Antibody-induced dimerization of HARPTPalpha-EGFR chimera suggests a ligand dependent mechanism of regulation for RPTPalpha.
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Structure determination of T cell protein-tyrosine phosphataseMultimerization of the protein-tyrosine phosphatase (PTP)-like insulin-dependent diabetes mellitus autoantigens IA-2 and IA-2beta with receptor PTPs (RPTPs). Inhibition of RPTPalpha enzymatic activityFunctional significance of the LAR receptor protein tyrosine phosphatase family in development and diseases.Redox-regulated rotational coupling of receptor protein-tyrosine phosphatase alpha dimers.Signal transduction using an artificial receptor system that undergoes dimerization upon addition of a bivalent leucine-zipper ligand.
P2860
Antibody-induced dimerization of HARPTPalpha-EGFR chimera suggests a ligand dependent mechanism of regulation for RPTPalpha.
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2000 nî lūn-bûn
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Antibody-induced dimerization ...... m of regulation for RPTPalpha.
@en
type
label
Antibody-induced dimerization ...... m of regulation for RPTPalpha.
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prefLabel
Antibody-induced dimerization ...... m of regulation for RPTPalpha.
@en
P2860
P1433
P1476
Antibody-induced dimerization ...... m of regulation for RPTPalpha.
@en
P2093
Blanchetot C
den Hertog J
P2860
P304
P356
10.1016/S0014-5793(00)02165-7
P407
P577
2000-11-01T00:00:00Z