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Volumn 350, Issue 1, 2014, Pages 110-123

Structure of the LINGO-1-anti-LINGO-1 Li81 antibody complex provides insights into the biology of LINGO-1 and the mechanism of action of the antibody therapys

Author keywords

[No Author keywords available]

Indexed keywords

EPITOPE; IMMUNOGLOBULIN F(AB) FRAGMENT; LEUCINE RICH REPEAT AND IMMUNOGLOBULIN CONTAINING NOGO RECEPTOR INTERACTING PROTEIN 1; LINGO 1 LI81 FAB COMPLEX; MEMBRANE PROTEIN; MONOCLONAL ANTIBODY; MONOCLONAL ANTIBODY LI81; UNCLASSIFIED DRUG;

EID: 84903523368     PISSN: 00223565     EISSN: 15210103     Source Type: Journal    
DOI: 10.1124/jpet.113.211771     Document Type: Article
Times cited : (21)

References (48)
  • 1
    • 84876193223 scopus 로고    scopus 로고
    • AMIGO3 is an NgR1/p75 co-receptor signalling axon growth inhibition in the acute phase of adult central nervous system injury
    • Ahmed Z, Douglas MR, John G, Berry M, and Logan A (2013) AMIGO3 is an NgR1/p75 co-receptor signalling axon growth inhibition in the acute phase of adult central nervous system injury. PLoS One 8:e61878.
    • (2013) PLoS One , vol.8
    • Ahmed, Z.1    Douglas, M.R.2    John, G.3    Berry, M.4    Logan, A.5
  • 2
    • 51549091266 scopus 로고    scopus 로고
    • Recombinant antibodies as therapeutic agents: Pathways for modeling new biodrugs
    • Aires da Silva F, Corte-Real S, and Goncalves J (2008) Recombinant antibodies as therapeutic agents: pathways for modeling new biodrugs. BioDrugs 22:301-314.
    • (2008) BioDrugs , vol.22 , pp. 301-314
    • Aires Da Silva, F.1    Corte-Real, S.2    Goncalves, J.3
  • 4
    • 77957969034 scopus 로고    scopus 로고
    • LINGO-1-mediated inhibition of oligodendrocyte differentiation does not require the leucine-rich repeats and is reversed by p75(NTR) antagonists
    • Bourikas D, Mir A, and Walmsley AR (2010) LINGO-1-mediated inhibition of oligodendrocyte differentiation does not require the leucine-rich repeats and is reversed by p75(NTR) antagonists. Mol Cell Neurosci 45:363-369.
    • (2010) Mol Cell Neurosci , vol.45 , pp. 363-369
    • Bourikas, D.1    Mir, A.2    Walmsley, A.R.3
  • 5
    • 84888339593 scopus 로고    scopus 로고
    • Local injection of lentivirus encoding LINGO-1-shRNA promotes functional recovery in rats with complete spinal cord transection
    • Cen J, Wu H, Wang J, Ren X, Zhang H, Wang J, Wan Y, and Deng Y (2013) Local injection of lentivirus encoding LINGO-1-shRNA promotes functional recovery in rats with complete spinal cord transection. Spine 38:1632-1639.
    • (2013) Spine , vol.38 , pp. 1632-1639
    • Cen, J.1    Wu, H.2    Wang, J.3    Ren, X.4    Zhang, H.5    Wang, J.6    Wan, Y.7    Deng, Y.8
  • 7
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project Number 4
    • Collaborative Computational Project, Number 4 (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr D Biol Crystallogr 50:760-763.
    • (1994) Acta Crystallogr D Biol Crystallogr , vol.50 , pp. 760-763
  • 9
    • 41949111140 scopus 로고    scopus 로고
    • Blocking LINGO-1 function promotes retinal ganglion cell survival following ocular hypertension and optic nerve transection
    • Fu QL, Hu B, Wu W, Pepinsky RB, Mi S, and So KF (2008) Blocking LINGO-1 function promotes retinal ganglion cell survival following ocular hypertension and optic nerve transection. Invest Ophthalmol Vis Sci 49:975-985.
    • (2008) Invest Ophthalmol Vis Sci , vol.49 , pp. 975-985
    • Fu, Q.L.1    Hu, B.2    Wu, W.3    Pepinsky, R.B.4    Mi, S.5    So, K.F.6
  • 10
    • 73349086530 scopus 로고    scopus 로고
