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Volumn 10, Issue 2, 1998, Pages 174-181

Protein tyrosine phosphatases in the developing nervous system

Author keywords

[No Author keywords available]

Indexed keywords

CELL PROTEIN; MEMBRANE PROTEIN; PROTEIN TYROSINE PHOSPHATASE;

EID: 0032053706     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-0674(98)80139-7     Document Type: Article
Times cited : (74)

References (95)
  • 1
    • 0028170817 scopus 로고
    • Receptor protein-tyrosine kinases and their signal transduction pathways
    • van der Geer P, Hunter T, Lindberg RA. Receptor protein-tyrosine kinases and their signal transduction pathways. Annu Rev Cell Biol. 10:1994;251-337.
    • (1994) Annu Rev Cell Biol , vol.10 , pp. 251-337
    • Van Der Geer, P.1    Hunter, T.2    Lindberg, R.A.3
  • 2
    • 0027736124 scopus 로고
    • Structural diversity of eukaryotic protein tyrosine phosphatases: Functional and evolutionary implications
    • Saito H. Structural diversity of eukaryotic protein tyrosine phosphatases: functional and evolutionary implications. Semin Cell Biol. 4:1993;379-387.
    • (1993) Semin Cell Biol , vol.4 , pp. 379-387
    • Saito, H.1
  • 3
    • 0028838971 scopus 로고
    • Protein kinases and phosphatases: The yin and yang of protein phosphorylation and signaling
    • Hunter T. Protein kinases and phosphatases: the yin and yang of protein phosphorylation and signaling. Cell. 80:1995;225-236.
    • (1995) Cell , vol.80 , pp. 225-236
    • Hunter, T.1
  • 4
    • 0029125639 scopus 로고
    • Protein tyrosine phosphatases as adhesion receptors
    • Brady-Kalnay SM, Tonks NK. Protein tyrosine phosphatases as adhesion receptors. Curr Opin Cell Biol. 7:1995;650-657.
    • (1995) Curr Opin Cell Biol , vol.7 , pp. 650-657
    • Brady-Kalnay, S.M.1    Tonks, N.K.2
  • 5
    • 0031886094 scopus 로고    scopus 로고
    • Genetic analysis of protein-tyrosine phosphatases
    • of special interest. A useful and recent review of PTP function, with excellent coverage of nontransmemebrane phosphatases.
    • Van Vactor D, O'Reilly AM, Neel BG. Genetic analysis of protein-tyrosine phosphatases. of special interest Curr Opin Genet Dev. 8:1998;112-126 A useful and recent review of PTP function, with excellent coverage of nontransmemebrane phosphatases.
    • (1998) Curr Opin Genet Dev , vol.8 , pp. 112-126
    • Van Vactor, D.1    O'Reilly, A.M.2    Neel, B.G.3
  • 6
    • 0028009549 scopus 로고
    • Protein tyrosine phosphatases: Characterization fo extracellular and intracellular domains
    • Mourey RJ, Dixon JE. Protein tyrosine phosphatases: characterization fo extracellular and intracellular domains. Curr Opin Genet Dev. 4:1994;31-39.
    • (1994) Curr Opin Genet Dev , vol.4 , pp. 31-39
    • Mourey, R.J.1    Dixon, J.E.2
  • 7
    • 0030297891 scopus 로고    scopus 로고
    • Form and function in protein dephosphorylation
    • of special interest. An excellent, compact review of PTP catalysis and structure.
    • Denu JM, Stuckey JA, Saper MA, Dixon JE. Form and function in protein dephosphorylation. of special interest Cell. 87:1996;365-368 An excellent, compact review of PTP catalysis and structure.
    • (1996) Cell , vol.87 , pp. 365-368
    • Denu, J.M.1    Stuckey, J.A.2    Saper, M.A.3    Dixon, J.E.4
  • 8
    • 0030005705 scopus 로고    scopus 로고
    • Protein tyrosine phosphatases in signaling
    • Streuli M. Protein tyrosine phosphatases in signaling. Curr Opin Cell Biol. 8:1996;182-188.
    • (1996) Curr Opin Cell Biol , vol.8 , pp. 182-188
    • Streuli, M.1
  • 9
    • 0030953448 scopus 로고    scopus 로고
    • Protein tyrosine phosphatases in signal transduction
    • of special interest. A useful and general review of PTP signaling pathways.
    • Tonks NK, Neel BG. Protein tyrosine phosphatases in signal transduction. of special interest Curr Opin Cell Biol. 9:1997;193-204 A useful and general review of PTP signaling pathways.
    • (1997) Curr Opin Cell Biol , vol.9 , pp. 193-204
    • Tonks, N.K.1    Neel, B.G.2
  • 10
    • 0027237709 scopus 로고
    • MPTPδ, a putative murine homologue of HPTPδ, is expressed in specialized regions of the brain and in the B-cell lineage
    • Mizuno K, Hasegawa K, Katagiri T, Ogimoto M, Ichikawa T, Yakura H. MPTPδ, a putative murine homologue of HPTPδ, is expressed in specialized regions of the brain and in the B-cell lineage. Mol Cell Biol. 13:1993;5513-5523.
    • (1993) Mol Cell Biol , vol.13 , pp. 5513-5523
    • Mizuno, K.1    Hasegawa, K.2    Katagiri, T.3    Ogimoto, M.4    Ichikawa, T.5    Yakura, H.6
  • 11
    • 0029096593 scopus 로고
    • Expression of PTPH1, a rat protein tyrosine phosphatase, is restricted to the derivatives of a specific diencephalic segment
    • Sahin M, Slaugenhaupt SA, Gusella JF, Hockfoeld S. Expression of PTPH1, a rat protein tyrosine phosphatase, is restricted to the derivatives of a specific diencephalic segment. Proc Natl Acad Sci USA. 92:1995;7859-7863.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 7859-7863
    • Sahin, M.1    Slaugenhaupt, S.A.2    Gusella, J.F.3    Hockfoeld, S.4
  • 12
    • 0029876734 scopus 로고    scopus 로고
    • Regional expression and subcellular localization of the tyrosine-specific phosphatase SH-PTP2 in the adult human nervous system
    • Reeves SA, Sinha UB, Difiglia M, Louis DN. Regional expression and subcellular localization of the tyrosine-specific phosphatase SH-PTP2 in the adult human nervous system. Neurosci. 71:1996;1037-1942.
    • (1996) Neurosci , vol.71 , pp. 1037-1942
    • Reeves, S.A.1    Sinha, U.B.2    Difiglia, M.3    Louis, D.N.4
  • 13
    • 0028899648 scopus 로고
    • Cellular and molecular characterization of a brain-enriched protein tyrosine phosphatase
    • Boulanger LM, Lombroso PJ, Raghunathan A, Wahle MJ, Naegele JR. Cellular and molecular characterization of a brain-enriched protein tyrosine phosphatase. J Neurosci. 15:1995;1532-1544.
