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Biochem. 37, 157–223.",{},{"id":20,"text":401,"url":20,"identifiers":402},"Ohnishi, M., Yamashita, T., and Hiromi, K. (1976) J. Biochem. 79, 1007–1012.",{},{"id":20,"text":404,"url":20,"identifiers":405},"Pazur, J. H., and Aronson, N. N. Jr. (1972). Adv. Carbohydrate Chem. Biochem. 27, 301–341.",{},{"id":20,"text":407,"url":20,"identifiers":408},"Pazur, J. H., and Kleppe, K. (1962). J. Biol. Chem. 237, 1002–1006.",{},{"id":20,"text":410,"url":20,"identifiers":411},"Pazur, J. H., French, D., and Knapp, D. W. (1950). Proc. Iowa. Acad. Sci. 57, 203–209.",{},{"id":20,"text":413,"url":20,"identifiers":414},"Pazur, J. H., Kleppe, K., and Anderson, J. S. (1962). Biochem. Biophys. Acta 65, 369–372.",{},{"id":20,"text":416,"url":20,"identifiers":417},"Pazur, J. H., Kleppe, K., and Ball, E. M. (1963). Arch. Biochem. Biophys. 103, 515–518.",{},{"id":20,"text":419,"url":20,"identifiers":420},"Pazur, J. H., Knull, H. R., and Simpson, D. L. (1970). Biochem. Biophys. Res. Commun. 40, 110–116.",{},{"id":20,"text":422,"url":20,"identifiers":423},"Pazur, J. H., Knull, H. R., and Cepure, A. (1971). Carbohydrate Res. 20, 83–96.",{},{"id":20,"text":425,"url":20,"identifiers":426},"Pazur, J. H., Tominaga, Y., Forsberg, L. S., and Simpson, D. L. (1980). Carbohydrate Res. 84, 103–114.",{},{"id":20,"text":428,"url":20,"identifiers":429},"Pazur, J. H., Forry, K. R., Tominaga, Y., and Ball, E. M. (1981). Biochem. Biophys. Res. Commun. 100, 420–426.",{},{"id":20,"text":431,"url":20,"identifiers":432},"Pazur, J. H., Tominaga, Y., and Kelly, S. (1984). J. Protein Chem. 3, 49–62.",{},{"id":20,"text":434,"url":20,"identifiers":435},"Pazur, J. H., DeHoff, D. K., Miskiel, F. J., and Baumrucker, C. R. (1986). Carbohydrate Res. 149, 137–147.",{},{"id":20,"text":437,"url":20,"identifiers":438},"Rosenthal, A. L., and Nordin, J. H. (1975). J. Biol. Chem. 256, 5295–5303.",{},{"id":20,"text":440,"url":20,"identifiers":441},"Simon, J. P., Schorr, J. M., and Phillips, A. T. (1974). J. Biol. Chem. 249, 1993–1999.",{},{"id":20,"text":443,"url":20,"identifiers":444},"Svensson, B., Pedersen, T. G., Svendsen, I., Sakai, T., and Ottensen, M. (1982). Carlsberg Res. Commun. 47, 55–69.",{},{"id":20,"text":446,"url":20,"identifiers":447},"Svensson, B., Larsen, K., Svendsen, I., and Boel, E. (1983). Carlsberg Res. Commun. 48, 529–544.",{},{"id":20,"text":449,"url":20,"identifiers":450},"Svensson, B., Larsen, K., and Gunnarsson, A. (1986) Eur. J. Biochem. 154, 497–502.",{},{"id":20,"text":452,"url":20,"identifiers":453},"Underkofler, L. A. (1969). Adv. Chem. Ser. 95, 343–358.",{},{"id":20,"text":455,"url":20,"identifiers":456},"Weber, K., and Osborn, M. (1969). J. Biol. Chem. 244, 4406–4412.",{},{"id":458,"createTime":459,"updateTime":460,"relativeEntities":461,"slug":462,"properties":463,"entityType":59,"verifyStatus":60,"verifyTime":474,"verifyNote":62,"languages":20,"translateLanguages":20,"viewCount":21,"primaryUrl":475,"fullTextUrl":20,"authors":476,"publicationType":155,"publisherRelationship":548,"citationCount":21,"citationInfo":568,"publishDate":571,"publishYear":569,"citationAnalyzeStatus":351,"lastCitationAnalyze":572,"indexDatabases":573,"openAccess":20,"references":20,"isForceReanalyzing":248},"8d6ba566-2465-4148-8159-587dcd3b6819","2024-01-13T17:24:03.746+00:00","2026-07-23T22:30:01.030+00:00",[],"Sequence-of-a-new-Bowman-Birk-inhibitor-fromTorresea-acreana-seeds-and-comparison-withTorresea-cearensis-trypsin-inhibitor-TcTI2-",{"abstract":464,"title":466,"gsPaper":468,"references":470,"doi":472},{"EN":465},"TaTI (Torresea acreana trypsin inhibitor), a new member of the Bowman-Birk trypsin inhibitor family, was purified from seeds ofTorresea acreana, one of the two known species ofTorresea, a Brazilian native Leguminosae of the Papilionoideae subfamily. Purification was performed by acetone fractionation, anion-exchange chromatography, and gel filtration. The TaTI appears asM\nr 7000 in SDS-PAGE under reducing conditions. There are 63 amino acid residues present in the TaTI sequence, which was confirmed by mass spectrometry (8388 daltons). The putative reactive sites residues were Lys-15 and Arg-42 at the first and second site, respectively. The antibodies raised against TcTI2,Torresea cearensis trypsin inhibitor 2, showed a cross-reaction with TaTI, but not with other Bowman-Birk inhibitors purified from Leguminosae. The inhibition constants of TaTI and TcTI2 were comparable when measured against trypsin, chymotrypsin, and factor XIIa, but not on plasmin. The latter was tenfold more effectively inhibited by TcTI2 then by TaTI. Neither TaTI nor TcTI2 affects thrombin, plasma kallikrein, or factor Xa.",{"EN":467},"Sequence of a new Bowman-Birk inhibitor fromTorresea acreana seeds and comparison withTorresea cearensis trypsin inhibitor (TcTI2)",{"VOID":469},"[\"17774925645999158532\"]",{"VOID":471},"Chase, T., and Shaw, E. (1970). Titration of trypsin, plasmin and thrombin withp-nitrophenyl-p-guanidinobenzoate HCl,Meth. Enzymol. 19, 20–27.\nErlanger, B. F., Kokowsky, N., and Cohen, E. (1961). Preparation and properties of two new chromogenic substrates of trypsin,Arch. Biochem. Biophys. 95, 271–278.\nGreen, T. R., and Ryan, C. (1972). Wound-induced proteinase inhibitor in plant leaves. A possible defense mechanism against insects,Science 175, 776–777.\nHopp, T. P., and Woods, K. R. (1981). Prediction of protein determinants from amino acid sequences,Proc. Natl. Acad. Sci. USA 78, 3824–3828.\nKennedy, A. R. (1993a).In vitro studies of anticarcinogenic protease inhibitors, inProtease Inhibitors as Cancer Chemopreventive Agents (Troll, W., and Kennedy, A. R., eds.), Plenum Press, New York, pp. 65–91.\nKennedy, A. R. (1993b). Overview of anticarcinogenic activity of protease inhibitors, inProtease Inhibitors as Cancer Chemopreventive Agents (Troll, W., and Kennedy, A. R., eds.), Plenum Press, New York, pp. 9–64.\nLaemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4,Nature 227, 680–685.\nLaskowski, M., Jr., and Kato, I. (1980). Protein inhibitors of proteinases,Annu. Rev. Biochem. 49, 593–626.\nLin, G., Bode, W., Huber, R., Chi, C., and Engh, R. A. (1993). The 0.25-nm X-ray structure of the Bowman-Birk-type inhibitor from mung bean in ternary complex with porcine trypsin,Eur. J. Biochem. 212, 549–555.\nNeurath, H. (1984). Evolution of proteolytic enzymes,Science 224, 350–357.\nNilsson, B. O., and Larsson, A. (1990). Intrasplenic immunization with minute amounts of antigen,Immunol. Today 11, 10–12.\nOdani, S., and Ikenaka, T. (1972). Studies on soybean trypsin inhibitors. IV. Complete amino acid sequence and the anti-proteinase sites of Bowman-Birk soybean proteinase inhibitor,J. Biochem. 71, 839–848.\nOdani, S., Koide, T., and Ono, T. (1986). Wheat germ trypsin inhibitors. Isolation and structural characterization of single-headed and double-headed inhibitors of the Bowman-Birk type,J. Biochem. 100, 975–983.\nOliva, M. L. V., Grisolia, D., Sampaio, M. U., and Sampaio, C. A. M. (1982). Properties of highly purified human plasma kallikrein,Agents Actions 9, 52–57.\nRichardson, M. (1987). The proteinase inhibitors of plants and microorganisms,Phytochemistry 16, 159–169.