Institut for Molekylærbiologi og Genetik

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Peer-review'ede publikationer ved MBG - alle år

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Okada, Y., Morodomi, T., Enghild, J. J., Suzuki, K., Yasui, A., Nakanishi, I., Salvesen, G. & Nagase, H. (1990). Matrix metalloproteinase 2 from human rheumatoid synovial fibroblasts. Purification and activation of the precursor and enzymic properties. FEBS journal, 194(3), 721-30.
Suzuki, K., Enghild, J. J., Morodomi, T., Salvesen, G. & Nagase, H. (1990). Mechanisms of activation of tissue procollagenase by matrix metalloproteinase 3 (stromelysin). Biochemistry, 29(44), 10261-70.
Heegaard, C. W., le Maire, M., Gulik-Krzywicki, T. & Møller, J. V. (1990). Monomeric state and Ca2+ transport by sarcoplasmic-reticulum Ca2+-ATPase, reconstituted with an excess of phospholipid. Journal of Biological Chemistry, 265(20), 12020-12028.
Edelberg, J. M., Enghild, J. J., Pizzo, S. V. & Gonzalez-Gronow, M. (1990). Neonatal plasminogen displays altered cell surface binding and activation kinetics. Correlation with increased glycosylation of the protein. Journal of Clinical Investigation, 86(1), 107-12. https://doi.org/10.1172/JCI114671
Cooper, D. L., Baptist, E. W., Enghild, J., Lee, H., Isola, N. & Klintworth, G. K. (1990). Partial amino acid sequence determination of bovine corneal protein 54 K (BCP 54). Current Eye Research, 9(8), 781-6.
Pedersen, L., Strauss, P. G., Schmidt, J., Luz, A., Erfle, V., Jørgensen, P., Kjeldgaard, N. O. & Pedersen, F. S. (1990). Pathogenicity of BALB/c-derived N-tropic murine leukemia viruses. Virology, 179(2), 931-5.
Nagase, H., Enghild, J. J., Suzuki, K. & Salvesen, G. (1990). Stepwise activation mechanisms of the precursor of matrix metalloproteinase 3 (stromelysin) by proteinases and (4-aminophenyl)mercuric acetate. Biochemistry, 29(24), 5783-9.
Clark, B. F., Kjeldgaard, M., la Cour, T. F., Thirup, S. & Nyborg, J. (1990). Structural determination of the functional sites of E. coli elongation factor Tu. BBA General Subjects, 1050(1-3), 203-8.
Gebhard, W., Hochstrasser, K., Fritz, H., Enghild, J. J., Pizzo, S. V. & Salvesen, G. (1990). Structure of inter-alpha-inhibitor (inter-alpha-trypsin inhibitor) and pre-alpha-inhibitor: current state and proposition of a new terminology. Biological Chemistry Hoppe-Seyler , 371 Suppl, 13-22.
Suzuki, K., Nagase, H., Ito, A., Enghild, J. J. & Salvesen, G. (1990). The role of matrix metalloproteinase 3 in the stepwise activation of human rheumatoid synovial procollagenase. Biological Chemistry Hoppe-Seyler , 371 Suppl, 305-10.
Zechiedrich, E. L., Christiansen, K., Andersen, A. H., Westergaard, O. & Osheroff, N. (1989). Double-stranded DNA cleavage/religation reaction of eukaryotic topoisomerase II: evidence for a nicked DNA intermediate. Biochemistry, 28(15), 6229-36.
Andersen, A. H., Christiansen, K., Zechiedrich, E. L., Jensen, P. S., Osheroff, N. & Westergaard, O. (1989). Strand specificity of the topoisomerase II mediated double-stranded DNA cleavage reaction. Biochemistry, 28(15), 6237-44.