    • (1995) J Neurosci , vol.15 , pp. 1532-1544
    • Boulanger, L.M.1    Lombroso, P.J.2    Raghunathan, A.3    Wahle, M.J.4    Naegele, J.R.5
  • 14
    • 0026630991 scopus 로고
    • Corkscrew encodes a putative portein tyrosine phosphatase that functions to transduce the terminal signal from the receptor tyrosine kinase torso
    • Perkins LA, Larson I, Perrimon N. Corkscrew encodes a putative portein tyrosine phosphatase that functions to transduce the terminal signal from the receptor tyrosine kinase torso. Cell. 70:1992;225-236.
    • (1992) Cell , vol.70 , pp. 225-236
    • Perkins, L.A.1    Larson, I.2    Perrimon, N.3
  • 15
    • 0030056718 scopus 로고    scopus 로고
    • A Drosophila protein-tyrosine phosphatase associates with an adapter protein required for axonal guidance
    • Clemens JC, Ursuliak Z, Clemens KK, Price JV, Dixon JE. A Drosophila protein-tyrosine phosphatase associates with an adapter protein required for axonal guidance. J Biol Chem. 2:1996;17002-17005.
    • (1996) J Biol Chem , vol.2 , pp. 17002-17005
    • Clemens, J.C.1    Ursuliak, Z.2    Clemens, K.K.3    Price, J.V.4    Dixon, J.E.5
  • 16
    • 0024211451 scopus 로고
    • A new member of the immunoglobulin superfamily that has a cytoplasmic region homologous to the leukocyte common antigen
    • Streuli M, Krueger NX, Hall LR, Schlossman SF, Saito H. A new member of the immunoglobulin superfamily that has a cytoplasmic region homologous to the leukocyte common antigen. J Exp Med. 168:1988;1523-1530.
    • (1988) J Exp Med , vol.168 , pp. 1523-1530
    • Streuli, M.1    Krueger, N.X.2    Hall, L.R.3    Schlossman, S.F.4    Saito, H.5
  • 17
    • 0028934929 scopus 로고
    • Molecular characterization of the human transmembrane protein-tyrosine phosphatase δ
    • Pulido R, Krueger NX, Serra-Pages C, Saito H, Streuli M. Molecular characterization of the human transmembrane protein-tyrosine phosphatase δ J Biol Chem. 270:1994;6722-6728.
    • (1994) J Biol Chem , vol.270 , pp. 6722-6728
    • Pulido, R.1    Krueger, N.X.2    Serra-Pages, C.3    Saito, H.4    Streuli, M.5
  • 18
    • 0029417204 scopus 로고
    • The LAR/PTPd/PTPs subfamily of transmembrane protein-tyrosine-phosphatases: Multiple human LAR, PTPd, and PTPs isoforms are expressed in a tissue-specific manner and associate with the LAR-interacting protein LIP1
    • Pulido R, Serra-Pages C, Tang M, Streuli M. The LAR/PTPd/PTPs subfamily of transmembrane protein-tyrosine-phosphatases: Multiple human LAR, PTPd, and PTPs isoforms are expressed in a tissue-specific manner and associate with the LAR-interacting protein LIP1. Proc Natl Acad Sci USA. 92:1995;11686-11690.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 11686-11690
    • Pulido, R.1    Serra-Pages, C.2    Tang, M.3    Streuli, M.4
  • 19
    • 0028926584 scopus 로고
    • LAR tryosine phosphatase receptor: Alternative splicing is preferential to the nervous system, coordinated with cell growth and generates novel isofroms containing extensive CAG repeats
    • Zhang JS, Longo FM. LAR tryosine phosphatase receptor: alternative splicing is preferential to the nervous system, coordinated with cell growth and generates novel isofroms containing extensive CAG repeats. J Cell Biol. 128:1995;415-431.
    • (1995) J Cell Biol , vol.128 , pp. 415-431
    • Zhang, J.S.1    Longo, F.M.2
  • 20
    • 0029021132 scopus 로고
    • Axonal localization of the CAM-like tyrosine phosphatase CRYPa: A signalling molecule of embryonic growth cones
    • Stoker AW, Gehrig B, Haj F, Bay BH. Axonal localization of the CAM-like tyrosine phosphatase CRYPa: a signalling molecule of embryonic growth cones. Development. 121:1995;1833-1844.
    • (1995) Development , vol.121 , pp. 1833-1844
    • Stoker, A.W.1    Gehrig, B.2    Haj, F.3    Bay, B.H.4
  • 21
    • 0031895886 scopus 로고    scopus 로고
    • The leech receptor tyrosine phosphatase HmLAR2 is concentrated in growth cones and is involved in process outgrowth
    • of special interest. This paper describes the localization of a LAR family member to the surface of the growth cone, and antibody purturbation experiments that suggest a role in direction guidance.
    • Gershon TR, Baker MW, Nitabach M, Macagno ER. The leech receptor tyrosine phosphatase HmLAR2 is concentrated in growth cones and is involved in process outgrowth. of special interest Development. 125:1998;1183-1190 This paper describes the localization of a LAR family member to the surface of the growth cone, and antibody purturbation experiments that suggest a role in direction guidance.
    • (1998) Development , vol.125 , pp. 1183-1190
    • Gershon, T.R.1    Baker, M.W.2    Nitabach, M.3    MacAgno, E.R.4
  • 22
    • 0024378995 scopus 로고
    • A family of receptor-linked protein tyrosine phosphatases in humans and Drosophila
    • Streuli M, Krueger NX, Tsai AYM, Saito H. A family of receptor-linked protein tyrosine phosphatases in humans and Drosophila. Proc Natl Acad Sci USA. 86:1989;8698-8702.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 8698-8702
    • Streuli, M.1    Krueger, N.X.2    Tsai, A.Y.M.3    Saito, H.4
  • 23
    • 0026037643 scopus 로고
    • Three receptor-linked protein-tyrosine phosphatases are selectively expressed on central nervous system axons in the Drosophila embryo
    • Tian SS, Tsoulfas P, Zinn K. Three receptor-linked protein-tyrosine phosphatases are selectively expressed on central nervous system axons in the Drosophila embryo. Cell. 67:1991;675-685.
    • (1991) Cell , vol.67 , pp. 675-685
    • Tian, S.S.1    Tsoulfas, P.2    Zinn, K.3
  • 25
    • 0031032676 scopus 로고    scopus 로고
    • RPTPδ and the novel protein tyrosine phosphatase RPTPψ are expressed in restricted regions of the developing central nervous system
    • of special interest. Detailed developmental expression data of high quality are presented in this paper on members of two distinct RPTP subfamilies.
    • Sommer L, Rao M, Anderson DJ. RPTPδ and the novel protein tyrosine phosphatase RPTPψ are expressed in restricted regions of the developing central nervous system. of special interest Dev Dyn. 208:1997;48-61 Detailed developmental expression data of high quality are presented in this paper on members of two distinct RPTP subfamilies.
    • (1997) Dev Dyn , vol.208 , pp. 48-61
    • Sommer, L.1    Rao, M.2    Anderson, D.J.3
  • 26
    • 0030030320 scopus 로고    scopus 로고
    • The transmembrane tyrosine phosphatase DLAR control motor axons guidance in Drosophila
    • of outstanding interest. One of the two papers providing the first genetic analysis of RPTP function during axon guidance.
