacuoles. Protoplasmatologia 3: Ch D3b, 1–54 (1956)\nLevandowsky, M., &S. H. Hutner: Utilization of Fe3 by the inshore colorless marine dinoflagellateCrypthecodinium cohnii. Ann. N. Y. Acad. Sci. 245: 16–25 (1975)\nMast, S. O.: The food vacuole inParamecium. Biol. Bull. 92: 31–72 (1947)\nNeilands, J. B.: Iron and its role in microbial physiology. In J. B. Neilands (ed.) Microbial Iron Metabolism. A Comprehensive Treatise, 3–34. Academic Press, New York-London (1974)\nOrias, E., &N. A. Pollock: Heat-sensitive development of the phagocytotic organelle in aTetrahymena mutant. Exptl. Cell. Res. 90: 345–357 (1975)\nRasmussen L., H. E. Buhse, Jr., &K. Groh: Efficiency of filter feeding in two species ofTetrahymena. J. Protozool 22: 110–111 (1975)\nRasmussen, L., &I. Modeweg-Hansen: Cell multiplication inTetrahymena cultures after addition of particulate material. J. Cell Sci. 12: 275–286 (1973)\nRasmussen, L., &E. Orias:Tetrahymena: Growth without phagocytosis. Science 190: 464–465 (1975)\nRosenberg, H., &I. G. Young: Iron transport in the enteric bacteria. In J. B. Neilands (ed.) Microbial Iron Metabolism, 67–82. Academic Press, New York-London (1974)\nSillén, I. G., &A. E. Martell: Stability constants of metal-ion complexes. Special Publication. No. 17 of the Chemical Society, Burlington House, London, W. I. (1964)\nWichterman, R.: The Biology of Paramecium. The Blakiston Co., Inc., New-York-Toronto. (1953)",{"EN":829},"We have reported that a mutant ofTetrahymena pyriformis with heat-sensitive development of the oral apparatus can be grown indefinitely without food vacuoles if the medium is supplemented with folinic acid and a mixture of trace metal salts. We report here that the trace metal mixture can be replaced completely and specifically by salts of iron and copper. Fe(II) and Fe(III) are interchangeable. Addition of citrate has proven useful to reduce precipitate formation and improve the reproducibility of growth of the mutant cell. Thus it appears to serve as an Fe buffer. From the increased concentrations of Fe and Cu required to permit good growth of the mutant strain at 37°C, we conclude that the oral uptake system plays a much more important role in the case of these two metals than the surface uptake system. The oral uptake system may facilitate Fe uptake in at least two ways: a) by a mechanical concentration of precipitates affected by the ciliary membranelles surrounding the oral cavity and, b) by lowering of the pH of the food vacuole and thereby releasing Fe from precipitates and from complexes which cannot be transported across the membrane as such. The second factor may also be important in Cu uptake. A specific effect of Mg and Fe uptake or retention in the mutant strain growing without food vacuoles has been detected. The significance of this effect remains unclear. Practical implications of the findings are discussed.",{"EN":831},"Dual capacity for nutrient uptake in tetrahymena importance of the oral uptake system for Fe and Cu uptake",{"VOID":833},"10.1007\u002FBF02906419","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002FBF02906419",[836,851],{"id":837,"sortIndex":101,"researcher":18,"roles":838,"affiliations":839,"properties":848},"f582e222-37bc-4852-a9f3-5fac90f9ae54",[586],[840],{"id":18,"sortIndex":19,"affiliation":841,"properties":18},{"id":842,"createTime":843,"updateTime":843,"relativeEntities":844,"slug":18,"properties":845,"entityType":114,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},"1b4260db-5daf-4413-b9e2-54681ec13cc0","2023-12-14T05:12:47.647+00:00",[],{"title":846},{"VI":847},"The Biological Institute of the Carlsberg