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Summary Anatomy Item Literature (421) Expression Attributions Wiki
XB-ANAT-682

Papers associated with acellular anatomical structure (and adam28.2)

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ADAMTS9, a member of the ADAMTS family, in Xenopus development., Desanlis I., Gene Expr Patterns. September 1, 2018; 29 72-81.                

Identification of genes expressed in the migrating primitive myeloid lineage of Xenopus laevis., Agricola ZN., Dev Dyn. January 1, 2016; 245 (1): 47-55.                      

The ADAMTS (A Disintegrin and Metalloproteinase with Thrombospondin motifs) family., Kelwick R., Genome Biol. May 30, 2015; 16 (1): 113.    

Inhibition of integrin-mediated adhesion and signaling disrupts retinal development., Li M., Dev Biol. November 1, 2004; 275 (1): 202-14.

The cysteine-rich domain regulates ADAM protease function in vivo., Smith KM., J Cell Biol. December 9, 2002; 159 (5): 893-902.                

ADAM13 disintegrin and cysteine-rich domains bind to the second heparin-binding domain of fibronectin., Gaultier A., J Biol Chem. June 28, 2002; 277 (26): 23336-44.

Xenopus ADAM 13 is a metalloprotease required for cranial neural crest-cell migration., Alfandari D, Alfandari D., Curr Biol. June 26, 2001; 11 (12): 918-30.            

Voltage-dependent activation of frog eggs by a sperm surface disintegrin peptide., Shilling FM., Dev Biol. October 1, 1998; 202 (1): 113-24.              

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