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Page 1
Organization of the inter-alpha-inhibitor heavy chains on the chondroitin sulfate originating from Ser(10) of bikunin: posttranslational modification of IalphaI-derived bikunin.
Enghild JJ, Thøgersen IB, Cheng F, Fransson LA, Roepstorff P, Rahbek-Nielsen H. Enghild JJ, et al. Biochemistry. 1999 Sep 7;38(36):11804-13. doi: 10.1021/bi9908540. Biochemistry. 1999. PMID: 10512637
Heavy chain 1 (HC1) and heavy chain 2 (HC2) are attached to the CS by a novel cross-link [Enghild, J. J., Salvesen, G., Hefta, S. A., Thogersen, I. B., Rutherfurd, S., and Pizzo, S. ...
Heavy chain 1 (HC1) and heavy chain 2 (HC2) are attached to the CS by a novel cross-link [Enghild, J. J., Salvesen, G., Hefta, S. A., …
Characterization of the 46-kDa intermediates of matrix metalloproteinase 3 (stromelysin 1) obtained by site-directed mutation of phenylalanine 83.
Benbow U, Butticè G, Nagase H, Kurkinen M. Benbow U, et al. J Biol Chem. 1996 May 3;271(18):10715-22. doi: 10.1074/jbc.271.18.10715. J Biol Chem. 1996. PMID: 8631880 Free article.
The precursor of matrix metalloproteinase 3 (MMP-3/ stromelysin 1) is activated in vitro by proteinases or mercurial compounds by stepwise processes which include the initial formation of short-lived intermediates and the subsequent intermolecular cleavage of the His82-Phe83 bond …
The precursor of matrix metalloproteinase 3 (MMP-3/ stromelysin 1) is activated in vitro by proteinases or mercurial compounds by stepwise p …
Characterization of glycosaminoglycan-binding domains present in insulin-like growth factor-binding protein-3.
Fowlkes JL, Serra DM. Fowlkes JL, et al. J Biol Chem. 1996 Jun 21;271(25):14676-9. doi: 10.1074/jbc.271.25.14676. J Biol Chem. 1996. PMID: 8663298 Free article.
Matrix metalloproteinase 3 cleaves insulin-like growth factor-binding protein-3 (IGFBP-3) into six fragments, four of which bind heparin-Sepharose (Fowlkes, J. L., Enghild, J. J., Suzuki, K., and Nagase, H. (1994) J. Biol. Chem. 269, 25742-25746). ...
Matrix metalloproteinase 3 cleaves insulin-like growth factor-binding protein-3 (IGFBP-3) into six fragments, four of which bind heparin-Sep …
Posttranslational modifications of human inter-alpha-inhibitor: identification of glycans and disulfide bridges in heavy chains 1 and 2.
Olsen EH, Rahbek-Nielsen H, Thogersen IB, Roepstorff P, Enghild JJ. Olsen EH, et al. Biochemistry. 1998 Jan 6;37(1):408-16. doi: 10.1021/bi971137d. Biochemistry. 1998. PMID: 9425062
The three polypeptide chains are covalently assembled via a carbohydrate cross-link [Enghild, J. J., Salvesen, G., Hefta, S. A., Thogersen, I. B., Rutherfurd, S., & Pizzo, S. ...
The three polypeptide chains are covalently assembled via a carbohydrate cross-link [Enghild, J. J., Salvesen, G., Hefta, S. A., Thog …
Analysis of factor XIII substrate specificity using recombinant human factor XIII and tissue transglutaminase chimeras.
Hettasch JM, Peoples KA, Greenberg CS. Hettasch JM, et al. J Biol Chem. 1997 Oct 3;272(40):25149-56. doi: 10.1074/jbc.272.40.25149. J Biol Chem. 1997. PMID: 9312126
Other work from this laboratory (Achyuthan, K. E., Slaughter, T. F., Santiago, M. A., Enghild, J. J., and Greenberg, C. S. (1993) J. Biol. Chem. 268, 21284-21292) using synthetic peptides identified two other domains that might play a role in substrate recognition (located …
Other work from this laboratory (Achyuthan, K. E., Slaughter, T. F., Santiago, M. A., Enghild, J. J., and Greenberg, C. S. (1993) J. …
The heparin-binding domain of extracellular superoxide dismutase is proteolytically processed intracellularly during biosynthesis.
Enghild JJ, Thogersen IB, Oury TD, Valnickova Z, Hojrup P, Crapo JD. Enghild JJ, et al. J Biol Chem. 1999 May 21;274(21):14818-22. doi: 10.1074/jbc.274.21.14818. J Biol Chem. 1999. PMID: 10329680
During the purification of human EC-SOD, the intact/cleaved ratio remains constant, suggesting that proteolytic removal of the heparin-binding domain does not occur during purification (Oury, T. D., Crapo, J. D., Valnickova, Z., and Enghild, J. J. (1996) Biochem. J. 317, 5 …
During the purification of human EC-SOD, the intact/cleaved ratio remains constant, suggesting that proteolytic removal of the heparin-bindi …
Chondroitin sulphate covalently cross-links the three polypeptide chains of inter-alpha-trypsin inhibitor.
Morelle W, Capon C, Balduyck M, Sautiere P, Kouach M, Michalski C, Fournet B, Mizon J. Morelle W, et al. Eur J Biochem. 1994 Apr 15;221(2):881-8. doi: 10.1111/j.1432-1033.1994.tb18803.x. Eur J Biochem. 1994. PMID: 7513643 Free article.
In order to demonstrate that the three chains are covalently linked by a chondroitin sulphate chain as previously proposed [Enghild, J. J., Salvesen, G., Hefta, S. A., Thogersen, I. B., Rutherford, S. and Pizzo, S. ...
In order to demonstrate that the three chains are covalently linked by a chondroitin sulphate chain as previously proposed [Enghild, …
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