Foundation, Copenhagen N",{"title":849},{"VI":850},"Eduardo Orias",{"id":852,"sortIndex":19,"researcher":18,"roles":853,"affiliations":854,"properties":860},"5eeb9cdf-8357-4d3d-a973-60890423a7fc",[586],[855],{"id":18,"sortIndex":19,"affiliation":856,"properties":18},{"id":842,"createTime":843,"updateTime":843,"relativeEntities":857,"slug":18,"properties":858,"entityType":114,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":859},{"VI":847},{"title":861},{"VI":862},"Leif Rasmussen",{"url":834,"publisher":864,"properties":877},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":865,"slug":10,"properties":866,"entityType":16,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19,"subjectFields":869,"manageAffiliations":870,"indexDatabases":871,"url":18,"thumbnailPath":18,"statistic":872,"gsStatistic":18,"type":18,"analyzePriority":18},[],{"issn":867,"title":868},{"VOID":13},{"EN":15},[],[],[],{"impactFactor":19,"impactFactorByYear":873,"i10Index":25,"i10IndexLast5Year":19,"totalPublication":26,"totalPublicationByYear":874,"totalCitation":39,"totalCitationByYear":875,"totalCitationPerPublication":55,"totalCitationPerPublicationByYear":876,"hindexLast5Year":30,"hindex":30},{},{"1976":28,"1977":29,"1978":30,"1979":31,"1980":32,"1981":33,"1982":34,"1983":35,"1984":36,"1985":33,"1986":37,"1987":29,"1988":31,"1989":38},{"1976":41,"1977":42,"1978":43,"1979":44,"1980":45,"1981":46,"1982":47,"1983":48,"1984":49,"1985":50,"1986":51,"1987":52,"1988":53,"1989":54},{"1976":57,"1977":58,"1978":59,"1979":60,"1980":61,"1981":62,"1982":63,"1983":64,"1984":65,"1985":66,"1986":67,"1987":68,"1988":69,"1989":70},{"volume":878,"pages":880},{"VOID":879},"41",{"VOID":881},"81-90","1976-03-01",1976,{"id":885,"createTime":886,"updateTime":887,"relativeEntities":888,"slug":889,"properties":890,"entityType":92,"verifyStatus":93,"verifyTime":899,"verifyNote":94,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19,"primaryUrl":900,"fullTextUrl":18,"authors":901,"publicationType":136,"publisherRelationship":968,"citationCount":18,"citationInfo":18,"publishDate":297,"publishYear":298,"citationAnalyzeStatus":17,"lastCitationAnalyze":18,"indexDatabases":18,"openAccess":18,"references":18,"isForceReanalyzing":225},"17540e73-d799-4107-96be-823540c3dc2c","2023-12-29T23:43:09.510+00:00","2025-01-06T23:34:47.619+00:00",[],"Molecular-basis-of-cooperativity-in-vertebrate-muscle-thin-filaments",{"references":891,"abstract":893,"title":895,"doi":897},{"VOID":892},"Brandt, P.W., J.P. Reuben, H. Grundfest: Regulation of tension in the skinned crayfish muscle fiber. II. Role of calcium. J. Gen. Physiol. 59, 305–317 (1972)\nBrandt, P.W., E. Chappel &B.R. Jewel: A robust transducer suitable for measuring forces of 1 μN. J. Physiol., London 258, 43–44 (1976)\nBrandt, P.W., R.N. Cox &M. Kawai: Can the binding of Ca2+ to two regulatory sites on troponin-C determine the steeps pCa\u002Ftension relationship of skeletal muscle? Proc. Natl. Acad. Sci. USA 77, 4717–4720 (1980)\nBrandt, P.W., R.N. Cox, M. Kawai &T. Robinson: Regulation of tension in skinned muscle fibers: Effect of cross-bridge kinetics on apparent Ca2+ sensitivity. J. Gen. Physiol. 