메뉴 건너뛰기




Volumn 17, Issue 7-8, 2012, Pages 379-387

Diverse roles of the scaffolding protein RanBPM

Author keywords

[No Author keywords available]

Indexed keywords

RAN BINDING PROTEIN MICROTUBULE ORGANIZING CENTER; SCAFFOLD PROTEIN; UNCLASSIFIED DRUG;

EID: 84859227238     PISSN: 13596446     EISSN: 18785832     Source Type: Journal    
DOI: 10.1016/j.drudis.2011.10.030     Document Type: Review
Times cited : (38)

References (68)
  • 2
    • 0035845013 scopus 로고    scopus 로고
    • Full-sized RanBPM cDNA encodes a protein possessing a long stretch of proline and glutamine within the N-terminal region, comprising a large protein complex
    • DOI 10.1016/S0378-1119(01)00553-4, PII S0378111901005534
    • H. Nishitani Full-sized RanBPM cDNA encodes a protein possessing a long stretch of proline and glutamine within the N-terminal region, comprising a large protein complex Gene 272 2001 25 33 (Pubitemid 32695395)
    • (2001) Gene , vol.272 , Issue.1-2 , pp. 25-33
    • Nishitani, H.1    Hirose, E.2    Uchimura, Y.3    Nakamura, M.4    Umeda, M.5    Nishii, K.6    Mori, N.7    Nishimoto, T.8
  • 3
    • 0028955712 scopus 로고
    • The Ran/TC4 GTPase-binding domain: Identification by expression cloning and characterization of a conserved sequence motif
    • A.L. Beddow The Ran/TC4 GTPase-binding domain: identification by expression cloning and characterization of a conserved sequence motif Proc. Natl. Acad. Sci. U. S. A. 92 1995 3328 3332
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 3328-3332
    • Beddow, A.L.1
  • 4
    • 2242481119 scopus 로고    scopus 로고
    • RanBPM, a nuclear protein that interacts with and regulates transcriptional activity of androgen receptor and glucocorticoid receptor
    • DOI 10.1074/jbc.M209741200
    • M.A. Rao RanBPM, a nuclear protein that interacts with and regulates transcriptional activity of androgen receptor and glucocorticoid receptor J. Biol. Chem. 277 2002 48020 48027 (Pubitemid 35470747)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.50 , pp. 48020-48027
    • Rao, M.A.1    Cheng, H.2    Quayle, A.N.3    Nishitani, H.4    Nelson, C.C.5    Rennie, P.S.6
  • 5
    • 0037183982 scopus 로고    scopus 로고
    • Activation of Ras/Erk pathway by a novel MET-interacting protein RanBPM
    • D. Wang Activation of Ras/Erk pathway by a novel MET-interacting protein RanBPM J. Biol. Chem. 277 2002 36216 36222
    • (2002) J. Biol. Chem. , vol.277 , pp. 36216-36222
    • Wang, D.1
  • 6
    • 34547702087 scopus 로고    scopus 로고
    • RanBPM, a scaffolding protein in the immune and nervous systems
    • L.C. Murrin, and J.N. Talbot RanBPM, a scaffolding protein in the immune and nervous systems J. Neuroimmune Pharmacol. 2 2007 290 295
    • (2007) J. Neuroimmune Pharmacol. , vol.2 , pp. 290-295
    • Murrin, L.C.1    Talbot, J.N.2
  • 8
    • 28244438788 scopus 로고    scopus 로고
    • Relationship between SPRY and B30.2 protein domains. Evolution of a component of immune defence
    • DOI 10.1111/j.1365-2567.2005.02248.x
    • D.A. Rhodes Relationship between SPRY and B30.2 protein domains. Evolution of a component of immune defence? Immunology 116 2005 411 417 (Pubitemid 41713172)
    • (2005) Immunology , vol.116 , Issue.4 , pp. 411-417
    • Rhodes, D.A.1    De Bono, B.2    Trowsdale, J.3
  • 9
    • 4644366904 scopus 로고    scopus 로고
    • The C terminus of fragile X mental retardation protein interacts with the multi-domain ran-binding protein in the microtubule-organising centre
    • DOI 10.1016/j.jmb.2004.08.024, PII S0022283604010022
    • R.P. Menon The C terminus of fragile X mental retardation protein interacts with the multi-domain Ran-binding protein in the microtubule- organising centre J. Mol. Biol. 343 2004 43 53 (Pubitemid 39277447)
    • (2004) Journal of Molecular Biology , vol.343 , Issue.1 , pp. 43-53
    • Menon, R.P.1    Gibson, T.J.2    Pastore, A.3
  • 10
    • 73849127134 scopus 로고    scopus 로고
    • RanBPM has proapoptotic activities that regulate cell death pathways in response to DNA damage
    • E. Atabakhsh RanBPM has proapoptotic activities that regulate cell death pathways in response to DNA damage Mol. Cancer Res. 7 2009 1962 1972
    • (2009) Mol. Cancer Res. , vol.7 , pp. 1962-1972
    • Atabakhsh, E.1
  • 11
    • 77953170345 scopus 로고    scopus 로고
    • P73 tumor suppressor protein: A close relative of p53 not only in structure but also in anti-cancer approach?
