Solution structure and dynamics of linked cell attachment modules of mouse fibronectin containing the RGD and synergy regions: comparison with the human fibronectin crystal structure 1 1Edited by P. E. Wright

Author:

é Valérie,Tomita York,Akiyama Steven K.,Aota Shin-ichi,Yamada Kenneth M.,Venable Richard M.,Pastor Richard W.,Krueger Susan,Torchia Dennis A.

Publisher

Elsevier BV

Subject

Molecular Biology,Structural Biology

Reference59 articles.

1. Characterization of regions of fibronectin besides the arginine-glycine-aspartic acid sequence required for adhesive function of the cell-binding domain using site-directed mutagenesis;Aota;J. Biol. Chem.,1991

2. The short amino acid sequence Pro-His-Ser-Arg-Asn in human fibronectin enhances cell-adhesive function;Aota;J. Biol. Chem.,1994

3. An alternative 3D NMR technique for correlating backbone 15N with side chain Hβresonances in larger proteins;Archer;J. Magn. Reson. ser. B,1991

4. Backbone dynamics of calmodulin studied by 15N relaxation using inverse detected two-dimensional NMR spectroscopy;Barbato;Biochemistry,1992

5. Sensitivity enhanced two-dimensional heteronuclear shift correlation NMR spectroscopy;Bax;J. Magn. Reson. ser. B,1986

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