메뉴 건너뛰기




Volumn 61, Issue 8, 2012, Pages 1266-1275

Structural, biological, and pharmacological strategies for the inhibition of nerve growth factor

Author keywords

Antagonist; Neurotrophin; NGF; p75; Tanezumab; TrkA

Indexed keywords

HYBRID PROTEIN; K 252A; KYNURENIC ACID; METAL ION; NERVE GROWTH FACTOR; NERVE GROWTH FACTOR RECEPTOR; NEUROTROPHIN; NEUROTROPHIN RECEPTOR P75; NONSTEROID ANTIINFLAMMATORY AGENT; PROTEIN TYROSINE KINASE A; ZINC;

EID: 84870295768     PISSN: 01970186     EISSN: 18729754     Source Type: Journal    
DOI: 10.1016/j.neuint.2012.10.008     Document Type: Short Survey
Times cited : (58)

References (78)
  • 1
    • 48249146140 scopus 로고    scopus 로고
    • Probing the binding mechanism and affinity of Tanezumab, a recombinant humanized anti-NGF monoclonal antibody, using a repertoire of biosensors
    • Y.N. Abdiche, D.S. Malashock, and J. Pons Probing the binding mechanism and affinity of Tanezumab, a recombinant humanized anti-NGF monoclonal antibody, using a repertoire of biosensors Protein Sci. 17 2008 1326 1335
    • (2008) Protein Sci. , vol.17 , pp. 1326-1335
    • Abdiche, Y.N.1    Malashock, D.S.2    Pons, J.3
  • 3
    • 0036369587 scopus 로고    scopus 로고
    • Nerve growth factor for the treatment of diabetic neuropathy: What went wrong, what went right, and what does the future hold?
    • S.C. Apfel Nerve growth factor for the treatment of diabetic neuropathy: what went wrong, what went right, and what does the future hold? Int. Rev. Neurobiol. 50 2002 393 413
    • (2002) Int. Rev. Neurobiol. , vol.50 , pp. 393-413
    • Apfel, S.C.1
  • 4
    • 0027211704 scopus 로고
    • Crystal structure of the soluble human 55 kd TNF receptor-human TNF beta complex: Implications for TNF receptor activation
    • D.W. Banner, A. D'Arcy, W. Janes, R. Gentz, H.J. Schoenfeld, C. Broger, H. Loetscher, and W. Lesslauer Crystal structure of the soluble human 55 kd TNF receptor-human TNF beta complex: implications for TNF receptor activation Cell 73 1993 431 445
    • (1993) Cell , vol.73 , pp. 431-445
    • Banner, D.W.1    D'Arcy, A.2    Janes, W.3    Gentz, R.4    Schoenfeld, H.J.5    Broger, C.6    Loetscher, H.7    Lesslauer, W.8
  • 5
    • 33845707629 scopus 로고    scopus 로고
    • High affinity not in the vicinity?
