메뉴 건너뛰기




Volumn 8, Issue 4, 2016, Pages

Detection and quantification of ADP-ribosylated RhoA/B by monoclonal antibody

Author keywords

ADP ribosylated RhoA; ADP Ribosyltransferase; C3 transferase

Indexed keywords

ADP RIBOSYLATED RHOA; ADP RIBOSYLATED RHOB; MONOCLONAL ANTIBODY; NICOTINAMIDE ADENINE DINUCLEOTIDE; RECOMBINANT PROTEIN; RHO FACTOR; UNCLASSIFIED DRUG; ADENOSINE DIPHOSPHATE RIBOSE; BOTULINUM TOXIN; EXOENZYME C3, CLOSTRIDIUM BOTULINUM; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; RHOA GUANINE NUCLEOTIDE BINDING PROTEIN; RHOB GUANINE NUCLEOTIDE BINDING PROTEIN;

EID: 85011982250     PISSN: None     EISSN: 20726651     Source Type: Journal    
DOI: 10.3390/toxins8040100     Document Type: Article
Times cited : (9)

References (34)
  • 1
    • 0024353843 scopus 로고
    • Asparagine residue in the Rho gene product is the modification site for botulinum ADP-ribosyltransferase
    • PubMed
    • Sekine, A.; Fujiwara, M.; Narumiya, S. Asparagine residue in the Rho gene product is the modification site for botulinum ADP-ribosyltransferase. J. Biol. Chem. 1989, 264, 8602–8605. [PubMed]
    • (1989) J. Biol. Chem , vol.264 , pp. 8602-8605
    • Sekine, A.1    Fujiwara, M.2    Narumiya, S.3
  • 2
    • 0028170820 scopus 로고
    • Small GTP-binding proteins and the regulation of the actin cytoskeleton
    • CrossRefPubMed
    • Hall, A. Small GTP-binding proteins and the regulation of the actin cytoskeleton. Annu. Rev. Cell Biol. 1994, 10, 31–54. [CrossRef] [PubMed]
    • (1994) Annu. Rev. Cell Biol , vol.10 , pp. 31-54
    • Hall, A.1
  • 5
    • 0037031945 scopus 로고    scopus 로고
    • Characterization of new cell permeable C3-like proteins that inactivate Rho and stimulate neurite outgrowth on inhibitory substrates
    • CrossRefPubMed
    • Winton, M.J.; Dubreuil, C.I.; Lasko, D.; Leclerc, N.; McKerracher, L. Characterization of new cell permeable C3-like proteins that inactivate Rho and stimulate neurite outgrowth on inhibitory substrates. J. Biol. Chem. 2002, 277, 32820–32829. [CrossRef] [PubMed]
    • (2002) J. Biol. Chem. , vol.277 , pp. 32820-32829
    • Winton, M.J.1    Dubreuil, C.I.2    Lasko, D.3    Leclerc, N.4    McKerracher, L.5
  • 6
    • 0024495952 scopus 로고
    • Endogenous ADP-ribosylation of elongation factor 2 in polyoma virus-transformed baby hamster kidney cells
    • CrossRefPubMed
    • Fendrick, J.L.; Iglewski, W.J. Endogenous ADP-ribosylation of elongation factor 2 in polyoma virus-transformed baby hamster kidney cells. Proc. Natl. Acad. Sci. USA 1989, 86, 554–557. [CrossRef] [PubMed]
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 554-557
    • Fendrick, J.L.1    Iglewski, W.J.2
  • 7
    • 84863817351 scopus 로고    scopus 로고
    • Distinct biological activities of C3 and ADP-ribosyltransferase-deficient C3-E174Q
    • PubMed
    • Rohrbeck, A.; Kolbe, T.; Hagemann, S.; Genth, H.; Just, I. Distinct biological activities of C3 and ADP-ribosyltransferase-deficient C3-E174Q. FEBS J. 2012, 279, 2657–2671. [PubMed]
    • (2012) FEBS J , vol.279 , pp. 2657-2671
    • Rohrbeck, A.1    Kolbe, T.2    Hagemann, S.3    Genth, H.4    Just, I.5
  • 11
    • 77953155470 scopus 로고    scopus 로고
    • Fragmentation behavior of Amadori-peptides obtained by non-enzymatic glycosylation of lysine residues with ADP-ribose in tandem mass spectrometry
    • CrossRefPubMed