    • Krueger NX, van Vactor D, Wan HI, Gelbart WM, Goodman CS, Saito H. The transmembrane tyrosine phosphatase DLAR control motor axons guidance in Drosophila. of outstanding interest Cell. 84:1996;611-622 One of the two papers providing the first genetic analysis of RPTP function during axon guidance.
    • (1996) Cell , vol.84 , pp. 611-622
    • Krueger, N.X.1    Van Vactor, D.2    Wan, H.I.3    Gelbart, W.M.4    Goodman, C.S.5    Saito, H.6
  • 28
    • 0027372789 scopus 로고
    • Protein tyrosine phosphatases expressed in the developing rat brain
    • Sahin M, Hockfield S. Protein tyrosine phosphatases expressed in the developing rat brain. J Neurosci. 13:1993;4968-4978.
    • (1993) J Neurosci , vol.13 , pp. 4968-4978
    • Sahin, M.1    Hockfield, S.2
  • 29
    • 0028861680 scopus 로고
    • Seven protein tyrosine phosphatases are differentially expressed in the developing rat brain
    • Sahin M, Dowling JJ, Hockfield S. Seven protein tyrosine phosphatases are differentially expressed in the developing rat brain. J Comp Neurol. 351:1995;617-631.
    • (1995) J Comp Neurol , vol.351 , pp. 617-631
    • Sahin, M.1    Dowling, J.J.2    Hockfield, S.3
  • 30
    • 0029012482 scopus 로고
    • Expression if receptor protein tyrosine phosphatase-σ (RPTP-σ) in the nervous system of the developing and adult rat
    • Wang H, Yan H, Canoll PD, Silvennoinen O, Schlessinger J, Musacchio JM. Expression if receptor protein tyrosine phosphatase-σ (RPTP-σ) in the nervous system of the developing and adult rat. J Neurosci Res. 41:1995;297-310.
    • (1995) J Neurosci Res , vol.41 , pp. 297-310
    • Wang, H.1    Yan, H.2    Canoll, P.D.3    Silvennoinen, O.4    Schlessinger, J.5    Musacchio, J.M.6
  • 31
    • 0026040037 scopus 로고
    • Two Drosophila receptor-like tyrosine phosphatase genes are expressed in a subset of developing axons and pioneer neurons in the embryonic CNS
    • Yang XH, Seow KT, Bahri SM, Oon SH, Chia W. Two Drosophila receptor-like tyrosine phosphatase genes are expressed in a subset of developing axons and pioneer neurons in the embryonic CNS. Cell. 67:1991;661-673.
    • (1991) Cell , vol.67 , pp. 661-673
    • Yang, X.H.1    Seow, K.T.2    Bahri, S.M.3    Oon, S.H.4    Chia, W.5
  • 32
    • 0026323004 scopus 로고
    • Cloning and characterization of a receptor-class phosphotvrosine phosphatase gene expressed on central nervous system axons in Drosophila melanogaster
    • Hariharan IK, Chuang PT, Rubin GM. Cloning and characterization of a receptor-class phosphotvrosine phosphatase gene expressed on central nervous system axons in Drosophila melanogaster. Proc Natl Acad Sci USA. 88:1991;11266-11270.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 11266-11270
    • Hariharan, I.K.1    Chuang, P.T.2    Rubin, G.M.3
  • 33
    • 0029809548 scopus 로고    scopus 로고
    • CRYP-2: A receptor-type tyrosine phosphatase selectively expressed by devloping vertebrate neurons
    • Bodden K, Bixby JL. CRYP-2: a receptor-type tyrosine phosphatase selectively expressed by devloping vertebrate neurons. J Neurobiol. 31:1996;309-324.
    • (1996) J Neurobiol , vol.31 , pp. 309-324
    • Bodden, K.1    Bixby, J.L.2
  • 34
    • 0031045678 scopus 로고    scopus 로고
    • Identification of a receptor-type protein tyrosine phosphatase expressed in postmitotic maturing neurons: Its structure and expression in the central nervous system
    • Tagawa M, Shirasawa T, Yahagi Y, Tomoda T, Kuroyanagi H, Fujimora S, Sakiyama S, Maruyama N. Identification of a receptor-type protein tyrosine phosphatase expressed in postmitotic maturing neurons: its structure and expression in the central nervous system. Biochem J. 321:1997;865-871.
    • (1997) Biochem J , vol.321 , pp. 865-871
    • Tagawa, M.1    Shirasawa, T.2    Yahagi, Y.3    Tomoda, T.4    Kuroyanagi, H.5    Fujimora, S.6    Sakiyama, S.7    Maruyama, N.8
  • 35
    • 0030596534 scopus 로고    scopus 로고
    • Binary expression of olfactory bulb-protein tyrosine phosphatase in rat central nervous system: Developmental gene regulation in neonate cerebral cortex and constitutive expression in olfactory-rhinencephalon
    • Yahagi Y, Tagawa M, Tomoda T, Shirasawa T. Binary expression of olfactory bulb-protein tyrosine phosphatase in rat central nervous system: developmental gene regulation in neonate cerebral cortex and constitutive expression in olfactory-rhinencephalon. Neurosci Lett. 211:1996;125-128.
    • (1996) Neurosci Lett , vol.211 , pp. 125-128
    • Yahagi, Y.1    Tagawa, M.2    Tomoda, T.3    Shirasawa, T.4
  • 36
    • 0030904004 scopus 로고    scopus 로고
    • A novel protein-tyrosine phosphatase related to the homophillically adhering κ and μ receptors
    • Cheng J, Wu K, Armanini M, O'Rourke N, Dowbenko D, Laskey LA. A novel protein-tyrosine phosphatase related to the homophillically adhering κ and μ receptors. J Biol Chem. 272:1997;7264-7277.
    • (1997) J Biol Chem , vol.272 , pp. 7264-7277
    • Cheng, J.1    Wu, K.2    Armanini, M.3    O'Rourke, N.4    Dowbenko, D.5    Laskey, L.A.6
  • 37
    • 0030010991 scopus 로고    scopus 로고
    • Characterization of PCP-2, a novel receptor protein tyrosine phosphatase of the MAM domain family
    • Wang H, Lian Z, Lerch MM, Chen Z, Xie W, Ullrich A. Characterization of PCP-2, a novel receptor protein tyrosine phosphatase of the MAM domain family. Oncogene. 12:1996;2555-2562.
    • (1996) Oncogene , vol.12 , pp. 2555-2562
    • Wang, H.1    Lian, Z.2    Lerch, M.M.3    Chen, Z.4    Xie, W.5    Ullrich, A.6
  • 39
    • 0030036465 scopus 로고    scopus 로고
    • PTP-NP, a new member fo the receptor protein tyrosine phosphatase family, implicated in development of nervous system and pancreatic endocrine cells
    • Chiang MK, Flanagan JG. PTP-NP, a new member fo the receptor protein tyrosine phosphatase family, implicated in development of nervous system and pancreatic endocrine cells. Development. 122:1996;2239-2250.