    • Investigation of the influence of FcRn on the distribution of IgG to the brain
    • Garg A and Balthasar JP (2009) Investigation of the influence of FcRn on the distribution of IgG to the brain. AAPS J 11:553-557.
    • (2009) AAPS J , vol.11 , pp. 553-557
    • Garg, A.1    Balthasar, J.P.2
  • 12
    • 84862667140 scopus 로고    scopus 로고
    • LINGO-1, a transmembrane signaling protein, inhibits oligodendrocyte differentiation and myelination through intercellular selfinteractions
    • Jepson S, Vought B, Gross CH, Gan L, Austen D, Frantz JD, Zwahlen J, Lowe D, Markland W, and Krauss R (2012) LINGO-1, a transmembrane signaling protein, inhibits oligodendrocyte differentiation and myelination through intercellular selfinteractions. J Biol Chem 287:22184-22195.
    • (2012) J Biol Chem , vol.287 , pp. 22184-22195
    • Jepson, S.1    Vought, B.2    Gross, C.H.3    Gan, L.4    Austen, D.5    Frantz, J.D.6    Zwahlen, J.7    Lowe, D.8    Markland, W.9    Krauss, R.10
  • 14
    • 80855156672 scopus 로고    scopus 로고
    • Crystal structure and role of glycans and dimerization in folding of neuronal leucine-rich repeat protein AMIGO-1
    • Kajander T, Kuja-Panula J, Rauvala H, and Goldman A (2011) Crystal structure and role of glycans and dimerization in folding of neuronal leucine-rich repeat protein AMIGO-1. J Mol Biol 413:1001-1015.
    • (2011) J Mol Biol , vol.413 , pp. 1001-1015
    • Kajander, T.1    Kuja-Panula, J.2    Rauvala, H.3    Goldman, A.4
  • 15
    • 33645768162 scopus 로고    scopus 로고
    • A role for fibronectin-leucine-rich transmembrane cell-surface proteins in homotypic cell adhesion
    • Karaulanov EE, Böttcher RT, and Niehrs C (2006) A role for fibronectin-leucine-rich transmembrane cell-surface proteins in homotypic cell adhesion. EMBO Rep 7:283-290.
    • (2006) EMBO Rep , vol.7 , pp. 283-290
    • Karaulanov, E.E.1    Böttcher, R.T.2    Niehrs, C.3
  • 16
    • 67649843650 scopus 로고    scopus 로고
    • Strategies to extend plasma half-lives of recombinant antibodies
    • Kontermann RE (2009) Strategies to extend plasma half-lives of recombinant antibodies. BioDrugs 23:93-109.
    • (2009) BioDrugs , vol.23 , pp. 93-109
    • Kontermann, R.E.1
  • 17
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • DOI 10.1016/j.jmb.2007.05.022, PII S0022283607006420
    • Krissinel E and Henrick K (2007) Inference of macromolecular assemblies from crystalline state. J Mol Biol 372:774-797. (Pubitemid 47321791)
    • (2007) Journal of Molecular Biology , vol.372 , Issue.3 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 18
    • 0027772959 scopus 로고
    • Shape complementarity at protein/protein interfaces
    • DOI 10.1006/jmbi.1993.1648
    • Lawrence MC and Colman PM (1993) Shape complementarity at protein/protein interfaces. J Mol Biol 234:946-950. (Pubitemid 24027225)
    • (1993) Journal of Molecular Biology , vol.234 , Issue.4 , pp. 946-950
    • Lawrence, M.C.1    Colman, P.M.2
  • 20
    • 84897832359 scopus 로고    scopus 로고
    • LINGO-1 regulates oligodendrocyte differentiation by inhibiting ErbB2 translocation and activation in lipid rafts
    • Lee X, Shao Z, Sheng G, Pepinsky B, and Mi S (2014) LINGO-1 regulates oligodendrocyte differentiation by inhibiting ErbB2 translocation and activation in lipid rafts. Mol Cell Neurosci 60C:36-42.
    • (2014) Mol Cell Neurosci , vol.60 C , pp. 36-42
    • Lee, X.1    Shao, Z.2    Sheng, G.3    Pepinsky, B.4    Mi, S.5
  • 22
    • 33846426122 scopus 로고    scopus 로고
    • Solving structures of protein complexes by molecular replacement with Phaser
