Clostridial C3 proteins: Recent approaches to improve neuronal growth and regeneration
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Ahnert-Hilger, 2004, Differential effects of Rho GTPases on axonal and dendritic development in hippocampal neurones, J. Neurochem., 90, 9, 10.1111/j.1471-4159.2004.02475.x
Aktories, 1987, Clostridium botulinum type C produces a novel ADP-ribosyltransferase distinct from botulinum C2 toxin, FEBS Lett., 212, 109, 10.1016/0014-5793(87)81566-1
Aktories, 1989, The rho gene product expressed in E. coli is a substrate of botulinum ADP-ribosyltransferase C3, Biochem. Biophys. Res. Commun., 158, 209, 10.1016/S0006-291X(89)80199-8
Aktories, 1995, Studies on the active-site structure of C3-like exoenzymes: involvement of glutamic acid in catalysis of ADP-ribosylation, Biochimie, 77, 326, 10.1016/0300-9084(96)88142-9
Basso, 1995, A sensitive and reliable locomotor rating scale for open field testing in rats, J. Neurotrauma, 12, 1, 10.1089/neu.1995.12.1
Benson, 2005, Ephrin-B3 is a myelin-based inhibitor of neurite outgrowth, Proc. Natl. Acad. Sci. U. S. A., 102, 10694, 10.1073/pnas.0504021102
Bertrand, 2005, Application of Rho antagonist to neuronal cell bodies promotes neurite growth in compartmented cultures and regeneration of retinal ganglion cell axons in the optic nerve of adult rats, J. Neurosci., 25, 1113, 10.1523/JNEUROSCI.3931-04.2005
Bertrand, 2007, Enhanced survival and regeneration of axotomized retinal neurons by repeated delivery of cell-permeable C3-like Rho antagonists, Neurobiol. Dis., 25, 65, 10.1016/j.nbd.2006.08.008
Boato, 2010, C3 peptide enhances recovery from spinal cord injury by improved regenerative growth of descending fiber tracts, J. Cell Sci., 123, 1652, 10.1242/jcs.066050
Borisoff, 2003, Suppression of Rho-kinase activity promotes axonal growth on inhibitory CNS substrates, Mol. Cell. Neurosci., 22, 405, 10.1016/S1044-7431(02)00032-5
Chen, 2000, Nogo-A is a myelin-associated neurite outgrowth inhibitor and an antigen for monoclonal antibody IN-1, Nature, 403, 434, 10.1038/35000219
Conrad, 2005, Prolonged lesional expression of RhoA and RhoB following spinal cord injury, J. Comp. Neurol., 487, 166, 10.1002/cne.20561
Del Río, 2007, Overcoming chondroitin sulphate proteoglycan inhibition of axon growth in the injured brain: lessons from chondroitinase ABC, Curr. Pharm. Des., 13, 2485, 10.2174/138161207781368639
Dergham, 2002, Rho signalling pathway targeted to promote spinal cord repair, J. Neurosci., 22, 6570, 10.1523/JNEUROSCI.22-15-06570.2002
Dubreuil, 2003, Rho activation patterns after spinal cord injury and the role of activated Rho in apoptosis in the central nervous system, J. Cell Biol., 162, 233, 10.1083/jcb.200301080
Duffy, 2009, Rho-associated kinase II (ROCKII) limits axonal growth after trauma within the adult mouse spinal cord, J. Neurosci., 29, 15266, 10.1523/JNEUROSCI.4650-09.2009
Fournier, 2003, Rho kinase inhibition enhances axonal regeneration in the injured CNS, J. Neurosci., 23, 1416, 10.1523/JNEUROSCI.23-04-01416.2003
Freund, 2006, Nogo-A-specific antibody treatment enhances sprouting and functional recovery after cervical lesion in adult primates, Nat. Med., 12, 790, 10.1038/nm1436
Frotscher, 1993, Formation of layer-specific fiber projections to the hippocampus in vitro, Proc. Natl. Acad. Sci. U. S. A., 90, 10400, 10.1073/pnas.90.21.10400
Fu, 2007, Nonsteroidal anti-inflammatory drugs promote axon regeneration via RhoA inhibition, J. Neurosci., 27, 4154, 10.1523/JNEUROSCI.4353-06.2007
Genth, 2003, Entrapment of rho ADP-ribosylated by Clostridium botulinum C3 exoenzyme in the Rho-guanine nucleotide dissociation inhibitor-1 complex, J. Biol. Chem., 278, 28523, 10.1074/jbc.M301915200
Hall, 1998, Rho GTPases and the actin cytoskeleton, Science, 279, 509, 10.1126/science.279.5350.509
Hall, 2010, Rho and Ras GTPases in axon growth, guidance, and branching, Cold Spring Harb. Perspect. Biol., 2, a001818, 10.1101/cshperspect.a001818
Hoffmann, 2008, Inhibition of Rho-dependent pathways by Clostridium botulinum C3 protein induces a proinflammatory profile in microglia, Glia, 56, 1162, 10.1002/glia.20687