    • Fedorova, M.; Frolov, A.; Hoffmann, R. Fragmentation behavior of Amadori-peptides obtained by non-enzymatic glycosylation of lysine residues with ADP-ribose in tandem mass spectrometry. J. Mass Spectrom. 2010, 45, 664–669. [CrossRef] [PubMed]
    • (2010) J. Mass Spectrom , vol.45 , pp. 664-669
    • Fedorova, M.1    Frolov, A.2    Hoffmann, R.3
  • 12
    • 84946854668 scopus 로고    scopus 로고
    • Proteome alterations of hippocampal cells caused by clostridium botulinum C3 exoenzyme
    • CrossRefPubMed
    • Schröder, A.; Rohrbeck, A.; Just, I.; Pich, A. Proteome alterations of hippocampal cells caused by clostridium botulinum C3 exoenzyme. J. Proteome Res. 2015, 14, 4721–4733. [CrossRef] [PubMed]
    • (2015) J. Proteome Res , vol.14 , pp. 4721-4733
    • Schröder, A.1    Rohrbeck, A.2    Just, I.3    Pich, A.4
  • 13
    • 84931264473 scopus 로고    scopus 로고
    • Construction of human antibody gene libraries and selection of antibodies by phage display
    • PubMed
    • Frenzel, A.; Kügler, J.; Wilke, S.; Schirrmann, T.; Hust, M. Construction of human antibody gene libraries and selection of antibodies by phage display. Methods Mol. Biol. 2014, 1060, 215–243. [PubMed]
    • (2014) Methods Mol. Biol , vol.1060 , pp. 215-243
    • Frenzel, A.1    Kügler, J.2    Wilke, S.3    Schirrmann, T.4    Hust, M.5
  • 15
    • 84938223026 scopus 로고    scopus 로고
    • Subcellular localization of Rho GTPases: Implications for axon regeneration
    • CrossRefPubMed
    • Hynds, D.L. Subcellular localization of Rho GTPases: Implications for axon regeneration. Neural Regen Res. 2015, 10, 1032–1033. [CrossRef] [PubMed]
    • (2015) Neural Regen Res , vol.10 , pp. 1032-1033
    • Hynds, D.L.1
  • 16
    • 84939958665 scopus 로고    scopus 로고
    • Ezrin-related Phosphoinositide pathway modifies RhoA and Rac1 in human osteosarcoma cell lines
    • CrossRefPubMed
    • Lo Vasco, V.R.; Leopizzi, M.; Rocca, C.D. Ezrin-related Phosphoinositide pathway modifies RhoA and Rac1 in human osteosarcoma cell lines. J. Cell Commun. Signal. 2015, 9, 55–62. [CrossRef] [PubMed]
    • (2015) J. Cell Commun. Signal , vol.9 , pp. 55-62
    • Lo Vasco, V.R.1    Leopizzi, M.2    Rocca, C.D.3
  • 17
    • 0031970317 scopus 로고    scopus 로고
    • Membrane association and targeting of prenylated Ras-like GTPases
    • CrossRef
    • Seabra, M.C. Membrane association and targeting of prenylated Ras-like GTPases. Cell Signal. 1998, 10, 167–172. [CrossRef]
    • (1998) Cell Signal , vol.10 , pp. 167-172
    • Seabra, M.C.1
  • 18
    • 84878568921 scopus 로고    scopus 로고
    • ERM/Rho protein expression in ductal breast cancer: A 15 year follow-up
    • CrossRefPubMed
    • Halon, A.; Donizy, P.; Surowiak, P.; Matkowski, R. ERM/Rho protein expression in ductal breast cancer: A 15 year follow-up. Cell Oncol. 2013, 36, 181–190. [CrossRef] [PubMed]
    • (2013) Cell Oncol. , vol.36 , pp. 181-190
    • Halon, A.1    Donizy, P.2    Surowiak, P.3    Matkowski, R.4
  • 19
    • 0036443970 scopus 로고    scopus 로고
    • Isoprenylation is necessary for the full invasive potential of RhoA overexpression in human melanoma cells
    • CrossRefPubMed
    • Collisson, E.A.; Carranza, D.C.; Chen, I.Y.; Kolodney, M.S. Isoprenylation is necessary for the full invasive potential of RhoA overexpression in human melanoma cells. J. Investig. Dermatol. 2002, 119, 1172–1176. [CrossRef] [PubMed]
    • (2002) J. Investig. Dermatol , vol.119 , pp. 1172-1176
