Abbaszade, I., Liu, R. Q., Yang, F., Rosenfeld, S. A., Ross, O. H., Link, J. R., Ellis, D. M., Tortorella, M. D., Pratta, M. A., Hollis, J. M., Wynn, R., Duke, J. L., George, H. J., Hillman ,M. C. Jr., Murphy, K., Wiswall, B. H., Copeland, R. A., Decicco, C. P., Bruckner, R., Nagase, H., Itoh, Y., Newton, R. C., Magolda, R. L., Trzaskos, J. M., Burn, T. C. Cloning and characterization of ADAMTS11, an aggrecanase from the ADAMTS family. J. Biol. Chem. 274(33), 23443-23450 (1999)

Adham, I. M., Kim, Y., Shamsadin, R., Heinlein, U. A. O., Von Beust, G., Mattei, M. G., Engel, W. Molecular cloning, chromosomal localization, and expression analysis of CYRN1 and CYRN2, two human genes coding for cyritestin, a sperm protein involved in gamete interaction. DNA Cell Biol. 17(2), 161-168 (1998)

Albeda, S. M., Mette, S. A., Elder, D. E., Stewart, R., Damjanovich, L., Herlyn, M., Buck, C. A. Integrin distibution in malignant melanoma: association of the b3 subunit with tumor progression. Cancer Res. 50, 6757-6764 (1991)

Alfandari, D., Wolfsberg, T. G., White, J. M., DeSimone, D. W. ADAM 13: a novel ADAM expressed in somitic mesoderm and neural crest cells during Xenopus laevis development. Dev. Biol. 182(2), 314-330 (1997)

Almeida, E. A., Huovila, A. P., Sutherland, A. E., Stephens, L. E., Calarco, P. G., Shaw, L. M., Mercurio, A. M., Sonnenberg, A., Primakoff, P., Myles, D. G. Mouse egg integrin a6b1 functions as a sperm receptor. Cell 81(7), 1095-1104 (1995)

Amour, A., Slocombe, P. M., Webster, A., Butler, M., Knight, C. G., Smith, B. J., Stephens, P. E., Shelley, C., Hutton, M., Knäuper, V., Docherty, A. J. P., Murphy, G. TNF-a converting enzyme (TACE) is inhibited by TIMP-3. FEBS Lett. 435(1), 39-44 (1998)

Amour, A., Knight, C. G., Webster, A., Slocombe, P. M., Stephens, P. E., Knäuper, V., Docherty, A. J., Murphy, G. The in vitro activity of ADAM-10 is inhibited by TIMP-1 and TIMP-3. FEBS Lett. 473(3), 275-279 (2000)

Anfinsen, C. B. Principles that govern the folding of protein chains. Science 181(96), 223-230 (1973)

Bazzoni, F. und Beutler, B. The tumor necrosis factor ligand and receptor families. N. Engl. J. Med. 334(26), 1717-1725 (1996)

Bedford, J. M. The contraceptive potential of fertilization: A physiological perspective. Hum. Reprod. 9, 842-858 (1994)

Bigler, D., Takahashi, Y., Chen, M. S., Almeida, E. A., Osbourne, L., White, J. M. Sequence-specific interaction between the disintegrin domain of mouse ADAM 2 (fertilin b) and murine eggs. Role of the a6 integrin subunit. J. Biol. Chem. 275(16), 11576-11584 (2000)

Birkedal-Hansen, H., Moore W. G. I., Bodden, M. K., Windsor, L. J., Birkedal-Hansen, B., DeCarlo, A., Engler, J. A. Martix Metalloproteinases: A Review. Crit. Rev. in Oral. Biol. Med. 4(2), 197-250 (1993)

Bjarnason, J. B. und Fox, J. W. Snake venom metalloendopeptidases: reprolysins. Methods Enzymol. 248, 345-368 (1995)

Black, R. A., Rauch, C. T., Kozlosky, C. J., Peschon, J. J., Slack, J. L., Wolfson, M. F., Castner, B. J., Stocking, K. L., Reddy, P., Srinivasan, S., Nelson, N., Boiani, N., Schooley, K. A., Gerhart, M., Davis, R., Fitzner, J. N., Johnson, R. S., Paxton, R. J., March, C. J., Cerretti, D. P. A metalloproteinase disintegrin that releases tumour-necrosis factor-a from cells. Nature 385(6618), 729-733 (1997)

Blobel, C. P., Myles, D. G., Primakoff, P., White, J. M. Proteolytic processing of a protein involved in sperm-egg fusion correlates with acquisition of fertilazation competence. J. Cell Biol. 111, 69-78 (1990)

Blobel, C. P., Wolfsberg, T. G., Turck, C. W., Myles, D. G., Primakoff, P., White, J. M. A potential fusion peptide and an integrin ligand domain in a protein active in sperm-egg fusion. Nature 356, 248-252 (1992)

Blobel, C. P. Functional processing of fertilin: evidence for a critical role of proteolysis in sperm maturation and activation. Rev. Reprod. 5(2), 75-83 (2000)

Bode, W., Gomis-Rüth, F. X., Stöckler, W. Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc-binding environments (HEXXHXXGXXH and Met-turn) and topologies and should be grouped into a common family, the metzincins. FEBS Lett. 331(1,2), 134-140 (1993)

Bode, W., Fernandez-Catalan, C., Tschesche, H., Grams, F., Nagase, H., Maskos, K. Structural properties of matrix metalloproteinases. Cell Mol. Life Sci. 55, 639-652 (1999)

Böhm, B. B., Aigner, T., Gehrsitz, A., Blobel, C. P., Kalden, J. R., Burkhardt, H. Up-regulation of MDC15 (metargidin) messenger RNA in human osteoarthritic cartilage. Arthritis Rheum. 42(9), 1946-1950 (1999)

Bosse, F., Petzold, G., Greiner-Petter, R., Pippirs, U., Gillen, C., Muller, H. W. Cellular localization of the disintegrin CRII-7/rMDC15 mRNA in rat PNS and CNS and regulated expression in postnatal development and after nerve injury. Glia 32(3), 313-327 (2000)

Brou, C., Logeat, F., Gupta, N., Bessia, C., LeBail, O., Doedens, J. R., Cumano, A., Roux, P., Black, R. A., Israel, A. A novel proteolytic cleavage involved in Notch signaling: the role of the disintegrin-metalloprotease TACE. Mol. Cell. 5(2), 207-216 (2000) Buchner, J., Pastan, I., Brinkmann, U. A method for increasing the yield of properly folded recombinant fusion proteins: single-chain immunotoxins from renaturation of bacterial inclusion bodies. Anal. Biochem. 205(2), 263-270 (1992)

