Biomaterial Database

Nogo domains and a Nogo receptor: implications for axon regeneration. 2001

P A Brittis, and J G Flanagan

Department of Cell Biology and, Program in Neuroscience, Harvard Medical School, Boston, MA 02115, USA.

UI	MeSH Term	Description	Entries
D009185	Myelin Proteins	MYELIN-specific proteins that play a structural or regulatory role in the genesis and maintenance of the lamellar MYELIN SHEATH structure.	Myelin Protein,Protein, Myelin,Proteins, Myelin
D009416	Nerve Regeneration	Renewal or physiological repair of damaged nerve tissue.	Nerve Tissue Regeneration,Nervous Tissue Regeneration,Neural Tissue Regeneration,Nerve Tissue Regenerations,Nervous Tissue Regenerations,Neural Tissue Regenerations,Regeneration, Nerve,Regeneration, Nerve Tissue,Regeneration, Nervous Tissue,Regeneration, Neural Tissue,Tissue Regeneration, Nerve,Tissue Regeneration, Nervous,Tissue Regeneration, Neural
D011956	Receptors, Cell Surface	Cell surface proteins that bind signalling molecules external to the cell with high affinity and convert this extracellular event into one or more intracellular signals that alter the behavior of the target cell (From Alberts, Molecular Biology of the Cell, 2nd ed, pp693-5). Cell surface receptors, unlike enzymes, do not chemically alter their ligands.	Cell Surface Receptor,Cell Surface Receptors,Hormone Receptors, Cell Surface,Receptors, Endogenous Substances,Cell Surface Hormone Receptors,Endogenous Substances Receptors,Receptor, Cell Surface,Surface Receptor, Cell
D006801	Humans	Members of the species Homo sapiens.	Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000070798	Nogo Proteins	Myelin proteins that are expressed as three isoforms: Nogo-A, Nogo-B, and Nogo-C. These share a C-terminal reticulon homology domain (RHD), consisting of two hydrophobic membrane domains flanking a 66 amino acid (Nogo-66) hydrophilic region. A long transmembrane region allows conformations that either span the entire membrane or fold into a hairpin conformation. Nogo inhibits NEURITE outgrowth and modulates wiring and the restriction of SYNAPTIC PLASTICITY in the adult central nervous system. It also regulates neurite fasciculation, branching, and extension in the developing nervous system.	NI-220 Protein,NI-250 Protein,NI-35 Protein,NI-35-250,Neurite Growth Inhibitor 35-350,Nogo Protein,Nogo-66 Protein,Nogo-A Protein,Nogo-B Protein,Nogo-C Protein,Reticulon 4-B Protein,Reticulon-4 Protein,NI 220 Protein,NI 250 Protein,NI 35 250,NI 35 Protein,Neurite Growth Inhibitor 35 350,Nogo 66 Protein,Nogo A Protein,Nogo B Protein,Nogo C Protein,Reticulon 4 B Protein,Reticulon 4 Protein
D000070816	Nogo Receptor 1	A high affinity receptor for myelin-associated inhibitors (MAIs) that include NOGO-A PROTEIN; OLIGODENDROCYTE MYELIN GLYCOPROTEIN; and MYELIN-ASSOCIATED GLYCOPROTEIN. It is expressed primarily by neurons in the brain and OLFACTORY BULBS. During embryonic development, it is expressed in the PERIPHERAL NERVOUS SYSTEM. It localizes to GROWTH CONES and may inhibit neurite outgrowth following SPINAL INJURY.	NgR1 Protein,Nogo-66 Receptor,RTN4R Protein,Reticulon-4 Receptor,Nogo 66 Receptor,Protein, NgR1,Protein, RTN4R,Receptor, Nogo-66,Receptor, Reticulon-4,Reticulon 4 Receptor
D000818	Animals	Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA.	Animal,Metazoa,Animalia
D001369	Axons	Nerve fibers that are capable of rapidly conducting impulses away from the neuron cell body.	Axon
D013119	Spinal Cord Injuries	Penetrating and non-penetrating injuries to the spinal cord resulting from traumatic external forces (e.g., WOUNDS, GUNSHOT; WHIPLASH INJURIES; etc.).	Myelopathy, Traumatic,Injuries, Spinal Cord,Post-Traumatic Myelopathy,Spinal Cord Contusion,Spinal Cord Laceration,Spinal Cord Transection,Spinal Cord Trauma,Contusion, Spinal Cord,Contusions, Spinal Cord,Cord Contusion, Spinal,Cord Contusions, Spinal,Cord Injuries, Spinal,Cord Injury, Spinal,Cord Laceration, Spinal,Cord Lacerations, Spinal,Cord Transection, Spinal,Cord Transections, Spinal,Cord Trauma, Spinal,Cord Traumas, Spinal,Injury, Spinal Cord,Laceration, Spinal Cord,Lacerations, Spinal Cord,Myelopathies, Post-Traumatic,Myelopathies, Traumatic,Myelopathy, Post-Traumatic,Post Traumatic Myelopathy,Post-Traumatic Myelopathies,Spinal Cord Contusions,Spinal Cord Injury,Spinal Cord Lacerations,Spinal Cord Transections,Spinal Cord Traumas,Transection, Spinal Cord,Transections, Spinal Cord,Trauma, Spinal Cord,Traumas, Spinal Cord,Traumatic Myelopathies,Traumatic Myelopathy
D017434	Protein Structure, Tertiary	The level of protein structure in which combinations of secondary protein structures (ALPHA HELICES; BETA SHEETS; loop regions, and AMINO ACID MOTIFS) pack together to form folded shapes. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure.	Tertiary Protein Structure,Protein Structures, Tertiary,Tertiary Protein Structures