    • Collisson, E.A.1    Carranza, D.C.2    Chen, I.Y.3    Kolodney, M.S.4
  • 20
    • 80053096028 scopus 로고    scopus 로고
    • Factors influencing RhoA protein distribution in the nucleus
    • PubMed
    • Li, Y.; Chen, Y.; Xu, J. Factors influencing RhoA protein distribution in the nucleus. Mol. Med. Rep. 2011, 4, 1115–1119. [PubMed]
    • (2011) Mol. Med. Rep , vol.4 , pp. 1115-1119
    • Li, Y.1    Chen, Y.2    Xu, J.3
  • 21
    • 84861738385 scopus 로고    scopus 로고
    • Analysis of RhoA and Rho GEF activity in whole cells and the cell nucleus
    • CrossRefPubMed
    • Guilluy, C.; Dubash, A.D.; García-Mata, R. Analysis of RhoA and Rho GEF activity in whole cells and the cell nucleus. Nat. Protoc. 2011, 6, 2050–2060. [CrossRef] [PubMed]
    • (2011) Nat. Protoc , vol.6 , pp. 2050-2060
    • Guilluy, C.1    Dubash, A.D.2    García-Mata, R.3
  • 22
    • 79952084024 scopus 로고    scopus 로고
    • The small GTPase RhoA localizes to the nucleus and is activated by Net1 and DNA damage signals
    • CrossRefPubMed
    • Dubash, A.D.; Guilluy, C.; Srougi, M.C.; Boulter, E.; Burridge, K.; García-Mata, R. The small GTPase RhoA localizes to the nucleus and is activated by Net1 and DNA damage signals. PLoS ONE 2011, 2. [CrossRef] [PubMed]
    • (2011) Plos ONE , pp. 2
    • Dubash, A.D.1    Guilluy, C.2    Srougi, M.C.3    Boulter, E.4    Burridge, K.5    García-Mata, R.6
  • 23
    • 84882660853 scopus 로고    scopus 로고
    • Nuclear translocation of small G protein RhoA via active transportation in gastric cancer cells
    • PubMed
    • Xu, J.; Li, Y.; Yang, X.; Chen, Y.; Chen, M. Nuclear translocation of small G protein RhoA via active transportation in gastric cancer cells. Oncol. Rep. 2013, 30, 1878–1882. [PubMed]
    • (2013) Oncol. Rep , vol.30 , pp. 1878-1882
    • Xu, J.1    Li, Y.2    Yang, X.3    Chen, Y.4    Chen, M.5
  • 24
    • 84859452123 scopus 로고    scopus 로고
    • LPS-induced nuclear translocation of RhoA is dependent on NF-κB in the human lung cancer cell line A549. Oncol
    • CrossRefPubMed
    • Tao, Y.; Chen, Y.C.; Lan, T.; Qian, H.; Wang, Y.; Jiang, L. LPS-induced nuclear translocation of RhoA is dependent on NF-κB in the human lung cancer cell line A549. Oncol. Lett. 2012, 3, 1283–1287. [CrossRef] [PubMed]
    • (2012) Lett , vol.3 , pp. 1283-1287
    • Tao, Y.1    Chen, Y.C.2    Lan, T.3    Qian, H.4    Wang, Y.5    Jiang, L.6
  • 25
    • 84931309371 scopus 로고    scopus 로고
    • Bilobol inhibits the lipopolysaccharide-induced expression and distribution of RhoA in HepG2 human hepatocellular carcinoma cells
    • PubMed
    • Xu, J.; Li, Y.; Yang, X.; Liu, Y.; Chen, Y.; Chen, C.M. Bilobol inhibits the lipopolysaccharide-induced expression and distribution of RhoA in HepG2 human hepatocellular carcinoma cells. Oncol. Lett. 2015, 10, 962–966. [PubMed]
    • (2015) Oncol. Lett , vol.10 , pp. 962-966
    • Xu, J.1    Li, Y.2    Yang, X.3    Liu, Y.4    Chen, Y.5    Chen, C.M.6
  • 26
    • 77649216057 scopus 로고    scopus 로고
    • Selective and specific internalization of clostridial C3 ADP-ribosyltransferases into macrophages and monocytes
    • CrossRefPubMed
    • Fahrer, J.; Kuban, J.; Heine, K.; Rupps, G.; Kaiser, E.; Felder, E.; Benz, R.; Barth, B.H. Selective and specific internalization of clostridial C3 ADP-ribosyltransferases into macrophages and monocytes. Cell Microbiol. 2010, 12, 233–247. [CrossRef] [PubMed]
    • (2010) Cell Microbiol , vol.12 , pp. 233-247
