Structure-function relationships in the ferritins.
Harrison
P M
PM
Krebs Institute, University of Sheffield, UK.
Hempstead
P D
PD
Artymiuk
P J
PJ
Andrews
S C
SC
D000595:Amino Acid Sequence; D000818:Animals; D001426:Bacterial Proteins / Q000737:chemistry; D001665:Binding Sites; D003573:Cytochrome b Group / Q000737:chemistry; D005288:Ferredoxins / Q000737:chemistry; D005293:Ferritins / Q000737:chemistry*; D006422:Hemerythrin; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010802:Phylogeny; D011487:Protein Conformation; D017510:Protein Folding; D011994:Recombinant Proteins; D012416:Rubredoxins; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D013329:Structure-Activity Relationship; D014867:Water; D014961:X-Ray Diffraction
D001426:Bacterial Proteins; D003573:Cytochrome b Group; D005288:Ferredoxins; D006422:Hemerythrin; D011994:Recombinant Proteins; D012416:Rubredoxins; C055857:rubrerythrins; D014867:Water; D005293:Ferritins; C018032:bacterioferritin