[1] Elafin: an elastase-specific inhibitor of human skin. Purification, characterization, and complete amino acid sequence: O. Wiedow, et al.; J. Biol. Chem. 265, 14791 (1990) Abstract; Full Text
[2] Skin-derived antileucoproteases (SKALPs): characterization of two new elastase inhibitors from psoriatic epidermis: J. Schalkwijk, et al.; Br. J. Dermatol. 122, 631 (1990) Abstract
[3] Purification and characterization of elastase-specific inhibitor. Sequence homology with mucus proteinase inhibitor: J.M. Sallenave and A.P. Ryle; Biol. Chem. Hoppe Seyler 372, 13 (1991) Abstract
[4] Primary structure of the human elafin precursor preproelafin deduced from the nucleotide sequence of its gene and the presence of unique repetitive sequences in the prosegment: Saheki, et al.; Biochem. Biophys. Res. Commun. 185, 240 (1992) Abstract
[5] Kinetics of the inhibition of human leukocyte elastase by elafin, a 6-kilodalton elastase-specific inhibitor from human skin: Q.L. Ying and S.R. Simon; Biochemistry 32, 1866 (1993) Abstract
[6] SKALP/elafin: an elastase inhibitor from cultured human keratinocytes. Purification, cDNA sequence, and evidence for transglutaminase cross-linking: H.O. Molhuizen, et al.; J. Biol. Chem. 268, 12028 (1993) Abstract
[7] Characterization and gene sequence of the precursor of elafin, an elastase-specific inhibitor in bronchial secretions: J.M. Sallenave and A. Silva; Am. J. Respir. Cell. Mol. Biol. 8, 439 (1993) Abstract
[8] Kinetics of the inhibition of human leukocyte elastase by elafin, a 6-kilodalton elastase-specific inhibitor from human skin: Q.L. Ying and S.R. Simon; Biochemistry 32, 1866 (1993) Abstract
[9] Elastase inhibitor elafin is a new type of proteinase inhibitor which has a transglutaminase-mediated anchoring sequence termed "cementoin": K. Nara, et al.; J. Biochem. (Tokyo) 115, 441 (1994) Abstract
[10] Accelerated evolution in inhibitor domains of porcine elafin family members: I. Tamechika, et al.; J. Biol. Chem. 271, 7012 (1996) Abstract; Full Text
[11] Identification and sequence analysis of two new members of the SKALP/elafin and SPAI-2 gene family. Biochemical properties of the transglutaminase substrate motif and suggestions for a new nomenclature: P.L. Zeeuwen, et al.; J. Biol. Chem. 272, 20471 (1997) Abstract; Full Text
[12] The trappin gene family: proteins defined by an N-terminal transglutaminase substrate domain and a C-terminal four-disulphide core: J. Schalkwijk, et al.; Biochem. J. 340, 569 (1999) Abstract; Full Text
[13] The role of secretory leukocyte proteinase inhibitor and elafin (elastase-specific inhibitor/skin-derived antileukoprotease) as alarm antiproteinases in inflammatory lung disease: J.M. Sallenave; Respir. Res. 1, 87 (2000) Abstract
[14] Kinetics of the inhibition of proteinase 3 by elafin: Q.L. Ying and S.R. Simon; Am. J. Respir. Cell Mol. Biol. 24, 83 (2001) Abstract
[15] Trappin ovine molecule (TOM), the ovine ortholog of elafin, is an acute phase reactant in the lung: T.I. Brown, et al.; Physiol. Genomics 19, 11 (2004) Abstract; Full Text
[16] Elafin and Its Precursor Trappin-2 Still Inhibit Neutrophil Serine Proteinases when They Are Covalently Bound to Extracellular Matrix Proteins by Tissue Transglutaminase: N. Guyot, et al.; Biochemistry 44, 15610 (2005) Abstract
[17] SLPI and elafin: one glove, many fingers: S.E. Williams, et al.; Clin. Sci. (Lond) 110, 21 (2006) Abstract
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