    • P.A. Barker High affinity not in the vicinity? Neuron 53 2007 1 4
    • (2007) Neuron , vol.53 , pp. 1-4
    • Barker, P.A.1
  • 6
    • 0027966170 scopus 로고
    • Disruption of NGF binding to the low affinity neurotrophin receptor p75LNTR reduces NGF binding to TrkA on PC12 cells
    • P.A. Barker, and E.M. Shooter Disruption of NGF binding to the low affinity neurotrophin receptor p75LNTR reduces NGF binding to TrkA on PC12 cells Neuron 13 1994 203 215
    • (1994) Neuron , vol.13 , pp. 203-215
    • Barker, P.A.1    Shooter, E.M.2
  • 7
    • 0032508715 scopus 로고    scopus 로고
    • Solution structure and internal motion of a bioactive peptide derived from nerve growth factor
    • N. Beglova, L. LeSauteur, I. Ekiel, H.U. Saragovi, and K. Gehring Solution structure and internal motion of a bioactive peptide derived from nerve growth factor J. Biol. Chem. 273 1998 23652 23658
    • (1998) J. Biol. Chem. , vol.273 , pp. 23652-23658
    • Beglova, N.1    Lesauteur, L.2    Ekiel, I.3    Saragovi, H.U.4    Gehring, K.5
  • 8
    • 0025886463 scopus 로고
    • The low-affinity p75 nerve growth factor (NGF) receptor mediates NGF-induced tyrosine phosphorylation
    • M.M. Berg, D.W. Sternberg, B.L. Hempstead, and M.V. Chao The low-affinity p75 nerve growth factor (NGF) receptor mediates NGF-induced tyrosine phosphorylation Proc. Natl. Acad. Sci. USA 88 1991 7106 7110
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 7106-7110
    • Berg, M.M.1    Sternberg, D.W.2    Hempstead, B.L.3    Chao, M.V.4
  • 9
    • 0033081042 scopus 로고    scopus 로고
    • Biochemical and functional interactions between the neurotrophin receptors trk and p75NTR
    • M. Bibel, E. Hoppe, and Y.A. Barde Biochemical and functional interactions between the neurotrophin receptors trk and p75NTR EMBO J. 18 1999 616 622
    • (1999) EMBO J. , vol.18 , pp. 616-622
    • Bibel, M.1    Hoppe, E.2    Barde, Y.A.3
  • 11
    • 0032387835 scopus 로고    scopus 로고
    • Crystal structure of neurotrophin-3 homodimer shows distinct regions are used to bind its receptors
    • M.J. Butte, P.K. Hwang, W.C. Mobley, and R.J. Fletterick Crystal structure of neurotrophin-3 homodimer shows distinct regions are used to bind its receptors Biochemistry 37 1998 16846 16852
    • (1998) Biochemistry , vol.37 , pp. 16846-16852
    • Butte, M.J.1    Hwang, P.K.2    Mobley, W.C.3    Fletterick, R.J.4
  • 12
    • 76749118433 scopus 로고    scopus 로고
    • Tanezumab, a recombinant humanized mAb against nerve growth factor for the treatment of acute and chronic pain
    • A. Cattaneo Tanezumab, a recombinant humanized mAb against nerve growth factor for the treatment of acute and chronic pain Curr. Opin. Mol. Ther. 12 2010 94 106
    • (2010) Curr. Opin. Mol. Ther. , vol.12 , pp. 94-106
    • Cattaneo, A.1
  • 13
    • 32644451922 scopus 로고    scopus 로고
    • Neurotrophin signalling in health and disease
    • M.V. Chao, R. Rajagopal, and F.S. Lee Neurotrophin signalling in health and disease Clin. Sci. (Lond.) 110 2006 167 173
    • (2006) Clin. Sci. (Lond.) , vol.110 , pp. 167-173
    • Chao, M.V.1    Rajagopal, R.2    Lee, F.S.3
  • 14
    • 3342917323 scopus 로고    scopus 로고
    • Differential activity of the nerve growth factor (NGF) antagonist PD90780 [7-(benzolylamino)-4,9-dihydro-4-methyl-9-oxo-pyrazolo[5,1-b]quinazoline-2- carboxylic acid] suggests altered NGF-p75NTR interactions in the presence of TrkA