79, 997–1016 (1982)\nBrandt, P.W., B. Gluck, M. Mini & C.E. Cerri: Regulation of tension in skinned muscle fibers: Hysteresis of the mammalian pCa\u002Ftension relation is small and muscle specific. Submitted\nBremel, R.D. &A. Weber: Cooperation within actin filament in vertebrate skeletal muscle. Nature New Biol. 238, 97–101 (1972)\nBriggs, M.M. &F.H. Schachat: Heterogeneity of thin filament calcium regulatory proteins of rabbit skeletal muscle. Biophysical J. 41, 297a (1983)\nBronson, D.D. &F.H. Schachat: Heterogeneity of contractile proteins: Differences in tropomyosin from fast, slow, and mixed skeletal muscles of the rabbit. J. Biol. Chem. 257, 3937–3945 (1982)\nChalovich, J.M. &E. Eisenberg: Inhibition of actomyosin ATPase activity by troponin-tropomyosin without blocking the binding of myosin to actin. J. Biol. Chem. 257(5), 2432–2437 (1982)\nChantler, P.: Retreats from the steric blocking of muscle-contraction. Nature 298(5870), 120–121 (1982)\nCox, J.A., M. Comte &E.A. Stein: Calmodulin-free skeletal muscle troponin C prepared in the absence of urea. Biochem. J. 195, 205–211 (1981)\nEastwood, A.B., D.S. Wood, K.L. Bock &M.M. Sorenson: Chemically skinned mammalian skeletal muscle. I. The structure of skinned rabbit psoas. Tissue & Cell 11, 553–566 (1979)\nEisenberg, E. &W.W. Kielley: Troponin-tropomyosin complex. Column chromatographic separation and activity of the three, active troponin components with and without tropomyosin present. J. Biol. Chem. 249(15), 4742–4748 (1974)\nFerenzi, M.A., R.M. Simmons &J.A. Sleep: General considerations of cross-bridge models in relation to the dependence on MgATP concentration or mechanical parameters of skinned fibers from frog. In Basic biology of muscle: A comparative approach. B.M. Twarog, R.J.C. Levine & M. Dewey Eds. Raven Press, N.Y., USA, pp. 223–243 (1982)\nFlicker, P.F., G.N. Phillips &C. Cohen: Troponin and its interactions with tropomyosin: An electron microscope study. J. Mol. Biol. 162, 495–501 (1982)\nGreene, L.E. &E. Eisenberg: Cooperative binding of myosin subfragment-1 to the actin-troponin-tropomyosin complex. Proc. Nat. Aca. Sci. USA 77, 2616–2620 (1980)\nGreene, L.: The effect of nucleotide on the binding of myosin subfragment 1 to regulated actin. J. Biol. Chem. 257, 13993–13999 (1982)\nHazelgrove, J.C.: X-ray evidence for a comformational change in the actin-containing filaments of vertebrate striated muscle. Cold Spring Harbor Symp. Quan Biol. 37, 341–359 (1972)\nHill, T.L., E. Eisenberg &L. Greene: Theoretical model for the cooperative equilibrium binding of myosin subfragment 1 to the actin-troponin-tropomyosin complex. Proc. Natl. Acad. Aci. USA 77, 3186–3190 (1980)\nHill, T.L., E. Eisenberg &L.E. Greene: Alternate model for the cooperative equilibrium binding of myosin subfragment-1-nucleotide complex to actin-troponin-tropomyosin. Proc. Natl. Acad. Sci. USA 80(1), 60–64 (1983)\nHuxley, H.E.: Structural changes in the actin- and myosin-containing filaments during contraction. Cold Spring Harbor Symp. Quan Biol. 37, 361–376 (1972)\nKawai, M. &M. Orentlicher: Effect of inorganic phosphate (P1), substrate (MgATP), and excess ATP on complex stiffness of skinned crayfish muscle fibers and glycerinated rabbit psoas muscle bundles. Biophysical J. 16, 152a (1976)\nLaemmli, U.K.: Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227(259), 680–685 (1970)\nLoxdale, H.D. &R.T. Tregear: Generation of tension by glycerol-extracted vertebrate skeletal fibres in the absence of calcium. J. Muscle Research & Cell Motility 4, 543–556 (1983)\nMoss, R.L., G.G. Giulian &M.L. Greaser: Effects of EDTA treatment upon the protein subunit composition and mechanical properties of mammalian single skeletal muscle fibers. J. Cell Biol. 96, 970–978 (1983a)\nMoss, R.L., A.E. Swinford &M.L. Greaser: Alterations in the Ca2+ sensitivity of tension development by single skeletal muscle fibers at stretched lengths. Biophysical J. 43, 115–120 (1983b)\nNagashima, H. &S. Asakura: Studies on cooperative properties of tropomyosin-actin and tropomyosin-troponin-actin complexes by the use of N-ethylmaleimide treated and untreated species of myosin subfragment-1. J. Mol. Biol. 155, 409–428 (1982)\nOrentlicher, M., J.P. Reuben, H. Grundfest &P.W. Brandt: Calcium binding and tension development in detergent-treated muscle fibers. J. Gen. Physiol. 