Hansen, J., Jørgensen, J. E., Stougaard, J. & Marcker, K. A. (1989). Hairy roots - a short cut to transgenic root nodules. Plant Cell Reports, 8(1), 12-15. https://doi.org/10.1007/BF00735768
Petersen, C. M., Ejlersen, E., Moestrup, S. K., Jensen, P. H., Sand, O. & Sottrup-Jensen, L. (1989). Immunosuppressive properties of electrophoretically "slow" and "fast" form alpha 2-macroglobulin. Effects on cell-mediated cytotoxicity and (allo-) antigen-induced T cell proliferation. Journal of Immunology, 142(2), 629-635. http://www.jimmunol.org/content/142/2/629.abstract
Christensen, T., Sandal, N., Stougaard, J. & Marcker, K. A. (1989). 5' flanking sequence of the soybean leghemoglobin lbc3 gene. Nucleic Acids Research, 17(11), 4383.
Enghild, J. J., Thøgersen, I. B., Roche, P. A. & Pizzo, S. V. (1989). A conserved region in alpha-macroglobulins participates in binding to the mammalian alpha-macroglobulin receptor. Biochemistry, 28(3), 1406-12.
Enghild, J. J., Thøgersen, I. B., Pizzo, S. V. & Salvesen, G. (1989). Analysis of inter-alpha-trypsin inhibitor and a novel trypsin inhibitor, pre-alpha-trypsin inhibitor, from human plasma. Polypeptide chain stoichiometry and assembly by glycan. Journal of Biological Chemistry, 264(27), 15975-81.
Ramakrishnan, S., Enghild, J. J., Bryant, H. L. & Xu, F. J. (1989). Characterization of a translation inhibitory protein from Luffa aegyptiaca. Biochemical and Biophysical Research Communications, 160(2), 509-16.
Enghild, J. J., Salvesen, G., Brew, K. & Nagase, H. (1989). Interaction of human rheumatoid synovial collagenase (matrix metalloproteinase 1) and stromelysin (matrix metalloproteinase 3) with human alpha 2-macroglobulin and chicken ovostatin. Binding kinetics and identification of matrix metalloproteinase cleavage sites. Journal of Biological Chemistry, 264(15), 8779-85.
Stevnsner, T., Mortensen, U. H., Westergaard, O. & Bonven, B. J. (1989). Interactions between eukaryotic DNA topoisomerase I and a specific binding sequence. Journal of Biological Chemistry, 264(17), 10110-10113.
Zarnegar, R., Muga, S., Enghild, J. & Michalopoulos, G. (1989). NH2-terminal amino acid sequence of rabbit hepatopoietin A, a heparin-binding polypeptide growth factor for hepatocytes. Biochemical and Biophysical Research Communications, 163(3), 1370-6.
Enghild, J. J., Salvesen, G., Thøgersen, I. B. & Pizzo, S. V. (1989). Proteinase binding and inhibition by the monomeric alpha-macroglobulin rat alpha 1-inhibitor-3. Journal of Biological Chemistry, 264(19), 11428-35.
Sandal, N. N. & Marcker, K. A. (1988). Soybean nodulin 26 is homologous to the major intrinsic protein of the bovine lens fiber membrane. Nucleic Acids Research, 16(19), 9347. https://doi.org/10.1093/nar/16.19.9347
Jensen, P. H., Moestrup, S. K., Sottrup-Jensen, L., Petersen, C. M. & Gliemann, J. (1988). Receptors for a2-Macroglobulin- and pregnancy zone protein-proteinase complexes in the human placental syncytiotrophoblast. Placenta, 9(5), 463-477. https://doi.org/10.1016/0143-4004(88)90019-7
Kjeldsen, E., Mollerup, S., Thomsen, B., Bonven, B. J., Bolund, L. & Westergaard, O. (1988). Sequence-dependent effect of camptothecin on human topoisomerase I DNA cleavage. Journal of Molecular Biology, 202(2), 333-342. https://doi.org/10.1016/0022-2836(88)90462-7
Strauss, P. G., Schmidt, J., Pedersen, L. & Erfle, V. (1988). Amplification of endogenous proviral MuLV sequences in radiation-induced osteosarcomas. International Journal of Cancer, 41(4), 616-621. https://doi.org/10.1002/ijc.2910410423
Jørgensen, J. E., Stougaard, J., Marcker, A. & Marcker, K. A. (1988). Root nodule specific gene regulation: analysis of the soybean nodulin N23 gene promoter in heterologous symbiotic systems. Nucleic Acids Research, 16(1), 39-50.