    • J. Zawacka-Pankau p73 tumor suppressor protein: a close relative of p53 not only in structure but also in anti-cancer approach? Cell Cycle 9 2010 720 728
    • (2010) Cell Cycle , vol.9 , pp. 720-728
    • Zawacka-Pankau, J.1
  • 12
    • 13444257491 scopus 로고    scopus 로고
    • Protein stability and function of p73 are modulated by a physical interaction with RanBPM in mammalian cultured cells
    • DOI 10.1038/sj.onc.1208257
    • S. Kramer Protein stability and function of p73 are modulated by a physical interaction with RanBPM in mammalian cultured cells Oncogene 24 2005 938 944 (Pubitemid 40216101)
    • (2005) Oncogene , vol.24 , Issue.5 , pp. 938-944
    • Kramer, S.1    Ozaki, T.2    Miyazaki, K.3    Kato, C.4    Hanamoto, T.5    Nakagawara, A.6
  • 13
    • 78149250369 scopus 로고    scopus 로고
    • Stability and function of mammalian lethal giant larvae-1 oncoprotein are regulated by the scaffolding protein RanBPM
    • B. Suresh Stability and function of mammalian lethal giant larvae-1 oncoprotein are regulated by the scaffolding protein RanBPM J. Biol. Chem. 285 2010 35340 35349
    • (2010) J. Biol. Chem. , vol.285 , pp. 35340-35349
    • Suresh, B.1
  • 14
    • 0034617129 scopus 로고    scopus 로고
    • Cooperative regulation of cell polarity and growth by Drosophila tumor suppressors
    • DOI 10.1126/science.289.5476.113
    • D. Bilder Cooperative regulation of cell polarity and growth by Drosophila tumor suppressors Science 289 2000 113 116 (Pubitemid 30463303)
    • (2000) Science , vol.289 , Issue.5476 , pp. 113-116
    • Bilder, D.1    Li, M.2    Perrimon, N.3
  • 15
    • 0036156362 scopus 로고    scopus 로고
    • Mammalian homolog of Drosophila tumor suppressor lethal (2) giant larvae interacts with basolateral exocytic machinery in Madin-Darby canine kidney cells
    • DOI 10.1091/mbc.01-10-0496
    • A. Musch Mammalian homolog of Drosophila tumor suppressor lethal (2) giant larvae interacts with basolateral exocytic machinery in Madin-Darby canine kidney cells Mol. Biol. Cell 13 2002 158 168 (Pubitemid 34106066)
    • (2002) Molecular Biology of the Cell , vol.13 , Issue.1 , pp. 158-168
    • Musch, A.1    Cohen, D.2    Yeaman, C.3    Nelson, W.J.4    Rodriguez-Boulan, E.5    Brennwald, P.J.6
  • 17
    • 75149190463 scopus 로고    scopus 로고
    • A fragment of the scaffolding protein RanBP9 is increased in Alzheimer's disease brains and strongly potentiates amyloid-beta peptide generation
    • M.K. Lakshmana A fragment of the scaffolding protein RanBP9 is increased in Alzheimer's disease brains and strongly potentiates amyloid-beta peptide generation FASEB J. 24 2010 119 127
    • (2010) FASEB J. , vol.24 , pp. 119-127
    • Lakshmana, M.K.1
  • 18
    • 57049140013 scopus 로고    scopus 로고
    • + channels by the ran binding protein RanBPM
    • + channels by the ran binding protein RanBPM Biochem. Biophys. Res. Commun. 378 2009 15 20
    • (2009) Biochem. Biophys. Res. Commun. , vol.378 , pp. 15-20
    • Kim, T.1
  • 22
    • 79957654916 scopus 로고    scopus 로고
    • RanBPM is essential for mouse spermatogenesis and oogenesis
    • S. Puverel RanBPM is essential for mouse spermatogenesis and oogenesis Development 138 2011 2511 2521
    • (2011) Development , vol.138 , pp. 2511-2521
    • Puverel, S.1
  • 23
    • 55549103030 scopus 로고    scopus 로고
    • The rho-guanine nucleotide exchange factor domain of obscurin regulates assembly of titin at the Z-disk through interactions with Ran binding protein 9