\nRichardson, M. (1991). Seed storage proteins. The enzyme inhibitors,Meth. Plant Biochem. 5, 259–305.\nSampaio, C. A. M., Wong, S. C., and Shaw, E. (1974). Human kallikrein. Purification and preliminary characterization,Arch. Biochem. Biophys. 165, 133–139.\nSampaio, M. U., Tanaka, A. T., Oliva, M. L. V., Batista, I. F. C., Motta, G., Stella, R. C. R., and Sampaio, C. A. M. (1992). Plant proteinase inhibitor. Action on blood clotting contact phase enzymes, inProceedings from I CONBRAP, pp. 57–65.\nSuzuki, A., Tsunogae, Y., Tanaka, I., Yamane, T., Ashida, T., Norioka, S., Hara, S., and Ikenaka, T. (1987). The structure of Bowman-Birk type protease inhibitor A-II from peanut (Arachis hypogaea) at 3.3 A resolution,J. Biochem. 101, 267–274.\nTanaka, A. S., Sampaio, M. U., Marangoni, S., Oliveira, B., Novello, J. C., Oliva, M. L. V., Fink, E., Fritz, H., and Sampaio, C. A. M. (1996). Purification and primary structure determination of a Bowman-Birk trypsin inhibitor fromTorresea cearensis seeds, In preparation.\nTsunogae, Y., Tanaka, I., Yamane, T., Kikkawa, J., Ashida, T., Ishikawa, C., Watanabe, K., Nakamura, S., and Takahashi, K. (1986). Structure of the trypsin-binding domain of Bowman-Birk type inhibitor and its interation with trypsin,J. Biochem. 100, 1637–1646.\nVoller, A. (1980). Heterogeneous enzyme-immunoassays and their applications, inEnzyme-Immunoassay (Maggio, E. T., ed.), CRC Press, Boca Raton, Florida, pp. 181–196.\nWilson, K. A., and Chen, J. C. (1983). Amino acid sequence of mung bean trypsin inhibitor and its modified forms appearing during germination,Plant Physiol. 71, 341–349.",{"VOID":473},"10.1007\u002FBF01908537","2024-06-25T03:31:58.023+00:00","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002FBF01908537",[477,494,507,522,535],{"id":478,"sortIndex":21,"researcher":20,"roles":479,"affiliations":480,"properties":489,"displayName":491,"givenName":20,"familyName":20},"d443998e-99d7-41d6-a29a-a7709269bc76",[270],[481],{"id":482,"sortIndex":21,"affiliation":483,"properties":20},"b86c06d6-f816-4d28-8008-e196641de175",{"id":482,"createTime":20,"updateTime":20,"relativeEntities":484,"slug":20,"properties":485,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":488,"statistic":20},[],{"title":486},{"VI":487},"Department of Biochemistry, Universidade Federal de S. Paulo, São Paulo SP, Brazil",[],{"title":490,"gsAuthor":492},{"VI":491},"A. S. Tanaka",{"VOID":493},"[\"EBp0R_oAAAAJ\"]",{"id":495,"sortIndex":30,"researcher":20,"roles":496,"affiliations":497,"properties":504,"displayName":506,"givenName":20,"familyName":20},"7a583092-daa4-4cfb-8dea-3017049e3a45",[270],[498],{"id":482,"sortIndex":21,"affiliation":499,"properties":20},{"id":482,"createTime":20,"updateTime":20,"relativeEntities":500,"slug":20,"properties":501,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":503,"statistic":20},[],{"title":502},{"VI":487},[],{"title":505},{"VI":506},"M. U. Sampaio",{"id":508,"sortIndex":31,"researcher":20,"roles":509,"affiliations":510,"properties":519,"displayName":521,"givenName":20,"familyName":20},"56e45a99-637f-4c48-a4e5-a806c819ec2b",[270],[511],{"id":512,"sortIndex":21,"affiliation":513,"properties":20},"8ffbc801-478a-4656-8490-488d89290738",{"id":512,"createTime":20,"updateTime":20,"relativeEntities":514,"slug":20,"properties":515,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":518,"statistic":20},[],{"title":516},{"VI":517},"Abteilung für Klinische Chemie und Klinische Biochemie in der Chirurgischen Klinik und Poliklinik, Klinikum Innenstadt, Ludwig-Maximilians-Universität München, Munich, Germany",[],{"title":520},{"VI":521},"R. Mentele",{"id":523,"sortIndex":32,"researcher":20,"roles":524,"affiliations":525,"properties":532,"displayName":534,"givenName":20,"familyName":20},"f3d6bc4c-4fe8-47ba-89c2-a8563561126c",[270],[526],{"id":512,"sortIndex":21,"affiliation":527,"properties":20},{"id":512,"createTime":20,"updateTime":20,"relativeEntities":528,"slug":20,"properties":529,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":531,"statistic":20},[],{"title":530},{"VI":517},[],{"title":533},{"VI":534},"E. A. Auerswald",{"id":536,"sortIndex":141,"researcher":20,"roles":537,"affiliations":538,"properties":545,"displayName":547,"givenName":20,"familyName":20},"537038b1-49e0-4bd1-922d-51ef5f476c8a",[270],[539],{"id":482,"sortIndex":21,"affiliation":540,"properties":20},{"id":482,"createTime":20,"updateTime":20,"relativeEntities":541,"slug":20,"properties":542,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":544,"statistic":20},[],{"title":543},{"VI":487},[],{"title":546},{"VI":547},"C. A. M. Sampaio",{"url":475,"publisher":549,"properties":563},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":550,"slug":10,"properties":551,"entityType":18,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":21,"subjectFields":555,"manageAffiliations":556,"indexDatabases":557,"url":25,"thumbnailPath":20,"statistic":558,"gsStatistic":20,"type":35,"analyzePriority":20},[],{"issn":552,"title":553,"eissn":554},{"VOID":13},{"EN":15},{"VOID":17},[],[],[],{"impactFactor":21,"impactFactorByYear":559,"i10Index":21,"i10IndexLast5Year":21,"totalPublication":28,"totalPublicationByYear":560,"totalCitation":21,"totalCitationByYear":561,"totalCitationPerPublication":21,"totalCitationPerPublicationByYear":562,"hindexLast5Year":21,"hindex":21},{},{"1984":30,"1986":30,"1989":30,"1990":31,"1992":30,"1993":30,"1995":32,"1998":30,"1999":30,"2000":30,"2002":30},{},{},{"pages":564,"volume":566},{"VOID":565},"553-560",{"VOID":567},"15",{"total":21,"publishYear":569,"statisticByYear":570},1996,{},"1996-08-01","2026-07-23T22:30:01.029+00:00",[],{"id":575,"createTime":576,"updateTime":577,"relativeEntities":578,"slug":579,"properties":580,"entityType":59,"verifyStatus":60,"verifyTime":591,"verifyNote":62,"languages":20,"translateLanguages":20,"viewCount":21,"primaryUrl":592,"fullTextUrl":20,"authors":593,"publicationType":155,"publisherRelationship":637,"citationCount":21,"citationInfo":657,"publishDate":660,"publishYear":658,"citationAnalyzeStatus":19,"lastCitationAnalyze":577,"indexDatabases":661,"openAccess":20,"references":20,"isForceReanalyzing":248},"aff20939-3503-40c5-812d-ffe1aca45d93","2024-01-05T02:59:16.881+00:00","2026-07-21T15:22:45.493+00:00",[],"The-amino-acid-sequence-of-the-rabbit-lutropin-beta-subunit",{"abstract":581,"title":583,"gsPaper":585,"references":587,"doi":589},{"EN":582},"The amino acid sequence of the beta subunit of rabbit lutropin (lLH) has been determined. The amino terminus of about 97% of the beta subunit has a two amino acid extension (pyro-Glu-Pro) compared to other lutropin beta sequences. Overlapping peptides from trypsin and chymotrypsin digestions of the performic acid-oxidized beta subunit and trypsin digestion of the S-aminoethylated cysteine beta subunit were isolated by chromatography on TSK Fractogel 40F and high-pressure liquid chromatography (HPLC). Sequencing was by a combination of the dansyl-Edman method and the direct Edman method. Amide placements were established by HPLC analysis of the PTH amino acid derivatives. The proposed sequence of lLHβ subunit is:\n                \n                  \n                \n               This sequence is highly homologous to the other known lutropin beta subunits, especially rat and pig lutropin beta (91%). Partial cleavage of the peptide bond between Asp-79 and Pro-80 was observed during cyanogen bromide treatment. Rabbit thyrotropin and thyrotropin beta subunit copurified with lLH and lLHβ except at a final chromatography on Sephadex G-100.",{"EN":584},"The amino acid sequence of the rabbit lutropin beta subunit",{"VOID":586},"[\"13056660479908699410\"]",{"VOID":588},"Boothby, M., Ruddon, R. W., Anderson, C., McWilliams, D., and Boime, I. (1981).J. Biol. Chem. 256, 5121–5127.