    • (1996) Development , vol.122 , pp. 2239-2250
    • Chiang, M.K.1    Flanagan, J.G.2
  • 40
    • 0029967767 scopus 로고    scopus 로고
    • Characterization of chicken protein tyrosine phosphatase α and its expression in the central nervous system
    • Fang KS, Martins-Green M, Williams LT, Hanafusa H. Characterization of chicken protein tyrosine phosphatase α and its expression in the central nervous system. Brain Res Mol Brain Res. 37:1996;1-14.
    • (1996) Brain Res Mol Brain Res , vol.37 , pp. 1-14
    • Fang, K.S.1    Martins-Green, M.2    Williams, L.T.3    Hanafusa, H.4
  • 41
    • 0030219741 scopus 로고    scopus 로고
    • Expression of receptor protein-tyrosine phophatase α mRNA and protein during mouse embryogenesis
    • den Hertog J, Overvoode J, de Laat SW. Expression of receptor protein-tyrosine phophatase α mRNA and protein during mouse embryogenesis. Mech Dev. 58:1996;89-101.
    • (1996) Mech Dev , vol.58 , pp. 89-101
    • Den Hertog, J.1    Overvoode, J.2    De Laat, S.W.3
  • 42
    • 0026754494 scopus 로고
    • A human transmembrane protein-tyrosine-phosphatase, PTPζ, is expressed in brain and has an N-terminal receptor domain homologous to carbonic anhydrases
    • Krueger NX, Saito H. A human transmembrane protein-tyrosine-phosphatase, PTPζ, is expressed in brain and has an N-terminal receptor domain homologous to carbonic anhydrases. Proc Natl Acad Sci USA. 89:1992;7417-7421.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 7417-7421
    • Krueger, N.X.1    Saito, H.2
  • 44
    • 0030339415 scopus 로고    scopus 로고
    • Neurocan and phosphacan: Two major nervous tissue-specific chondroitin sulfate proteoglycans
    • of special interest. This review, like its companion below, provides a broad overview with considerable factual detail pn phosphacan expression, biochemistry and function.
    • Margolis RK, Rauch U, Maurel P, Margolis RU. Neurocan and phosphacan: two major nervous tissue-specific chondroitin sulfate proteoglycans. of special interest Perspectives Dev Neurobiol. 3:1996;273-290 This review, like its companion below, provides a broad overview with considerable factual detail pn phosphacan expression, biochemistry and function.
    • (1996) Perspectives Dev Neurobiol , vol.3 , pp. 273-290
    • Margolis, R.K.1    Rauch, U.2    Maurel, P.3    Margolis, R.U.4
  • 45
    • 0030340041 scopus 로고    scopus 로고
    • Functions of brain chondroitin sulfate proteoglycans during development interactions with adhesion molecules
    • of special interest. See annotation to [44].
    • Grumet M, Friedlander DR, Sakurai T. Functions of brain chondroitin sulfate proteoglycans during development interactions with adhesion molecules. of special interest Perspectives Dev Neurobiol. 3:1996;319-330 See annotation to [44].
    • (1996) Perspectives Dev Neurobiol , vol.3 , pp. 319-330
    • Grumet, M.1    Friedlander, D.R.2    Sakurai, T.3
  • 47
    • 0030932770 scopus 로고    scopus 로고
    • STEP: A family of brain-enriched PTPs. Alternative splicing produces transmembrane, cytosolic and truncated isoforms
    • Bult A, Zhao F, Dirkx R, Raghunathan A, Solimena M, Lombroso PJ. STEP: a family of brain-enriched PTPs. Alternative splicing produces transmembrane, cytosolic and truncated isoforms. Eur J Cell Biol. 72:1997;337-344.
    • (1997) Eur J Cell Biol , vol.72 , pp. 337-344
    • Bult, A.1    Zhao, F.2    Dirkx, R.3    Raghunathan, A.4    Solimena, M.5    Lombroso, P.J.6
  • 49
    • 0028339608 scopus 로고
    • Vanadate stimulates differentiation and neurite outgrowth in rat pheochromocytoma PC12 cells and neurite extension in human neuroblastoma SH-SY5Y cells
    • Roger MV, Buensuceso C, Montague F, Mahadevan L. Vanadate stimulates differentiation and neurite outgrowth in rat pheochromocytoma PC12 cells and neurite extension in human neuroblastoma SH-SY5Y cells. Neuroscience. 60:1994;479-494.
    • (1994) Neuroscience , vol.60 , pp. 479-494
    • Roger, M.V.1    Buensuceso, C.2    Montague, F.3    Mahadevan, L.4
  • 50
    • 0028353694 scopus 로고
    • Determination of neuronal cell fate: Lessons from the R7 neuron of Drosophila
    • Zipursky SL, Rubin G. Determination of neuronal cell fate: lessons from the R7 neuron of Drosophila. Annu Rev Neurosci. 17:1994;373-397.
    • (1994) Annu Rev Neurosci , vol.17 , pp. 373-397
    • Zipursky, S.L.1    Rubin, G.2
  • 51
    • 0026471539 scopus 로고
    • Identification of a human src homology 2-containing protein-tyrosine-phosphatase: A putative homolog of Drosophila corkscrew
    • Freeman RM Jr, Plutzky J, Neel BG. Identification of a human src homology 2-containing protein-tyrosine-phosphatase: a putative homolog of Drosophila corkscrew. Proc Natl Acad Sci USA. 89:1992;11239-11243.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 11239-11243
    • Freeman R.M., Jr.1    Plutzky, J.2    Neel, B.G.3
  • 52
    • 0025997867 scopus 로고
    • Ras1 and a putative guanine nucleotide exchange factor perform crucial steps in signaling by the sevenless protein tyrosine kinase
    • Simon MA, Bowtell DD, Dodson GS, Laverty TR, Rubin GM. Ras1 and a putative guanine nucleotide exchange factor perform crucial steps in signaling by the sevenless protein tyrosine kinase. Cell. 67:1991;701-716.
    • (1991) Cell , vol.67 , pp. 701-716
    • Simon, M.A.1    Bowtell, D.D.2    Dodson, G.S.3    Laverty, T.R.4    Rubin, G.M.5
  • 53
    • 0029975822 scopus 로고    scopus 로고
    • The SH2-containing tyrosine phosphatase corkscrew is required during signaling by sevenless, Ras1 and Raf
    • of special interest. Analysis of loss-of-function and gain-of-function mutations in Corkscrew reveals its role in the sevenless RTK signaling pathway, and its genetic relationship with Ras and Raf.
    • Allard JD, Chang HC, Herbst R, McNeill H, Simon M. The SH2-containing tyrosine phosphatase corkscrew is required during signaling by sevenless, Ras1 and Raf. of special interest Development. 122:1996;1137-1146 Analysis of loss-of-function and gain-of-function mutations in Corkscrew reveals its role in the sevenless RTK signaling pathway, and its genetic relationship with Ras and Raf.