Buxbaum, J. D., Liu, K. N., Luo, Y., Slack, J. L., Stocking, K. L., Peschon, J. J., Johnson, R. S., Castner, B. J., Cerretti, D. P., Black, R. A. Evidence that tumor necrosis factor a converting enzyme is involved in regulated a-secretase cleavage of the Alzheimer amyloid protein precursor. J. Biol. Chem. 273(43), 27765-27767 (1998)

Byzova, T. V., Rabbani, R., D'Souza, S. E., Plow, E. F. Role of integrin avb3 in vascular biology. Thromb. Haemost. 80(5), 726-734 (1998)

Cailleau, R., Young, R., Olive, M., Reeves, W. J. Breast tumor cell lines from pleural effusions. J. Natl. Cancer Inst. 53, 661-674 (1974)

Cal, S., Freije, J. M., Lopez, J. M., Takada, Y., Lopez-Otin, C. ADAM 23/MDC3, a human disintegrin that promotes cell adhesion via interaction with the avb3 integrin through an RGD-independent mechanism. Mol. Biol. Cell. 11(4), 1457-1469 (2000)

Cal, S., Argüelles, J. M., Fernández, P. L., López-Otin, C. Identification, characterization and intracellular processing of ADAM-TS12, a novel human disintegrin with a complex structrual organization involving multiple thrombospondin-1 repeats. J. Biol. Chem. (2001) im Druck

Camaioni, A., Salustri, A., Yanagishita, M., Hascall, V. C. Proteoglycans and proteins in the extracellular matrix of mouse cumulus cell-oocyte comlex. Arch. Biochem. Biophys. 325, 190-198 (1996)

Carmichael, J., DeGraff, W. G., Gazdar, A. F., Minna, J. D., Mitchell, J. B. Evaluation of a tetrazolium-based semiautomated colorimetric assay: assessment of chemosensitivity testing. Cancer Res. 47, 936-942 (1987)

Cereghino, J. L. und Cregg, J. M. Heterologous protein expression in the methylotrophic yeast Pichia pastoris. FEMS Microbiol. Rev. 24, 45-66 (2000)

Cerretti, D. P., Poindexter, K., Castner, B. J., Means, G., Copeland, N. G., Gilbert, D. J., Jenkins, N. A., Black, R. A., Nelson, N. Characterization of the cDNA and gene for mouse tumour necrosis factor a converting enzyme (TACE/ADAM17) and its location to mouse chromosome 12 and human chromosome 2p25. Cytokine 11(8), 541-551 (1999a)

Cerretti, D. P., DuBose, R. F., Black, R. A., Nelson, N. Isolation of two novel Metalloproteinase-Disintegrin (ADAM) cDNAs that show testis-specific gene expression. Biochem. Biophys. Res. Commun. 263, 810-815 (1999b)

Chen, H., Sampson, N. S. Mediation of sperm-egg fusion: evidence that mouse egg a6b1 integrin is the receptor for sperm fertilin b. Chem. Biol. 6(1), 1-10 (1999a)

Chen, M. S., Almeida, E. A., Huovila, A. P., Takahashi, Y., Shaw, L. M., Mercurio, A. M., White, J. M. Evidence that distinct states of the integrin a6b1 interact with laminin and an ADAM. J. Cell Biol. 144(3), 549-561 (1999b)

Chen, M. S., Tung, K. S., Coonrod, S. A., Takahashi, Y., Bigler, D., Chang, A., Yamashita, Y., Kincade, P. W., Herr, J. C., White, J. M. Role of the integrin-associated protein CD9 in binding between sperm ADAM 2 and the egg integrin a6b1: implications for murine fertilization. Proc. Natl. Acad. Sci. USA 96(21), 11830-11835 (1999c)

Cho, C., O´Dell Bunch, D., Faure, J.-E., Goulding, E. H., Eddy, E. M., Primakoff, P., Myles, D. G. Fertilization defects in sperm form mice lacking fertilin b. Science 281, 1857-1859 (1998)

Choi, S. J., Han, J. H., Roodman, G. D. ADAM8: a novel osteoclast stimulating factor. J. Bone Miner. Res. 16(5), 814-822 (2001)

Chubinskaya, S., Cs-Szabo, G., Kuettner, K. E. ADAM-10 message is expressed in human articular cartilage. J. Histochem. Cytochem. 46(6), 723-729 (1998)

Clark, M. E., Kelner, G. S., Turbeville, L. A., Boyer, A., Arden, K. C., Maki, R. A. ADAMTS9, a novel member of the ADAM-TS/metallospondin gene family. Genomics 67(3), 343-350 (2000)

Clarke, H. R., Wolfson, M. F., Rauch, C. T., Castner, B. J., Huang, C. P., Gerhart, M. J., Johnson, R. S., Cerretti, D. P., Paxton, R. J., Price, V. L., Black, R. A. Expression and purification of correctly processed, active human TACE catalytic domain in Saccharomyces cerevisiae. Protein Expr. Purif. 13(1), 104-10 (1998)

Colige, A., Li, S. W., Sieron, A. L., Nusgens, B. V., Prockop, D. J., Lapiere, C. M. cDNA cloning and expression of bovine procollagen I N-proteinase: a new member of the superfamily of zinc-metalloproteinases with binding sites for cells and other matrix components. Proc. Natl. Acad. Sci. USA 94(6), 2374-2379 (1997)

Condon, T. P., Flournoy, S., Sawyer, G. J., Baker, B. F., Kishimoto, T. K., Bennett, C. F. ADAM17 but not ADAM10 mediates tumor necrosis factor-a and L-selectin shedding from leukocyte membranes. Antisense Nucleic Acid Drug Dev. 11(2), 107-116 (2001)

Cornwall, G. A., Hsia, N. ADAM7, a member of the ADAM (a disintegrin and metalloprotease) gene family is specifically expressed in the mouse anterior pituitary and epididymis. Endocrinology 138(10), 4262-4272 (1997)

Cousin, H., Gaultier, A., Bleux, C., Darribere, T., Alfandari, D. PACSIN2 is a regulator of the metalloprotease/disintegrin ADAM13. Dev. Biol. 227(1), 197-210 (2000)

