Zobrazeno 1 - 10
of 35
pro vyhledávání: '"JoséM. Musacchio"'
Publikováno v:
Brain Research. 826:157-171
Receptor protein tyrosine phosphatases (RPTPs) comprise a family of proteins that feature intracellular phosphatase domains and an ectodomain with putative ligand-binding motifs. Several RPTPs are expressed in the brain, including RPTP-kappa which pa
Publikováno v:
Journal of Neuroscience Research. 44:199-215
In situ hybridization and Northern analysis demonstrate that the three splicing variants of RPTP-β have different spatial and temporal patterns of expression in the developing brain. The 9.5-kb and 6.4-kb transcripts, which encode transmembrane prot
Autor:
Peter Canoll, Ricardo Martinez, Herman Moreno, JoséM. Musacchio, Joseph Schlessinger, Bernardo Rudy, Elior Peles, Sima Lev, Gregory D. Plowman
Publikováno v:
Nature. 376:737-745
The protein tyrosine kinase PYK2, which is highly expressed in the central nervous system, is rapidly phosphorylated on tyrosine residues in response to various stimuli that elevate the intracellular calcium concentration, as well as by protein kinas
Publikováno v:
Journal of Neuroscience Research. 41:297-310
The expression of receptor protein tyrosine phosphatase-sigma (RPTP-sigma) mRNA during rat development was examined by Northern blot and in situ hybridization analyses. Northern blot analysis revealed that the two transcripts (5.7 kb and 6.9 kb) had
Autor:
JoséM. Musacchio, Peter Canoll, Joseph Schlessinger, Joan B. Levy, Michelle E. Ehrlich, Olli Silvennoinen, Jan Sap, Gilad Barnea
Publikováno v:
Developmental Brain Research. 75:293-298
Analysis of the localization of receptor-type protein tyrosine phosphatase-beta (RPTP-beta) by in situ hybridization and immunocytochemistry indicates that it is predominantly expressed in the developing central nervous system (CNS). RPTP-beta is hig
Publikováno v:
Europe PubMed Central
We describe a new member of the receptor protein tyrosine phosphatase family, R-PTP-kappa, cDNA cloning predicts that R-PTP-kappa is synthesized from a precursor protein of 1,457 amino acids. Its intracellular domain displays the classical tandemly r
Publikováno v:
Life Sciences. 48:543-550
The DM 1 σ 1 site binds dextromethorphan (DM) and σ receptor ligands. The broad binding specificity of this site and its peculiar subcellular distribution prompted us to explore the possibility that this site is a member of the cytochrome P-450 sup
Publikováno v:
European journal of pharmacology. 254(3)
The s.c. administration of a single dose of 0.1 mg/kg of reduced haloperidol to guinea pigs produced a marked inhibition of the binding of [3H]dextromethorphan and [3H]3-(3-hydroxyphenyl)-N-(n-propyl)piperidine ([3H](+)-3-PPP) to brain. The inhibitio
Autor:
Hai Yan, Albert Grossman, Olli Silvennoinen, JoséM. Musacchio, Joseph Schlessinger, K. Mossie, Hong Wang, Peter D'Eustachio
Publikováno v:
Europe PubMed Central
A novel transmembrane receptor protein tyrosine phosphatase-sigma (RPTP-sigma) was cloned from a rat brain stem cDNA library. The extracellular segment of one form of RPTP-sigma contains 824 amino acids and is composed of three immunoglobulin-like an
Autor:
JoséM. Musacchio, Guang-Zhao Zhou
Publikováno v:
European journal of pharmacology. 206(4)
Computer-assisted, simultaneous analysis of self- and cross-displacement experiments demonstrated the existence of several binding sites in guinea pig brain for dextromethorphan, (+)-3-(3-hydroxyphenyl)-N-(1-propyl)piperidine ((+)-3-PPP), and 1,3-di-