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Q35648424-1B39AD6F-DC0E-4A06-BC2B-BE7CCCC0E92D
Q35648424-1B39AD6F-DC0E-4A06-BC2B-BE7CCCC0E92D
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http://www.wikidata.org/entity/statement/Q35648424-1B39AD6F-DC0E-4A06-BC2B-BE7CCCC0E92D
Influence of substrate modification and C-terminal truncation on the active site structure of substrate-bound heme oxygenase from Neisseriae meningitidis. A 1H NMR study.
P2860
Q35648424-1B39AD6F-DC0E-4A06-BC2B-BE7CCCC0E92D
BestRank
Statement
http://www.wikidata.org/entity/statement/Q35648424-1B39AD6F-DC0E-4A06-BC2B-BE7CCCC0E92D
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wasDerivedFrom
69e54e48813ea03765d2def53d1bf4afada817a6
P2860
Alteration of the regiospecificity of human heme oxygenase-1 by unseating of the heme but not disruption of the distal hydrogen bonding network