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Volumn 280, Issue 25, 2005, Pages 23540-23548
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The periplasmic chaperone SurA exploits two features characteristic of integral outer membrane proteins for selective substrate recognition
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Author keywords
[No Author keywords available]
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Indexed keywords
AMINO ACIDS;
ASSOCIATION REACTIONS;
BINDING ENERGY;
BIOLOGICAL MEMBRANES;
CELLULOSE;
ENZYMES;
ESCHERICHIA COLI;
CHAPERONE ACTIVITY;
MEMBRANE PROTEINS;
PEPTIDYL-PROLYL ISOMERASE (PPIASE);
PERIPLASMIC CHAPERONE;
PROTEINS;
CHAPERONE;
CYCLOPHILIN;
OUTER MEMBRANE PROTEIN;
PEPTIDE LIBRARY;
PERIPLASMIC PROTEIN;
PROLINE;
PROTEIN SUBUNIT;
PROTEIN SURA;
UNCLASSIFIED DRUG;
ARTICLE;
CONTROLLED STUDY;
ENZYME SPECIFICITY;
NONHUMAN;
PRIORITY JOURNAL;
PROTEIN BINDING;
PROTEIN FOLDING;
PROTEIN FUNCTION;
PROTEIN LOCALIZATION;
PROTEIN MOTIF;
PROTEIN STRUCTURE;
AMINO ACID SEQUENCE;
BACTERIAL OUTER MEMBRANE PROTEINS;
CARRIER PROTEINS;
ESCHERICHIA COLI PROTEINS;
MOLECULAR CHAPERONES;
MOLECULAR SEQUENCE DATA;
PEPTIDYLPROLYL ISOMERASE;
PERIPLASM;
PROTEIN BINDING;
SUBSTRATE SPECIFICITY;
SURFACE PLASMON RESONANCE;
AMINO ACIDS;
CELLULOSE;
ENZYMES;
PROTEINS;
ESCHERICHIA COLI;
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EID: 21244447713
PISSN: 00219258
EISSN: None
Source Type: Journal
DOI: 10.1074/jbc.M413742200 Document Type: Article |
Times cited : (90)
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References (30)
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