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Volumn 290, Issue 14, 2015, Pages 9087-9100

HypE-specific nanobodies as tools to modulate HypE-mediated target AMPylation

Author keywords

[No Author keywords available]

Indexed keywords

GENE EXPRESSION; GENE EXPRESSION REGULATION;

EID: 84926482896     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.634287     Document Type: Article
Times cited : (31)

References (46)
  • 1
    • 0015173256 scopus 로고
    • Modulation of glutamine synthetase adenylylation and deadenylylation is mediated by metabolic transformation of the PII regulatory protein
    • Brown, M. S., Segal, A., and Stadtman, E. R. (1971) Modulation of glutamine synthetase adenylylation and deadenylylation is mediated by metabolic transformation of the PII regulatory protein. Proc. Natl. Acad. Sci. U.S.A. 68, 2949-2953
    • (1971) Proc. Natl. Acad. Sci. U.S.A. , vol.68 , pp. 2949-2953
    • Brown, M.S.1    Segal, A.2    Stadtman, E.R.3
  • 2
    • 84872065897 scopus 로고    scopus 로고
    • JAKs and STATs in immunity, immunodeficiency, and cancer
    • O'Shea, J. J., Holland, S. M., and Staudt, L. M. (2013) JAKs and STATs in immunity, immunodeficiency, and cancer. N. Engl. J. Med. 368, 161-170
    • (2013) N. Engl. J. Med. , vol.368 , pp. 161-170
    • O'Shea, J.J.1    Holland, S.M.2    Staudt, L.M.3
  • 3
    • 0018823802 scopus 로고
    • Interconvertible enzyme cascades in cellular regulation
    • Chock, P. B., Rhee, S. G., and Stadtman, E. R. (1980) Interconvertible enzyme cascades in cellular regulation. Annu. Rev. Biochem. 49, 813-843
    • (1980) Annu. Rev. Biochem. , vol.49 , pp. 813-843
    • Chock, P.B.1    Rhee, S.G.2    Stadtman, E.R.3
  • 4
    • 80052751144 scopus 로고    scopus 로고
    • Comparative analysis of Histophilus somni immunoglobulin-binding protein A (IbpA) with other Fic domain-containing enzymes reveals differences in substrate and nucleotide specificities
    • Mattoo, S., Durrant, E., Chen, M. J., Xiao, J., Lazar, C. S., Manning, G., Dixon, J. E., and Worby, C. A. (2011) Comparative analysis of Histophilus somni immunoglobulin-binding protein A (IbpA) with other Fic domain-containing enzymes reveals differences in substrate and nucleotide specificities. J. Biol. Chem. 286, 32834-32842
    • (2011) J. Biol. Chem. , vol.286 , pp. 32834-32842
    • Mattoo, S.1    Durrant, E.2    Chen, M.J.3    Xiao, J.4    Lazar, C.S.5    Manning, G.6    Dixon, J.E.7    Worby, C.A.8
  • 5
    • 58149400542 scopus 로고    scopus 로고
    • AMPylation of Rho GTPases by Vibrio VopS disrupts effector binding and downstream signaling
    • Yarbrough, M. L., Li, Y., Kinch, L. N., Grishin, N. V., Ball, H. L., and Orth, K. (2009) AMPylation of Rho GTPases by Vibrio VopS disrupts effector binding and downstream signaling. Science 323, 269-272
    • (2009) Science , vol.323 , pp. 269-272
    • Yarbrough, M.L.1    Li, Y.2    Kinch, L.N.3    Grishin, N.V.4    Ball, H.L.5    Orth, K.6
  • 6
    • 79952128780 scopus 로고    scopus 로고
    • Fic domain-catalyzed adenylylation: Insight provided by the structural analysis of the type IV secretion system effector BepA
    • Palanivelu, D. V., Goepfert, A., Meury, M., Guye, P., Dehio, C., and Schirmer, T. (2011) Fic domain-catalyzed adenylylation: insight provided by the structural analysis of the type IV secretion system effector BepA. Protein Sci. 20, 492-499
    • (2011) Protein Sci. , vol.20 , pp. 492-499
    • Palanivelu, D.V.1    Goepfert, A.2    Meury, M.3    Guye, P.4    Dehio, C.5    Schirmer, T.6
  • 9
    • 77953766744 scopus 로고    scopus 로고
    • Kinetic and structural insights into the mechanism of AMPylation by VopS Fic domain
    • Luong, P., Kinch, L. N., Brautigam, C. A., Grishin, N. V., Tomchick, D. R., and Orth, K. (2010) Kinetic and structural insights into the mechanism of AMPylation by VopS Fic domain. J. Biol. Chem. 285, 20155-20163
    • (2010) J. Biol. Chem. , vol.285 , pp. 20155-20163