Stougaard, J. & Kennedy, C. (1988). Regulation of nitrogenase synthesis in histidine auxotrophs of Klebsiella pneumoniae with altered levels of adenylate nucleotides. Journal of Bacteriology, 170(1), 250-7.
Roche, P. A., Strickland, D. K., Enghild, J. J. & Pizzo, S. V. (1988). Evidence that the platinum-reactive methionyl residue of the alpha 2-macroglobulin receptor recognition site is not in the carboxyl-terminal receptor binding domain. Journal of Biological Chemistry, 263(14), 6715-21.
Jensen, E. Ø., Marcker, K. A., Schell, J. & de Bruijn, F. J. (1988). Interaction of a nodule specific, trans-acting factor with distinct DNA elements in the soybean leghaemoglobin Ibc(3) 5' upstream region. EMBO Journal, 7(5), 1265-1271.
Greenberg, C. S., Enghild, J. J., Mary, A., Dobson, J. V. & Achyuthan, K. E. (1988). Isolation of a fibrin-binding fragment from blood coagulation factor XIII capable of cross-linking fibrin(ogen). Biochemical Journal, 256(3), 1013-9.
Metz, B. A., Welters, P., Hoffmann, H. J., Jensen, E. O. & Schell, J. (1988). Primary structure and promoter analysis of leghemoglobin genes of the stem-nodulated tropical legume Sesbania rostrata: conserved coding sequences, cis-elements and trans-acting factors. Molecular Genetics and Genomics, 214(2), 181-91.
Stougaard, J., Sandal, N. N., Grøn, A., Kühle, A. & Marcker, K. A. (1987). 5' Analysis of the soybean leghaemoglobin lbc(3) gene: regulatory elements required for promoter activity and organ specificity. EMBO Journal, 6(12), 3565-9.
Stougaard, J., Petersen, T. E. & Marcker, K. A. (1987). Expression of a complete soybean leghemoglobin gene in root nodules of transgenic Lotus corniculatus. Proceedings of the National Academy of Sciences (PNAS), 84(16), 5754-7.
Stougaard, J., Abildsten, D. & Marcker, K. A. (1987). The Agrobacterium rhizogenes pRi TL-DNA segment as a gene vector system for transformation of plants. MGG Molecular & General Genetics, 207(2-3), 251-255. https://doi.org/10.1007/BF00331586
Petit, A., Stougaard, J., Kühle, A., Marcker, K. A. & Tempé, J. (1987). Transformation and regeneration of the legume Lotus corniculatus: A system for molecular studies of symbiotic nitrogen fixation. MGG Molecular & General Genetics, 207(2-3), 245-250. https://doi.org/10.1007/BF00331585
Sandal, N. N., Bojsen, K. & Marcker, K. A. (1987). A small family of nodule specific genes from soybean. Nucleic Acids Research, 15(4), 1507-1519. https://doi.org/10.1093/nar/15.4.1507
Moestrup, S. K., Christensen, E. I., Sottrup-Jensen, L. & Gliemann, J. (1987). Binding and receptor-mediated endocytosis of pregnancy zone protein-proteinase complex in rat macrophages. BBA General Subjects, 930(3), 297-303.
Konieczny, A., Jensen, E. O., Marcker, K. A. & Legocki, A. (1987). Molecular cloning of lupin leghemoglobin cDNA. Molecular Biology Reports, 12(1), 61-6.