    • McCoy AJ (2007) Solving structures of protein complexes by molecular replacement with Phaser. Acta Crystallogr D Biol Crystallogr 63:32-41.
    • (2007) Acta Crystallogr D Biol Crystallogr , vol.63 , pp. 32-41
    • McCoy, A.J.1
  • 23
    • 78751514071 scopus 로고    scopus 로고
    • Targeting the Nogo receptor complex in diseases of the central nervous system
    • McDonald CL, Bandtlow C, and Reindl M (2011) Targeting the Nogo receptor complex in diseases of the central nervous system. Curr Med Chem 18:234-244.
    • (2011) Curr Med Chem , vol.18 , pp. 234-244
    • McDonald, C.L.1    Bandtlow, C.2    Reindl, M.3
  • 24
    • 33747781400 scopus 로고    scopus 로고
    • Structural correlations in the family of small leucine-rich repeat proteins and proteoglycans
    • DOI 10.1016/j.jsb.2006.01.016, PII S1047847706001237, Fibrous Protein Structure
    • McEwan PA, Scott PG, Bishop PN, and Bella J (2006) Structural correlations in the family of small leucine-rich repeat proteins and proteoglycans. J Struct Biol 155:294-305. (Pubitemid 44278663)
    • (2006) Journal of Structural Biology , vol.155 , Issue.2 , pp. 294-305
    • McEwan, P.A.1    Scott, P.G.2    Bishop, P.N.3    Bella, J.4
  • 29
    • 65249142739 scopus 로고    scopus 로고
    • Promotion of central nervous system remyelination by induced differentiation of oligodendrocyte precursor cells
    • Mi S, Miller RH, Tang W, Lee X, Hu B, Wu W, Zhang Y, Shields CB, Zhang Y, and Miklasz S, et al. (2009) Promotion of central nervous system remyelination by induced differentiation of oligodendrocyte precursor cells. Ann Neurol 65:304-315.
    • (2009) Ann Neurol , vol.65 , pp. 304-315
    • Mi, S.1    Miller, R.H.2    Tang, W.3    Lee, X.4    Hu, B.5    Wu, W.6    Zhang, Y.7    Shields, C.B.8    Zhang, Y.9    Miklasz, S.10
  • 30
    • 84880521310 scopus 로고    scopus 로고
    • Blocking LINGO-1 as a therapy to promote CNS repair: From concept to the clinic
    • Mi S, Pepinsky RB, and Cadavid D (2013) Blocking LINGO-1 as a therapy to promote CNS repair: from concept to the clinic. CNS Drugs 27:493-503.
    • (2013) CNS Drugs , vol.27 , pp. 493-503
    • Mi, S.1    Pepinsky, R.B.2    Cadavid, D.3
  • 32
    • 0026688573 scopus 로고
    • Connectin: A homophilic cell adhesion molecule expressed on a subset of muscles and the motoneurons that innervate them in Drosophila
    • Nose A, Mahajan VB, and Goodman CS (1992) Connectin: a homophilic cell adhesion molecule expressed on a subset of muscles and the motoneurons that innervate them in Drosophila. Cell 70:553-567.
    • (1992) Cell , vol.70 , pp. 553-567
    • Nose, A.1    Mahajan, V.B.2    Goodman, C.S.3
  • 33
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • DOI 10.1016/S0076-6879(97)76066-X
    • Otwinowski Z and Minor W (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 276:307-326. (Pubitemid 27085611)
    • (1997) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 34
    • 13244255374 scopus 로고    scopus 로고
    • A TNF receptor family member, TROY, is a coreceptor with Nogo receptor in mediating the inhibitory activity of myelin inhibitors
    • DOI 10.1016/j.neuron.2004.12.040, PII S0896627305000127
    • Park JB, Yiu G, Kaneko S, Wang J, Chang J, He XL, Garcia KC, and He Z (2005) A TNF receptor family member, TROY, is a coreceptor with Nogo receptor in mediating the inhibitory activity of myelin inhibitors. Neuron 45:345-351. (Pubitemid 40188202)
    • (2005) Neuron , vol.45 , Issue.3 , pp. 345-351
    • Park, J.B.1    Yiu, G.2    Kaneko, S.3    Wang, J.4    Chang, J.5    He, Z.6
  • 35
    • 80054787044 scopus 로고    scopus 로고
