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Gene Review

Rfwd2  -  ring finger and WD repeat domain 2

Mus musculus

Synonyms: AI316802, C80879, Constitutive photomorphogenesis protein 1 homolog, Cop1, E3 ubiquitin-protein ligase RFWD2, ...
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Disease relevance of Rfwd2


High impact information on Rfwd2


Chemical compound and disease context of Rfwd2


Biological context of Rfwd2


Anatomical context of Rfwd2

  • Cop 1 exhibited the most extensive and fast binding to antigen-presenting cells [11].
  • In addition, several anti-Cop 1 hybridomas cross-reacted with BP [3].
  • Adoptively transferred labeled Cop 1-specific suppressor cells were found in brain sections 7 and 10 days after their injection to the periphery, whereas lysozyme-specific cells were absent in the CNS [12].
  • In contrast, the number of surviving retinal ganglion cells per square millimeter in glutamate-injected retinas was significantly larger in mice immunized 10 days previously with Cop-1 emulsified in complete Freund's adjuvant than in mice injected with PBS in the same adjuvant (2,133 +/- 270 and 1,329 +/- 121, respectively, mean +/- SEM; P < 0.02) [5].
  • Thus, the use of mAbs has uncovered specificities that are not evident in antisera and has revealed pronounced cross-reactivity between BP and Cop 1 at the B-cell level [3].

Associations of Rfwd2 with chemical compounds

  • Cycloheximide, a protein synthesis inhibitor, had no effect on the enhanced staining intensity with anti-DR antibody of cells treated with Cop 1 or MBP, whereas it inhibited the enhanced staining of both DR and DQ molecules caused by the respective antibodies, in the absence of these antigens [13].

Regulatory relationships of Rfwd2

  • Our findings indicate that the polarization of the Cop 1-induced lines did not result from the immunization vehicle or the in vitro growing conditions, but rather from the tendency of Cop 1 to preferentially induce a Th2 response [6].
  • Furthermore, Cop 1 Ts cells ameliorated EAE induced by two unrelated encephalitogenic epitopes of PLP: p139-151 and p178-191, that produced different forms of disease [14].
  • In the present study we further investigated the mechanism of Cop 1 suppressive activity and tested whether Cop 1 could inhibit the specific T-cell response to myelin basic protein (BP) [9].

Other interactions of Rfwd2


Analytical, diagnostic and therapeutic context of Rfwd2


  1. Novel synthetic amino acid copolymers that inhibit autoantigen-specific T cell responses and suppress experimental autoimmune encephalomyelitis. Fridkis-Hareli, M., Santambrogio, L., Stern, J.N., Fugger, L., Brosnan, C., Strominger, J.L. J. Clin. Invest. (2002) [Pubmed]
  2. Therapeutic vaccine for acute and chronic motor neuron diseases: implications for amyotrophic lateral sclerosis. Angelov, D.N., Waibel, S., Guntinas-Lichius, O., Lenzen, M., Neiss, W.F., Tomov, T.L., Yoles, E., Kipnis, J., Schori, H., Reuter, A., Ludolph, A., Schwartz, M. Proc. Natl. Acad. Sci. U.S.A. (2003) [Pubmed]
  3. Cross-reactions and specificities of monoclonal antibodies against myelin basic protein and against the synthetic copolymer 1. Teitelbaum, D., Aharoni, R., Sela, M., Arnon, R. Proc. Natl. Acad. Sci. U.S.A. (1991) [Pubmed]
  4. Therapeutic vaccines in autoimmunity. Sela, M., Mozes, E. Proc. Natl. Acad. Sci. U.S.A. (2004) [Pubmed]
  5. Vaccination for protection of retinal ganglion cells against death from glutamate cytotoxicity and ocular hypertension: implications for glaucoma. Schori, H., Kipnis, J., Yoles, E., WoldeMussie, E., Ruiz, G., Wheeler, L.A., Schwartz, M. Proc. Natl. Acad. Sci. U.S.A. (2001) [Pubmed]
  6. Copolymer 1 induces T cells of the T helper type 2 that crossreact with myelin basic protein and suppress experimental autoimmune encephalomyelitis. Aharoni, R., Teitelbaum, D., Sela, M., Arnon, R. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
  7. Binding of random copolymers of three amino acids to class II MHC molecules. Fridkis-Hareli, M., Aharoni, R., Teitelbaum, D., Arnon, R., Sela, M., Strominger, J.L. Int. Immunol. (1999) [Pubmed]
  8. Copolymer 1 acts against the immunodominant epitope 82-100 of myelin basic protein by T cell receptor antagonism in addition to major histocompatibility complex blocking. Aharoni, R., Teitelbaum, D., Arnon, R., Sela, M. Proc. Natl. Acad. Sci. U.S.A. (1999) [Pubmed]
  9. Specific inhibition of the T-cell response to myelin basic protein by the synthetic copolymer Cop 1. Teitelbaum, D., Aharoni, R., Arnon, R., Sela, M. Proc. Natl. Acad. Sci. U.S.A. (1988) [Pubmed]
  10. Copolymer 1 inhibits manifestations of graft rejection. Aharoni, R., Teitelbaum, D., Arnon, R., Sela, M. Transplantation (2001) [Pubmed]
  11. Direct binding of myelin basic protein and synthetic copolymer 1 to class II major histocompatibility complex molecules on living antigen-presenting cells--specificity and promiscuity. Fridkis-Hareli, M., Teitelbaum, D., Gurevich, E., Pecht, I., Brautbar, C., Kwon, O.J., Brenner, T., Arnon, R., Sela, M. Proc. Natl. Acad. Sci. U.S.A. (1994) [Pubmed]
  12. Specific Th2 cells accumulate in the central nervous system of mice protected against experimental autoimmune encephalomyelitis by copolymer 1. Aharoni, R., Teitelbaum, D., Leitner, O., Meshorer, A., Sela, M., Arnon, R. Proc. Natl. Acad. Sci. U.S.A. (2000) [Pubmed]
  13. Binding of copolymer 1 and myelin basic protein leads to clustering of class II MHC molecules on antigen-presenting cells. Fridkis-Hareli, M., Teitelbaum, D., Pecht, I., Arnon, R., Sela, M. Int. Immunol. (1997) [Pubmed]
  14. Bystander suppression of experimental autoimmune encephalomyelitis by T cell lines and clones of the Th2 type induced by copolymer 1. Aharoni, R., Teitelbaum, D., Sela, M., Arnon, R. J. Neuroimmunol. (1998) [Pubmed]
  15. Immunomodulation of experimental autoimmune encephalomyelitis by oral administration of copolymer 1. Teitelbaum, D., Arnon, R., Sela, M. Proc. Natl. Acad. Sci. U.S.A. (1999) [Pubmed]
  16. Oral tolerance to copolymer 1 in myelin basic protein (MBP) TCR transgenic mice: cross-reactivity with MBP-specific TCR and differential induction of anti-inflammatory cytokines. Maron, R., Slavin, A.J., Hoffmann, E., Komagata, Y., Weiner, H.L. Int. Immunol. (2002) [Pubmed]
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