Addition of a Glycophosphatidylinositol to Acetylcholinesterase
Open Access
- 1 July 2001
- journal article
- Published by Elsevier
- Vol. 276 (30) , 27881-27892
- https://doi.org/10.1074/jbc.m010817200
Abstract
No abstract availableKeywords
This publication has 39 references indexed in Scilit:
- Prediction of Potential GPI-modification Sites in Proprotein SequencesJournal of Molecular Biology, 1999
- Residues in Torpedo californica acetylcholinesterase necessary for processing to a glycosyl phosphatidylinositol-anchored formPublished by Elsevier ,1999
- Quaternary Associations of AcetylcholinesterasePublished by Elsevier ,1997
- Preferred Sites of Glycosylphosphatidylinositol Modification in Folate Receptors and Constraints in the Primary Structure of the Hydrophobic Portion of the SignalBiochemistry, 1995
- Proteins containing an uncleaved signal for glycophosphatidylinositol membrane anchor attachment are retained in a post-ER compartment.The Journal of cell biology, 1992
- Fusion of sequence elements from non-anchored proteins to generate a fully functional signal for glycophosphatidylinositol membrane anchor attachment.The Journal of cell biology, 1991
- An internally positioned signal can direct attachment of a glycophospholipid membrane anchor.The Journal of cell biology, 1991
- CELL-SURFACE ANCHORING OF PROTEINS VIA GLYCOSYL-PHOSPHATIDYLINOSITOL STRUCTURESAnnual Review of Biochemistry, 1988
- Identification of covalently bound inositol in the hydrophobic membrane-anchoring domain of Torpedo acetylcholinesteraseBiochemical and Biophysical Research Communications, 1985
- A hydrophobic dimer of acetylcholinesterase from Torpedo californica electric organ is solubilized by phosphatidylinositol-specific phospholipase CNeuroscience Letters, 1983