    • (1996) Development , vol.122 , pp. 1137-1146
    • Allard, J.D.1    Chang, H.C.2    Herbst, R.3    McNeill, H.4    Simon, M.5
  • 54
    • 0029861448 scopus 로고    scopus 로고
    • Signaling by ectopically expressed Drosophila Src64 requires the protein-tyrosine phosphatase Corkscrew and the adapter downstream of receptor kinases
    • Cooper JA, Simon MA, Kussick SJ. Signaling by ectopically expressed Drosophila Src64 requires the protein-tyrosine phosphatase Corkscrew and the adapter downstream of receptor kinases. Cell Growth Differ. 7:1996;1435-1441.
    • (1996) Cell Growth Differ , vol.7 , pp. 1435-1441
    • Cooper, J.A.1    Simon, M.A.2    Kussick, S.J.3
  • 55
    • 0030601974 scopus 로고    scopus 로고
    • The nonreceptor protein tyrosine phosphatase corkscrew functions in multiple receptor tyrosine kinase pathways in Drosophila
    • of special interest. Genetic analysis reveals that corkscrew acts downstream of DER (EGF receptor) and breathless (FGF receptor), in addition to other RTKs. Vertebrate Shp-2 is shown to substitute functionally for corkscrew in Drosophila.
    • Perkins LA, Johnson MR, Melnick MB, Perrimon N. The nonreceptor protein tyrosine phosphatase corkscrew functions in multiple receptor tyrosine kinase pathways in Drosophila. of special interest Dev Biol. 180:1996;63-81 Genetic analysis reveals that corkscrew acts downstream of DER (EGF receptor) and breathless (FGF receptor), in addition to other RTKs. Vertebrate Shp-2 is shown to substitute functionally for corkscrew in Drosophila.
    • (1996) Dev Biol , vol.180 , pp. 63-81
    • Perkins, L.A.1    Johnson, M.R.2    Melnick, M.B.3    Perrimon, N.4
  • 56
    • 0030003293 scopus 로고    scopus 로고
    • Daughter of sevenless is a substrate of the phosphotyrosine phosphatase corkscrew and functions during seveless signaling
    • of outstanding interest. This and a companion paper [57] demonstrate that Corkscrew functions through interactions with daughter of sevenless (DOS), a phosphoprotein PTP substrate that is required for R7 cell fate in the Drosophila compound eye. Dos is one of very few relevant PTP substrates.
    • Herbst R, Carroll PM, Allard JD, Schilling J, Raabe T, Simon MA. Daughter of sevenless is a substrate of the phosphotyrosine phosphatase corkscrew and functions during seveless signaling. of outstanding interest Cell. 85:1996;899-909 This and a companion paper [57] demonstrate that Corkscrew functions through interactions with daughter of sevenless (DOS), a phosphoprotein PTP substrate that is required for R7 cell fate in the Drosophila compound eye. Dos is one of very few relevant PTP substrates.
    • (1996) Cell , vol.85 , pp. 899-909
    • Herbst, R.1    Carroll, P.M.2    Allard, J.D.3    Schilling, J.4    Raabe, T.5    Simon, M.A.6
  • 57
    • 0029984739 scopus 로고    scopus 로고
    • DOS, a novel pleckstrin homology domain-containing protein required for signal transduction between sevenless and Ras1 in Drosophila
    • of outstanding interest. See annotation to [56].
    • Raabe T, Riesgo-Escovar J, Liu X, Bausenwein BS, Deak P, Maroy P, Hafen E. DOS, a novel pleckstrin homology domain-containing protein required for signal transduction between sevenless and Ras1 in Drosophila. of outstanding interest Cell. 85:1996;911-920 See annotation to [56].
    • (1996) Cell , vol.85 , pp. 911-920
    • Raabe, T.1    Riesgo-Escovar, J.2    Liu, X.3    Bausenwein, B.S.4    Deak, P.5    Maroy, P.6    Hafen, E.7
  • 58
    • 0030921502 scopus 로고    scopus 로고
    • Abnormal mesoderm patterning in mouse embryos mutant for the SH2 tyrosine phosphatase Shp-2
    • of outstanding interest. Genetic analysis of murine Shp-2 reveals multiple phenotypes during embryogenesis, including malformation of the nervous system.
    • Saxton TM, Henkemeyer M, Gasca S, Shen R, Rossi DJ, Shalaby F, Feng GS, Pawson T. Abnormal mesoderm patterning in mouse embryos mutant for the SH2 tyrosine phosphatase Shp-2. of outstanding interest EMBO J. 16:1997;2352-2364 Genetic analysis of murine Shp-2 reveals multiple phenotypes during embryogenesis, including malformation of the nervous system.
    • (1997) EMBO J , vol.16 , pp. 2352-2364
    • Saxton, T.M.1    Henkemeyer, M.2    Gasca, S.3    Shen, R.4    Rossi, D.J.5    Shalaby, F.6    Feng, G.S.7    Pawson, T.8
  • 60
    • 0022397461 scopus 로고
    • Differential of PC12 phaeochromocytoma cells induced by v-src oncogene
    • Alema S, Casalbore P, Agostini E, Tato F. Differential of PC12 phaeochromocytoma cells induced by v-src oncogene. Nature. 316:1985;557-559.
    • (1985) Nature , vol.316 , pp. 557-559
    • Alema, S.1    Casalbore, P.2    Agostini, E.3    Tato, F.4
  • 61
    • 0025298083 scopus 로고
    • Distinct and different effects of the oncogenes v-myc and v-src on avian sympathetic neurons: Retroviral transfer of v-myc stimulates neuronal proliferation whereas v-src transfer enhances neuronal differentiation
    • Haltmeier H, Rohrer H. Distinct and different effects of the oncogenes v-myc and v-src on avian sympathetic neurons: retroviral transfer of v-myc stimulates neuronal proliferation whereas v-src transfer enhances neuronal differentiation. J Cell Biol. 110:1990;2087-2098.
    • (1990) J Cell Biol , vol.110 , pp. 2087-2098
    • Haltmeier, H.1    Rohrer, H.2
  • 62
    • 0030176078 scopus 로고    scopus 로고
    • PY in the fly: Receptor-like tyrosine phosphatases in axonal pathfinding
    • Chein CB. PY in the fly: receptor-like tyrosine phosphatases in axonal pathfinding. Neuron. 16:1996;1065-1068.
    • (1996) Neuron , vol.16 , pp. 1065-1068
    • Chein, C.B.1
  • 63
    • 0031051796 scopus 로고    scopus 로고
    • Tyrosine phosphorlation and axon guidance: Of mice and flies
    • of special interest. A useful review of Drosophila RPTP function during axon guidance.
    • Desai CJ, Sun Q, Zinn K. Tyrosine phosphorlation and axon guidance: of mice and flies. of special interest Curr Opin Neurobiol. 7:1997;70-74 A useful review of Drosophila RPTP function during axon guidance.
    • (1997) Curr Opin Neurobiol , vol.7 , pp. 70-74
    • Desai, C.J.1    Sun, Q.2    Zinn, K.3
  • 64
    • 0030026858 scopus 로고    scopus 로고
    • Receptor tyrosine phosphatases are required for motor axon guidnace in the Drosophila embryo
    • of outstanding interest. This, and a companion paper in Dlar, provide the first evidence that Drosophila RPTPs control distinct aspects of axon defasciculation and guidance.