\nBurleigh, B. D., Liu, W-K., and Ward, D. N. (1976).J. Biol. Chem. 251, 308–315.\nCheng, K.-W. (1976a).Biochem. J. 159, 71–77.\nCheng, K.-W. (1976b).Biochem. J. 159, 79–87.\nChin, W. W., Godine, J. E., Klein, D. R., Chang, A. S., Tan, L. K., and Habener, J. F. (1983).Proc. Natl. Acad. Sci. (USA)80, 4649–4653.\nCole, R. D. (1967).Meth. Enzymol. 11, 315–317.\nGlenn, S. D., Nahm, H. S., and Ward, D. N. (1984).J. Prot. Chem. 3, 143–156.\nGordon, W. L., and Ward, D. N. (1984). InLuteinizing Hormone Receptors and Actions (Ascoli, M., ed.), CRC Press, Boca Raton, Florida.\nHartley, B. S. (1980).Biochem. J. 119, 805–822.\nKeutmann, H. T., Williams, R. M., and Ryan, R. J. (1979).Biochem. Biophys. Res. Commun. 90, 842.\nLiu, W.-K., Nahm, H. S., Sweeney, C. M., Holcomb, G. N., and Ward, D. N. (1972).J. Biol. Chem. 247, 4365–4381.\nLiu, W.-K., Yang, K.-P., Nakagawa, Y., and Ward, D. N. (1974).J. Biol. Chem. 249, 5544–5550.\nMaghuin-Rogister, G., and Hennen, G. (1973).Eur. J. Biochem. 39, 235–253.\nMueller, J. M., Pierce, J. G., Davoll, H., and duVigneaud, V. (1951).J. Biol. Chem. 191, 309–313.\nPodell, D. N., and Abraham, G. N. (1978).Biochem. Biophys. Res. Commun. 81, 176–185.\nReichert, Jr., L. E., Leidenberger, F., and Trowbridge, C. G. (1973).Rec. Prog. Hormone Res. 29, 497–532.\nSairam, M. R., and Li, C.-H. (1975).Biochim. Biophys. Acta 412, 70–81.\nSairam, M. R., Samy, T. S. A., Papkoff, H., and Li, C.-H. (1972).Arch. Biochem. Biophys. 153, 572–586.\nStrickland, T. W., and Puett, D. (1981).Endocrinology 109, 1933–1942.\nTarr, G. E. (1981).Anal. Biochem. 111, 27–32.\nWard, D. N., and Liu, W.-K. (1972a). InStructure-Activity Relationships of Protein and Polypeptide Hormones (Margoulis, M., and Greenwood, F. C., eds.), Excerpta Medica Series, no. 241, Part 1, pp. 80–90.\nWard, D. N., and Liu, W.-K. (1972b). InStructure-Activity Relationships of Protein and Polypeptide Hormones (Margoulis, M., and Greenwood, F. D., eds.), Excerpta Medica Series, no. 241, Part 2, pp. 303–307.\nWard, D. N., and Moore, Jr., W. T. (1979). InAnimal Models for Research on Contraception and Fertility (Alexander, N. J., ed.), Harper and Row, Hagerstown, Maryland, pp. 151–164.\nWard, D. N., Reichert, Jr., L. E., Liu, W.-K., Nahm, H. S., Hsia, J., Lamkin, W. M., and Jones, N. S. (1973).Rec. Prog. Hormone Res. 29, 533–561.\nWard, D. N., Desjardins, C., Moore, Jr., W. T., and Nahm, H. S. (1979).Int. J. Peptide Protein Res. 13, 62–70.\nWard, D. N., Moore, Jr., W. T., and Burleigh, B. D. (1982).J. Protein Chem. 1, 263–280.",{"VOID":590},"10.1007\u002FBF01034894","2024-05-29T03:59:43.071+00:00","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002FBF01034894",[594,609,624],{"id":595,"sortIndex":21,"researcher":20,"roles":596,"affiliations":597,"properties":606,"displayName":608,"givenName":20,"familyName":20},"347880c7-d7ca-42a0-9686-32fd587f8ed1",[270],[598],{"id":599,"sortIndex":21,"affiliation":600,"properties":20},"e18ffe58-16f7-48fa-8fa1-7c58b2887aaa",{"id":599,"createTime":20,"updateTime":20,"relativeEntities":601,"slug":20,"properties":602,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":605,"statistic":20},[],{"title":603},{"VI":604},"W. Alton Jones Cell Science Center, Lake Placid",[],{"title":607},{"VI":608},"Stephan D. Glenn",{"id":610,"sortIndex":30,"researcher":20,"roles":611,"affiliations":612,"properties":621,"displayName":623,"givenName":20,"familyName":20},"dddada7d-c76b-41e7-8f82-a02c4bcd907b",[270],[613],{"id":614,"sortIndex":21,"affiliation":615,"properties":20},"319c0e35-0750-443b-82a5-f71a007d0cb1",{"id":614,"createTime":20,"updateTime":20,"relativeEntities":616,"slug":20,"properties":617,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":620,"statistic":20},[],{"title":618},{"VI":619},"Department of Biochemistry and Molecular Biology, University of Texas M. D. Anderson Hospital and Tumor Institute at Houston, Houston",[],{"title":622},{"VI":623},"Hyun S. Nahm",{"id":625,"sortIndex":31,"researcher":20,"roles":626,"affiliations":627,"properties":634,"displayName":636,"givenName":20,"familyName":20},"c38d7cb4-2337-4df6-ac6b-62f084dcb15a",[270],[628],{"id":614,"sortIndex":21,"affiliation":629,"properties":20},{"id":614,"createTime":20,"updateTime":20,"relativeEntities":630,"slug":20,"properties":631,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":633,"statistic":20},[],{"title":632},{"VI":619},[],{"title":635},{"VI":636},"Darrell N. Ward",{"url":592,"publisher":638,"properties":652},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":639,"slug":10,"properties":640,"entityType":18,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":21,"subjectFields":644,"manageAffiliations":645,"indexDatabases":646,"url":25,"thumbnailPath":20,"statistic":647,"gsStatistic":20,"type":35,"analyzePriority":20},[],{"issn":641,"title":642,"eissn":643},{"VOID":13},{"EN":15},{"VOID":17},[],[],[],{"impactFactor":21,"impactFactorByYear":648,"i10Index":21,"i10IndexLast5Year":21,"totalPublication":28,"totalPublicationByYear":649,"totalCitation":21,"totalCitationByYear":650,"totalCitationPerPublication":21,"totalCitationPerPublicationByYear":651,"hindexLast5Year":21,"hindex":21},{},{"1984":30,"1986":30,"1989":30,"1990":31,"1992":30,"1993":30,"1995":32,"1998":30,"1999":30,"2000":30,"2002":30},{},{},{"pages":653,"volume":655},{"VOID":654},"259-273",{"VOID":656},"3",{"total":21,"publishYear":658,"statisticByYear":659},1984,{},"1984-06-08",[],{"id":663,"createTime":664,"updateTime":665,"relativeEntities":666,"slug":667,"properties":668,"entityType":59,"verifyStatus":60,"verifyTime":679,"verifyNote":62,"languages":20,"translateLanguages":20,"viewCount":21,"primaryUrl":680,"fullTextUrl":20,"authors":681,"publicationType":155,"publisherRelationship":755,"citationCount":21,"citationInfo":775,"publishDate":778,"publishYear":776,"citationAnalyzeStatus":19,"lastCitationAnalyze":665,"indexDatabases":779,"openAccess":20,"references":20,"isForceReanalyzing":248},"e1ea9e27-6d1a-4b5e-80ef-f60ec42bf88d","2024-02-09T03:33:33.066+00:00","2026-07-21T00:52:57.693+00:00",[],"Temperature-pH-and-Solvent-Isotope-Effects-on-Cytochrome-c-Peroxidase-Mutant-N82A-Studied-by-Proton-NMR",{"abstract":669,"title":671,"gsPaper":673,"references":675,"doi":677},{"EN":670},"The mutant of baker's yeast cytochrome c peroxidase-CN with Ala82 in place of Asn82, [N82A]CcPCN, exhibits a complex solution behavior featuring dynamic interconversion among three enzyme forms that so far have only been detected by NMR spectroscopy. Proton NMR studies of [N82A]CcPCN reveal resonances from each of the three enzyme forms and show that the interconversion among forms is controlled by the pH, temperature, and isotope composition (H2O vs. D2O) of the buffer solution. No evidence for a key hydrogen bond between His52 and heme-coordinated cyanide is found in any of the enzyme forms, indicating that disruption of the extensive distal hydrogen bonding network is the source of this phenomenon.",{"EN":672},"Temperature, pH, and Solvent Isotope Effects on Cytochrome c Peroxidase Mutant N82A Studied by Proton NMR",{"VOID":674},"[\"3717771453634444209\"]",{"VOID":676},"Alam, S. L., Satterlee, J. D., Mauro, J. M., Poulos, T. L., and Erman, J. E. (1995). Biochemistry 34, 15496–15503.