63, 168–186 (1974)\nParry, D.A.D. &J.M. Squires: Structural role of tropomyosin in muscle regulation. Analysis of the X-ray patterns from relaxed and contracting muscle. J. Mol. Biol. 37, 251–262 (1973)\nPemrick, S. &A. Weber: Mechanism of inhibition of relaxation by N-ethylmaleimide treatment of myosin. Biochemistry 15, 5193–5198 (1976)\nPotter, J.D. &J. Gergely: The calcium and magnesium binding sites on troponin and their role in the regulation of myofibrillar adenosine triphosphatase. J. Biol. Chem. 250, 4628–4633 (1975)\nReuben, J.P., P.W. Brandt, M. Berman &H. Grundfest: Regulation of tension in the skinned crayfish muscle fiber. I. Contraction and relaxation in the absence of Ca (pCa>9). J. Gen. Physiol. 57, 385–407 (1971)\nSchachat, F.H., A.D. Magid, D.D. Bronson &O.B. McDonald: Gene expression in single muscle fibers from rabbit skeletal muscles. J. Cell Biol. 87, 263a (1980)\nSchachat, F.H., D.D. Bronson &O.B. McDonald: Two different kinds of SO muscle fibers which differ in their myosin light chain complements. FEBS lett. 122, 80–82 (1980)\nSobieszek, A.: Steady-state kinetic studies on the actin activation of skeletal-muscle heavy-meromyosin subfragments-effects of skeletal, smooth and non-muscle tropomyosins. J. Mol. Biol. 157(2), 275–286 (1982)\nTrueblood, C.E., T.P. Walsh &A. Weber: Is the steric model of tropomyosin actin valid? In: Basic Biology of Muscle: A comparative approach. B.M. Twarog, R.J.C. Levine & M. Dewey Eds. Ravel Press, N.Y. USA, pp. 223–243 (1982)\nWalsh, T.P. &Wegner A.: Effect of the state of cysteine 190 of tropomyosin on the assembly of the actin-tropomyosin complex. Biochim. Biophys. Acta 626, 79–87 (1980)\nWeber, A.: Parallel response of myofibrillar contraction and relaxation to four different nucleotide triphosphates. J. Gen. Physiol. 55, 781–791 (1969)\nWood, D.S., J. Zollman, J.P. Reuben &P.W. Brandt: Human skeletal muscle: properties of the “chemically skinned” fiber. Science 187, 1075–1076 (1975)",{"EN":894},"Extraction of as little as one troponin C per regulatory strand on a thin filament reduces the slope of the pCa\u002Ftension relation thus the regulatory units along a thin filament of rabbit psoas fibers are linked cooperatively so that a thin filament activates as a unit. This explains why the pCa\u002Ftension relation in skinned fibers has a slope much higher than can be expected by binding of Ca2+ to one regulatory unit (Brandt et al. 1980;Brandt et al. 1982). These results also show that troponin C is the only myfibrillar component responsible for calcium sensitivity in psoas muscle.",{"EN":896},"Molecular basis of cooperativity in vertebrate muscle thin filaments",{"VOID":898},"10.1007\u002FBF02913943","2025-01-06T23:34:47.618+00:00","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002FBF02913943",[902,917,929,944,956],{"id":903,"sortIndex":58,"researcher":18,"roles":904,"affiliations":905,"properties":914},"16ba5f46-7a85-4e85-8d9b-4e0d21a29a06",[586],[906],{"id":18,"sortIndex":19,"affiliation":907,"properties":18},{"id":908,"createTime":909,"updateTime":909,"relativeEntities":910,"slug":18,"properties":911,"entityType":114,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},"eeef7254-1f96-4bdd-bcbc-d57c40054fd0","2024-01-08T21:19:57.533+00:00",[],{"title":912},{"VI":913},"Department of Anatomy and Cell Biology, Columbia University, New York, USA",{"title":915},{"VI":916},"M. 