    • A.L. Bowman The rho-guanine nucleotide exchange factor domain of obscurin regulates assembly of titin at the Z-disk through interactions with Ran binding protein 9 Mol. Biol. Cell 19 2008 3782 3792
    • (2008) Mol. Biol. Cell , vol.19 , pp. 3782-3792
    • Bowman, A.L.1
  • 24
    • 51649085370 scopus 로고    scopus 로고
    • RanBPM regulates cell shape, arrangement, and capacity of the female germline stem cell niche in Drosophila melanogaster
    • D.A. Dansereau, and P. Lasko RanBPM regulates cell shape, arrangement, and capacity of the female germline stem cell niche in Drosophila melanogaster J. Cell Biol. 182 2008 963 977
    • (2008) J. Cell Biol. , vol.182 , pp. 963-977
    • Dansereau, D.A.1    Lasko, P.2
  • 25
    • 73849137808 scopus 로고    scopus 로고
    • RanBPM regulates the progression of neuronal precursors through M-phase at the surface of the neocortical ventricular zone
    • Y. Chang RanBPM regulates the progression of neuronal precursors through M-phase at the surface of the neocortical ventricular zone Dev. Neurobiol. 70 2010 1 15
    • (2010) Dev. Neurobiol. , vol.70 , pp. 1-15
    • Chang, Y.1
  • 26
    • 50249108395 scopus 로고    scopus 로고
    • Novel role of the muskelin-RanBP9 complex as a nucleocytoplasmic mediator of cell morphology regulation
    • M. Valiyaveettil Novel role of the muskelin-RanBP9 complex as a nucleocytoplasmic mediator of cell morphology regulation J. Cell Biol. 182 2008 727 739
    • (2008) J. Cell Biol. , vol.182 , pp. 727-739
    • Valiyaveettil, M.1
  • 27
    • 6944228920 scopus 로고    scopus 로고
    • Structural and functional conservation of the lgl recessive oncogenes (review)
    • K.H. Baek Structural and functional conservation of the lgl recessive oncogenes (review) Int. J. Oncol. 24 2004 1257 1261
    • (2004) Int. J. Oncol. , vol.24 , pp. 1257-1261
    • Baek, K.H.1
  • 28
    • 39149123478 scopus 로고    scopus 로고
    • RanBP10 acts as a novel coactivator for the androgen receptor
    • N. Harada RanBP10 acts as a novel coactivator for the androgen receptor Biochem. Biophys. Res. Commun. 368 2008 121 125
    • (2008) Biochem. Biophys. Res. Commun. , vol.368 , pp. 121-125
    • Harada, N.1
  • 29
    • 33646128733 scopus 로고    scopus 로고
    • Identification and characterization of RanBPM, a novel coactivator of thyroid hormone receptors
    • M.B. Poirier Identification and characterization of RanBPM, a novel coactivator of thyroid hormone receptors J. Mol. Endocrinol. 36 2006 313 325
    • (2006) J. Mol. Endocrinol. , vol.36 , pp. 313-325
    • Poirier, M.B.1
  • 31
    • 43049127401 scopus 로고    scopus 로고
    • Enhancement of transactivation activity of Rta of Epstein-Barr virus by RanBPM
    • L.K. Chang Enhancement of transactivation activity of Rta of Epstein-Barr virus by RanBPM J. Mol. Biol. 379 2008 231 242
    • (2008) J. Mol. Biol. , vol.379 , pp. 231-242
    • Chang, L.K.1
  • 32
    • 0026541305 scopus 로고
    • Characterization of an R-binding site mediating the R-induced activation of the Epstein-Barr virus BMLF1 promoter
    • H. Gruffat Characterization of an R-binding site mediating the R-induced activation of the Epstein-Barr virus BMLF1 promoter J. Virol. 66 1992 46 52
    • (1992) J. Virol. , vol.66 , pp. 46-52
    • Gruffat, H.1
  • 33
    • 0030760456 scopus 로고    scopus 로고
    • Reactivation of Epstein-Barr virus: Regulation and function of the BZLF1 gene
    • DOI 10.1016/S0966-842X(97)01129-3, PII S0966842X97011293