    • Desai CJ, Gindhart JG, Goldstein LSB, Zinn K. Receptor tyrosine phosphatases are required for motor axon guidnace in the Drosophila embryo. of outstanding interest Cell. 84:1996;599-609 This, and a companion paper in Dlar, provide the first evidence that Drosophila RPTPs control distinct aspects of axon defasciculation and guidance.
    • (1996) Cell , vol.84 , pp. 599-609
    • Desai, C.J.1    Gindhart, J.G.2    Goldstein, L.S.B.3    Zinn, K.4
  • 65
    • 0030974135 scopus 로고    scopus 로고
    • Competition and cooperation among receptor tyrosine phosphatases control growth cone guidance in Drosophila
    • of special interest. Genetic interactions between Drosophila RPTPs reveal complexity and context-dependance in the signaling that controls both axonal fasciculation and guidance.
    • Desai CJ, Krueger NX, Saito H, Zinn K. Competition and cooperation among receptor tyrosine phosphatases control growth cone guidance in Drosophila. of special interest Development. 124:1997;1941-1952 Genetic interactions between Drosophila RPTPs reveal complexity and context-dependance in the signaling that controls both axonal fasciculation and guidance.
    • (1997) Development , vol.124 , pp. 1941-1952
    • Desai, C.J.1    Krueger, N.X.2    Saito, H.3    Zinn, K.4
  • 66
    • 0031031229 scopus 로고    scopus 로고
    • Deficient LAR expression decreases basal forbrain cholinergic size and hippocampal cholinergic innervation
    • Yeo TT, Yang T, Massa SM, Zhang JS, Honkaniemi J, Butcher LL, Longo FM. Deficient LAR expression decreases basal forbrain cholinergic size and hippocampal cholinergic innervation. J Neurosci Res. 47:1997;348-360.
    • (1997) J Neurosci Res , vol.47 , pp. 348-360
    • Yeo, T.T.1    Yang, T.2    Massa, S.M.3    Zhang, J.S.4    Honkaniemi, J.5    Butcher, L.L.6    Longo, F.M.7
  • 67
    • 0002753511 scopus 로고    scopus 로고
    • Targeted disruption fo the murine protein tyrosine phosphatase d (MPTPd) gene results in growth retardation and behavioral abnormalities
    • Yakura H. Berlin: Springer-Verlag
    • Uetani N, Asano M, Mizuno K, Yakura H, Iwakura Y. Targeted disruption fo the murine protein tyrosine phosphatase d (MPTPd) gene results in growth retardation and behavioral abnormalities. Yakura H. Kinases and Phosphatases in Lymphocyte and Neuronal Signaling. 1997;313-314 Springer-Verlag, Berlin.
    • (1997) Kinases and Phosphatases in Lymphocyte and Neuronal Signaling , pp. 313-314
    • Uetani, N.1    Asano, M.2    Mizuno, K.3    Yakura, H.4    Iwakura, Y.5
  • 68
    • 0029896991 scopus 로고    scopus 로고
    • TAG-1/axonin-1 is a high affinity ligand of neurocan, phosphacan/protein-tyrosine phosphatase-ζ/β, and N-CAM
    • Milev P, Maurel P, Haring M, Margolis RK, Margolis RU. TAG-1/axonin-1 is a high affinity ligand of neurocan, phosphacan/protein-tyrosine phosphatase-ζ/β, and N-CAM. J Biol Chem. 271:1996;15716-15723.
    • (1996) J Biol Chem , vol.271 , pp. 15716-15723
    • Milev, P.1    Maurel, P.2    Haring, M.3    Margolis, R.K.4    Margolis, R.U.5
  • 69
    • 0031034895 scopus 로고    scopus 로고
    • Induction if neurite outgrowth through contactin and Nr-CAM by extracellular regions of glial receptor tyrosine phosphatase β
    • of outstanding interest. Analysis of PTPζ/β extracellular domain function in vitro reveals that interactions between multiple axonal receptors promote axon outgrowth, in contrast to the growth inhibitory effects of phosphacan that been observed in other assays.
    • Sakurai T, Lustig M, Nativ M, Hemperly JJ, Schlessinger J, Peles E, Grumet M. Induction if neurite outgrowth through contactin and Nr-CAM by extracellular regions of glial receptor tyrosine phosphatase β of outstanding interest J Cell Biol. 136:1997;907-918 Analysis of PTPζ/β extracellular domain function in vitro reveals that interactions between multiple axonal receptors promote axon outgrowth, in contrast to the growth inhibitory effects of phosphacan that been observed in other assays.
    • (1997) J Cell Biol , vol.136 , pp. 907-918
    • Sakurai, T.1    Lustig, M.2    Nativ, M.3    Hemperly, J.J.4    Schlessinger, J.5    Peles, E.6    Grumet, M.7
  • 70
    • 0028091984 scopus 로고
    • Interactions of the chondroitin sulfate proteoglycan phosphacan, the extracellular domain of a receptor-type protein tyrosine phosphatase, with neurons, glia and neural cell adhesion molecules
    • Milev P, Friedlander DR, Sakurai T, Karthikeyan L, Flad M, Margolis RK, Grumet M, Margolis RU. Interactions of the chondroitin sulfate proteoglycan phosphacan, the extracellular domain of a receptor-type protein tyrosine phosphatase, with neurons, glia and neural cell adhesion molecules. J Cell Biol. 127:1994;1703-1715.
    • (1994) J Cell Biol , vol.127 , pp. 1703-1715
    • Milev, P.1    Friedlander, D.R.2    Sakurai, T.3    Karthikeyan, L.4    Flad, M.5    Margolis, R.K.6    Grumet, M.7    Margolis, R.U.8
  • 71
    • 0029923452 scopus 로고    scopus 로고
    • Three forms of RPTP-β are differentially expressed during gliogenesis in the developing rat brain and during glial cell differentiation in culture
    • Canoll PD, Petancesk S, Schlessinger J, Musacchio JM. Three forms of RPTP-β are differentially expressed during gliogenesis in the developing rat brain and during glial cell differentiation in culture. J Neurosci Res. 44:1996;199-215.
    • (1996) J Neurosci Res , vol.44 , pp. 199-215
    • Canoll, P.D.1    Petancesk, S.2    Schlessinger, J.3    Musacchio, J.M.4
  • 72
    • 0027296921 scopus 로고
    • Homophilic binding of PTP mu, a receptor-type protein tyrosine phosphatase, can mediate cell-cell aggregation
    • Brady-Kalnay SM, Flint AJ, Tonks NK. Homophilic binding of PTP mu, a receptor-type protein tyrosine phosphatase, can mediate cell-cell aggregation. J Cell Biol. 122:1993;72-961.
