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Volumn 320, Issue 2, 2002, Pages 321-332
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Solution structure of the single-domain prolyl cis/trans isomerase PIN1At from Arabidopsis thaliana
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Author keywords
Arabidopsis thaliana; Nuclear magnetic resonance; Phosphorylated substrate; PIN1; PIN1At
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Indexed keywords
AMIDE;
AMINO ACID;
ARGININE;
CELL CYCLE PROTEIN;
ISOMERASE;
PHOSPHOSERINE;
PHOSPHOTHREONINE;
PROTEIN PIN1AT;
PROTON;
SODIUM SULFATE;
SULFATE;
UNCLASSIFIED DRUG;
AMINO TERMINAL SEQUENCE;
ARABIDOPSIS;
ARTICLE;
CALCULATION;
CATALYSIS;
CRYSTAL STRUCTURE;
ENZYME SPECIFICITY;
ENZYME STRUCTURE;
ENZYME SUBSTRATE;
HYDROPHOBICITY;
ISOMERISM;
NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY;
PRIORITY JOURNAL;
PROTEIN ANALYSIS;
PROTEIN DOMAIN;
PROTEIN FOLDING;
PROTEIN FUNCTION;
PROTEIN PROTEIN INTERACTION;
ARABIDOPSIS;
ARABIDOPSIS THALIANA;
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EID: 0036296327
PISSN: 00222836
EISSN: None
Source Type: Journal
DOI: 10.1016/S0022-2836(02)00429-1 Document Type: Article |
Times cited : (37)
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References (41)
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