    • S.H. Speck Reactivation of Epstein-Barr virus: regulation and function of the BZLF1 gene Trends Microbiol. 5 1997 399 405 (Pubitemid 27417826)
    • (1997) Trends in Microbiology , vol.5 , Issue.10 , pp. 399-405
    • Speck, S.H.1    Chatlla, T.2    Flemington, E.3
  • 34
    • 29644434669 scopus 로고    scopus 로고
    • Ran binding protein 9 interacts with Raf kinase but does not contribute to downstream ERK1/2 activation in skeletal myoblasts
    • DOI 10.1016/j.bbrc.2005.12.023, PII S0006291X05027713
    • S.E. Johnson Ran binding protein 9 interacts with Raf kinase but does not contribute to downstream ERK1/2 activation in skeletal myoblasts Biochem. Biophys. Res. Commun. 340 2006 409 416 (Pubitemid 43021763)
    • (2006) Biochemical and Biophysical Research Communications , vol.340 , Issue.2 , pp. 409-416
    • Johnson, S.E.1    Winner Jr., D.G.2    Wang, X.3
  • 36
  • 37
    • 1542572178 scopus 로고    scopus 로고
    • Serine/threonine kinase Mirk/Dyrk1B is an inhibitor of epithelial cell migration and is negatively regulated by the Met adaptor Ran-binding protein M
    • Y. Zou Serine/threonine kinase Mirk/Dyrk1B is an inhibitor of epithelial cell migration and is negatively regulated by the Met adaptor Ran-binding protein M J. Biol. Chem. 278 2003 49573 49581
    • (2003) J. Biol. Chem. , vol.278 , pp. 49573-49581
    • Zou, Y.1
  • 39
    • 0037762690 scopus 로고    scopus 로고
    • Neurotrophins and their receptors: A convergence point for many signalling pathways
    • DOI 10.1038/nrn1078
    • M.V. Chao Neurotrophins and their receptors: a convergence point for many signalling pathways Nat. Rev. Neurosci. 4 2003 299 309 (Pubitemid 37271375)
    • (2003) Nature Reviews Neuroscience , vol.4 , Issue.4 , pp. 299-309
    • Chao, M.V.1
  • 40
    • 33748552695 scopus 로고    scopus 로고
    • The Ran binding protein RanBPM interacts with TrkA receptor
    • DOI 10.1016/j.neulet.2006.06.059, PII S0304394006006550
    • Y. Yuan The Ran binding protein RanBPM interacts with TrkA receptor Neurosci. Lett. 407 2006 26 31 (Pubitemid 44363132)
    • (2006) Neuroscience Letters , vol.407 , Issue.1 , pp. 26-31
    • Yuan, Y.1    Fu, C.2    Chen, H.3    Wang, X.4    Deng, W.5    Huang, B.-R.6
  • 42
    • 0041488911 scopus 로고    scopus 로고
    • Trk receptors: Roles in neuronal signal transduction
    • DOI 10.1146/annurev.biochem.72.121801.161629
    • E.J. Huang, and L.F. Reichardt Trk receptors: roles in neuronal signal transduction Annu. Rev. Biochem. 72 2003 609 642 (Pubitemid 36930455)
    • (2003) Annual Review of Biochemistry , vol.72 , pp. 609-642
    • Huang, E.J.1    Reichardt, L.F.2
  • 43
    • 0037806030 scopus 로고    scopus 로고
    • Neurotrophins and netrins require calcineurin/NFAT signaling to stimulate outgrowth of embryonic axons
    • DOI 10.1016/S0092-8674(03)00390-8
    • I.A. Graef Neurotrophins and netrins require calcineurin/NFAT signaling to stimulate outgrowth of embryonic axons Cell 113 2003 657 670 (Pubitemid 36694190)
    • (2003) Cell , vol.113 , Issue.5 , pp. 657-670
    • Graef, I.A.1    Wang, F.2    Charron, F.3    Chen, L.4    Neilson, J.5    Tessier-Lavigne, M.6    Crabtree, G.R.7
  • 44
    • 77953301128 scopus 로고    scopus 로고
    • RanBPM contributes to TrkB signaling and regulates brain-derived neurotrophic factor-induced neuronal morphogenesis and survival
    • Y.X. Yin RanBPM contributes to TrkB signaling and regulates brain-derived neurotrophic factor-induced neuronal morphogenesis and survival J. Neurochem. 114 2010 110 121
    • (2010) J. Neurochem. , vol.114 , pp. 110-121
    • Yin, Y.X.1