\nBosshard, H. R., Anni, H., and Yonetani, T. (1991). In Peroxidases in Chemistry and Biology (Everse, J., Everse, K. E., and Grisham, M. B., eds.), CRC Press, Boca Raton, Florida, Vol. 2, pp. 52–78.\nErman, J. E., Vitello, L. B., Miller, M. A., Shaw, A., Brown, K. A., and Kraut, J. (1993). Biochemistry 32, 9798–9806.\nFishel, L. A., Villafranca, J. E., Mauro, J. M., and Kraut, J. (1987). Biochemistry 26, 351–370.\nKunkel, T. A., Roberts, J. D., and Zakour, R. A. (1987). Meth. Enzymol. 154, 367–382.\nLa Mar, G. N., Satterlee, J. D., and De Ropp, J. S. (2000). In The Porphyrin Handbook (Kadish, K. M., Smith, K. M., and Guillard, R., eds.), Academic Press, San Diego, California, Vol. 5, pp. 185–298.\nNagano, S., Tanaka, M., Ishimori, K., Watanabe, Y., and Morishima, I. (1996). Biochemistry 35, 14251–14258.\nPalamakumbura, A. H., Foshay, M. C., Vitello, L. B., and Erman, J. E. (1999a). Biochemistry 38, 25647–15652.\nPalamakumbura, A. H., Vitello, L. B., and Erman, J. E. (1999b). Biochemistry 38, 15653–15658.\nPoulos, T. L. and Kraut, J. (1980). J. Biol. Chem. 255, 8199–8205.\nSatterlee, J. E. and Erman, J. E. (1983). J. Biol. Chem. 258, 1050–1056.\nSatterlee, J. D. and Erman, J. E. (1991). Biochemistry 30, 4398–4405.\nSatterlee, J. D., Erman, J. E., Mauro, J. M., and Kraut, J. (1990). Biochemistry 29, 8797–8804.\nSatterlee, J. D., Alam, S. L., Mauro, J. M., Erman, J. E., and Poulos, T. L. (1994). Eur. J. Biochem. 224, 81–87.\nSummers, F. E. and Erman, J. E. (1988). J. Biol. Chem. 263, 14267–14275.\nTanaka, M., Nagano, S., Ishimori, K., and Morishima, I. (1997). Biochemistry 36, 9791–9798.\nVitello, L. B., Erman, J. E., Miller, M. A., Wang, J., and Kraut, J. (1993). Biochemistry 32, 9807–9818.\nWang, J., Mauro, J. M., Edwards, S. L., Oatly, S. J., Fishel, L. A., Ashford, V. A., Xuong, N., and Kraut, J. (1990). Biochemistry 29, 7160–7173.",{"VOID":678},"10.1023\u002FA:1026513818176","2024-05-15T22:19:27.641+00:00","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1023\u002FA:1026513818176",[682,697,710,725,740],{"id":683,"sortIndex":21,"researcher":20,"roles":684,"affiliations":685,"properties":694,"displayName":696,"givenName":20,"familyName":20},"50dfa184-975e-47d1-ad8c-5aea7f1cf457",[270],[686],{"id":687,"sortIndex":21,"affiliation":688,"properties":20},"19646441-49bb-4931-a491-3d8eed9c1930",{"id":687,"createTime":20,"updateTime":20,"relativeEntities":689,"slug":20,"properties":690,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":693,"statistic":20},[],{"title":691},{"VI":692},"Department of Chemistry, Washington State University, Pullman",[],{"title":695},{"VI":696},"James D. Satterlee",{"id":698,"sortIndex":30,"researcher":20,"roles":699,"affiliations":700,"properties":707,"displayName":709,"givenName":20,"familyName":20},"6beb2374-fc4d-4559-ae9e-2b0035c86cd4",[270],[701],{"id":687,"sortIndex":21,"affiliation":702,"properties":20},{"id":687,"createTime":20,"updateTime":20,"relativeEntities":703,"slug":20,"properties":704,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":706,"statistic":20},[],{"title":705},{"VI":692},[],{"title":708},{"VI":709},"Jennifer G. Teske",{"id":711,"sortIndex":31,"researcher":20,"roles":712,"affiliations":713,"properties":722,"displayName":724,"givenName":20,"familyName":20},"37512bb2-2023-4f7b-be03-e1a9d2284492",[270],[714],{"id":715,"sortIndex":21,"affiliation":716,"properties":20},"a5dcd4f4-484e-4951-b71e-999e066dcb83",{"id":715,"createTime":20,"updateTime":20,"relativeEntities":717,"slug":20,"properties":718,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":721,"statistic":20},[],{"title":719},{"VI":720},"Department of Chemistry and Biochemistry, Northern Illinois University, DeKalb",[],{"title":723},{"VI":724},"James E. Erman",{"id":726,"sortIndex":32,"researcher":20,"roles":727,"affiliations":728,"properties":737,"displayName":739,"givenName":20,"familyName":20},"d21761db-c986-49bd-b98f-0b73f400cb25",[270],[729],{"id":730,"sortIndex":21,"affiliation":731,"properties":20},"ac4aca7f-fbaf-4104-94e2-1442509b6581",{"id":730,"createTime":20,"updateTime":20,"relativeEntities":732,"slug":20,"properties":733,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":736,"statistic":20},[],{"title":734},{"EN":735},"Geo-Centers, Inc., Fort Washington,",[],{"title":738},{"VI":739},"J. Matthew Mauro",{"id":741,"sortIndex":141,"researcher":20,"roles":742,"affiliations":743,"properties":752,"displayName":754,"givenName":20,"familyName":20},"047a6412-b550-4364-ae24-b50ff2f1b438",[270],[744],{"id":745,"sortIndex":21,"affiliation":746,"properties":20},"c51ee5f6-7ff7-4946-83c0-ea71ef9afa06",{"id":745,"createTime":20,"updateTime":20,"relativeEntities":747,"slug":20,"properties":748,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":751,"statistic":20},[],{"title":749},{"VI":750},"Department of Molecular Biology and Biochemistry, and Department of Physiology and Biophysics, University of California, Irvine",[],{"title":753},{"VI":754},"Thomas L. Poulos",{"url":680,"publisher":756,"properties":770},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":757,"slug":10,"properties":758,"entityType":18,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":21,"subjectFields":762,"manageAffiliations":763,"indexDatabases":764,"url":25,"thumbnailPath":20,"statistic":765,"gsStatistic":20,"type":35,"analyzePriority":20},[],{"issn":759,"title":760,"eissn":761},{"VOID":13},{"EN":15},{"VOID":17},[],[],[],{"impactFactor":21,"impactFactorByYear":766,"i10Index":21,"i10IndexLast5Year":21,"totalPublication":28,"totalPublicationByYear":767,"totalCitation":21,"totalCitationByYear":768,"totalCitationPerPublication":21,"totalCitationPerPublicationByYear":769,"hindexLast5Year":21,"hindex":21},{},{"1984":30,"1986":30,"1989":30,"1990":31,"1992":30,"1993":30,"1995":32,"1998":30,"1999":30,"2000":30,"2002":30},{},{},{"pages":771,"volume":773},{"VOID":772},"535-542",{"VOID":774},"19",{"total":21,"publishYear":776,"statisticByYear":777},2000,{},"2000-08-01",[],{"id":781,"createTime":782,"updateTime":783,"relativeEntities":784,"slug":785,"properties":786,"entityType":59,"verifyStatus":60,"verifyTime":797,"verifyNote":62,"languages":20,"translateLanguages":20,"viewCount":21,"primaryUrl":798,"fullTextUrl":20,"authors":799,"publicationType":155,"publisherRelationship":869,"citationCount":20,"citationInfo":20,"publishDate":889,"publishYear":890,"citationAnalyzeStatus":19,"lastCitationAnalyze":783,"indexDatabases":891,"openAccess":20,"references":20,"isForceReanalyzing":248},"77d10556-3dd4-414a-8160-549720601e31","2023-12-19T09:28:13.610+00:00","2026-07-20T09:11:11.157+00:00",[],"The-Effect-of-Active-Site-Mutations-in-the-Oxaloacetate-Decarboxylase-and-Pyruvate-Kinase-Like-Activities-of-Anaerobiospirillum-succiniciproducens-Phosphoenolpyruvate-Carboxykinase",{"abstract":787,"title":789,"gsPaper":791,"references":793,"doi":795},{"EN":788},"\nAnaerobiospirillum