Cregg, J. M., Vedvick, T. S., Raschke, W. C. Recent advances in the expression of foreign genes in Pichia pastoris. Biotechnology (NY) 11(8), 905-910 (1993)

Dallas, D. J., Genever, P. G., Patton, A. J., Millichip, M. I., McKie, N., Skerry, T. M. Localization of ADAM10 and notch receptors in bone. Bone 25(1), 9-15 (1999)

Doedens, J. R. und Black, R. A. Stimulation-induced down-regulation of tumor necrosis factor-a converting enzyme. J. Biol. Chem. 275(19), 14598-14607 (2000)

Emi, M., Katagiri, T., Harada, Y., Saito, H., Inazawa, J., Ito, I., Kasumi, F., Nakamura, Y. A novel metalloprotease/disintegrin-like gene at 17q21.3 is somatically rearranged in two primary breast cancers. Nature Gen. 5, 151-157 (1993)

Eppig, J. J., Obrien, M., Wigglesworth, K. Mammalian oocyte growth, and development in vitro. Mol. Reprod. Dev. 44, 260-273 (1996)

Eto, K., Puzon-McLaughlin, W., Sheppard, D., Sehara-Fujisawa, A., Zhang, X. P., Takada, Y. RGD-independent binding of integrin a9b1 to the ADAM-12 and -15 disintegrin domains mediates cell-cell interaction. J. Biol. Chem. 275(45), 34922-34930 (2000)

Evans, J. P., Schultz, R. M., Kopf G. S. Mouse sperm-egg plasma membrane interactions: analysis of roles of egg integrins and the mouse sperm homologue of PH-30 (fertilin) b. J. Cell Sci. 108, 3267-3278 (1995)

Fambrough, D., Pan, D., Rubin, G. M., Goodman, C. S. The cell surface metalloprotease/disintegrin Kuzbanian is required for axonal extension in Drosophila. Proc. Natl. Acad. Sci. USA 93(23), 13233-13238 (1996)

Frayne, J. und Hall, L. The gene for the human tMDC I sperm surface protein is non-functional: implications for its proposed role in mammalian sperm-egg recognition. Biochem. J. 334(1), 171-176 (1998a)

Frayne, J., Jury, J. A., Barker, H. L., Perry, A. C., Jones, R., Hall, L. Macaque MDC family of proteins: sequence analysis, tissue distribution and processing in the male reproductive tract. Mol. Hum. Reprod. 4(5), 429-437 (1998b)

Frayne, J., Dimsey, E. A. C., Jury, J. A., Hall, L. Transcripts encoding the sperm surface protein tMDC II are non-functional in the human. Biochem. J. 341(3), 771-775 (1999)

Fritsche, J., Moser, M., Faust, S., Peuker, A., Buttner, R., Andreesen, R., Kreutz, M. Molecular cloning and characterization of a human metalloprotease disintegrin - a novel marker for dendritic cell differentiation. Blood 96(2), 732-739 (2000)

Galliano, M. F., Huet, C., Frygelius, J., Polgren, A., Wewer, U. M., Engvall, E. Binding of ADAM12, a marker of skeletal muscle regeneration, to the muscle-specific actin-binding protein, a -actinin-2, is required for myoblast fusion. J. Biol. Chem. 275(18), 13933-13939 (2000)

Gill, S. C. und Hippel, P. H. Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem. 182(2), 319-326 (1989)

Gilpin, B. J., Loechel, F., Mattei, M.-G., Engvall, E., Albrechtsen, R., Wewer, U. M. A novel, secreted form of human ADAM 12 (Meltrin a) provokes myogenesis in vivo. J. Biol. Chem. 273(1), 157-166 (1998)

Gomis-Rüth, F.-X., Kress, L. F., Bode, W. First structure of a snake venom metalloproteinase: a prototype for matrix metalloproteinases / collagenases. EMBO J. 12(11), 4151-4157 (1993)

Gong, X. H., Dubois, D. H., Miller, D. J., Shur, B. D. Activation of a G protein complex by aggregation of b-1,4-galactosyltransferase on the surface of sperm. Science 269, 1718-1721 (1995)

Grams, F., Huber, R., Kress, L. F., Moroder, L., Bode, W. Activation of snake venom metalloproteinases by a cysteine switch-like mechanism. FEBS Lett. 335(1), 76-80 (1993)

Grinna, L. S. und Tschopp, J. F. Size distribution and general structural features of N-linked oligosaccharides from the methylotrophic yeast, Pichia pastoris. Yeast 5(2), 107-115 (1989)

Gupta, S. K., Alves, K., O´Neil Palladino, L., Mark, G. E., Hollis, G. F. Molecular cloning of human Fertilin b subunit. Biochem. Biophys. Res. Commun. 224, 318-326 (1996)

Hamilton, T. C., Young, R. C., McKoy, W. M., Grotzinger, K. R., Green, J. A., Chu, E. W., Whang-Peng, J., Rogan, A. M., Green, W. R., Ozols, R. F. Characterization of a human ovarian carcinoma cell line (NIH: OVCAR-3) with androgen and estrogen receptors. Cancer Res. 43(11), 5379-5389 (1983)

Haas, T. E., Plow, E. F. Integrin-ligand interactions: a year in review. Curr. Opin. Cell Biol. 6, 656-662 (1994)

Hardy, C. M., Holland, M. K. Cloning and expression of recombinant rabbit Fertilin. Mol. Reprod. Dev. 45, 107-116 (1996)

Hardy, C. M., Clarke, H. G., Nixon, B., Grigg, J. A., Hinds, L. A., Holland, M. K. Examination of the immunocontraceptive potential of recombinant rabbit fertilin subunits in rabbit. Biol. Reprod. 57, 879-886 (1997)

Hernandez, L. D., Hoffmann, L. R., Wolfsberg, T. G., White, J. M. Virus-Cell and Cell-Cell fusion. Annu. Rev. Cell Dev. Biol. 12, 627-661 (1996)

Herren, B., Raines, E. W., Ross, R. Expression of a disintegrin-like protein in cultured human vascular cells in vivo. FASEB 111(2), 173-180 (1997)

Hinsch, E., Hägele, W., Schill, W. B., Hinsch, K. D. The zona pellucida receptors. Adv. Exp. Med. Biol. 424, 313-328 (1997)

