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Volumn 9, Issue 12, 2001, Pages 1225-1236
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Crystallographic and modeling studies of RNase III suggest a mechanism for double-stranded RNA cleavage
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Author keywords
Compound active center; dsRNA; Endonuclease domain; RNA interference; RNA processing; RNase III
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Indexed keywords
DIMER;
DOUBLE STRANDED RNA;
ENDONUCLEASE;
LIGAND;
MANGANESE;
MONOMER;
POLYPEPTIDE;
RIBONUCLEASE III;
ACCURACY;
ARTICLE;
BINDING AFFINITY;
BIOLOGY;
COMPARATIVE STUDY;
COMPLEX FORMATION;
CRYSTAL STRUCTURE;
CRYSTALLOGRAPHY;
DIMERIZATION;
ENZYME ACTIVITY;
ENZYME STRUCTURE;
GENETICS;
HYDROPHOBICITY;
IMAGE ANALYSIS;
MODEL;
MOLECULAR INTERACTION;
PRIORITY JOURNAL;
PROTEIN DOMAIN;
PROTEIN FOLDING;
PROTEIN INTERACTION;
RNA CLEAVAGE;
STRUCTURE ANALYSIS;
AMINO ACID SEQUENCE;
BINDING SITES;
CRYSTALLOGRAPHY, X-RAY;
DIMERIZATION;
ENDORIBONUCLEASES;
ESCHERICHIA COLI PROTEINS;
LIGANDS;
MANGANESE;
MODELS, MOLECULAR;
MOLECULAR SEQUENCE DATA;
MUTATION;
NUCLEIC ACID CONFORMATION;
PROTEIN BINDING;
PROTEIN CONFORMATION;
PROTEIN FOLDING;
PROTEIN STRUCTURE, SECONDARY;
PROTEIN STRUCTURE, TERTIARY;
RIBONUCLEASE III;
RNA, DOUBLE-STRANDED;
SEQUENCE HOMOLOGY, AMINO ACID;
AQUIFEX AEOLICUS;
BACTERIA (MICROORGANISMS);
ESCHERICHIA COLI;
EUKARYOTA;
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EID: 0035662491
PISSN: 09692126
EISSN: None
Source Type: Journal
DOI: 10.1016/S0969-2126(01)00685-2 Document Type: Article |
Times cited : (211)
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References (63)
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