succiniciproducens His225Gln, Asp262Asn, Asp263Asn, and Thr249Asn phosphoenolpyruvate carboxykinases were analyzed for their oxaloacetate decarboxylase, and pyruvate kinase–like activities. The His225Gln and Asp263Asn enzymes showed increased K\nm values for Mn2+ and PEP compared with the native enzyme, suggesting a role of His225 and Asp263 in Mn2+ and PEP binding. No mayor alterations in K\nm values for oxaloacetate were detected for the varied enzymes. Alterations of His225, Asp262, Asp263, or Thr249, however, did not affect the V\nmax of the secondary activities as much as they affected the V\nmax for the main reaction. The results presented in this communication suggest different rate-limiting steps for the primary reaction and the secondary activities.",{"EN":790},"The Effect of Active Site Mutations in the Oxaloacetate Decarboxylase and Pyruvate Kinase-Like Activities of Anaerobiospirillum succiniciproducens Phosphoenolpyruvate Carboxykinase",{"VOID":792},"[\"2613571678669026246\"]",{"VOID":794},"Ash, D. E., Emig, F. A., Chowdhury, S. A., Satoh, Y., and Schramm, V. L. (1990). J. Biol. Chem. 265: 7377-7384.\nJabalquinto, A. M., Laivenieks, M., Zeikus, J. G., and Cardemil, E. (1999). J. Protein Chem. 18: 659-664.\nJabalquinto, A. M., Laivenieks, M., González-Nilo, F. D., Yevenes, A., Encinas, M. V., Zeikus, J. G., et al. (2002). J. Protein Chem. 21: 393-401.\nKrautwurst, H., Bazaes, S., González, F. D., Jabalquinto, A. M., Frey, P. A., and Cardemil, E. (1998). Biochemistry 37: 6295-6302.\nLlanos, L., Briones, R., Yévenes, A., González-Nilo, F. D., Frey, P. A., and Cardemil, E. (2001). FEBS Lett. 493: 1-5.\nMartel, A. E., and Smith, R. M. (1998). NIST Critically Selected Stability Constants of Metal Complexes, NIST standard references database 46 version 5.0.\nMatte, A., Tari, L. W., Goldie, H., and Delbaere, L. T. J. (1997). J. Biol. Chem. 272: 8105-8108.\nNoce, P. S., and Utter, M. F. (1975). J. Biol. Chem. 250: 9099-9105.\nParker, D. R., Norvell, W. A., and Chaney, R. L. (1995). GEOCHEMPC: A chemical speciation program for IBM and compatible personal computers. In: R. H. Loeppert, et al. (eds.), Chemical Equilibrium and Reaction Models, SSSA Spec. Publ. No. 42, American Society of Agronomy, Madison, WI.\nTari, L. W., Matte, A., Goldie, H., and Delbaere, L. T. J. (1997). Nat. Struct. Biol. 4: 990-994.\nUtter, M. F., and Kolenbrander, H. M. (1972). The Enzymes (3rd Ed., Vol. 6), Academic Press, New York, pp. 117-168.",{"VOID":796},"10.1023\u002FA:1021342918955","2024-06-26T08:07:02.816+00:00","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1023\u002FA:1021342918955",[800,815,830,843,856],{"id":801,"sortIndex":21,"researcher":20,"roles":802,"affiliations":803,"properties":812,"displayName":814,"givenName":20,"familyName":20},"a49cea05-8eca-4a3d-ba5a-78b75301b594",[270],[804],{"id":805,"sortIndex":21,"affiliation":806,"properties":20},"0f771b47-9beb-4082-837d-7a7f9fa616f0",{"id":805,"createTime":20,"updateTime":20,"relativeEntities":807,"slug":20,"properties":808,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":811,"statistic":20},[],{"title":809},{"VI":810},"Departamento de Ciencias Químicas, Facultad de Química y Biología, Universidad de Santiago de Chile, Santiago, Chile",[],{"title":813},{"VI":814},"Ana María Jabalquinto",{"id":816,"sortIndex":30,"researcher":20,"roles":817,"affiliations":818,"properties":827,"displayName":829,"givenName":20,"familyName":20},"6330b68c-2637-4b4a-a349-5941de214e88",[270],[819],{"id":820,"sortIndex":21,"affiliation":821,"properties":20},"72a03ae6-e327-431d-8886-a42250062268",{"id":820,"createTime":20,"updateTime":20,"relativeEntities":822,"slug":20,"properties":823,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":826,"statistic":20},[],{"title":824},{"VI":825},"Department of Biochemistry, Michigan State University, East Lansing",[],{"title":828},{"VI":829},"Maris Laivenieks",{"id":831,"sortIndex":31,"researcher":20,"roles":832,"affiliations":833,"properties":840,"displayName":842,"givenName":20,"familyName":20},"5da8f6ba-1304-4946-9c8d-9624748bced9",[270],[834],{"id":805,"sortIndex":21,"affiliation":835,"properties":20},{"id":805,"createTime":20,"updateTime":20,"relativeEntities":836,"slug":20,"properties":837,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":839,"statistic":20},[],{"title":838},{"VI":810},[],{"title":841},{"VI":842},"Mauricio Cabezas",{"id":844,"sortIndex":32,"researcher":20,"roles":845,"affiliations":846,"properties":853,"displayName":855,"givenName":20,"familyName":20},"884c3b4e-e7cc-4821-8350-7af1a4dac562",[270],[847],{"id":820,"sortIndex":21,"affiliation":848,"properties":20},{"id":820,"createTime":20,"updateTime":20,"relativeEntities":849,"slug":20,"properties":850,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":852,"statistic":20},[],{"title":851},{"VI":825},[],{"title":854},{"VI":855},"J. Gregory Zeikus",{"id":857,"sortIndex":141,"researcher":20,"roles":858,"affiliations":859,"properties":866,"displayName":868,"givenName":20,"familyName":20},"a244f951-5615-4565-a151-00a73a5bd04b",[270],[860],{"id":805,"sortIndex":21,"affiliation":861,"properties":20},{"id":805,"createTime":20,"updateTime":20,"relativeEntities":862,"slug":20,"properties":863,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":865,"statistic":20},[],{"title":864},{"VI":810},[],{"title":867},{"VI":868},"Emilio Cardemil",{"url":798,"publisher":870,"properties":884},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":871,"slug":10,"properties":872,"entityType":18,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":21,"subjectFields":876,"manageAffiliations":877,"indexDatabases":878,"url":25,"thumbnailPath":20,"statistic":879,"gsStatistic":20,"type":35,"analyzePriority":20},[],{"issn":873,"title":874,"eissn":875},{"VOID":13},{"EN":15},{"VOID":17},[],[],[],{"impactFactor":21,"impactFactorByYear":880,"i10Index":21,"i10IndexLast5Year":21,"totalPublication":28,"totalPublicationByYear":881,"totalCitation":21,"totalCitationByYear":882,"totalCitationPerPublication":21,"totalCitationPerPublicationByYear":883,"hindexLast5Year":21,"hindex":21},{},{"1984":30,"1986":30,"1989":30,"1990":31,"1992":30,"1993":30,"1995":32,"1998":30,"1999":30,"2000":30,"2002":30},{},{},{"pages":885,"volume":887},{"VOID":886},"443-445",{"VOID":888},"21","2002-10-01",2002,[],{"id":893,"createTime":894,"updateTime":895,"relativeEntities":896,"slug":897,"properties":898,"entityType":59,"verifyStatus":60,"verifyTime":909,"verifyNote":62,"languages":20,"translateLanguages":20,"viewCount":21,"primaryUrl":910,"fullTextUrl":20,"authors":911,"publicationType":155,"publisherRelationship":975,"citationCount":20,"citationInfo":20,"publishDate":995,"publishYear":996,"citationAnalyzeStatus":997,"lastCitationAnalyze":998,"indexDatabases":999,"openAccess":20,"references":20,"isForceReanalyzing":248},"4e1a459c-af23-4c53-8138-fdc3f4745838","2023-12-07T00:06:10.307+00:00","2026-07-06T12:57:11.493+00:00",[],"Limulus-amebocyte-clotting-cascade-Roles-of-endotoxin-and-adenylate-cyclase",{"abstract":899,"title":901,"gsPaper":903,"references":905,"doi":907},{"EN":900},"Endotoxin, the