Holbourn, 2005, Molecular recognition of an ADP-ribosylating Clostridium botulinum C3 exoenzyme by RalA GTPase, Proc. Natl. Acad. Sci. U. S. A., 102, 5357, 10.1073/pnas.0501525102
Höltje, 2005, Role of Rho GTPase in astrocyte morphology and migratory response during in vitro wound healing, J. Neurochem., 95, 1237, 10.1111/j.1471-4159.2005.03443.x
Höltje, 2008, Glutamate uptake and release by astrocytes are enhanced by Clostridium botulinum C3 protein, J. Biol. Chem., 283, 9289, 10.1074/jbc.M706499200
Höltje, 2009, A 29-amino acid fragment of Clostridium botulinum C3 protein enhances neuronal outgrowth, connectivity, and reinnervation, FASEB J., 23, 1115, 10.1096/fj.08-116855
Jalink, 1994, Inhibition of lysophosphatidate- and thrombin-induced neurite retraction and neuronal cell rounding by ADP ribosylation of the small GTP-binding protein Rho, J. Cell Biol., 12, 801, 10.1083/jcb.126.3.801
Jin, 1997, Rac1 mediates collapsin-1-induced growth cone collapse, J. Neurosci., 17, 6256, 10.1523/JNEUROSCI.17-16-06256.1997
Just, 1992, Purification and characterization of an ADP-ribosyltransferase produced by Clostridium limosum, J. Biol. Chem., 267, 10274, 10.1016/S0021-9258(19)50014-X
Just, 1995, Rho-ADP ribosylating exoenzyme from Bacillus cereus – purification characterization and identification of the NAD-binding site, Biochemistry, 34, 334, 10.1021/bi00001a041
Jalink, 1994, Inhibition of lysophosphatidate- and thrombin-induced neurite retraction and neuronal cell rounding by ADP ribosylation of the small GTP-binding protein Rho, J. Cell Biol., 126, 801, 10.1083/jcb.126.3.801
Kozma, 1997, Rho family GTPases and neuronal growth cone remodelling: relationship between increased complexity induced by Cdc42Hs, Rac1, and acetylcholine and collapse induced by RhoA and lysophosphatidic acid, Mol. Cell. Biol., 17, 1201, 10.1128/MCB.17.3.1201
Lehmann, 1999, Inactivation of Rho signaling pathway promotes CNS axon regeneration, J. Neurosci., 19, 7537, 10.1523/JNEUROSCI.19-17-07537.1999
Lord-Fontaine, 2008, Local inhibition of Rho signaling by cell-permeable recombinant protein BA-210 prevents secondary damage and promotes functional recovery following acute spinal cord injury, J. Neurotrauma, 25, 1309, 10.1089/neu.2008.0613
McKerracher, 1994, Identification of myelin-associated glycoprotein as a major myelin-derived inhibitor of neurite growth, Neuron, 13, 805, 10.1016/0896-6273(94)90247-X
McKerracher, 2006, Targeting Rho to stimulate repair after spinal cord injury, J. Neurotrauma, 23, 309, 10.1089/neu.2006.23.309
Molinari, 2006, Localization of the C3-Like ADP-ribosyltransferase from Staphylococcus aureus during bacterial invasion of mammalian cells, Infect. Immun., 74, 3673, 10.1128/IAI.02013-05
Pautsch, 2005, Crystal structure of the C3bot-RalA complex reveals a novel type of action of a bacterial exoenzyme, EMBO J., 24, 3670, 10.1038/sj.emboj.7600813
Pearse, 2004, cAMP and Schwann cells promote axonal growth and functional recovery after spinal cord injury, Nat. Med., 10, 610, 10.1038/nm1056
Properzi, 2003, Chondroitin sulphate proteoglycans in the central nervous system: changes and synthesis after injury, Biochem. Soc. Trans., 31, 335, 10.1042/bst0310335
Rolls, 2008, Two faces of chondroitin sulfate proteoglycan in spinal cord repair: a role in microglia/macrophage activation, PLoS Med., 5, e171, 10.1371/journal.pmed.0050171
Sehr, 1998, Glucosylation and ADP-ribosylation of Rho proteins-effects on nucleotide binding, GTPase activity and effector-coupling, Biochemistry, 37, 5296, 10.1021/bi972592c
Sekine, 1989, Asparagine residue in the rho gene product is the modification site for botulinum ADP-ribosyltransferase, J. Biol. Chem., 264, 8602, 10.1016/S0021-9258(18)81834-8
Sheng, 2004, A no-laminectomy spinal cord compression injury model in mice, J. Neurotrauma, 21, 595, 10.1089/089771504774129928
Wilde, 2001, A novel C3-like ADP-ribosyltransferase from Staphylococcus aureus modifying RhoE and Rnd3, J. Biol. Chem., 276, 9537, 10.1074/jbc.M011035200
Wilde, 2002, Interaction of the Rho-ADP-ribosylating C3 exoenzyme with RalA, J. Biol. Chem., 277, 14771, 10.1074/jbc.M201072200