Gliemann, J., Moestrup, S. K., Jensen, P. H., Sottrup-Jensen, L., Andersen, H. B., Petersen, C. M., Sonne, O. & Madsen, P. (1986). Evidence for binding of human pregnancy zone protein-proteinase complex to a2-Macroglobulin receptors. BBA General Subjects, 883(3), 400-406. https://doi.org/10.1016/0304-4165(86)90276-X
Jensen, E. O., Marcker, K. A. & Villadsen, IS. (1986). Heme regulates the expression in Saccharomyces cerevisiae of chimaeric genes containing 5'-flanking soybean leghemoglobin sequences. EMBO Journal, 5(5), 843-7.
Jensen, J. S., Marcker, K. A., Otten, L. & Schell, J. (1986). Nodule-specific expression of a chimaeric soybean leghaemoglobin gene in transgenic Lotus corniculatus. Nature, 321(6071), 669-674. https://doi.org/10.1038/321669a0
Jones, T. A. & Thirup, S. (1986). Using known substructures in protein model building and crystallography. EMBO Journal, 5(4), 819-22.
Andersen, A. H., Gocke, E., Bonven, B. J., Nielsen, O. F. & Westergaard, O. (1985). Topoisomerase I has a strong binding preference for a conserved hexadecameric sequence in the promoter region of the rRNA gene from Tetrahymena pyriformis. Nucleic Acids Research, 13(5), 1543-57.
Sottrup-Jensen, L., Stepanik, T. M., Kristensen, T., Lønblad, P. B., Jones, C. M., Wierzbicki, D. M., Magnusson, S., Domdey, H., Wetzel, R. A. & Lundwall, A. (1985). Common evolutionary origin of alpha 2-macroglobulin and complement components C3 and C4. Proceedings of the National Academy of Sciences (PNAS), 82(1), 9-13.
la Cour, T. F., Nyborg, J., Thirup, S. & Clark, B. F. (1985). Structural details of the binding of guanosine diphosphate to elongation factor Tu from E. coli as studied by X-ray crystallography. EMBO Journal, 4(9), 2385-8.
Sottrup-Jensen, L., Folkersen, J., Kristensen, T. & Tack, B. F. (1984). Partial primary structure of human pregnancy zone protein: extensive sequence homology with human alpha 2-macroglobulin. Proceedings of the National Academy of Sciences (PNAS), 81(23), 7353-7357. http://www.pnas.org/content/81/23/7353.full.pdf+html?sid=e61630d2-2ac7-4ce8-a34f-c59a9b0aebc0
Sottrup-Jensen, L., Stepanik, T. M., Jones, C. M., Lønblad, P. B., Kristensen, T. & Wierzbicki, DM. (1984). Primary structure of human alpha 2-macroglobulin. I. Isolation of the 26 CNBr fragments, amino acid sequence of 13 small CNBr fragments, amino acid sequence of methionine-containing peptides, and alignment of all CNBr fragments. Journal of Biological Chemistry, 259(13), 8293-8303. http://www.jbc.org/content/259/13/8304.full.pdf+html
Kristensen, T., Wierzbicki, D. M. & Sottrup-Jensen, L. (1984). Primary structure of human alpha 2-macroglobulin. IV. Primary structure of two large CNBr fragments, located in the COOH-terminal part and accounting for 337 residues. Journal of Biological Chemistry, 259(13), 8313-8317. http://www.jbc.org/content/259/13/8313.full.pdf+html
Sottrup-Jensen, L., Stepanik, T. M., Kristensen, T., Wierzbicke, D. M., Jones, C. M., Lønblad, P. B., Magnusson, S. & Petersen, T. E. (1984). Primary structure of human alpha 2-macroglobulin. V. The complete structure. Journal of Biological Chemistry, 259(13), 8318-8327. http://www.jbc.org/content/259/13/8318.full.pdf+html?sid=65d5da7b-8eb4-4cec-aaee-fc252eb6ebde

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Helene Eriksen