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Bacteriol. 101, 505–512 (1970)\nBuckholz, R.G. &B.G. Adams: Induction and genetics of two α-galactosidase activities in Saccharomyces cerevisiae. Mol. Gen. Genet. 182, 77–81 (1981)\nCameron, J.R., P. Philippsen &R.W. Davis: Analysis of chromosomal integration and deletions of yeast plasmids. Nucl. Acids Res. 4, 1429–1448 (1977)\nCarlson M. &D. Botstein: Organization of the SUC gene family in Saccharomyces. Mol. Cell. Biol. 3, 351–359 (1983)\nCramer, J.H., F.W. Farrelly &R.H. Rownd: Restriction endonuclease analysis of ribosomal DNA from Saccharomyces cerevisiae. Mol. Gen. Genet. 148, 233–241 (1976)\nDelihas, N. &J. Andersen: Generalized structures of the 5S ribosomal RNAs. Nucl. Acids Res. 10, 7323–7344 (1982)\nDenhardt, D.T.: A membrane-filter technique for the detection of complementary DNA. Biochem. Biophys. Res. Comm. 23, 641–646 (1966)\nDonhauser, S., H. Ritter & J. Schmitt: Genetische Variabilität der Alkoholdehydrogenasen bei Saccharomyces. Proc. 18th Europ. Brewery Conv. Congr. Copenhagen. 187–196 (1981)\nErdmann, V.A., E. Huysmans, A. Vanderberghe &R. De Wachter: Collection of published 5S and 5.8S ribosomal sequences. Nucl. Acids Res. 11, r105-r123 (1983)\nGjermansen, C. &P. Sigsgaard: Construction of a hybrid brewing strain of Saccharomyces carlsbergensis by mating of meiotic segregants. Carlsberg Res. Commun. 46, 1–11 (1981)\nHolmberg, S., J.G.L. Petersen, T. Nilsson-Tillgren &M.C. Kielland-Brandt: Molecular characterization of a Saccharomyces plasmid containing theHIS4 gene. Carlsberg Res. Commun. 44, 269–282 (1979)\nHolmberg, S.: Genetic differences between Saccharomyces carlsbergensis and S. cerevisiae II. Restriction endonuclease analysis of genes in chromosome III. Carlsberg Res. Commun. 47, 233–244 (1982)\nHolmes, D.S. &M. Quigley: A rapid boiling method for the preparation of bacterial plasmids. Anal. Biochem. 114, 193–197 (1981)\nJeffreys, A.J. &R.A. Flavell: A physical map of the DNA regions flanking the rabbit β-globin gene. Cell 12, 429–439 (1977)\nJohannsen, E. &J.P. van der Walt: Interfertility as basis for the delimitation of Kluyveromyces marxianus. Arch. Microbiol. 118, 45–48 (1978)\nManiatis T., E.F. Fritsch & J. Sambrook: Molecular cloning. A laboratory manual. Cold Spring Harbor Laboratory (1982)\nNilsson-Tillgren, T., C. Gjermansen, M.C. Kielland-Brandt, J.G.L. Petersen &S. Holmberg: Genetic differences between Saccharomyces carlsbergensis and S. cerevisiae. Analysis of chromosome III by single chromosome transfer. Carlsberg Res. Commun. 46, 65–76 (1981)\nPeacock, A.C. &C.W. Dingman: Molecular weight estimation and separation of ribonucleic acid by electrophoresis in agarose-acrylamide composite gels. Biochemistry 7, 668–674 (1968)\nPedersen, M.B.: Fingerprinting of DNA in the identification of yeast. Proc. 19th Europ. Brewery Conv. Congr. London, pp. 457–463 (1983)\nPetes, T.D., L.M. Hereford &K.G. Skryabin: Characterization of two types of yeast ribosomal DNA genes. J. Bacteriol. 134, 295–305 (1978)\nPetes, T.D., S. Smolik-Utlaut &T. Zamb: Genetic analysis of the repeating ribosomal DNA genes of yeast. In: Molecular Genetics in Yeast. Alfred Benzon Symposium 16. Eds: D. von Wettstein, J. Friis, M. Kielland-Brandt & A. Stenderup. Munksgaard. Copenhagen, pp. 137–151 (1981)\nPetes, T.D.: Meiotic mapping of yeast ribosomal deoxyribonucleic acid on chromosome XII. J. Bacteriol. 