Hite, L. A., Jia, L.-G., Bjarnason, J. B., Fox, J. W. cDNA sequences for four snake venom metalloproteinases: Structure, classification, and their relationship to mammalian reproductive proteins. Arch. Biochem. Biophys. 308, 182-190 (1994)

Ho, S. N., Hunt, H. D., Horton, R. M., Pullen, J. K., Pease, L. R. Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 77(1), 51-59 (1989)

Hougaard, S., Loechel, F., Xu, X., Tajima, R., Albrechtsen, R., Wewer, U. M. Trafficking of human ADAM 12-L: retention in the trans-Golgi network. Biochem. Biophys. Res. Commun. 275(2), 261-267 (2000)

Howard, L., Lu, X., Mitchell, S., Griffiths, S., Glynn, P. Molecular cloning of MADM: a catalytically active mammalian disintegrin-metalloproteinase expressed in various cell types. Biochem. J. 317, 45-50 (1996)

Howard, L., Nelson, K. K., Maciewicz, R. A., Blobel, C. P. Interaction of the metalloprotease disintegrins MDC9 and MDC15 with two SH3 domain-containing proteins, endophilin I and SH3PX1. J. Biol. Chem. 274(44), 31693-31699 (1999)

Howard, L., Maciewicz, R. A., Blobel, C. P. Cloning and characterization of ADAM28: evidence for autocatalytic pro-domain removal and for cell surface localization of mature ADAM28. Biochem J. 348(1), 21-27 (2000)

Howard, L., Zheng, Y., Horrocks, M., Maciewicz, R. A., Blobel, C. P. Catalytic activity of ADAM28. FEBS Lett. (2001) im Druck

Hunnicutt, G. R., Koppel, D. E., Myles, D. G. Analysis of the process of localization of Fertilin to the sperm posterior head plasma membrane domain during sperm maturation in the epididymis. Dev. Biol. 191, 146-159 (1997)

Huovila, A. P., Almeida, E. A. C.,White, J. M. ADAMs and cell fusion. Curr. Opin.Cell Biol. 8, 692-699 (1996)

Hurskainen, T. L., Hirohata, S., Seldin, M. F., Apte, S. S. ADAM-TS5, ADAM-TS6, and ADAM-TS7, novel members of a new family of zinc metalloproteases - General features and genomic distribution of the ADAM-TS family. J. Biol. Chem. 274(36), 25555-25563 (1999)

Iba, K., Albrechtsen, R., Gilpin, B. J., Loechel, F., Wewer, U. M. Cysteine-rich domain of human ADAM 12 (meltrin a) supports tumor cell adhesion. Am. J. Pathol. 154(5), 1489-1501 (1999)

Inoue, D., Reid, M., Lum, L., Kraetzschmar, J., Weskamp, G., Myung, Y. M., Baron, R., Blobel, C. P. Cloning and initial characterization of mouse meltrin b and analysis of the expression of four metalloprotease-disintegrins in bone cells. J. Biol. Chem. 273(7), 4180-4187 (1998)

Izumi, Y., Hirata, M., Hasuwa, H., Iwamoto, R., Umata, T., Miyado, K.Tamai, Y., Kurisaki, T., Sehara-Fujisawa, A., Ohno, S., Mekada, E. A metalloprotease-disintegrin, MDC9/meltrin-g/ADAM9 and PKCd are involved in TPA-induced ectodomain shedding of membrane-anchored heparin-binding EGF-like growth factor. EMBO J. 17(24), 7260-7272 (1998)

Jia, L.-G., Shimokawa, K.-I., Bjarnason, J. B., Fox, J. W. Snake venom metalloproteinases: Structure, Function, and Relationship to the ADAMs Family of Proteins. Toxicon 34(11/12), 1269-1276 (1996)

Jiang, W. und Bond, J. S. Families of metalloendopeptidases and their relationships. FEBS Lett. 312(2,3), 110-114 (1992)

Jury, J. A., Frayne, J., Hall, L. The human fertilin a gene is non-functional: implications for its proposed role in fertilization. Biochem. J. 321, 577-581 (1997)

Jury, J. K., Frayne, J., Hall, L. Sequence analysis of a variety of primate fertilin a genes: Evidence for non-functional genes in the gorilla and man. Mol. Reprod. Dev. 51(1), 92-97 (1998)

Kärkkäinen, I., Karhu, R., Huovila, A.-P. J. Assignment of the ADAM 15 gene to human chromosome band 1q21.3 by in situ hybridization. Cytogenet. Cell Genet. 88, 206-207 (2000)

Kang, Q., Cao, Y.,Zolkiewska, A. Metalloproteinase-disintegrin ADAM 12 binds to the SH3 domain of Src and activates Src tyrosine kinase in C2C12 cells. Biochem. J. 352, 883-892 (2000)

Kashiwagi, M., Tortorella, M., Nagase, H., Brew, K. TIMP-3 Is a Potent Inhibitor of ADAM-TS4 (Aggrecanase 1) and ADAM-TS5 (Aggrecanase 2). J. Biol. Chem. (2001) im Druck

Koike, H., Tomioka, S., Sorimachi, H., Saido, T. C., Maruyama, K., Okuyama, A., Fujisawa-Sehara, A., Ohno, S., Suzuki, K., Ishiura, S. Membrane-anchored metalloprotease MDC9 has an a-secretase activity responsible for processing the amyloid precursor protein. Biochem. J. 343, 371-375 (1999)

Krätzschmar, J., Lum, L., Blobel, C. P. Metargidin, a membrane-anchored metalloprotease-disintegrin protein with an RGD integrin binding sequence. J. Biol. Chem. 271(9), 4593-4596 (1996)

Kuno, K., Kanada, N., Nakashima, E., Fujiki, F., Ichimura, F., Matsushima, K. Molecular cloning of a gene encoding a new type of metalloproteinase-disintegrin family protein with thrombospondin motifs an an inflammation associated gene. J. Biol. Chem. 272(1), 556-562 (1997)

Kuno, K. und Matsushima, K. ADAMTS-1 protein anchors at the extracellular matrix through the thrombospondin type I motifs and its spacing region. J. Biol. Chem. 273(22), 13912-13917 (1998)

Kuno, K., Terashima, Y., Matsushima, K. ADAMTS-1 is an active metalloproteinase associated extracellular matrix. J. Biol. Chem. 274(26), 18821-18826 (1999)