    • A. Colquhoun, G.M. Lawrance, I.L. Shamovsky, R.J. Riopelle, and G.M. Ross Differential activity of the nerve growth factor (NGF) antagonist PD90780 [7-(benzolylamino)-4,9-dihydro-4-methyl-9-oxo-pyrazolo[5,1-b] quinazoline-2-carboxylic acid] suggests altered NGF-p75NTR interactions in the presence of TrkA J. Pharmacol. Exp. Ther. 310 2004 505 511
    • (2004) J. Pharmacol. Exp. Ther. , vol.310 , pp. 505-511
    • Colquhoun, A.1    Lawrance, G.M.2    Shamovsky, I.L.3    Riopelle, R.J.4    Ross, G.M.5
  • 15
    • 48649089156 scopus 로고    scopus 로고
    • Dissecting NGF interactions with TrkA and p75 receptors by structural and functional studies of an anti-NGF neutralizing antibody
    • S. Covaceuszach, A. Cassetta, P.V. Konarev, S. Gonfloni, R. Rudolph, D.I. Svergun, D. Lamba, and A. Cattaneo Dissecting NGF interactions with TrkA and p75 receptors by structural and functional studies of an anti-NGF neutralizing antibody J. Mol. Biol. 381 2008 881 896
    • (2008) J. Mol. Biol. , vol.381 , pp. 881-896
    • Covaceuszach, S.1    Cassetta, A.2    Konarev, P.V.3    Gonfloni, S.4    Rudolph, R.5    Svergun, D.I.6    Lamba, D.7    Cattaneo, A.8
  • 16
    • 0036830562 scopus 로고    scopus 로고
    • The neurotrophin receptor p75(NTR): Novel functions and implications for diseases of the nervous system
    • G. Dechant, and Y.A. Barde The neurotrophin receptor p75(NTR): novel functions and implications for diseases of the nervous system Nat. Neurosci. 5 2002 1131 1136
    • (2002) Nat. Neurosci. , vol.5 , pp. 1131-1136
    • Dechant, G.1    Barde, Y.A.2
  • 18
    • 45849128645 scopus 로고    scopus 로고
    • Neuropathic pain: Emerging treatments
    • A. Dray Neuropathic pain: emerging treatments Br. J. Anaesth. 101 2008 48 58
    • (2008) Br. J. Anaesth. , vol.101 , pp. 48-58
    • Dray, A.1
  • 19
    • 76749142917 scopus 로고    scopus 로고
    • Multipotent neurotrophin antagonist targets brain-derived neurotrophic factor and nerve growth factor
    • J.K. Eibl, S.A. Chapelsky, and G.M. Ross Multipotent neurotrophin antagonist targets brain-derived neurotrophic factor and nerve growth factor J. Pharmacol. Exp. Ther. 332 2010 446 454
    • (2010) J. Pharmacol. Exp. Ther. , vol.332 , pp. 446-454
    • Eibl, J.K.1    Chapelsky, S.A.2    Ross, G.M.3
  • 20
    • 0035980009 scopus 로고    scopus 로고
    • The cytoplasmic and transmembrane domains of the p75 and Trk A receptors regulate high affinity binding to nerve growth factor
    • D. Esposito, P. Patel, R.M. Stephens, P. Perez, M.V. Chao, D.R. Kaplan, and B.L. Hempstead The cytoplasmic and transmembrane domains of the p75 and Trk A receptors regulate high affinity binding to nerve growth factor J. Biol. Chem. 276 2001 32687 32695
    • (2001) J. Biol. Chem. , vol.276 , pp. 32687-32695
    • Esposito, D.1    Patel, P.2    Stephens, R.M.3    Perez, P.4    Chao, M.V.5    Kaplan, D.R.6    Hempstead, B.L.7
  • 21
    • 0348110429 scopus 로고    scopus 로고
    • ProNGF: A neurotrophic or an apoptotic molecule?
    • M. Fahnestock, G. Yu, and M.D. Coughlin ProNGF: a neurotrophic or an apoptotic molecule? Prog. Brain Res. 146 2004 101 110
    • (2004) Prog. Brain Res. , vol.146 , pp. 101-110
    • Fahnestock, M.1    Yu, G.2    Coughlin, M.D.3
  • 22
    • 0032707644 scopus 로고    scopus 로고
    • The three-dimensional solution structure of Aesculus hippocastanum antimicrobial protein 1 determined by 1H nuclear magnetic resonance
    • F. Fant, W.F. Vranken, and F.A. Borremans The three-dimensional solution structure of Aesculus hippocastanum antimicrobial protein 1 determined by 1H nuclear magnetic resonance Proteins 37 1999 388 403
