Related references
Note: Only part of the references are listed.Characterization of the human CUTA isoform2 present in the stably transfected HeLa cells
Jingchun Yang et al.
MOLECULAR BIOLOGY REPORTS (2009)
Old and new questions about cholinesterases
Jean Massoulie et al.
CHEMICO-BIOLOGICAL INTERACTIONS (2008)
Acetylcholinesterase associates differently with its anchoring proteins ColQ and PRiMA
Hiba Noureddine et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2008)
Assembly of acetylcholinesterase tetramers by peptidic motifs from the proline-rich membrane anchor, PRiMA -: Competition between degradation and secretion pathways of heteromeric complexes
Hiba Noureddine et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2007)
Cloning, crystallization and preliminary X-ray studies of XC2981 from Xanthomonas campestris, a putative CutA1 protein involved in copper-ion homeostasis
Chien-Hung Lin et al.
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS (2006)
Determinants of the t peptide involved in folding, degradation, and secretion of acetylcholinesterase
C Falasca et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2005)
Elements of the C-terminal t peptide of acetylcholinesterase that determine amphiphilicity, homomeric and heteromeric associations, secretion and degradation
S Belbeoc'h et al.
EUROPEAN JOURNAL OF BIOCHEMISTRY (2004)
Structural implications for heavy metal-induced reversible assembly and aggregation of a protein:: the case of Pyrococcus horikoshii CutA
Y Tanaka et al.
FEBS LETTERS (2004)
X-ray crystal structure of CutA from Thermotoga maritima at 1.4 angstrom resolution
A Savchenko et al.
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS (2004)
The evolutionarily conserved trimeric structure of CutA1 proteins suggests a role in signal transduction
F Arnesano et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2003)
The C-terminal T peptide of acetylcholinesterase enhances degradation of unassembled active subunits through the ERAD pathway
S Belbeoc'h et al.
EMBO JOURNAL (2003)
PRiMA:: The membrane anchor of acetylcholinesterase in the brain
AL Perrier et al.
NEURON (2002)
Acetylcholinesterase H and T dimers are associated through the same contact -: Mutations at this interface interfere with the C-terminal T peptide, inducing degradation rather than secretion
N Morel et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2001)
Th structure of the PII-ATP complex
YB Xu et al.
EUROPEAN JOURNAL OF BIOCHEMISTRY (2001)
Hydrophobic protein that copurifies with human brain acetylcholinesterase: Amino acid sequence, genomic organization, and chromosomal localization
DS Navaratnam et al.
JOURNAL OF NEUROCHEMISTRY (2000)
Two distinct proteins are associated with tetrameric acetylcholinesterase on the cell surface
AL Perrier et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2000)