Structural Studies of Complexed FK-506 Binding Protein
Author:
Publisher
Wiley
Subject
History and Philosophy of Science,General Biochemistry, Genetics and Molecular Biology,General Neuroscience
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1749-6632.1993.tb35848.x/fullpdf
Reference18 articles.
1. Chemistry and Biology of the Immunophilins and Their Immunosuppressive Ligands
2. Natural Products as Probes of Cellular Function: Studies of Immunophilins
3. Cyclophilin: A Specific Cytosolic Binding Protein for Cyclosporin A
4. A receptor for the immuno-suppressant FK506 is a cis–trans peptidyl-prolyl isomerase
5. A cytosolic binding protein for the immunosuppressant FK506 has peptidyl-prolyl isomerase activity but is distinct from cyclophilin
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1. Structure and Activity of the Peptidyl-Prolyl Isomerase Domain from the Histone Chaperone Fpr4 toward Histone H3 Proline Isomerization;Journal of Biological Chemistry;2013-09
2. CYCLOSPORINE AND TACROLIMUS;Clinics in Liver Disease;1997-08
3. Structure comparison of native and mutant human recombinant FKBP12 complexes with the immunosuppressant drug FK506 (tacrolimus);Protein Science;1995-11
4. ESCHERICHIA-COLI AND OTHER SPECIES OF THE ENTEROBACTERIACEAE ENCODE A PROTEIN SIMILAR TO THE FAMILY OF MIP-LIKE FK506-BINDING PROTEINS;ARCH MICROBIOL;1995
5. Escherichia coli and other species of the enterobacteriaceae encode a protein similar to the family of Mip-like FK506-binding proteins;Archives of Microbiology;1995-05
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