    • (1993) J Cell Biol , vol.122 , pp. 72-961
    • Brady-Kalnay, S.M.1    Flint, A.J.2    Tonks, N.K.3
  • 74
    • 0026583744 scopus 로고
    • Expression of the receptor-linked protein tyrosine phosphatase LAR: Proteolytic cleavage and shedding of the CAM-like extracellular region
    • Streuli M, Krueger NX, Ariniello PD, Tamg M, Munro JM, Blattler WA, Adler DA, Dsiteche CM, Saito H. Expression of the receptor-linked protein tyrosine phosphatase LAR: proteolytic cleavage and shedding of the CAM-like extracellular region. EMBO J. 11:1992;897-907.
    • (1992) EMBO J , vol.11 , pp. 897-907
    • Streuli, M.1    Krueger, N.X.2    Ariniello, P.D.3    Tamg, M.4    Munro, J.M.5    Blattler, W.A.6    Adler, D.A.7    Dsiteche, C.M.8    Saito, H.9
  • 75
    • 0030836799 scopus 로고    scopus 로고
    • Cellular redistribution of protein tyrosine phosphatases LAR and PTPs by inducible proteolytic processing
    • of special interest. Although many RPTPs are proceed, this paper suggests an active role for processing in the induction of alterations in subcellular localization.
    • Aicher B, Lerch MM, Muller T, Schilling J, Ullrich A. Cellular redistribution of protein tyrosine phosphatases LAR and PTPs by inducible proteolytic processing. of special interest J Cell Biol. 138:1997;681-696 Although many RPTPs are proceed, this paper suggests an active role for processing in the induction of alterations in subcellular localization.
    • (1997) J Cell Biol , vol.138 , pp. 681-696
    • Aicher, B.1    Lerch, M.M.2    Muller, T.3    Schilling, J.4    Ullrich, A.5
  • 76
    • 0029759927 scopus 로고    scopus 로고
    • Structural basis of inhibition of receptor protein-tyrosine phosphatase-α By dimerization
    • of outstanding interest. The cyrstal structure determination of PTPα D1 PTP domain suggests a possible role for dimerization in the inactivation fo catalytic activity.
    • Bilwes AM, Hertog J, Hunter T, Noel JP. Structural basis of inhibition of receptor protein-tyrosine phosphatase-α by dimerization. of outstanding interest Nature. 1996:1996;555-559 The cyrstal structure determination of PTPα D1 PTP domain suggests a possible role for dimerization in the inactivation fo catalytic activity.
    • (1996) Nature , vol.1996 , pp. 555-559
    • Bilwes, A.M.1    Hertog, J.2    Hunter, T.3    Noel, J.P.4
  • 77
    • 0027266773 scopus 로고
    • Ligand-mediated negative regulation of a chimeric transmembrane receptor tyrosine phosphatase
    • Desai DM, Sap J, Schlessinger J, Weiss A. Ligand-mediated negative regulation of a chimeric transmembrane receptor tyrosine phosphatase. Cell. 73:1993;541-554.
    • (1993) Cell , vol.73 , pp. 541-554
    • Desai, D.M.1    Sap, J.2    Schlessinger, J.3    Weiss, A.4
  • 78
    • 0032472226 scopus 로고    scopus 로고
    • Dimerization-induced inhibition of receptor protein tyrosine phosphatase function through an inhibitory wedge
    • of outstanding interest. Site-directed mutatgenesis of this PTP supports the model that a loop region in the D1 domain can inactivate PTP activity when PTPs dimerize.
    • Majeti R, Bilwes AM, Noel JP, Hunter T, Weiss A. Dimerization-induced inhibition of receptor protein tyrosine phosphatase function through an inhibitory wedge. of outstanding interest Science. 279:1998;88-91 Site-directed mutatgenesis of this PTP supports the model that a loop region in the D1 domain can inactivate PTP activity when PTPs dimerize.
    • (1998) Science , vol.279 , pp. 88-91
    • Majeti, R.1    Bilwes, A.M.2    Noel, J.P.3    Hunter, T.4    Weiss, A.5
  • 79
    • 0030735366 scopus 로고    scopus 로고
    • The crystal structure of domain 1 of receptor protein-tyrosine phosphatase μ
    • of outstanding interest. In contrast to PTPα, the D1 domain dimer structure for PTPμ suggests that cross-inactivation of PTP active sites via loop insertion is not a general rule.
    • Hoffmann KMV, Tonks NK, Barford D. The crystal structure of domain 1 of receptor protein-tyrosine phosphatase μ of outstanding interest J Biol Chem. 272:1997;27505-27508 In contrast to PTPα, the D1 domain dimer structure for PTPμ suggests that cross-inactivation of PTP active sites via loop insertion is not a general rule.
    • (1997) J Biol Chem , vol.272 , pp. 27505-27508
    • Hoffmann, K.M.V.1    Tonks, N.K.2    Barford, D.3
  • 80
    • 0029782711 scopus 로고    scopus 로고
    • Regulated binding of a PTP1B-like phosphatase to N-cadherin: Control of cadherin-mediated adhesion by dephosphorylation of β-catenin
    • Balsamo J, Leung TC, Ernst H, Zanin MKB, Hoffman S, Lilien J. Regulated binding of a PTP1B-like phosphatase to N-cadherin: control of cadherin-mediated adhesion by dephosphorylation of β-catenin. J Cell Biol. 134:1996;801-813.
    • (1996) J Cell Biol , vol.134 , pp. 801-813
    • Balsamo, J.1    Leung, T.C.2    Ernst, H.3    Zanin, M.K.B.4    Hoffman, S.5    Lilien, J.6
  • 81
    • 0030861051 scopus 로고    scopus 로고
    • Axon patterning requires DN-cadherin a novel neuronal adhesion receptor, in the Drosophila CNS
    • Iwai Y, Usui T, Hirano S, Steward R, Takeichi M, Uemura T. Axon patterning requires DN-cadherin a novel neuronal adhesion receptor, in the Drosophila CNS. Neuron. 19:1997;77-89.
    • (1997) Neuron , vol.19 , pp. 77-89
    • Iwai, Y.1    Usui, T.2    Hirano, S.3    Steward, R.4    Takeichi, M.5    Uemura, T.6
  • 82
    • 0030012613 scopus 로고    scopus 로고
    • Association of human protein-tyrosine phosphatase κ with members of the armadillo family
    • Fuchs M, Muller T, Lerch MM, Ullrich A. Association of human protein-tyrosine phosphatase κ with members of the armadillo family. J Biol Chem. 271:1996;16712-16719.
    • (1996) J Biol Chem , vol.271 , pp. 16712-16719
    • Fuchs, M.1    Muller, T.2    Lerch, M.M.3    Ullrich, A.4
  • 83
    • 0029797378 scopus 로고    scopus 로고
    • Association between a transmembrane protein tyrosine phosphatase and the cadherin-catenin complex
    • Kypta RM, Su H, Reichardt LF. Association between a transmembrane protein tyrosine phosphatase and the cadherin-catenin complex. J Cell Biol. 134:1996;1519-1529.
    • (1996) J Cell Biol , vol.134 , pp. 1519-1529
    • Kypta, R.M.1    Su, H.2    Reichardt, L.F.3
  • 84
    • 0029149746 scopus 로고
    • Receptor protein tyrosine phosphatase PTPmu associates with cadherins and catenins in vivo
    • Brady-Kalnay SM, Rimm DL, Tonks NK. Receptor protein tyrosine phosphatase PTPmu associates with cadherins and catenins in vivo. J Cell Biol. 130:1995;977-986.