138, 185–192 (1979)\nPhilippsen, P., R.A. Kramer &R.W. Davis: Cloning of the yeast ribosomal DNA repeat unit in SstI and HindIII lambda vectors using genetic and physical size selection. J. Mol. Biol. 123, 371–386 (1978)\nPhilippsen, P., M. Thomas, R.A. Kramer &R.W. Davis: Unique arrangement of coding sequences for 5S, 5.8S, 18S, 25S ribosomal RNA in Saccharomyces cerevisiae as determined by R-loop and hybridization analysis. J. Mol. Biol. 123, 287–404 (1978)\nPrice, C.W., G.B. Fuson &H.J. Phaff: Genome comparison in yeast systematics: Species within the genera Schwanniomyces, Saccharomyces, Debaryomyces and Picia. Microbiol. Rev. 42, 161–193 (1978)\nRigby, P.W.J., M. Dieckmann, C. Rhodes &P. Berg: Labeling deoxyribonucleic acid to high specific activity in vitro by nick translation with DNA polymerase I. J. Mol. Biol. 113, 237–251 (1977)\nRosenthal, A.L. &A. Saifer: Continuous monitoring of fluorogenic substrates I. Kinetic analysis of N-acetyl-β-D-hexosaminidases. Anal. Biochem. 55, 85–92 (1973)\nRosini, G., F. Federici, A.E. Vaughan &A. Martini: Systematics of the species of the genus Saccharomyces associated with the fermentation industry. European J. Appl. Microbiol. Biotechnol. 15, 188–193 (1982)\nSchweitzer, E., C. MacKechnie &H.O. Halvorson: The redundancy of ribosomal and transfer RNA genes in Saccharomyces cerevisiae. J. Mol. Biol. 40, 261–277 (1969)\nSherman, F., G.R. Fink &J.B. Hicks: Methods in Yeast Genetics. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y. 11724. pp 61–64 (1979)\nSouthern, E.M.: Detection of specific sequences among DNA fragments separated by gel electrophoresis. J. Mol. Biol. 98, 504–517 (1975)\nTorczynski, R., A.P. Bollon &M. Fuke: The complete nucleotide sequence of the rat 18S ribosomal RNA gene and comparison with the respective yeast and frog genes. Nucl. Acids Res. 11, 4879–4890 (1983)\nvan der Walt, J.P.: Genus Saccharomyces. In: The Yeasts, a Taxonomic Study. J. Lodder, ed. North-Holland Publishing Company. Amsterdam London pp. 555–718 (1970)\nVerbeet, M.Ph., J. Klootwijk, H. van Heerikshuisen, R. Fontijn, E. Vreugdenhil &R.J. Planta: Molecular cloning of the rDNA of Saccharomyces rosei and comparison of its transcription initiation region with that of Saccharomyces carlsbergensis. Gene 23, 53–63 (1983)\nWettstein, D. von: Emil Christian Hansen Centennial Lecture. From pure culture to genetic engineering of brewers yeast. Proc. 19th Europ. Brewery Conv. Congr. London, pp. 97–119 (1983)\nWinge, Ø. &O. Laustsen: On 14 new yeast types, produced by hybridization. Compt. Rend. Lab. Carlsberg, Ser. Physiol., 22, 337–352 (1939)\nYamazak, M., S. Goto &K. Komagata: Comparison of enzymes from strains of wine yeast and their related yeasts on electrophoresis. J. Inst. Enol. Vitic. Yamanashi Univ. 17, 11–19 (1982)\nYarrow, D. &T. Nakase: DNA base compositions of the genus Saccharomyces. Antonie van Leeuwenhoek 41, 81–88 (1975)",{"EN":1303},"The region of chromosome XII containing theRDN1 gene which encodes the cytosolic ribosomal RNA molecules and the region of chromosome III containing theHIS4 (histidine 4) gene were analysed in 30 lager yeast strains, 11 ale strains and 20 strains from a number of different species in the genus Saccharomyces. With the aid of restriction endonuclease fragment patterns and cloned probes to theRDN1 gene of S. cerevisiae three forms of this gene were identified, two of them corresponding to the previously known forms I and II and a third one characterized by an additional HindIII site located in the 3′ spacer region. A more distantly related form of theRDN1 gene containing a single HindIII restriction site was found in Saccharomyces fermentati and one form without any HindIII site in a wild yeast contaminant. With the help of the restriction endonuclease fragments derived from theHIS4 region seven genotypes can be