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IUBMB Life|August 19, 2007
Ligand pathways in myoglobin: a review of Trp cavity mutationsJ S Olson, J Soman, G N PhillipsJournal of Molecular Biology|May 20, 1989
Structure of myoglobin-ethyl isocyanide. Histidine as a swinging door for ligand entryK A Johnson, J S Olson, G N PhillipsBiochemistry|February 15, 1994
Structural determinants of the stretching frequency of CO bound to myoglobinT Li, M L Quillin, G N Phillips, et al.Journal of Molecular Biology|November 5, 1993
High-resolution crystal structures of distal histidine mutants of sperm whale myoglobinM L Quillin, R M Arduini, J S Olson, et al.Proteins|April 9, 1998
Nitric oxide myoglobin: crystal structure and analysis of ligand geometryE A Brucker, J S Olson, M Ikeda-Saito, et al.The Journal of Biological Chemistry|December 1, 2000
Waterproofing the heme pocket. Role of proximal amino acid side chains in preventing hemin loss from myoglobinE C Liong, Y Dou, E E Scott, et al.The Journal of Biological Chemistry|October 11, 1996
High resolution crystal structures of the deoxy, oxy, and aquomet forms of cobalt myoglobinE A Brucker, J S Olson, G N Phillips, et al.Proteins|August 1, 1995
Phe-46(CD4) orients the distal histidine for hydrogen bonding to bound ligands in sperm whale myoglobinH H Lai, T Li, D S Lyons, et al.Biochemistry|September 6, 1994
Nitric oxide recombination to double mutants of myoglobin: role of ligand diffusion in a fluctuating heme pocketM L Carlson, R Regan, R Elber, et al.The Journal of Biological Chemistry|February 11, 1994
His64(E7)-->Tyr apomyoglobin as a reagent for measuring rates of hemin dissociationM S Hargrove, E W Singleton, M L Quillin, et al.Pageof 18