Kuno, K., Okada, Y., Kawashima, H., Nakamura, H., Miyasaka, M., Ohno, H., Matsushima, K. ADAMTS-1 cleaves a cartilage proteoglycan, aggrecan. FEBS Lett. 478(3), 241-245 (2000)

Lammich, S., Kojro, E., Postina, R., Gilbert, S., Pfeiffer, R., Jasionowski, M., Haass, C., Fahrenholz, F. Constitutive and regulated a-secretase cleavage of Alzheimer's amyloid precursor protein by a disintegrin metalloprotease. Proc. Natl. Acad. Sci. USA 96, 3922-3927 (1999)

Lee, M. H., Knäuper, V., Becherer, J. D., Murphy, G. Full-length and N-TIMP-3 display equal inhibitory activities toward TNF-a convertase. Biochem. Biophys. Res. Commun. 280(3), 945-950 (2001)

Li, S. W., Arita, M., Fertala, A., Bao, Y., Kopen, G. C., Langsjo, T. K., Hyttinen, M. M., Helminen, H. J., Prockop, D. J. Transgenic mice with inactive alleles for procollagen N-proteinase (ADAMTS-2) develop fragile skin and male sterility. Biochem. J. 355(Pt 2), 271-278 (2001)

Linder, B. und Heinlein, U. A. Decreased in vitro fertilization efficiencies in the presence of specific cyritestin peptides. Dev. Growth Differ. 39(2), 243-247 (1997)

Liu, L. und Smith, J. W. Identification of ADAM 31: a protein expressed in Leydig cells and specialized epithelia. Endocrinology 141(6), 2033-2042 (2000)

Loechel, F., Gilpin, B. J., Engvall, E., Albrechtsen, R., Wewer, U. M. Human ADAM 12 (meltrin a) is an active metalloprotease. J. Biol. Chem. 273(27), 16993-16997 (1998)

Loechel, F., Overgaard, M. T., Oxvig, C., Albrechtsen, R., Wewer, U. M. Regulation of human ADAM 12 protease by the prodomain - Evidence for a functional, cysteine switch. J. Biol. Chem. 274(19), 13427-13433 (1999)

Loechel, F., Fox, J. W., Murphy, G., Albrechtsen, R., Wewer, U. M. ADAM 12-S cleaves IGFBP-3 and IGFBP-5 and is inhibited by TIMP-3. Biochem. Biophys. Res. Commun. 278, 511-515 (2000)

Lum, L., Blobel, C. P. Evidence for distinct serine protease activities with a potential role in processing the sperm protein fertilin. Dev. Biol. 191(1), 131-145 (1997)

Lum, L., Reid, M. S., Blobel, C. P. Intracellular maturation of the mouse metalloprotease disintegrin MDC15. J. Biol. Chem. 273(40), 26236-26247 (1998)

Lum, L., Wong, B. R., Josien, R., Becherer, J. D., Erdjument-Bromage, H., Schlöndorff, J., Tempst, P., Choi, Y., Blobel, C. P. Evidence for a role of a tumor necrosis factor-a (TNF-a)-converting enzyme-like protease in shedding of TRANCE, a TNF family member involved in osteoclastogenesis and dendritic cell survival. J. Biol. Chem. 274(19), 13613-13618 (1999)

Lunn, C. A., Fan, X., Dalie, B., Miller, K., Zavodny, P. J., Narula, S. K., Lundell, D. Purification of ADAM 10 from bovine spleen as a TNFa convertase. FEBS Lett. 400, 333-335 (1997)

Markland, F. S., Jr. Snake venoms. Drugs 54(Suppl. 3), 1-10 (1997)

Maskos, K., Fernandez-Catalan, C., Huber, R., Bourenkov, G. P., Bartunik, H., Ellestad, G. A., Reddy, P., Wolfson, M. F., Rauch, C. T., Castner, B. J., Davis, R., Clarke, H. R., Petersen, M., Fitzner, J. N., Cerretti, D. P., March, C. J., Paxton, R. J., Black, R. A., Bode, W. Crystal structure of the catalytic domain of human tumor necrosis factor-a-converting enzyme. Proc. Natl. Acad. Sci. USA 95(7), 3408-3412 (1998)

Matthews, R. T., Gary, S. C., Zerillo, C., Pratta, M., Solomon, K., Arner, E. C., Hockfield, S. Brain-enriched hyaluronan binding (BEHAB)/brevican cleavage in a glioma cell line is mediated by a disintegrin and metalloproteinase with thrombospondin motifs (ADAMTS) family member. J. Biol. Chem. 275(30), 22695-22703 (2000)

McCulloch, D. R., Harvey, M., Herington, A. C. The expression of the ADAMs proteases in prostate cancer cell lines and their regulation by dihydrotestosterone. Mol. Cell Endocrinol. 167(1-2), 11-21 (2000)

McKie, N., Edwards, T., Dallas, D. J., Houghton, A., Stringer, B., Graham, R., Russel, G., Croucher, P. I. Expression of members of a novel membrane linked metalloproteinase family (ADAM) in human articular chondrocytes. Biochem. Biophys. Res. Commun. 230, 335-339 (1997)

McLeskey, S. B., Dowds, C., Carballada, R., White, R. R., Saling, P. M. Molecules involved in mammalian sperm-egg interaction. Int. Rev. Cytol. 177, 57-113 (1998)

Milla, M. E., Leesnitzer, M. A., Moss, M. L., Clay, W. C., Carter, H. L., Miller, A. B., Su ,J. L., Lambert, M. H., Willard, D. H., Sheeley, D. M., Kost, T. A., Burkhart, W., Moyer, M., Blackburn, R. K., Pahel, G. L., Mitchell, J. L., Hoffman, C. R., Becherer, J. D. Specific sequence elements are required for the expression of functional tumor necrosis factor-a-converting enzyme (TACE). J. Biol. Chem. 274(43), 30563-30570 (1999)

Millichip, M. I., Dallas, D. J., Wu, E. X., Dale, S., McKie, N. The metallo-disintegrin ADAM10 (MADM) from bovine kidney has type IV collagenase activity in vitro. Biochem. Biophys. Res. Commun. 245(2), 594-598 (1998)

Möbus, V., Gerharz, C. D., Press, U., Moll, R., Beck, T., Mellin, W., Pollow, K., Knapstein, P. G., Kreienberg, R. Morphological, immunohistochemical and biochemical characterization of 6 newly established human ovarian carcinoma cell lines. Int. J. Cancer 52(1), 76-84 (1992)