    • (1999) Proteins , vol.37 , pp. 388-403
    • Fant, F.1    Vranken, W.F.2    Borremans, F.A.3
  • 24
    • 79960081481 scopus 로고    scopus 로고
    • Fate of novel painkiller mAbs hangs in balance
    • K. Garber Fate of novel painkiller mAbs hangs in balance Nat. Biotechnol. 29 2011 173 174
    • (2011) Nat. Biotechnol. , vol.29 , pp. 173-174
    • Garber, K.1
  • 25
    • 0346849774 scopus 로고    scopus 로고
    • The p75 neurotrophin receptor: Multiple interactors and numerous functions
    • J.J. Gentry, P.A. Barker, and B.D. Carter The p75 neurotrophin receptor: multiple interactors and numerous functions Prog. Brain Res. 146 2004 25 39
    • (2004) Prog. Brain Res. , vol.146 , pp. 25-39
    • Gentry, J.J.1    Barker, P.A.2    Carter, B.D.3
  • 26
    • 49649094883 scopus 로고    scopus 로고
    • Crystal structure of the neurotrophin-3 and p75NTR symmetrical complex
    • Y. Gong, P. Cao, H.J. Yu, and T. Jiang Crystal structure of the neurotrophin-3 and p75NTR symmetrical complex Nature 454 2008 789 793
    • (2008) Nature , vol.454 , pp. 789-793
    • Gong, Y.1    Cao, P.2    Yu, H.J.3    Jiang, T.4
  • 27
    • 2442434770 scopus 로고    scopus 로고
    • Structure of nerve growth factor complexed with the shared neurotrophin receptor p75
    • X.L. He, and K.C. Garcia Structure of nerve growth factor complexed with the shared neurotrophin receptor p75 Science 304 2004 870 875
    • (2004) Science , vol.304 , pp. 870-875
    • He, X.L.1    Garcia, K.C.2
  • 29
    • 70349900360 scopus 로고    scopus 로고
    • Commentary: Regulating proNGF action: Multiple targets for therapeutic intervention
    • B.L. Hempstead Commentary: Regulating proNGF action: multiple targets for therapeutic intervention Neurotox. Res. 16 2009 255 260
    • (2009) Neurotox. Res. , vol.16 , pp. 255-260
    • Hempstead, B.L.1
  • 30
    • 0025774207 scopus 로고
    • High-affinity NGF binding requires coexpression of the trk proto-oncogene and the low-affinity NGF receptor
    • B.L. Hempstead, D. Martin-Zanca, D.R. Kaplan, L.F. Parada, and M.V. Chao High-affinity NGF binding requires coexpression of the trk proto-oncogene and the low-affinity NGF receptor Nature 350 1991 678 683
    • (1991) Nature , vol.350 , pp. 678-683
    • Hempstead, B.L.1    Martin-Zanca, D.2    Kaplan, D.R.3    Parada, L.F.4    Chao, M.V.5
  • 31
    • 80052495481 scopus 로고    scopus 로고
    • Potential mechanisms for hypoalgesia induced by anti-nerve growth factor immunoglobulin are identified using autoimmune nerve growth factor deprivation
    • E.M. Hoffman, Z. Zhang, M.B. Anderson, R. Schechter, and K.E. Miller Potential mechanisms for hypoalgesia induced by anti-nerve growth factor immunoglobulin are identified using autoimmune nerve growth factor deprivation Neuroscience 193 2011 452 465
    • (2011) Neuroscience , vol.193 , pp. 452-465
    • Hoffman, E.M.1    Zhang, Z.2    Anderson, M.B.3    Schechter, R.4    Miller, K.E.5
  • 32
    • 0028286686 scopus 로고
    • Nerve growth factor in different crystal forms displays structural flexibility and reveals zinc binding sites
    • D.R. Holland, L.S. Cousens, W. Meng, and B.W. Matthews Nerve growth factor in different crystal forms displays structural flexibility and reveals zinc binding sites J. Mol. Biol. 239 1994 385 400
    • (1994) J. Mol. Biol. , vol.239 , pp. 385-400
    • Holland, D.R.1    Cousens, L.S.2    Meng, W.3    Matthews, B.W.4
  • 33
    • 84860377399 scopus 로고    scopus 로고
    • Anti-NGF painkillers back on track?
