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Person
ISNI: 
0000 0001 2428 9257
Name: 
Henderson, R.
Henderson, R M
Henderson, Robert
Creation class: 
Text
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Creation role: 
author
Related names: 
University of Cambridge
Titles: 
Atomic force microscopy of the EcoKI Type I DNA restriction enzyme bound to DNA shows enzyme dimerization and DNA looping
Atomic force microscopy study of the structural effects induced by echinomycin binding to DNA.
DNA looping and translocation provide an optimal cleavage mechanism for the type III restriction enzymes.
Fast-scan atomic force microscopy reveals that the type III restriction enzyme EcoP15I is capable of DNA translocation and looping
Investigation of Protein Partnerships Using Atomic Force Microscopy
Pushing, pulling, dragging, and vibrating renal epithelia by using atomic force microscopy.
Structural perturbations in DNA caused by bis-intercalation of ditercalinium visualised by atomic force microscopy.
Structure of Ocr from bacteriophage T7, a protein that mimics B-form DNA.
Translocation-independent dimerization of the EcoKI endonuclease visualized by atomic force microscopy.
X-ray analysis of α -chymotrypsin : substrate and inhibitor binding
Notes: 
Sources: 
JNAM