Montgomery, A. M. P., Reisfeld, R. A., Cheresh, D. A. Integrin avb3 rescues melanoma cells from apoptosis in three-dimensional dermal collagen. Proc. Natl. Acad. Sci. USA 91, 8856-8860 (1994)

Moss, M. L., Jin, S. L. C., Becherer, J. D., Bicket, D. M., Burkhart, W., Chen, W.-J., Hassler, D., Leesnitzer, M. A., McGeehan, G., Milla, M. E., Moyer, M., Rocque, W., Seaton, T., Schönen, F., Warner, J., Willard, D. Structural features and biochemical properties of TNF-a converting enzyme (TACE). J. Neuroimmunol. 72, 127-129 (1997)

Moss, M. L., Jin, S. L. C., Milla, M. E., Burkhart, W., Carter, H. L., Chen, W.-J., Clay, W. C., Didsbury, J. R., Hassler, D., Hoffmann, C. R., Kost, T. A., Lambert, M. H., Leesnitzer, M. A., McCauley, P., McGeehan, G., Mitchell, J., Moyer, M., Pahel, G., Rocque, W., Overton, L. K., Schoenen, F., Seaton, T., Su, J.-L., Warner, J., Willard, D., Becherer, J. D. Cloning of a disintegrin metalloproteinase that processes precursor tumour-necrosis factor-a. Nature 385, 733-736 (1997)

Muga, A., Neugebauer, W., Hirama, T., Surewicz, W. K. Membrane Interactions and Conformational Properties of the Putative Fusion Peptide of PH-30, a Protein Active in Sperm-Egg Fusion. Biochemistry 33, 4444-4448 (1994)

Myles, D. G., Primakoff, P. Why did the sperm cross the cumulus? To get to the oocyte. Functions of the sperm surface proteins PH-20 and Fertilin in arriving at, and fusing with, the egg. Biol. Reprod. 56, 320-327 (1997)

Nagase, T., Ishikawa, K., Nakajima, D., Ohira, M., Seki, N., Miyajima, N., Tanaka, A., Kotani, H., Nomura, N., Ohara, O. Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA. Res. 4(2), 141-150 (1997)

Nakamura, H., Fujii, Y., Inoki, I., Sugimoto, K., Tanzawa, K., Matsuki, H., Miura, R., Yamaguchi, Y., Okada, Y. Brevican is degraded by matrix metalloproteinases and aggrecanase-1 (ADAMTS4) at different sites. J. Biol. Chem. 275(49), 38885-38890 (2000)

Nakayama, K. Furin: a mammalian subtilisin/kex2p-like endoprotease involved in processing of a wide variety of precursor proteins. Biochem. J. 327, 625-635 (1997)

Nath, D., Slocombe, P. M., Webster, A., Stephens, P. E., Docherty, A. J., Murphy, G. Meltrin g (ADAM-9) mediates cellular adhesion through a6b1 integrin, leading to a marked induction of fibroblast cell motility. J. Cell Sci. 113, 2319-2328 (2000)

Nelson, K. K., Schlöndorff, J., Blobel, C. P. Evidence for an interaction of the metalloprotease-disintegrin tumour necrosis factor a convertase (TACE) with mitotic arrest deficient 2 (MAD2), and of the metalloprotease-disintegrin MDC9 with novel MAD2-related protein, MAD2b. Biochem. J. 343, 673-680 (1999)

Pan, D., Rubin, G. M. Kuzbanian controls proteolytic processing of Notch and mediates lateral inhibition during Drosophila and vertebrate neurogenesis. Cell 90(2), 271-280 (1997)

Perry, A. C. F., Jones, R., Barker, P. J., Hall, L. A mammalian epididymal protein with remarkable sequence similarity to snake venom hämorrhagic peptides. Biochem. J. 286, 671-675 (1992)

Perry, A. C. F., Gichuhi, P. M., Jones, R., Hall, L. Cloning and analysis of monkey fertilin reveals novel a subunit isoforms. Biochem. J. 307, 843-850 (1995)

Peschon, J. J., Slack, J. L., Reddy, P., Stocking, K. L., Sunnarborg, S. W., Lee, D. C., Russell, W. E., Castner, B. J., Johnson, R. S., Fitzner, J. N., Boyce, R. W., Nelson, N., Kozlosky, C. J., Wolfson, M. F., Rauch, C. T., Cerretti, D. P., Paxton, R. J., March, C. J., Black, R. A. An essential role for ectodomain shedding in mammalian development. Science 282(5392), 1281-1284 (1998)

Phelps B. M., Koppel, D. E., Primakoff, P., Myles, D. G. Evidence that proteolysis of the surface is an initial step in the mechanism of formation of sperm cell surface domains. J. Cell Biol. 111, 1839-1847 (1990)

Plantefaber, L. C. und Hynes, R. O. Changes in integrin receptors on oncogenically transformed cells. Cell 56, 281-290 (1989)

Podbilewicz, B. ADM-1, a protein with metalloprotease- and disintegrin-like domains, is expressed in syncytial organs, sperm, and sheath cells of sensory organs in a. Mol. Biol. Cell 7(12), 1877-1893 (1996)

Poindexter, K., Nelson, N., DuBose, R. F., Black, R. A., Cerretti, D. P. The identification of seven metalloproteinase-disintegrin (ADAM) genes from genomic libraries. Gene 237(1), 61-70 (1999)

Primakoff, P., Hyatt, H., Tredick-Kline, J. Identification and purification of a sperm surface protein with a potential role in sperm-egg membrane fusion. J. Cell Biol. 104, 141-149 (1987)

Ramarao, C. S., Myles, D. G., White, J. M., Primakoff, P. Initial evaluation of Fertilin as an immunocontraceptive antigen and molecular cloning of the cynomolgus monkey Fertilin b subunit. Mol. Reprod. Dev. 43, 70-75 (1996)

Reddy, P., Slack, J. L., Davis, R., Cerretti, D. P., Kozlosky, C. J., Blanton, R. A., Shows, D., Peschon, J. J., Black, R. A. Functional analysis of the domain structure of tumor necrosis factor-a converting enzyme. J. Biol. Chem. 275(19), 14608-14614 (2000)

Rio, C., Buxbaum, J. D., Peschon, J. J., Corfas, G. Tumor necrosis factor-a-converting enzyme is required for cleavage of erbB4/HER4. J. Biol. Chem. 275(14), 10379-10387 (2000)