    • D. Holmes Anti-NGF painkillers back on track? Nat. Rev. Drug Discov. 11 2012 337 338
    • (2012) Nat. Rev. Drug Discov. , vol.11 , pp. 337-338
    • Holmes, D.1
  • 34
    • 0036250154 scopus 로고    scopus 로고
    • Genetics of congenital insensitivity to pain with anhidrosis (CIPA) or hereditary sensory and autonomic neuropathy type IV. Clinical, biological and molecular aspects of mutations in TRKA(NTRK1) gene encoding the receptor tyrosine kinase for nerve growth factor
    • Y. Indo Genetics of congenital insensitivity to pain with anhidrosis (CIPA) or hereditary sensory and autonomic neuropathy type IV. Clinical, biological and molecular aspects of mutations in TRKA(NTRK1) gene encoding the receptor tyrosine kinase for nerve growth factor Clin. Auton. Res. 12 Suppl. 1 2002 I20 I32
    • (2002) Clin. Auton. Res. , vol.12 , Issue.SUPPL.. 1
    • Indo, Y.1
  • 35
    • 64649105296 scopus 로고    scopus 로고
    • Nerve growth factor, interoception, and sympathetic neuron: Lesson from congenital insensitivity to pain with anhidrosis
    • Y. Indo Nerve growth factor, interoception, and sympathetic neuron: lesson from congenital insensitivity to pain with anhidrosis Auton. Neurosci. 147 2009 3 8
    • (2009) Auton. Neurosci. , vol.147 , pp. 3-8
    • Indo, Y.1
  • 39
    • 62949123326 scopus 로고    scopus 로고
    • Inhibition of p75(NTR) in glia potentiates TrkA-mediated survival of injured retinal ganglion cells
    • F. Lebrun-Julien, B. Morquette, A. Douillette, H.U. Saragovi, and A. Di Polo Inhibition of p75(NTR) in glia potentiates TrkA-mediated survival of injured retinal ganglion cells Mol. Cell. Neurosci. 40 2009 410 420
    • (2009) Mol. Cell. Neurosci. , vol.40 , pp. 410-420
    • Lebrun-Julien, F.1    Morquette, B.2    Douillette, A.3    Saragovi, H.U.4    Di Polo, A.5
  • 41
    • 0035976524 scopus 로고    scopus 로고
    • Regulation of cell survival by secreted proneurotrophins
    • R. Lee, P. Kermani, K.K. Teng, and B.L. Hempstead Regulation of cell survival by secreted proneurotrophins Science 294 2001 1945 1948
    • (2001) Science , vol.294 , pp. 1945-1948
    • Lee, R.1    Kermani, P.2    Teng, K.K.3    Hempstead, B.L.4
  • 42
    • 0028912281 scopus 로고
    • Small peptide mimics of nerve growth factor bind TrkA receptors and affect biological responses
    • L. LeSauteur, L. Wei, B.F. Gibbs, and H.U. Saragovi Small peptide mimics of nerve growth factor bind TrkA receptors and affect biological responses J. Biol. Chem. 270 1995 6564 6569
    • (1995) J. Biol. Chem. , vol.270 , pp. 6564-6569
    • Lesauteur, L.1    Wei, L.2    Gibbs, B.F.3    Saragovi, H.U.4
  • 43
    • 0041379342 scopus 로고    scopus 로고
    • Pro-region of neurotrophins: Role in synaptic modulation
    • B. Lu Pro-region of neurotrophins: role in synaptic modulation Neuron 39 2003 735 738
    • (2003) Neuron , vol.39 , pp. 735-738
    • Lu, B.1
  • 44
    • 23044488902 scopus 로고    scopus 로고
    • The yin and yang of neurotrophin action
    • B. Lu, P.T. Pang, and N.H. Woo The yin and yang of neurotrophin action Nat. Rev. Neurosci. 6 2005 603 614
    • (2005) Nat. Rev. Neurosci. , vol.6 , pp. 603-614
    • Lu, B.1    Pang, P.T.2    Woo, N.H.3
  • 45
    • 70450250025 scopus 로고    scopus 로고
    • Identification of critical residues within the conserved and specificity patches of nerve growth factor leading to survival or differentiation
    • S. Mahapatra, H. Mehta, S.B. Woo, and K.E. Neet Identification of critical residues within the conserved and specificity patches of nerve growth factor leading to survival or differentiation J. Biol. Chem. 284 2009 33600 33613
