Expression of transglutaminase substrate activity on Candida albicans germ tubes through a coiled, disulfide-bonded N-terminal domain of Hwp1 requires C-terminal glycosylphosphatidylinositol modification. [electronic resource]
Producer: 20041026Description: 40737-47 p. digitalISSN:- 0021-9258
- Amines -- chemistry
- Animals
- Biophysical Phenomena
- Biophysics
- Biotin -- analogs & derivatives
- Blotting, Western
- Candida albicans -- enzymology
- Cell Adhesion
- Cell Wall -- chemistry
- Circular Dichroism
- Disulfides -- chemistry
- Electrophoresis, Polyacrylamide Gel
- Epithelial Cells -- metabolism
- Fungal Proteins -- chemistry
- GTP-Binding Proteins -- chemistry
- Glycoside Hydrolases -- metabolism
- Glycosylation
- Glycosylphosphatidylinositols -- chemistry
- Guinea Pigs
- Liver -- metabolism
- Lysine -- chemistry
- Membrane Glycoproteins -- chemistry
- Mutation
- Open Reading Frames
- Phosphatidylinositols -- chemistry
- Pichia -- metabolism
- Precipitin Tests
- Proline -- chemistry
- Protein Glutamine gamma Glutamyltransferase 2
- Protein Structure, Tertiary
- Recombinant Proteins -- chemistry
- Spectrometry, Fluorescence
- Streptavidin -- chemistry
- Subcellular Fractions
- Sulfhydryl Compounds -- chemistry
- Transglutaminases -- chemistry
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Publication Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S.
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