  • 45
    • 77956289564 scopus 로고    scopus 로고
    • The Drosophila gene RanBPM functions in the mushroom body to regulate larval behavior
    • N. Scantlebury The Drosophila gene RanBPM functions in the mushroom body to regulate larval behavior PLoS ONE 5 2010 E10652
    • (2010) PLoS ONE , vol.5 , pp. 10652
    • Scantlebury, N.1
  • 46
    • 33646916006 scopus 로고    scopus 로고
    • RanBPM contributes to Semaphorin3A signaling through Plexin-A receptors
    • DOI 10.1523/JNEUROSCI.0704-06.2006
    • H. Togashi RanBPM contributes to Semaphorin3A signaling through plexin-A receptors J. Neurosci. 26 2006 4961 4969 (Pubitemid 44315339)
    • (2006) Journal of Neuroscience , vol.26 , Issue.18 , pp. 4961-4969
    • Togashi, H.1    Schmidt, E.F.2    Strittmatter, S.M.3
  • 47
    • 23844476742 scopus 로고    scopus 로고
    • RanBPM is an L1-interacting protein that regulates L1-mediated mitogen-activated protein kinase activation
    • DOI 10.1111/j.1471-4159.2005.03254.x
    • L. Cheng RanBPM is an L1-interacting protein that regulates L1-mediated mitogen-activated protein kinase activation J. Neurochem. 94 2005 1102 1110 (Pubitemid 41170596)
    • (2005) Journal of Neurochemistry , vol.94 , Issue.4 , pp. 1102-1110
    • Cheng, L.1    Lemmon, S.2    Lemmon, V.3
  • 48
    • 0030760042 scopus 로고    scopus 로고
    • L1-associated diseases: Clinical geneticists divide, molecular geneticists unite
    • DOI 10.1093/hmg/6.10.1625
    • E. Fransen L1-associated diseases: clinical geneticists divide, molecular geneticists unite Hum. Mol. Genet. 6 1997 1625 1632 (Pubitemid 27401604)
    • (1997) Human Molecular Genetics , vol.6 , Issue.REV. ISS. , pp. 1625-1632
    • Fransen, E.1    Van Camp, G.2    Vits, L.3    Willems, P.J.4
  • 50
    • 45549090742 scopus 로고    scopus 로고
    • RanBPM is expressed in synaptic layers of the mammalian retina and binds to metabotropic glutamate receptors
    • A. Seebahn RanBPM is expressed in synaptic layers of the mammalian retina and binds to metabotropic glutamate receptors FEBS Lett. 582 2008 2453 2457
    • (2008) FEBS Lett. , vol.582 , pp. 2453-2457
    • Seebahn, A.1
  • 53
    • 0033818112 scopus 로고    scopus 로고
    • Expanded polyglutamine stretches interact with TAFII130, interfering with CREB-dependent transcription
    • T. Shimohata Expanded polyglutamine stretches interact with TAFII130, interfering with CREB-dependent transcription Nat. Genet. 26 2000 29 36
    • (2000) Nat. Genet. , vol.26 , pp. 29-36
    • Shimohata, T.1
  • 55
    • 66449128617 scopus 로고    scopus 로고
    • Novel role of RanBP9 in BACE1 processing of amyloid precursor protein and amyloid beta peptide generation
    • M.K. Lakshmana Novel role of RanBP9 in BACE1 processing of amyloid precursor protein and amyloid beta peptide generation J. Biol. Chem. 284 2009 11863 11872
    • (2009) J. Biol. Chem. , vol.284 , pp. 11863-11872
    • Lakshmana, M.K.1
  • 56
    • 0037448607 scopus 로고    scopus 로고
    • A novel nuclear protein, Twa1, and Muskelin comprise a complex with RanBPM
    • DOI 10.1016/S0378-1119(02)01153-8
    • M. Umeda A novel nuclear protein, Twa1, and Muskelin comprise a complex with RanBPM Gene 303 2003 47 54 (Pubitemid 36151769)
    • (2003) Gene , vol.303 , Issue.1-2 , pp. 47-54
    • Umeda, M.1    Nishitani, H.2    Nishimoto, T.3
  • 57
    • 34250674456 scopus 로고    scopus 로고
    • RanBPM, Muskelin, p48EMLP, p44CTLH, and the armadillo-repeat proteins ARMC8α and ARMC8β are components of the CTLH complex