Roberts, C. M., Tani, P. H., Bridges, L. C., Laszik, Z., Bowditch, R. D. MDC-L, a novel metalloprotease disintegrin cysteine-rich protein family member expressed by human lymphocytes. J. Biol. Chem. 274(41), 29251-29259 (1999)

Roghani, M., Becherer, J. D., Moss, M. L., Atherton, R. E., Erdjument-Bromage, H., Arribas, J., Blackburn, R. K., Weskamp, G., Tempst, P., Blobel, C. P. Metalloprotease-disintegrin MDC9: Intracellular maturation and catalytic activity. J. Biol. Chem. 274(6), 3531-3540 (1999)

Rosendahl, M. S., Ko, S. C., Long, D. L., Brewer, M. T., Rosenzweig, B., Hedl, E., Anderson, L., Pyle, S. M., Moreland, J., Meyers, M. A., Kohno, T., Lyons, D., Lichenstein, H. S. Identification and characterization of a pro-tumor necrosis factor-a-processing enzyme from the ADAM family of zinc metalloproteases. J. Biol. Chem. 272(39), 24588-24593 (1997)

Sagane, K., Ohya, Y., Hasegawa, Y., Tanaka, I. Metalloproteinase-like, disintegrin-like, cysteine-rich proteins MDC2 and MDC3: novel human cellular disintegrins highly expressed in the brain. Biochem. J. 334(1), 93-98 (1998)

Saling, P. M. Mammalian sperm interaction with extracellular matrices of the egg. Oxf. Rev. Reprod. Biol. 11, 339-388 (1989)

Satoh, K., Suzuki, N., Yokota, H. ADAMTS-4 (a disintegrin and metalloproteinase with thrombospondin motifs) is transcriptionally induced in beta-amyloid treated rat astrocytes. Neurosci. Lett. 289(3), 177-180 (2000)

Schlöndorff, J. und Blobel, C. P. Metalloprotease-disintegrins: modular proteins capable of promoting cell-cell interactions and triggering signals by protein-ectodomain shedding. J. Cell Sci. 112(21), 3603-3617 (1999)

Schlöndorff, J., Becherer, J. D., Blobel, C. P. Intracellular maturation and localization of the tumour necrosis factor a convertase (TACE). Biochem. J. 347(1), 131-138 (2000)

Schoenle, E. J., Adams, L. D., Sammons, D. W. Insulin-induced rapid decrease of a major protein in fat cell plasma membranes. J. Biol. Chem. 259(19), 12112-12116 (1984)

Schwettmann, L. und Tschesche, H. Cloning and Expression in Pichia pastoris of Metalloprotease Domain of ADAM 9 Catalytically Active against Fibronectin. Protein Expr. Purif. 21(1), 65-70 (2001)

Shi, Z., Xu, W., Loechel, F., Wewer, U. M., Murphy, L. J. ADAM 12, a disintegrin metalloprotease, interacts with insulin-like growth factor-binding protein-3. J. Biol. Chem. 275(24), 18574-18580 (2000)

Shilling, F. M., Kratzschmar, J., Cai, H., Weskamp, G., Gayko, U., Leibow, J., Myles, D. G., Nuccitelli, R., Blobel, C. P. Identification of metalloprotease/disintegrins in Xenopus laevis testis with a potential role in fertilization. Dev. Biol. 186(2), 155-164 (1997)

Shindo, T., Kurihara, H., Kuno, K., Yokoyama, H., Wada, T., Kurihara, Y., Imai, T., Wang, Y., Ogata, M., Nishimatsu, H., Moriyama, N., Oh-hashi, Y., Morita, H., Ishikawa, T., Nagai, R., Yazaki, Y., Matsushima, K. ADAMTS-1: a metalloproteinase-disintegrin essential for normal growth, fertility, and organ morphology and function. J. Clin. Invest. 105(10), 1345-1352 (2000)

Snell, W. J., White, J. M. The molecules of mammalian fertilization. Cell 85, 629-637 (1996)

Sotillos, S., Roch, F., Campuzano, S. The metalloprotease-disintegrin Kuzbanian participates in Notch activation during growth and patterning of Drosophila imaginal discs. Development 124(23), 4769-4779 (1997)

Takahashi, Y., Bigler, D., Ito, Y., White, J. M. Sequence-Specific Interaction between the Disintegrin Domain of Mouse ADAM 3 and Murine Eggs: Role of b1 Integrin-associated Proteins CD9, CD81, and CD98. Mol. Biol. Cell 12(4), 809-820 (2001)

Tang, B. L. ADAMTS: a novel family of extracellular matrix proteases. Int. J. Biochem. Cell Biol. 33(1), 33-44 (2001)

Töpfer-Petersen, E., Dostalova, Z., Calvete, J. J. The role of carbohydrates in sperm-egg interaction. Adv. Exp. Med. Biol. 424, 301-310 (1997)

Tortorella, M. D., Burn, T. C., Pratta, M. A., Abbaszade, I., Hollis, J. M., Liu, R., Rosenfeld, S. A., Copeland, R. A., Decicco, C. P., Wynn, R., Rockwell, A., Yang, F., Duke, J. L., Solomon, K., George, H., Bruckner, R., Nagase, H., Itoh, Y., Ellis, D.M., Ross, H., Wiswall, B. H., Murphy, K., Hillman, M. C. Jr., Hollis, G. F., Arner, E. C. Purification and cloning of aggrecanase-1: a member of the ADAMTS family of proteins. Science 284(5420), 1664-1666 (1999)

Tortorella, M., Pratta, M., Liu, R. Q., Abbaszade, I., Ross, H., Burn, T., Arner, E. The thrombospondin motif of aggrecanase-1 (ADAMTS-4) is critical for aggrecan substrate recognition and cleavage. J. Biol. Chem. 275(33), 25791-25797 (2000)

Tulsiani, D. R. P., Yoshida-Komiya, H., Araki, Y. Mammalian fertilization: A carbohydrate-mediated event. Biol. Reprod. 57, 487-494 (1997)

van Dyk, D. E., Marchand, P., Bruckner, R. C., Fox, J. W., Jaffee, B. D., Gunyuzlu, P. L., Davis, G. L., Nurnberg, S., Covington, M., Decicco, C. P., Trzaskos, J. M., Magolda, R. L., Copeland, R. A. Comparison of snake venom reprolysin and matrix metalloproteinases as models of TNF-a converting enzyme. Bioorg. Med. Chem. Lett. 7(10), 1219-1224 (1997)

van Huijsduijnen, R. H. ADAM 20 and 21; two novel human testis-specific membrane metalloproteases with similarity to fertilin a. Gene 206, 273-282 (1998) van Wart, H. E. und Birkedal-Hansen, H. The cysteine switch: a principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family. Proc. Natl. Acad. Sci. USA 87, 5578-5582 (1990)