    • (2009) J. Biol. Chem. , vol.284 , pp. 33600-33613
    • Mahapatra, S.1    Mehta, H.2    Woo, S.B.3    Neet, K.E.4
  • 46
    • 0032705588 scopus 로고    scopus 로고
    • Anti-tumour necrosis factor specific antibody (infliximab) treatment provides insights into the pathophysiology of rheumatoid arthritis
    • R.N. Maini, P.C. Taylor, E. Paleolog, P. Charles, S. Ballara, F.M. Brennan, and M. Feldmann Anti-tumour necrosis factor specific antibody (infliximab) treatment provides insights into the pathophysiology of rheumatoid arthritis Ann. Rheum. Dis. 58 Suppl. 1 1999 I56 60
    • (1999) Ann. Rheum. Dis. , vol.58 , Issue.SUPPL.. 1 , pp. 56-60
    • Maini, R.N.1    Taylor, P.C.2    Paleolog, E.3    Charles, P.4    Ballara, S.5    Brennan, F.M.6    Feldmann, M.7
  • 47
    • 0004414433 scopus 로고    scopus 로고
    • Differential effects of transition metal cations on the conformation and biological activities of nerve growth factor
    • R. Maitra, I.L. Shamovsky, W. Wang, M. Solc, G. Lawrance, S.M. Dostaler, G.M. Ross, and R.J. Riopelle Differential effects of transition metal cations on the conformation and biological activities of nerve growth factor Neurotox Res 2 2000 311 320
    • (2000) Neurotox Res , vol.2 , pp. 311-320
    • Maitra, R.1    Shamovsky, I.L.2    Wang, W.3    Solc, M.4    Lawrance, G.5    Dostaler, S.M.6    Ross, G.M.7    Riopelle, R.J.8
  • 49
    • 0036931575 scopus 로고    scopus 로고
    • Neutralizing intraspinal nerve growth factor with a trkA-IgG fusion protein blocks the development of autonomic dysreflexia in a clip-compression model of spinal cord injury
    • D.R. Marsh, S.T. Wong, S.O. Meakin, J.I. MacDonald, E.F. Hamilton, and L.C. Weaver Neutralizing intraspinal nerve growth factor with a trkA-IgG fusion protein blocks the development of autonomic dysreflexia in a clip-compression model of spinal cord injury J. Neurotrauma 19 2002 1531 1541
    • (2002) J. Neurotrauma , vol.19 , pp. 1531-1541
    • Marsh, D.R.1    Wong, S.T.2    Meakin, S.O.3    MacDonald, J.I.4    Hamilton, E.F.5    Weaver, L.C.6
  • 52
    • 0025986121 scopus 로고
    • New protein fold revealed by a 2.3-A resolution crystal structure of nerve growth factor
    • N.Q. McDonald, R. Lapatto, J. Murray-Rust, J. Gunning, A. Wlodawer, and T.L. Blundell New protein fold revealed by a 2.3-A resolution crystal structure of nerve growth factor Nature 354 1991 411 414
    • (1991) Nature , vol.354 , pp. 411-414
    • McDonald, N.Q.1    Lapatto, R.2    Murray-Rust, J.3    Gunning, J.4    Wlodawer, A.5    Blundell, T.L.6
  • 53
    • 0029085192 scopus 로고
    • The biological effects of endogenous nerve growth factor on adult sensory neurons revealed by a trkA-IgG fusion molecule
    • S.B. McMahon, D.L. Bennett, J.V. Priestley, and D.L. Shelton The biological effects of endogenous nerve growth factor on adult sensory neurons revealed by a trkA-IgG fusion molecule Nat. Med. 1 1995 774 780
    • (1995) Nat. Med. , vol.1 , pp. 774-780
    • McMahon, S.B.1    Bennett, D.L.2    Priestley, J.V.3    Shelton, D.L.4
  • 56
    • 0344118766 scopus 로고    scopus 로고
    • Molecular basis of neurotrophin-receptor interactions
    • M. Pattarawarapan, and K. Burgess Molecular basis of neurotrophin- receptor interactions J. Med. Chem. 46 2003 5277 5291
    • (2003) J. Med. Chem. , vol.46 , pp. 5277-5291
    • Pattarawarapan, M.1    Burgess, K.2
  • 59
    • 33748375335 scopus 로고    scopus 로고
    • Neurotrophins: Mediators and modulators of pain