    • DOI 10.1016/j.gene.2007.02.032, PII S0378111907001205
    • N. Kobayashi RanBPM, muskelin, p48EMLP, p44CTLH, and the armadillo-repeat proteins ARMC8alpha and ARMC8beta are components of the CTLH complex Gene 396 2007 236 247 (Pubitemid 46935398)
    • (2007) Gene , vol.396 , Issue.2 , pp. 236-247
    • Kobayashi, N.1    Yang, J.2    Ueda, A.3    Suzuki, T.4    Tomaru, K.5    Takeno, M.6    Okuda, K.7    Ishigatsubo, Y.8
  • 58
    • 77955337190 scopus 로고    scopus 로고
    • YPEL5 protein of the YPEL gene family is involved in the cell cycle progression by interacting with two distinct proteins RanBPM and RanBP10
    • K. Hosono YPEL5 protein of the YPEL gene family is involved in the cell cycle progression by interacting with two distinct proteins RanBPM and RanBP10 Genomics 96 2010 102 111
    • (2010) Genomics , vol.96 , pp. 102-111
    • Hosono, K.1
  • 59
    • 0041353461 scopus 로고    scopus 로고
    • A porphobilinogen deaminase (PBGD) Ran-binding protein interaction is implicated in nuclear trafficking of PBGD in differentiating glioma cells
    • DOI 10.1038/sj.onc.1206723
    • L. Greenbaum A porphobilinogen deaminase (PBGD) Ran-binding protein interaction is implicated in nuclear trafficking of PBGD in differentiating glioma cells Oncogene 22 2003 5221 5228 (Pubitemid 37056084)
    • (2003) Oncogene , vol.22 , Issue.34 , pp. 5221-5228
    • Greenbaum, L.1    Katcoff, D.J.2    Dou, H.3    Gozlan, Y.4    Malik, Z.5
  • 60
    • 0036083396 scopus 로고    scopus 로고
    • The ubiquitin-proteasome proteolytic pathway: Destruction for the sake of construction
    • M.H. Glickman, and A. Ciechanover The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction Physiol. Rev. 82 2002 373 428 (Pubitemid 34654457)
    • (2002) Physiological Reviews , vol.82 , Issue.2 , pp. 373-428
    • Glickman, M.H.1    Ciechanover, A.2
  • 63
    • 7444222868 scopus 로고    scopus 로고
    • Polo-box motif targets a centrosome regulator, RanGTPase
    • Y.J. Jang Polo-box motif targets a centrosome regulator, RanGTPase Biochem. Biophys. Res. Commun. 325 2004 257 264
    • (2004) Biochem. Biophys. Res. Commun. , vol.325 , pp. 257-264
    • Jang, Y.J.1
  • 65
    • 70350304034 scopus 로고    scopus 로고
    • Regulation of mu opioid receptor internalization by the scaffold protein RanBPM
    • J.N. Talbot Regulation of mu opioid receptor internalization by the scaffold protein RanBPM Neurosci. Lett. 466 2009 154 158
    • (2009) Neurosci. Lett. , vol.466 , pp. 154-158
    • Talbot, J.N.1
  • 66
    • 0034128416 scopus 로고    scopus 로고
    • Molecular mechanisms and regulation of opioid receptor signaling
    • P.Y. Law Molecular mechanisms and regulation of opioid receptor signaling Annu. Rev. Pharmacol. Toxicol. 40 2000 389 430
    • (2000) Annu. Rev. Pharmacol. Toxicol. , vol.40 , pp. 389-430
    • Law, P.Y.1
  • 67
    • 43049084429 scopus 로고    scopus 로고
    • Increased efficacy of micro-opioid agonist-induced antinociception by metabotropic glutamate receptor antagonists in C57BL/6 mice: Comparison with (-)-6-phosphonomethyl-deca-hydroisoquinoline-3-carboxylic acid (LY235959)
    • B.D. Fischer Increased efficacy of micro-opioid agonist-induced antinociception by metabotropic glutamate receptor antagonists in C57BL/6 mice: comparison with (-)-6-phosphonomethyl-deca-hydroisoquinoline-3-carboxylic acid (LY235959) Psychopharmacology (Berl.) 198 2008 271 278
    • (2008) Psychopharmacology (Berl.) , vol.198 , pp. 271-278
    • Fischer, B.D.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.