    • (1995) J Cell Biol , vol.130 , pp. 977-986
    • Brady-Kalnay, S.M.1    Rimm, D.L.2    Tonks, N.K.3
  • 85
    • 0029842115 scopus 로고    scopus 로고
    • Lack of association between receptor protein tyrosine phosphatase RPTPμ and cadherins
    • Zondag GCM, Moolenaar WH, Gebbink MFBG. Lack of association between receptor protein tyrosine phosphatase RPTPμ and cadherins. J Cell Biol. 134:1996;1513-1517.
    • (1996) J Cell Biol , vol.134 , pp. 1513-1517
    • Zondag, G.C.M.1    Moolenaar, W.H.2    Gebbink, M.F.B.G.3
  • 86
    • 0029019297 scopus 로고
    • The LAR transmembrane protein tyrosine phosphatase and a coiled-coil LAR interacting protein colocalize at focal adhesions
    • Serra-Pages C, Kedersha NL, Fazikas L, Medley Q, Debant A, Streuli M. The LAR transmembrane protein tyrosine phosphatase and a coiled-coil LAR interacting protein colocalize at focal adhesions. EMBO J. 14:1995;2827-2838.
    • (1995) EMBO J , vol.14 , pp. 2827-2838
    • Serra-Pages, C.1    Kedersha, N.L.2    Fazikas, L.3    Medley, Q.4    Debant, A.5    Streuli, M.6
  • 87
    • 0029952315 scopus 로고    scopus 로고
    • The multidomain protein Trio binds the LAR transmembrane tyrosine phosphatase, contains a protein kinase domain, and has separate rac-specific and rho-specific guanine nucleotide exchange factor domains
    • of special interest. Yeast interaction trap assays using LAR cytoplasmic domain identified a large protein that may recruit and activate Rac and Rho to the site of RPTP engagement.
    • Debant A, Serra-Pages C, Seipel K, O'Brien S, Tang M, Park S, Streuli M. The multidomain protein Trio binds the LAR transmembrane tyrosine phosphatase, contains a protein kinase domain, and has separate rac-specific and rho-specific guanine nucleotide exchange factor domains. of special interest Proc Natl Acad Sci USA. 93:1996;5466-5471 Yeast interaction trap assays using LAR cytoplasmic domain identified a large protein that may recruit and activate Rac and Rho to the site of RPTP engagement.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 5466-5471
    • Debant, A.1    Serra-Pages, C.2    Seipel, K.3    O'Brien, S.4    Tang, M.5    Park, S.6    Streuli, M.7
  • 88
    • 0031913612 scopus 로고    scopus 로고
    • Drosophila Rac1 controls motor axon guidance
    • of special interest. Genetic analysis of Rac function during motor axon guidance demonstrates a Rac phenotype identical to loss of Dlar. Genetic interactions between Rac and Dlar suggest that both protein function in a comon pathway, as suggested by the identification of human Trio.
    • Kaufmann N, Wills Z, Van Vactor D. Drosophila Rac1 controls motor axon guidance. of special interest Development. 125:1998;453-461 Genetic analysis of Rac function during motor axon guidance demonstrates a Rac phenotype identical to loss of Dlar. Genetic interactions between Rac and Dlar suggest that both protein function in a comon pathway, as suggested by the identification of human Trio.
    • (1998) Development , vol.125 , pp. 453-461
    • Kaufmann, N.1    Wills, Z.2    Van Vactor, D.3
  • 89
    • 0000072679 scopus 로고
    • Rapid activation of the T-cell tyrosine protein kinase pp56lck and CD45 phosphotyrosine phosphatase
    • Mustelin T, Coggeshall KM, Altman A. Rapid activation of the T-cell tyrosine protein kinase pp56lck and CD45 phosphotyrosine phosphatase. Proc Natl Acad Sci USA. 86:1989;6302-6306.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 6302-6306
    • Mustelin, T.1    Coggeshall, K.M.2    Altman, A.3
  • 91
    • 0030666623 scopus 로고    scopus 로고
    • Transmemebrane glycoprotein gp150 is a substrate fot receptor tyrosine phosphatase DPTP10D in Drosophila cells
    • of special interest. This study demonstates that gp150 is an in vivo substrate/binding partner for DPTP10D, and reveals its specificity as a substrate for particular TKs and PTPs.
    • Fashena SJ, Zinn K. Transmemebrane glycoprotein gp150 is a substrate fot receptor tyrosine phosphatase DPTP10D in Drosophila cells. of special interest Mol Cell Biol. 17:1997;6859-6867 This study demonstates that gp150 is an in vivo substrate/binding partner for DPTP10D, and reveals its specificity as a substrate for particular TKs and PTPs.
    • (1997) Mol Cell Biol , vol.17 , pp. 6859-6867
    • Fashena, S.J.1    Zinn, K.2
  • 92
    • 0028072331 scopus 로고
    • An adhesion molecule-like protein that interacts with and is a substrate for a Drosophila receptor-linked protein tyrosine phosphatase
    • Tian S, Zinn K. An adhesion molecule-like protein that interacts with and is a substrate for a Drosophila receptor-linked protein tyrosine phosphatase. J Biol Chem. 269:1994;28478-28486.
    • (1994) J Biol Chem , vol.269 , pp. 28478-28486
    • Tian, S.1    Zinn, K.2
  • 93
    • 0027971705 scopus 로고
    • NCAM-dependent neurite outgrowth is inhibited in neurons from Fyn-minus mice
    • Beggs HE, Soriano P, Maness PF. NCAM-dependent neurite outgrowth is inhibited in neurons from Fyn-minus mice. J Cell Biol. 127:1994;825-833.
    • (1994) J Cell Biol , vol.127 , pp. 825-833
    • Beggs, H.E.1    Soriano, P.2    Maness, P.F.3
  • 94
    • 0028347820 scopus 로고
    • Impared neurite outgrowth of src-minus cerebellar neurons on the cell adhesion molecule L1
    • Ignelzi MA, Miller DR, Soriano P, Maness PF. Impared neurite outgrowth of src-minus cerebellar neurons on the cell adhesion molecule L1. Neuron. 12:1994;873-884.
    • (1994) Neuron , vol.12 , pp. 873-884
    • Ignelzi, M.A.1    Miller, D.R.2    Soriano, P.3    Maness, P.F.4
  • 95
    • 0029949837 scopus 로고    scopus 로고
    • Tight association of GRB2 with receptor protein-tyrosine phosphatase α is mediated by the SH2 and C-trminal SH3 domains
    • den Hertog J, Hunter T. Tight association of GRB2 with receptor protein-tyrosine phosphatase α is mediated by the SH2 and C-trminal SH3 domains. EMBO J. 15:1996;3016-3027.
    • (1996) EMBO J , vol.15 , pp. 3016-3027
    • Den Hertog, J.1    Hunter, T.2


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