    • S. Pezet, and S.B. McMahon Neurotrophins: mediators and modulators of pain Annu. Rev. Neurosci. 29 2006 507 538
    • (2006) Annu. Rev. Neurosci. , vol.29 , pp. 507-538
    • Pezet, S.1    McMahon, S.B.2
  • 60
    • 20444394373 scopus 로고    scopus 로고
    • TrkA NGF receptor plays a role in the modulation of p75NTR expression
    • S.L. Rankin, C.S. Guy, and K.M. Mearow TrkA NGF receptor plays a role in the modulation of p75NTR expression Neurosci. Lett. 383 2005 305 310
    • (2005) Neurosci. Lett. , vol.383 , pp. 305-310
    • Rankin, S.L.1    Guy, C.S.2    Mearow, K.M.3
  • 61
    • 0033407459 scopus 로고    scopus 로고
    • The structures of the neurotrophin 4 homodimer and the brain-derived neurotrophic factor/neurotrophin 4 heterodimer reveal a common Trk-binding site
    • R.C. Robinson, C. Radziejewski, G. Spraggon, J. Greenwald, M.R. Kostura, L.D. Burtnick, D.I. Stuart, S. Choe, and E.Y. Jones The structures of the neurotrophin 4 homodimer and the brain-derived neurotrophic factor/neurotrophin 4 heterodimer reveal a common Trk-binding site Protein Sci. 8 1999 2589 2597
    • (1999) Protein Sci. , vol.8 , pp. 2589-2597
    • Robinson, R.C.1    Radziejewski, C.2    Spraggon, G.3    Greenwald, J.4    Kostura, M.R.5    Burtnick, L.D.6    Stuart, D.I.7    Choe, S.8    Jones, E.Y.9
  • 62
    • 0028913014 scopus 로고
    • Structure of the brain-derived neurotrophic factor/neurotrophin 3 heterodimer
    • R.C. Robinson, C. Radziejewski, D.I. Stuart, and E.Y. Jones Structure of the brain-derived neurotrophic factor/neurotrophin 3 heterodimer Biochemistry 34 1995 4139 4146
    • (1995) Biochemistry , vol.34 , pp. 4139-4146
    • Robinson, R.C.1    Radziejewski, C.2    Stuart, D.I.3    Jones, E.Y.4
  • 65
    • 35548937457 scopus 로고    scopus 로고
    • The neuropathic pain triad: Neurons, immune cells and glia
    • J. Scholz, and C.J. Woolf The neuropathic pain triad: neurons, immune cells and glia Nat. Neurosci. 10 2007 1361 1368
    • (2007) Nat. Neurosci. , vol.10 , pp. 1361-1368
    • Scholz, J.1    Woolf, C.J.2
  • 66
    • 0032586026 scopus 로고    scopus 로고
    • The interaction of neurotrophins with the p75NTR common neurotrophin receptor: A comprehensive molecular modeling study
    • I.L. Shamovsky, G.M. Ross, R.J. Riopelle, and D.F. Weaver The interaction of neurotrophins with the p75NTR common neurotrophin receptor: a comprehensive molecular modeling study Protein Sci. 8 1999 2223 2233
    • (1999) Protein Sci. , vol.8 , pp. 2223-2233
    • Shamovsky, I.L.1    Ross, G.M.2    Riopelle, R.J.3    Weaver, D.F.4
  • 67
    • 0026563244 scopus 로고
    • K252a is a selective inhibitor of the tyrosine protein kinase activity of the trk family of oncogenes and neurotrophin receptors
    • P. Tapley, F. Lamballe, and M. Barbacid K252a is a selective inhibitor of the tyrosine protein kinase activity of the trk family of oncogenes and neurotrophin receptors Oncogene 7 1992 371 381
    • (1992) Oncogene , vol.7 , pp. 371-381
    • Tapley, P.1    Lamballe, F.2    Barbacid, M.3
  • 68
    • 1642540257 scopus 로고    scopus 로고
    • Neurotrophins and their receptors: Signaling trios in complex biological systems
    • K.K. Teng, and B.L. Hempstead Neurotrophins and their receptors: signaling trios in complex biological systems Cell. Mol. Life Sci. 61 2004 35 48
    • (2004) Cell. Mol. Life Sci. , vol.61 , pp. 35-48
    • Teng, K.K.1    Hempstead, B.L.2
  • 72
    • 56149111648 scopus 로고    scopus 로고
    • Targeting nerve growth factor in pain: What is the therapeutic potential?