lipopolysaccharide from the cell wall of Gram-negative bacteria, causes blood clotting in the horseshoe crab,Limulus polyphemus. Minute amounts of endotoxin stimulate the amebocytes in the blood to undergo exocytosis, which release the contents of their secretory granules to form a clot. An endotoxin-binding protein that possesses calmodulin-like activity has been isolated from the amebocyte plasma membrane. This endotoxin-binding protein can activate adenylate cyclase fromBordetella pertussis to the same extent as rat testes calmodulin. The effect of endotoxin and the endotoxin-binding protein on cyclic AMP synthesis inLimulus amebocytes was examined. Amebocytes exposed to endotoxin have increased levels of intracellular cyclic AMP. Amebocyte membranes contain an adenylate cyclase which is stimulated by NaF, guanosine (β,r-imido)triphosphate, and for skolin. This adenylate cyclase is also stimulated by the endotoxin-binding protein and calcium. Exposure of amebocytes to forskolin or dibutyryl cyclic AMP are stimulated to secrete clot components. Activation of adenylate cyclasein vivo by endotoxin via the endotoxin-binding protein may be one of the ways in which endotoxin stimulates secretion. It is suggested that endotoxin may have two actions in theLimulus system: (1) binding of endotoxin to the endotoxin-binding protein activates adenylate cyclase, promoting secretion by the amebocytes; and (2) endotoxin catalyzes a reaction on the secreted material to form a blood clot. This latter reaction is not elicited by forskolin or dibutyryl cyclic AMP.",{"EN":902},"Limulus amebocyte clotting cascade: Roles of endotoxin and adenylate cyclase",{"VOID":904},"[]",{"VOID":906},"Armstrong, P. B. (1980).J. Cell. Sci. 44, 243–262.\nArmstrong, P. B., and Rickles, F. R. (1982).Exp. Cell Res. 140, 15–24.\nBender, J. L., and Neer, E. J. (1983).J. Biol. Chem. 258, 2432–2439.\nDumont, J. N., Anderson, E., and Winner, G. (1966).J. Morphol. 119, 181–208.\nHabermann, E. (1972).Science 177, 314–322.\nHochstein, H. D., Elin, R. J., Cooper, J. F., Seligmann Jr., E. B., and Wolff, S. M. (1973).Bull. Parenteral Drug Assoc. 27, 139–148.\nLevin, B., and Weiss, R. M. (1977).Mol. Pharmacol. 13, 690–697.\nLevin, J., and Bang, F. B. (1964).Bull. Johns Hopkins Hosp. 115, 265–274.\nLevin, J., and Bang, F. B. (1968).Thromb. Diathes. Haemorrh. 19, 186–197.\nLiang, S.-M., and Liu, T.-Y. (1982).Biochem. Biophys. Res. Commun. 105, 553–559.\nLiang, S.-M., Sakmar, T. P., and Liu, T.-Y. (1980).J. Biol. Chem. 255, 5586–5590.\nLiang, S.-M., Liang, C. M., and Liu, T.-Y. (1981).J. Biol. Chem. 256, 4698–4972.\nLiu, T.-Y., and Liang, S.-M. (1984). InBiochemical and Biophysical Studies of Proteins and Nucleic Acids (Lo, T. B., Liu, T.-Y., and Li, C. H., eds.), Elsevier\u002FNorth-Holland, New York.\nLowry, O. H., Rosebrough, N. J., Farr, A. L., and Randall, R. J. (1951).J. Biol. Chem. 193, 265–275.\nMeans, A. R., and Dedman, J. R. (1980).Nature 285, 73–77.\nMurer, E. H., Levin, J., and Holme, R. (1975).J. Cell Physiol. 86, 533–542.\nNakamura, S., and Levin, J. (1982a).Biochim. Biophys. Acta 707, 217–225.\nNakamura, S., and Levin, J. (1982b).Biochem. Biophys. Res. Commun. 108, 1619–1623.\nOrnberg, R. L., and Reese, T. S. (1981).J. Cell. Biol. 90, 40–54.\nRoss, E. M., Howlett, A. C., Fergusson, K. M., and Gilman, A. G. (1978).J. Biol. Chem. 1978, 6401–6412.\nSeamon, K. B., and Daly, J. W. (1981).J. Cyclic Nucleotide Res. 74, 201–224.\nSeid, R. C., and Liu, T.-Y. (1980). InFrontiers in Protein Chemistry (Liu, T.-Y.,et al., eds.), Elsevier\u002FNorth-Holland, New York, pp. 481–493.\nShands, J. W., Jr., Graham, J. A., and Nath, K. (1967).J. Mol. Biol. 25, 15–21.\nSolomon, Y., Londos, C., and Rodbell, M. (1974).Anal. Biochem. 58, 541–548.\nSteiner, A. L., Parker, C. W., and Kipnis, D. M. (1972).J. Biol. Chem. 247, 1106–1113.\nTai, J. Y., and Liu, T.-Y. (1977).J. Biol. Chem. 252, 2178–2182.\nTai, J. Y., Seid, R. C., Huhn, R. D., and Liu, T.-Y. (1977).J. Biol. Chem. 252, 4773–4776.\nTruffa-Bachi, P., Kaplan, J. G., and Bona, C. (1977).Cell. Immunol. 30, 1–11.\nYoung, N. S., Levin, J., and Prendergast, R. A. (1972).J. Clin. Invest. 51, 1790–1797.",{"VOID":908},"10.1007\u002FBF01025261","2024-06-24T21:20:59.491+00:00","https:\u002F\u002Flink.springer.com\u002F10.1007\u002FBF01025261",[912,936,949,962],{"id":913,"sortIndex":21,"researcher":20,"roles":914,"affiliations":915,"properties":933,"displayName":935,"givenName":20,"familyName":20},"24612132-825c-4e9d-8697-195b5b3d2ec1",[270],[916,924],{"id":917,"sortIndex":21,"affiliation":918,"properties":20},"7c73b13c-acb9-4bc9-842e-957e3092b403",{"id":917,"createTime":20,"updateTime":20,"relativeEntities":919,"slug":20,"properties":920,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":923,"statistic":20},[],{"title":921},{"VI":922},"Division of Biochemistry and Biophysics, Office of Biologics Research and Review, National Center for Drugs and Biologics, Food and Drug Administration, Bethesda",[],{"id":925,"sortIndex":30,"affiliation":926,"properties":932},"34129eae-3d51-4aa8-a1a1-dcbbd6accd2d",{"id":925,"createTime":20,"updateTime":20,"relativeEntities":927,"slug":20,"properties":928,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":931,"statistic":20},[],{"title":929},{"VI":930},"Biogen S.A., Geneva, Switzerland",[],{},{"title":934},{"VI":935},"Shu-Mei Liang",{"id":937,"sortIndex":30,"researcher":20,"roles":938,"affiliations":939,"properties":946,"displayName":948,"givenName":20,"familyName":20},"b5d82351-479c-44bf-b7dd-e380e734dcb0",[270],[940],{"id":917,"sortIndex":21,"affiliation":941,"properties":20},{"id":917,"createTime":20,"updateTime":20,"relativeEntities":942,"slug":20,"properties":943,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":945,"statistic":20},[],{"title":944},{"VI":922},[],{"title":947},{"VI":948},"Gretchen Hascall",{"id":950,"sortIndex":31,"researcher":20,"roles":951,"affiliations":952,"properties":959,"displayName":961,"givenName":20,"familyName":20},"429bed7e-7249-45cb-b930-b7119638440e",[270],[953],{"id":917,"sortIndex":21,"affiliation":954,"properties":20},{"id":917,"createTime":20,"updateTime":20,"relativeEntities":955,"slug":20,"properties":956,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":958,"statistic":20},[],{"title":957},{"VI":922},[],{"title":960},{"VI":961},"Teresa Liu",{"id":963,"sortIndex":32,"researcher":20,"roles":964,"affiliations":965,"properties":972,"displayName":974,"givenName":20,"familyName":20},"c49707e9-cae4-479c-8d72-4b8216d712cc",[270],[966],{"id":917,"sortIndex":21,"affiliation":967,"properties":20},{"id":917,"createTime":20,"updateTime":20,"relativeEntities":968,"slug":20,"properties":969,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":971,"statistic":20},[],{"title":970},{"VI":922},[],{"title":973},{"VI":974},"Teh-Yung