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Identification of Gln726 in nidogen as the amine acceptor in transglutaminase-catalyzed cross-linking of laminin-nidogen complexes.
Aeschlimann D, Paulsson M, Mann K. Aeschlimann D, et al. J Biol Chem. 1992 Jun 5;267(16):11316-21. J Biol Chem. 1992. PMID: 1350783 Free article.
The laminin-nidogen complex, the most abundant noncollagenous component of basement membranes, was recently shown to be a specific substrate for tissue transglutaminase (Aeschlimann, D., and Paulsson, M. (1991) J. Biol. Chem. 266, 15308-15317). Saturation experiment …
The laminin-nidogen complex, the most abundant noncollagenous component of basement membranes, was recently shown to be a specific substrate …
Transglutaminase-catalyzed matrix cross-linking in differentiating cartilage: identification of osteonectin as a major glutaminyl substrate.
Aeschlimann D, Kaupp O, Paulsson M. Aeschlimann D, et al. J Cell Biol. 1995 May;129(3):881-92. doi: 10.1083/jcb.129.3.881. J Cell Biol. 1995. PMID: 7730416 Free PMC article.
The expression of tissue transglutaminase in skeletal tissues is strictly regulated and correlates with chondrocyte differentiation and cartilage calcification in endochondral bone formation and in maturation of tracheal cartilage (Aeschlimann, D., A. Wetterwald, H. …
The expression of tissue transglutaminase in skeletal tissues is strictly regulated and correlates with chondrocyte differentiation and cart …
66 results