recognized. They result from various combinations of three restriction endonuclease fragment patterns designated I, II and III, each pattern represents a chromosome. All lager strains are homozygous for form II of the ribosomal RNA gene and heterozygous for patterns I and II of theHIS4 gene. An exception is one German brewing strain which is homozygous for pattern II. With one exception the ale strains were homozygous for form II of theRDN1 gene and for pattern I of theHIS4 gene. One British strain contains form I of theRDN1 gene. Bakers yeast, S. diastaticus and S. italicus are homozygous for form I of theRDN1 gene and for pattern I of theHIS4 gene. In S. bayanus and S. pastorianus homozygosity for form III of theRDN1 gene was combined with heterozygosity for patterns II and III of theHIS4 gene. S. uvarum is homozygous for both form III of theRDN1 gene and pattern III of theHIS4 gene. Form III of theRDN1 gene and patterns I and II of theHIS4 gene were combined in a Chinese brewing strain and a strain designated as a type strain of S. carlsbergensis. The nucleotide sequence polymorphisms are useful markers for strain characterization in addition to the generally used fermentation properties.",{"EN":1305},"DNA sequence polymorphisms in the genus Saccharomyces. I. Comparison of theHIS4 and ribosomal RNA genes in lager strains, ale strains and various species",{"VOID":1307},"10.1007\u002FBF02908692","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002FBF02908692",[1310],{"id":1311,"sortIndex":19,"researcher":18,"roles":1312,"affiliations":1313,"properties":1329},"c0329caa-8998-4646-9ef9-478683914f1a",[586],[1314,1324],{"id":1315,"sortIndex":101,"affiliation":1316,"properties":1323},"262f80a8-b9e2-42a9-a88b-031625bb4ea3",{"id":1317,"createTime":1318,"updateTime":1318,"relativeEntities":1319,"slug":18,"properties":1320,"entityType":114,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},"2bfa6a0e-fdb5-4468-82f3-8b1a2447b3ce","2023-12-05T21:53:39.510+00:00",[],{"title":1321},{"VI":1322},"Department of Brewing Chemistry, Carlsberg Research Laboratory, Copenhagen Valby",{},{"id":18,"sortIndex":19,"affiliation":1325,"properties":18},{"id":789,"createTime":790,"updateTime":790,"relativeEntities":1326,"slug":18,"properties":1327,"entityType":114,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":1328},{"VI":794},{"title":1330},{"VI":1331},"Mogens Bohl Pedersen",{"url":1308,"publisher":1333,"properties":1346},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":1334,"slug":10,"properties":1335,"entityType":16,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19,"subjectFields":1338,"manageAffiliations":1339,"indexDatabases":1340,"url":18,"thumbnailPath":18,"statistic":1341,"gsStatistic":18,"type":18,"analyzePriority":18},[],{"issn":1336,"title":1337},{"VOID":13},{"EN":15},[],[],[],{"impactFactor":19,"impactFactorByYear":1342,"i10Index":25,"i10IndexLast5Year":19,"totalPublication":26,"totalPublicationByYear":1343,"totalCitation":39,"totalCitationByYear":1344,"totalCitationPerPublication":55,"totalCitationPerPublicationByYear":1345,"hindexLast5Year":30,"hindex":30},{},{"1976":28,"1977":29,"1978":30,"1979":31,"1980":32,"1981":33,"1982":34,"1983":35,"1984":36,"1985":33,"1986":37,"1987":29,"1988":31,"1989":38},{"1976":41,"1977":42,"1978":43,"1979":44,"1980":45,"1981":46,"1982":47,"1983":48,"1984":49,"1985":50,"1986":51,"1987":52,"1988":53,"1989":54},{"1976":57,"1977":58,"1978":59,"1979":60,"1980":61,"1981":62,"1982":63,"1983":64,"1984":65,"1985":66,"1986":67,"1987":68,"1988":69,"1989":70},{"volume":1347,"pages":1349},{"VOID":1348},"48",{"VOID":1350},"485-503","1983-09-01",1983]