Liu",{"url":910,"publisher":976,"properties":990},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":977,"slug":10,"properties":978,"entityType":18,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":21,"subjectFields":982,"manageAffiliations":983,"indexDatabases":984,"url":25,"thumbnailPath":20,"statistic":985,"gsStatistic":20,"type":35,"analyzePriority":20},[],{"issn":979,"title":980,"eissn":981},{"VOID":13},{"EN":15},{"VOID":17},[],[],[],{"impactFactor":21,"impactFactorByYear":986,"i10Index":21,"i10IndexLast5Year":21,"totalPublication":28,"totalPublicationByYear":987,"totalCitation":21,"totalCitationByYear":988,"totalCitationPerPublication":21,"totalCitationPerPublicationByYear":989,"hindexLast5Year":21,"hindex":21},{},{"1984":30,"1986":30,"1989":30,"1990":31,"1992":30,"1993":30,"1995":32,"1998":30,"1999":30,"2000":30,"2002":30},{},{},{"pages":991,"volume":993},{"VOID":992},"151-162",{"VOID":994},"4","1985-06-01",1985,"ERROR_IN_GET_PLATFORM_ID","2026-07-06T12:57:11.492+00:00",[],{"id":1001,"createTime":1002,"updateTime":1003,"relativeEntities":1004,"slug":1005,"properties":1006,"entityType":59,"verifyStatus":60,"verifyTime":1015,"verifyNote":62,"languages":20,"translateLanguages":20,"viewCount":21,"primaryUrl":1016,"fullTextUrl":20,"authors":1017,"publicationType":155,"publisherRelationship":1074,"citationCount":1094,"citationInfo":1095,"publishDate":1097,"publishYear":1096,"citationAnalyzeStatus":19,"lastCitationAnalyze":1098,"indexDatabases":1099,"openAccess":20,"references":1100,"isForceReanalyzing":248},"934128f2-a653-4a76-8008-7659673cdd9d","2024-01-03T16:13:24.393+00:00","2026-06-17T06:56:28.411+00:00",[],"Characterization-of-a-subunit-structure-and-stability-of-the-recombinant-porin-fromNeisseria-gonorrhoeae",{"abstract":1007,"title":1009,"gsPaper":1011,"doi":1013},{"EN":1008},"An outer membrane PIA protein fromNeisseria gonorrhoeae strain FA19 was expressed inEscherichia coli and refoldedin vitro in the presence of zwitterionic detergent. Its proper folding and subunit organization was confirmed by comparison with the native counterpart. The unfolding of PIA has been investigated using fluorescence spectroscopy and analytical size-exclusion chromatography methods. Analysis of the denaturation pathway of the PIA revealed that it forms an unusually labile quaternary structure. In the presence of 1 M guanidinium chloride (GdmCl) or upon heating up to 50°C, dissociation of the PIA oligomer was observed resulting in the formation of folded monomeric intermediates. Unfolding of monomers occurs at 80°C or in the presence of 4.3 M GdmCl, indicating high intrinsic stability toward both GdmCl and elevated temperatures. Both oligomeric and monomeric forms of PIA exhibited affinity to the hydrophobic probe 1-anilinonaphthalene-8-sulfonic acid (ANS) and bind withK\nd=80 and 130 µM, respectively. Denaturation of the PIA completely abolished affinity to ANS, suggesting that hydrophobicity is a property of the folded state of the porin.",{"EN":1010},"Characterization of a subunit structure and stability of the recombinant porin fromNeisseria gonorrhoeae",{"VOID":1012},"[\"17058628183706808218\"]",{"VOID":1014},"10.1007\u002FBF02780975","2024-04-29T18:13:25.077+00:00","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002FBF02780975",[1018,1033,1048,1061],{"id":1019,"sortIndex":21,"researcher":20,"roles":1020,"affiliations":1021,"properties":1030,"displayName":1032,"givenName":20,"familyName":20},"01739fd2-87ad-438a-a3b5-98a89e5eaf10",[270],[1022],{"id":1023,"sortIndex":21,"affiliation":1024,"properties":20},"cb05a9a3-1d17-4163-bd5e-beed8e0f6961",{"id":1023,"createTime":20,"updateTime":20,"relativeEntities":1025,"slug":20,"properties":1026,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":1029,"statistic":20},[],{"title":1027},{"VI":1028},"Department of Protein and Analytical Chemistry, Wyeth-Lederle Vaccines and Pediatrics, West Henrietta",[],{"title":1031},{"VI":1032},"Yury V. Matsuka",{"id":1034,"sortIndex":30,"researcher":20,"roles":1035,"affiliations":1036,"properties":1045,"displayName":1047,"givenName":20,"familyName":20},"3200401c-a7c0-4967-9a0a-04cca3be7bf7",[270],[1037],{"id":1038,"sortIndex":21,"affiliation":1039,"properties":20},"a6c145fb-9e4b-43d9-b1e1-d07371fc7d73",{"id":1038,"createTime":20,"updateTime":20,"relativeEntities":1040,"slug":20,"properties":1041,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":1044,"statistic":20},[],{"title":1042},{"VI":1043},"Department of Molecular Biology, Wyeth-Lederle Vaccines and Pediatrics, West Henrietta",[],{"title":1046},{"VI":1047},"Deborah A. Dilts",{"id":1049,"sortIndex":31,"researcher":20,"roles":1050,"affiliations":1051,"properties":1058,"displayName":1060,"givenName":20,"familyName":20},"36672156-9577-4aa7-bb74-339da2bf522d",[270],[1052],{"id":1038,"sortIndex":21,"affiliation":1053,"properties":20},{"id":1038,"createTime":20,"updateTime":20,"relativeEntities":1054,"slug":20,"properties":1055,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":1057,"statistic":20},[],{"title":1056},{"VI":1043},[],{"title":1059},{"VI":1060},"Susan Hoiseth",{"id":1062,"sortIndex":32,"researcher":20,"roles":1063,"affiliations":1064,"properties":1071,"displayName":1073,"givenName":20,"familyName":20},"04675ae1-1997-4ac6-82f2-59cda8478248",[270],[1065],{"id":1023,"sortIndex":21,"affiliation":1066,"properties":20},{"id":1023,"createTime":20,"updateTime":20,"relativeEntities":1067,"slug":20,"properties":1068,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":1070,"statistic":20},[],{"title":1069},{"VI":1028},[],{"title":1072},{"VI":1073},"Rasappa Arumugham",{"url":1016,"publisher":1075,"properties":1089},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":1076,"slug":10,"properties":1077,"entityType":18,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":21,"subjectFields":1081,"manageAffiliations":1082,"indexDatabases":1083,"url":25,"thumbnailPath":20,"statistic":1084,"gsStatistic":20,"type":35,"analyzePriority":20},[],{"issn":1078,"title":1079,"eissn":1080},{"VOID":13},{"EN":15},{"VOID":17},[],[],[],{"impactFactor":21,"impactFactorByYear":1085,"i10Index":21,"i10IndexLast5Year":21,"totalPublication":28,"totalPublicationByYear":1086,"totalCitation":21,"totalCitationByYear":1087,"totalCitationPerPublication":21,"totalCitationPerPublicationByYear":1088,"hindexLast5Year":21,"hindex":21},{},{"1984":30,"1986":30,"1989":30,"1990":31,"1992":30,"1993":30,"1995":32,"1998":30,"1999":30,"2000":30,"2002":30},{},{},{"pages":1090,"volume":1092},{"VOID":1091},"719-728",{"VOID":1093},"17",12,{"total":1094,"publishYear":1096,"statisticByYear":20},1998,"1998-10-01","2026-06-17T06:56:28.407+00:00",[],[1101,1104,1107,1110,1113,1116,1119,1122,1125,1128,1131,1134,1137,1140,1143,1146,1149,1152,1155,1158,1161,1164,1167,1170,1173,1176,1179,1182,1185,1188,1191,1194,1197,1200],{"id":20,"text":1102,"url":20,"identifiers":1103},"Blake, M. S., and Gotschlich, E. S. (1982).Infect. Immun. 