Nogo Proteins
"Nogo Proteins" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
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.
Descriptor ID |
D000070798
|
MeSH Number(s) |
D12.776.543.620.738 D12.776.631.580.738
|
Concept/Terms |
Nogo Proteins- Nogo Proteins
- Nogo Protein
- Reticulon-4 Protein
- Reticulon 4 Protein
Nogo-A Protein- Nogo-A Protein
- Nogo A Protein
- NI-250 Protein
- NI 250 Protein
- NI-220 Protein
- NI 220 Protein
Nogo-B Protein- Nogo-B Protein
- Nogo B Protein
- Reticulon 4-B Protein
- Reticulon 4 B Protein
|
Below are MeSH descriptors whose meaning is more general than "Nogo Proteins".
Below are MeSH descriptors whose meaning is more specific than "Nogo Proteins".
This graph shows the total number of publications written about "Nogo Proteins" by people in this website by year, and whether "Nogo Proteins" was a major or minor topic of these publications.
To see the data from this visualization as text, click here.
Year | Major Topic | Minor Topic | Total |
---|
2006 | 0 | 1 | 1 | 2007 | 0 | 1 | 1 | 2010 | 0 | 1 | 1 | 2012 | 0 | 1 | 1 | 2013 | 0 | 1 | 1 | 2014 | 0 | 1 | 1 | 2019 | 1 | 0 | 1 | 2021 | 0 | 1 | 1 |
To return to the timeline, click here.
Below are the most recent publications written about "Nogo Proteins" by people in Profiles.
-
Wu H, Voeltz GK. Reticulon-3 Promotes Endosome Maturation at ER Membrane Contact Sites. Dev Cell. 2021 01 11; 56(1):52-66.e7.
-
Orfila JE, Dietz RM, Rodgers KM, Dingman A, Patsos OP, Cruz-Torres I, Grewal H, Strnad F, Schroeder C, Herson PS. Experimental pediatric stroke shows age-specific recovery of cognition and role of hippocampal Nogo-A receptor signaling. J Cereb Blood Flow Metab. 2020 03; 40(3):588-599.
-
Pathak GP, Shah R, Kennedy BE, Murphy JP, Clements D, Konda P, Giacomantonio M, Xu Z, Schlaepfer IR, Gujar S. RTN4 Knockdown Dysregulates the AKT Pathway, Destabilizes the Cytoskeleton, and Enhances Paclitaxel-Induced Cytotoxicity in Cancers. Mol Ther. 2018 08 01; 26(8):2019-2033.
-
Rowland AA, Chitwood PJ, Phillips MJ, Voeltz GK. ER contact sites define the position and timing of endosome fission. Cell. 2014 Nov 20; 159(5):1027-1041.
-
Wrzos C, Winkler A, Metz I, Kayser DM, Thal DR, Wegner C, Br?ck W, Nessler S, Bennett JL, Stadelmann C. Early loss of oligodendrocytes in human and experimental neuromyelitis optica lesions. Acta Neuropathol. 2014 Apr; 127(4):523-38.
-
Stahel PF, VanderHeiden T, Finn MA. Management strategies for acute spinal cord injury: current options and future perspectives. Curr Opin Crit Care. 2012 Dec; 18(6):651-60.
-
Zurek N, Sparks L, Voeltz G. Reticulon short hairpin transmembrane domains are used to shape ER tubules. Traffic. 2011 Jan; 12(1):28-41.
-
Kiseleva E, Morozova KN, Voeltz GK, Allen TD, Goldberg MW. Reticulon 4a/NogoA locates to regions of high membrane curvature and may have a role in nuclear envelope growth. J Struct Biol. 2007 Nov; 160(2):224-35.
-
Voeltz GK, Prinz WA, Shibata Y, Rist JM, Rapoport TA. A class of membrane proteins shaping the tubular endoplasmic reticulum. Cell. 2006 Feb 10; 124(3):573-86.
|
People People who have written about this concept. _
Similar Concepts
People who have written about this concept.
_
Top Journals
Top journals in which articles about this concept have been published.
|