A general model for nucleic acid helicases and their "coupling" within macromolecular machines.
von Hippel
P H
PH
Institute of Molecular Biology and, Department of Chemistry, University of Oregon, Eugene, OR 97403, USA. petevh@molbio.uoregon.edu
Delagoutte
E
E
D000255:Adenosine Triphosphate / Q000378:metabolism*; D004247:DNA / Q000378:metabolism*; D004265:DNA Helicases / Q000737:chemistry / Q000378:metabolism*; D004261:DNA Replication / Q000502:physiology; D004268:DNA-Binding Proteins / Q000378:metabolism; D046911:Macromolecular Substances; D020409:Molecular Motor Proteins / Q000378:metabolism; D009690:Nucleic Acid Conformation; D020365:RNA Helicases / Q000737:chemistry / Q000378:metabolism*; D012330:RNA, Double-Stranded / Q000378:metabolism; D013816:Thermodynamics; D014158:Transcription, Genetic / Q000235:genetics; D014764:Viral Proteins / Q000378:metabolism
D004268:DNA-Binding Proteins; D046911:Macromolecular Substances; D020409:Molecular Motor Proteins; D012330:RNA, Double-Stranded; D014764:Viral Proteins; C060035:gp32 protein, Enterobacteria phage T4; D000255:Adenosine Triphosphate; D004247:DNA; D004265:DNA Helicases; D020365:RNA Helicases