36, 277–283.",{},{"id":20,"text":1105,"url":20,"identifiers":1106},"Butt, N. J., Lambden, P. R., and Heckels, J. E. (1990).Nucleic Acids Res. 18, 4258.",{},{"id":20,"text":1108,"url":20,"identifiers":1109},"Carbonetti, N. H., and Sparling, P. F. (1987).Proc. Natl. Acad. Sci. USA 84, 9084–9088.",{},{"id":20,"text":1111,"url":20,"identifiers":1112},"Carbonetti, N. H., Simnad, V. I., Seifert, H. S., So, M., and Sparling, P. F. (1988).Proc. Natl. Acad. Sci. USA 85, 6841–6845.",{},{"id":20,"text":1114,"url":20,"identifiers":1115},"Cleary, S., Mulkerrin, M. G., and Kelley, R. F. (1989).Biochemistry 28, 1884–1891.",{},{"id":20,"text":1117,"url":20,"identifiers":1118},"Cowan, S. W., Schirmer, T., Rummel, G., Steiert, M., Ghosh, R., Pauptit, R. A., Jansonius, J. N., and Rosenbusch, J. P. (1992).Nature 358, 727–733.",{},{"id":20,"text":1120,"url":20,"identifiers":1121},"Douglas, J. T., Lee, M. D., and Nikaido, H. (1981).FEMS Microbiol. Lett. 12, 305–309.",{},{"id":20,"text":1123,"url":20,"identifiers":1124},"Edelhoch, H. (1967).Biochemistry 6, 1948–1954.",{},{"id":20,"text":1126,"url":20,"identifiers":1127},"Ferguson, R. N., and Cahnmann, H. J. (1975).Biochemistry 14, 282–289.",{},{"id":20,"text":1129,"url":20,"identifiers":1130},"Gotschlich, E. C., Seiff, M. E., Blake, M. S., and Koomey, M. (1987).Proc. Natl. Acad. Sci. USA 84, 8135–8139.",{},{"id":20,"text":1132,"url":20,"identifiers":1133},"Hancock, R. E. W. (1987). InBacterial Outer Membranes as Model Systems, Wiley, New York.",{},{"id":20,"text":1135,"url":20,"identifiers":1136},"Jaenicke, R. (1987).Prog. Biophys. Mol. Biol. 49, 117–237.",{},{"id":20,"text":1138,"url":20,"identifiers":1139},"Jaenicke, R., and Rudolph, R. (1986).Meth. Enzymol. 131, 218–250.",{},{"id":20,"text":1141,"url":20,"identifiers":1142},"Judd, R. C. (1989).Clin. Microbiol. Rev. 2, S41-S48.",{},{"id":20,"text":1144,"url":20,"identifiers":1145},"Kreusch, A., Neubuser, A., Schiltz, E., Weckesser, J., and Schulz, G. E. (1994).Protein Sci. 3, 58–63.",{},{"id":20,"text":1147,"url":20,"identifiers":1148},"Lakowicz, J. R. (1983). InPrinciples of Fluorescence Spectroscopy, Plenum Press, New York.",{},{"id":20,"text":1150,"url":20,"identifiers":1151},"Markovic-Housley, Z., and Garavito, R. M. (1986).Biochim. Biophys. Acta 869, 158–170.",{},{"id":20,"text":1153,"url":20,"identifiers":1154},"Matsuka, Y. V., Medved, L. V., Brew, S. A., and Ingham, K. C. (1994).J. Biol. Chem. 269, 9539–9546.",{},{"id":20,"text":1156,"url":20,"identifiers":1157},"Mauro, A., Blake, M., and Labarca, P. (1988).Proc. Natl. Acad. Sci. USA 85, 1071–1075.",{},{"id":20,"text":1159,"url":20,"identifiers":1160},"McDade, R. L., and Johnston, K. H. (1980).J. Bacteriol. 141, 1183–1191.",{},{"id":20,"text":1162,"url":20,"identifiers":1163},"Minetti, C. A. S. A., Tai, J. Y., Blake, M. S., Pullen, J. K., Liang, S., and Remeta, D. P. (1997).J. Biol. Chem. 272, 10710–10720.",{},{"id":20,"text":1165,"url":20,"identifiers":1166},"Nikaido, H. (1994).J. Biol. Chem. 269, 3905–3908.",{},{"id":20,"text":1168,"url":20,"identifiers":1169},"Pace, N. C., Vajdos, F., Fee, L., Grimsley, G., and Gray, T. (1995).Protein Sci. 4, 2411–2423.",{},{"id":20,"text":1171,"url":20,"identifiers":1172},"Puohiniemi, R., Butcher, S., Tarkka, E., and Sarvas, M. (1991).FEMS Microbiol. Lett. 83, 29–33.",{},{"id":20,"text":1174,"url":20,"identifiers":1175},"Qi, H. L., Tai, J. Y., and Blake, M. S. (1994).Infect. Immun. 62, 2432–2439.",{},{"id":20,"text":1177,"url":20,"identifiers":1178},"Schirmer, T., Keller, T. A., Wang, Y., and Rosenbusch, J. P. (1995).Science 267, 512–514.",{},{"id":20,"text":1180,"url":20,"identifiers":1181},"Schmid, B., Kromer, M., and Schulz, G. E. (1996).FEBS Lett. 381, 111–114.",{},{"id":20,"text":1183,"url":20,"identifiers":1184},"Schulz, G. E. (1996).Curr. Opin. Struct. Biol. 6, 485–490.",{},{"id":20,"text":1186,"url":20,"identifiers":1187},"Seed, B. (1987).Nature 329, 840–842.",{},{"id":20,"text":1189,"url":20,"identifiers":1190},"Semisotnov, G. V., Rodionova, N. A., Razgulyaev, O. I., Uversky, V. N., Gripas, A. F., and Gilmanshin, R. I. (1991).Biopolymers 31, 119–128.",{},{"id":20,"text":1192,"url":20,"identifiers":1193},"Surrey, T., and Jahnig, F. (1995).J. Biol. Chem. 270, 28199–28203.",{},{"id":20,"text":1195,"url":20,"identifiers":1196},"Weiss, M. F., and Schulz. G. E. (1992).J. Mol. Biol. 227, 493–509.",{},{"id":20,"text":1198,"url":20,"identifiers":1199},"Wetzler, L. M., Blake, M. S., and Gotschlich, E. C. (1988).J. Exp. Med. 168, 1883–1897.",{},{"id":20,"text":1201,"url":20,"identifiers":1202},"Young, J. D., Blake, M., Mauro, A., and Cohn, Z. (1983).Proc. Natl. Acad. Sci. USA 80, 3831–3835.",{},{"id":1204,"createTime":1205,"updateTime":1206,"relativeEntities":1207,"slug":1208,"properties":1209,"entityType":59,"verifyStatus":60,"verifyTime":1219,"verifyNote":62,"languages":20,"translateLanguages":20,"viewCount":31,"primaryUrl":1220,"fullTextUrl":20,"authors":1221,"publicationType":155,"publisherRelationship":1259,"citationCount":20,"citationInfo":20,"publishDate":1278,"publishYear":776,"citationAnalyzeStatus":997,"lastCitationAnalyze":1279,"indexDatabases":1280,"openAccess":20,"references":20,"isForceReanalyzing":248},"d66d42cc-d2b7-4a2f-8129-38a52fee1de6","2023-12-01T12:25:11.130+00:00","2026-06-08T18:22:18.386+00:00",[],"Effect-of-Mg2-During-Reactivation-and-Refolding-of-Guanidine-Hydrochloride-Denatured-Creatine-Kinase",{"abstract":1210,"title":1212,"gsPaper":1214,"references":1215,"doi":1217},{"EN":1211},"Creatine kinase (ATP: creatine N-phosphotransferase, EC 2.7.3.2) was completely denatured using 3 M guanidine hydrochloride for 2 h as in previous studies [Yao et al. (1982), Sci. Sin.\n25B, 1296–1302; Yao et al. (1984), Biochemistry\n23, 2740–2744; Yao et al. (1982), Sci. Sin.\n25B, 1186–1193]. Under suitable conditions, about 60–70% of the activity can be recovered in the presence of different Mg2+ concentrations. Both the reactivation and the refolding processes follow two-phase courses after dilution in the proper solutions. A comparison of the rate constants for the refolding of unfolded creatine kinase with those for the recovery of its catalytic activity at various Mg2+ concentrations shows that these are not synchronized. The reactivity of guanidine hydrochloride-denatured creatine kinase can be inhibited by Mg2+; however, the rates of reactivation are independent of the Mg2+ concentration. In addition, Mg2+ affects the fluorescence intensity, but the rate constants of refolding are independent of Mg2+ concentration. Although the reactivation of GdHCl-denatured creatine kinase is complete about 3 h after dilution with reactivation solutions, the conformational changes during refolding occur in a much slower reaction. Mg2+ can induce complex changes in the relative fluorescence intensity during refolding over a broad range of concentrations.",{"EN":1213},"Effect of Mg2+ During Reactivation and Refolding of Guanidine Hydrochloride-Denatured Creatine Kinase",{"VOID":904},{"VOID":1216},"Altura, B. M., Durlach, J., and Seelig, M. S. (1987). In Magnesium in Cellular Processes and Medicine (Altura, B. M., Durlach, J., and Seelig, M. S., eds.), pp 1–4.\nAzem, A., Diamant, S., and Goloubinoff, P. (1994). Biochemistry 33, 6671–6675.\nBeeckmans, S., Khan, A. S., and Driessche, E. V. (1997). Biochem. J. 327, 171–176.\nBhattacharya, A., Bhattacharyya, B., and Roy, S. (1994). J. Biol. Chem. 269, 28655–28661.\nBickerstaff, G. F., Paterson, C., and Price, N. C. (1980). Biochim. Biophys. 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