    • Fahrer, J.1    Kuban, J.2    Heine, K.3    Rupps, G.4    Kaiser, E.5    Felder, E.6    Benz, R.7    Barth, B.H.8
  • 27
    • 27744607630 scopus 로고    scopus 로고
    • Molecular identification of PAL-E, a widely used endothelial-cell marker
    • CrossRefPubMed
    • Niemelä, H.; Elima, K.; Henttinen, T.; Irjala, H.; Salmi, M.; Jalkanen, S. Molecular identification of PAL-E, a widely used endothelial-cell marker. Blood 2005, 106, 3405–3409. [CrossRef] [PubMed]
    • (2005) Blood , vol.106 , pp. 3405-3409
    • Niemelä, H.1    Elima, K.2    Henttinen, T.3    Irjala, H.4    Salmi, M.5    Jalkanen, S.6
  • 28
    • 67650558915 scopus 로고    scopus 로고
    • Recruitment of vimentin to the cell surface by β3 integrin and plectin mediates adhesion strength
    • CrossRefPubMed
    • Bhattacharya, R.; Gonzalez, A.M.; Debiase, P.J.; Trejo, H.E.; Goldman, R.D.; Flitney, F.W.; Jones, J.C. Recruitment of vimentin to the cell surface by β3 integrin and plectin mediates adhesion strength. J. Cell Sci. 2009, 122, 1390–1400. [CrossRef] [PubMed]
    • (2009) J. Cell Sci , vol.122 , pp. 1390-1400
    • Bhattacharya, R.1    Gonzalez, A.M.2    Debiase, P.J.3    Trejo, H.E.4    Goldman, R.D.5    Flitney, F.W.6    Jones, J.C.7
  • 30
    • 0031758820 scopus 로고    scopus 로고
    • Transport of residual endocytosed products into terminal lysosomes occurs slowly in rat liver endothelial cells
    • CrossRefPubMed
    • Hellevik, T.; Martinez, I.; Olsen, R.; Toh, B.H.; Webster, P.; Smedsrod, B. Transport of residual endocytosed products into terminal lysosomes occurs slowly in rat liver endothelial cells. Hepatology 1998, 28, 1378–1389. [CrossRef] [PubMed]
    • (1998) Hepatology , vol.28 , pp. 1378-1389
    • Hellevik, T.1    Martinez, I.2    Olsen, R.3    Toh, B.H.4    Webster, P.5    Smedsrod, B.6
  • 31
    • 0024501251 scopus 로고
    • Extremely rapid endocytosis mediated by the mannose receptor of sinusoidal endothelial rat liver cells
    • CrossRefPubMed
    • Magnusson, S.; Berg, T. Extremely rapid endocytosis mediated by the mannose receptor of sinusoidal endothelial rat liver cells. Biochem. J. 1989, 257, 651–656. [CrossRef] [PubMed]
    • (1989) Biochem. J , vol.257 , pp. 651-656
    • Magnusson, S.1    Berg, T.2
  • 32
    • 84861409641 scopus 로고    scopus 로고
    • Clathrin-mediated endocytosis regulates occludin, and not focal adhesion, distribution during epithelial wound healing
    • CrossRefPubMed
    • Fletcher, S.J.; Poulter, N.S.; Haining, E.J.; Rappoport, J.Z. Clathrin-mediated endocytosis regulates occludin, and not focal adhesion, distribution during epithelial wound healing. Biol. Cell 2012, 104, 238–256. [CrossRef] [PubMed]
    • (2012) Biol. Cell , vol.104 , pp. 238-256
    • Fletcher, S.J.1    Poulter, N.S.2    Haining, E.J.3    Rappoport, J.Z.4
  • 34
    • 84879446443 scopus 로고    scopus 로고
    • High level transient production of recombinant antibodies and antibody fusion proteins in HEK293 cells
    • CrossRefPubMed
    • Jäger, V.; Büssow, K.; Wagner, A.; Weber, S.; Hust, M.; Frenzel, A.; Schirrmann, T. High level transient production of recombinant antibodies and antibody fusion proteins in HEK293 cells. BMC Biotechnol. 2013, 13. [CrossRef] [PubMed]
    • (2013) BMC Biotechnol , pp. 13
    • Jäger, V.1    Büssow, K.2    Wagner, A.3    Weber, S.4    Hust, M.5    Frenzel, A.6    Schirrmann, T.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.