Vazquez, F., Hastings, G., Ortega, M. A., Lane, T. F., Oikemus, S., Lombardo, M., Iruela-Arispe, M. L. METH-1, a human ortholog of ADAMTS-1, and METH-2 are members of a new family of proteins with angio-inhibitory activity. J. Biol. Chem. 274(33), 23349-23357 (1999)

Vidäus, C. M., von Kap-Herr, C., Golden, W. L., Eddy, R. L., Shows, T. B., Herr, J. C. Human Fertilin b: Identification, characterization, and chromosomal mapping of an ADAM gene family member. Mol. Reprod. Dev. 46, 363-369 (1997)

Ward, C., Storey, B., Kopf, G. Selective activation of Gi1 and Gi2 in mouse sperm by zona pellucida, the eggs extracellular matrix. J. Biol. Chem. 269, 13254-13258 (1994)

Wassarman, P. M. Die Besamung des Säuger-Eies. Spektrum der Wissenschaft, 96-103 (1989)

Waters, S. I., White, J. M. Biochemical and molecular characterization of bovine fertilin a and b (ADAM 1 and ADAM 2): A candidate sperm-egg binding/fusion complex. Biol. Reprod. 56(5), 1245-1254 (1997)

Wei, P., Zhao, Y. G., Zhuang, L., Ruben, S., Sang, Q. X. Expression and enzymatic activity of human disintegrin and metalloproteinase ADAM19/meltrin beta. Biochem. Biophys. Res. Commun. 280(3), 744-755 (2001)

Weskamp, G., Krätzschmar, J., Reid, M. S., Blobel, C. P. MDC9, a widely expressed cellular disintegrin containing cytoplasmic SH3 ligand domains. J. Cell Biol. 132(4), 717-726 (1996)

Wessel, D. und Flügge, U. A method for the quantitative recovery of protein in dilute solution in the presence of detergents and lipids. Anal. Biochem. 138, 141-143 (1984)

Wolfsberg, T. G., Bazan, J. F., Blobel, C. P., Myles, D. G., Primakoff, P., White, J. M. The precursor region of a protein active in sperm-egg fusion contains a metalloproteinase and a disintegrin domain: Structural, functional and evolutionary implications. Proc. Natl. Acad. Sci. USA 90, 10783-10787 (1993)

Wolfsberg, T. G., Straight, P. D., Gerena, R. L., Huovila, A. P. J., Primakoff, P., Myles, D. G., White, J. M. ADAM, a Widley Distributed and Developmentally Regulated Gene Family Encoding Membrane Proteins with A Disintegrin And Metalloprotease Domain. Dev. Biol. 169, 378-383 (1995)

Wolfsberg, T. G., White, J. M. ADAMs in fertilazitation and development. Dev. Biol. 180, 389-401 (1996)

Wolfsberg, T. G. und White, J. M. ADAM metalloproteinases. Handbook of Proteolytic Enzymes 447, 1310-1313 (1998)

Wu, E., Croucher, P. I., McKie, N. Expression of members of the novel membrane linked metalloproteinase family ADAM in cells derived from a range of haematological malignancies. Biochem. Biophys. Res. Commun. 235(2), 437-442 (1997)

Yagami-Hiromasa, T., Sato, T., Kurisaki, T., Kamijo, K., Nabeshima, Y.-I., Fujisawa-Sehara, A. A metalloproteinase-disintegrin participating in myoblast fusion. Nature 377, 652-656 (1995)

Yeh, C. H., Peng, H. C., Yih, J. B., Huang, T. F. A new short chain RGD-containing disintegrin, accutin, inhibits the common pathway of human platelet aggregation. Biochim. Biophys. Acta 1425, 493-504 (1998)

Yoshiyama, K., Higuchi, Y., Kataoka, M., Matsuura, K., Yamamoto, S. CD156 (human ADAM8): expression, primary amino acid sequence, and gene location. Genomics 41(1), 56-62 (1997)

Yuan, R. Y., Primakoff, P., Myles, D. G. A role for the disintegrin domain of cyritestin, a sperm surface protein belonging to the ADAM family, in mouse sperm-egg plasma membrane adhesion and fusion. J. Cell Biol. 137(1), 105-112 (1997)

Zhang, X. P., Kamata, T., Yokoyama, K., Puzon-McLaughlin, W., Takada, Y. Specific interaction of the recombinant disintegrin-like domain of MDC-15 (metargidin, ADAM-15) with integrin avb3. J. Biol. Chem. 273(13), 7345-7350 (1998)

Zhang, Z., Kolls, J. K., Oliver, P., Good, D., Schwarzenberger, P. O., Joshi, M. S., Ponthier, J. L., Lancaster, J. R. Jr. Activation of tumor necrosis factor-a-converting enzyme-mediated ectodomain shedding by nitric oxide. J. Biol. Chem. 275(21), 15839-15844 (2000)

Zhao, J., Chen, H., Peschon, J. J., Shi, W., Zhang, Y., Frank, S. J., Warburton, D. Pulmonary Hypoplasia in Mice Lacking Tumor Necrosis Factor-a Converting Enzyme Indicates an Indispensable Role for Cell Surface Protein Shedding during Embryonic Lung Branching Morphogenesis. Dev. Biol. 232(1), 204-218 (2001)

Zhou, M., Graham, R., Russell, G., Croucher, P. I. MDC-9 (ADAM-9/Meltrin g) Functions as an Adhesion Molecule by Binding the avb5 Integrin. Biochem. Biophys. Res. Commun. 280(2), 574-580 (2001)

Zhu, G. Z., Lin, Y., Myles, D. G., Primakoff, P. Identification of four novel ADAMs with potential roles in spermatogenesis and fertilization. Gene 234(2), 227-237 (1999)

Zhu, X., Bansal, N. P., Evans, J. P. Identification of key functional amino acids of the mouse fertilin b (ADAM2) disintegrin loop for cell-cell adhesion during fertilization. J. Biol. Chem. 275(11), 7677-7683 (2000)