    • J.J. Watson, S.J. Allen, and D. Dawbarn Targeting nerve growth factor in pain: what is the therapeutic potential? BioDrugs 22 2008 349 359
    • (2008) BioDrugs , vol.22 , pp. 349-359
    • Watson, J.J.1    Allen, S.J.2    Dawbarn, D.3
  • 73
    • 33845695804 scopus 로고    scopus 로고
    • Structural and mechanistic insights into nerve growth factor interactions with the TrkA and p75 receptors
    • T. Wehrman, X. He, B. Raab, A. Dukipatti, H. Blau, and K.C. Garcia Structural and mechanistic insights into nerve growth factor interactions with the TrkA and p75 receptors Neuron 53 2007 25 38
    • (2007) Neuron , vol.53 , pp. 25-38
    • Wehrman, T.1    He, X.2    Raab, B.3    Dukipatti, A.4    Blau, H.5    Garcia, K.C.6
  • 74
    • 0033539065 scopus 로고    scopus 로고
    • Crystal structure of nerve growth factor in complex with the ligand-binding domain of the TrkA receptor
    • C. Wiesmann, M.H. Ultsch, S.H. Bass, and A.M. de Vos Crystal structure of nerve growth factor in complex with the ligand-binding domain of the TrkA receptor Nature 401 1999 184 188
    • (1999) Nature , vol.401 , pp. 184-188
    • Wiesmann, C.1    Ultsch, M.H.2    Bass, S.H.3    De Vos, A.M.4
  • 75
    • 0031967772 scopus 로고    scopus 로고
    • Characterization of the recombinant extracellular domain of the neurotrophin receptor TrkA and its interaction with nerve growth factor (NGF)
    • S.B. Woo, C. Whalen, and K.E. Neet Characterization of the recombinant extracellular domain of the neurotrophin receptor TrkA and its interaction with nerve growth factor (NGF) Protein Sci. 7 1998 1006 1016
    • (1998) Protein Sci. , vol.7 , pp. 1006-1016
    • Woo, S.B.1    Whalen, C.2    Neet, K.E.3
  • 76
    • 79951579664 scopus 로고    scopus 로고
    • Central sensitization: Implications for the diagnosis and treatment of pain
    • C.J. Woolf Central sensitization: implications for the diagnosis and treatment of pain Pain 152 2011 S2 15
    • (2011) Pain , vol.152 , pp. 2-15
    • Woolf, C.J.1
  • 77
    • 0034589387 scopus 로고    scopus 로고
    • Neurotrophin small-molecule mimetics
    • Y. Xie, and F.M. Longo Neurotrophin small-molecule mimetics Prog. Brain Res. 128 2000 333 347
    • (2000) Prog. Brain Res. , vol.128 , pp. 333-347
    • Xie, Y.1    Longo, F.M.2
  • 78
    • 0034703031 scopus 로고    scopus 로고
    • Nerve growth factor (NGF) loop 4 dimeric mimetics activate ERK and AKT and promote NGF-like neurotrophic effects
    • Y. Xie, M.A. Tisi, T.T. Yeo, and F.M. Longo Nerve growth factor (NGF) loop 4 dimeric mimetics activate ERK and AKT and promote NGF-like neurotrophic effects J. Biol. Chem. 275 2000 29868 29874
    • (2000) J. Biol. Chem. , vol.275 , pp. 29868-29874
    • Xie, Y.1    Tisi, M.A.2    Yeo, T.T.3    Longo, F.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.