    • Exposure levels of anti-LINGO-1 Li81 antibody in the central nervous system and dose-efficacy relationships in rat spinal cord remyelination models after systemic administration
    • Pepinsky RB, Shao Z, Ji B, Wang Q, Meng G, Walus L, Lee X, Hu Y, Graff C, and Garber E, et al. (2011) Exposure levels of anti-LINGO-1 Li81 antibody in the central nervous system and dose-efficacy relationships in rat spinal cord remyelination models after systemic administration. J Pharmacol Exp Ther 339:519-529.
    • (2011) J Pharmacol Exp Ther , vol.339 , pp. 519-529
    • Pepinsky, R.B.1    Shao, Z.2    Ji, B.3    Wang, Q.4    Meng, G.5    Walus, L.6    Lee, X.7    Hu, Y.8    Graff, C.9    Garber, E.10
  • 39
    • 58049204808 scopus 로고    scopus 로고
    • SPIDER image processing for single-particle reconstruction of biological macromolecules from electron micrographs
    • Shaikh TR, Gao H, Baxter WT, Asturias FJ, Boisset N, Leith A, and Frank J (2008) SPIDER image processing for single-particle reconstruction of biological macromolecules from electron micrographs. Nat Protoc 3:1941-1974.
    • (2008) Nat Protoc , vol.3 , pp. 1941-1974
    • Shaikh, T.R.1    Gao, H.2    Baxter, W.T.3    Asturias, F.J.4    Boisset, N.5    Leith, A.6    Frank, J.7
  • 41
    • 4744353974 scopus 로고    scopus 로고
    • Principles and applicability of CSF sampling for the assessment of CNS drug delivery and pharmacodynamics
    • DOI 10.1016/j.addr.2004.07.011, PII S0169409X04001589
    • Shen DD, Artru AA, and Adkison KK (2004) Principles and applicability of CSF sampling for the assessment of CNS drug delivery and pharmacodynamics. Adv Drug Deliv Rev 56:1825-1857. (Pubitemid 39307054)
    • (2004) Advanced Drug Delivery Reviews , vol.56 , Issue.12 , pp. 1825-1857
    • Shen, D.D.1    Artru, A.A.2    Adkison, K.K.3
  • 42
    • 84856226013 scopus 로고    scopus 로고
    • The leucine-rich repeats of LINGO-1 are not required for self-interaction or interaction with the amyloid precursor protein
    • Stein T and Walmsley AR (2012) The leucine-rich repeats of LINGO-1 are not required for self-interaction or interaction with the amyloid precursor protein. Neurosci Lett 509:9-12.
    • (2012) Neurosci Lett , vol.509 , pp. 9-12
    • Stein, T.1    Walmsley, A.R.2
  • 44
    • 0029785996 scopus 로고    scopus 로고
    • The plasma and cytoplasmic forms of human gelsolin differ in disulfide structure
    • DOI 10.1021/bi960920n
    • Wen D, Corina K, Chow EP, Miller S, Janmey PA, and Pepinsky RB (1996) The plasma and cytoplasmic forms of human gelsolin differ in disulfide structure. Biochemistry 35:9700-9709. (Pubitemid 26302982)
    • (1996) Biochemistry , vol.35 , Issue.30 , pp. 9700-9709
    • Wen, D.1    Corina, K.2    Pingchang Chow, E.3    Miller, S.4    Janmey, P.A.5    Blake Pepinsky, R.6
  • 46
    • 0000680432 scopus 로고
    • Studies of chemically reacting systems on Sephadex I. Chromatographic demonstration of the Gilbert theory
    • Winzor DJ and Scheraga HA (1963) Studies of chemically reacting systems on Sephadex I. Chromatographic demonstration of the Gilbert theory. Biochemistry 2:1263-1267.
    • (1963) Biochemistry , vol.2 , pp. 1263-1267
    • Winzor, D.J.1    Scheraga, H.A.2
  • 48
    • 46849107098 scopus 로고    scopus 로고
    • Light activation of the LOV protein vivid generates a rapidly exchanging dimer
    • DOI 10.1021/bi8007017
    • Zoltowski BD and Crane BR (2008) Light activation of the LOV protein vivid generates a rapidly exchanging dimer. Biochemistry 47:7012-7019. (Pubitemid 351956350)
    • (2008) Biochemistry , vol.47 , Issue.27 , pp. 7012-7019
    • Zoltowski, B.D.1    Crane, B.R.2


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