    • Luong, P.1    Kinch, L.N.2    Brautigam, C.A.3    Grishin, N.V.4    Tomchick, D.R.5    Orth, K.6
  • 10
    • 84856417389 scopus 로고    scopus 로고
    • Adenylylation control by intra- or intermolecular active-site obstruction in Fic proteins
    • Engel, P., Goepfert, A., Stanger, F. V., Harms, A., Schmidt, A., Schirmer, T., and Dehio, C. (2012) Adenylylation control by intra- or intermolecular active-site obstruction in Fic proteins. Nature 482, 107-110
    • (2012) Nature , vol.482 , pp. 107-110
    • Engel, P.1    Goepfert, A.2    Stanger, F.V.3    Harms, A.4    Schmidt, A.5    Schirmer, T.6    Dehio, C.7
  • 11
    • 80052399642 scopus 로고    scopus 로고
    • Modulation of Rab GTPase function by a protein phosphocholine transferase
    • Mukherjee, S., Liu, X., Arasaki, K., McDonough, J., Galán, J. E., and Roy, C. R. (2011) Modulation of Rab GTPase function by a protein phosphocholine transferase. Nature 477, 103-106
    • (2011) Nature , vol.477 , pp. 103-106
    • Mukherjee, S.1    Liu, X.2    Arasaki, K.3    McDonough, J.4    Galán, J.E.5    Roy, C.R.6
  • 12
    • 84878644184 scopus 로고    scopus 로고
    • Structure of the Legionella effector AnkX reveals the mechanism of phosphocholine transfer by the FIC domain
    • Campanacci, V., Mukherjee, S., Roy, C. R., and Cherfils, J. (2013) Structure of the Legionella effector AnkX reveals the mechanism of phosphocholine transfer by the FIC domain. EMBO J. 32, 1469-1477
    • (2013) EMBO J. , vol.32 , pp. 1469-1477
    • Campanacci, V.1    Mukherjee, S.2    Roy, C.R.3    Cherfils, J.4
  • 13
    • 84860541901 scopus 로고    scopus 로고
    • A Xanthomonas uridine 5′-monophosphate transferase inhibits plant immune kinases
    • Feng, F., Yang, F., Rong, W., Wu, X., Zhang, J., Chen, S., He, C., and Zhou, J. M. (2012) A Xanthomonas uridine 5′-monophosphate transferase inhibits plant immune kinases. Nature 485, 114-118
    • (2012) Nature , vol.485 , pp. 114-118
    • Feng, F.1    Yang, F.2    Rong, W.3    Wu, X.4    Zhang, J.5    Chen, S.6    He, C.7    Zhou, J.M.8
  • 17
    • 79954423286 scopus 로고    scopus 로고
    • Adenylylation: Renaissance of a forgotten post-translational modification
    • Itzen, A., Blankenfeldt, W., and Goody, R. S. (2011) Adenylylation: renaissance of a forgotten post-translational modification. Trends Biochem. Sci. 36, 221-228
    • (2011) Trends Biochem. Sci. , vol.36 , pp. 221-228
    • Itzen, A.1    Blankenfeldt, W.2    Goody, R.S.3
  • 18
    • 84861578674 scopus 로고    scopus 로고
    • Visual neurotransmission in Drosophila requires expression of Fic in glial capitate projections
    • Rahman, M., Ham, H., Liu, X., Sugiura, Y., Orth, K., and Krämer, H. (2012) Visual neurotransmission in Drosophila requires expression of Fic in glial capitate projections. Nat. Neurosci. 15, 871-875
    • (2012) Nat. Neurosci. , vol.15 , pp. 871-875
    • Rahman, M.1    Ham, H.2    Liu, X.3    Sugiura, Y.4    Orth, K.5    Krämer, H.6
  • 19
    • 84984801564 scopus 로고    scopus 로고
    • Unfolded protein response-regulated Drosophila Fic (dFic) reversibly AMPylates BiP during endoplasmic reticulum homeostasis
    • Ham, H., Woolery, A. R., Tracy, C., Stenesen, D., Krämer, H., and Orth, K. (2014) Unfolded protein response-regulated Drosophila Fic (dFic) reversibly AMPylates BiP during endoplasmic reticulum homeostasis. J. Biol. Chem. 289, 36059-36069
    • (2014) J. Biol. Chem. , vol.289 , pp. 36059-36069
    • Ham, H.1    Woolery, A.R.2    Tracy, C.3    Stenesen, D.4    Krämer, H.5    Orth, K.6
  • 23
    • 77951602822 scopus 로고    scopus 로고
    • Therapeutic antibodies: Past, present and future
    • Leavy, O. (2010) Therapeutic antibodies: past, present and future. Nat. Rev. Immunol. 10, 297
    • (2010) Nat. Rev. Immunol. , vol.10 , pp. 297
    • Leavy, O.1
  • 27
    • 84855425542 scopus 로고    scopus 로고
    • Fluorescent fusion protein knockout mediated by anti-GFP nanobody
    • Caussinus, E., Kanca, O., and Affolter, M. (2012) Fluorescent fusion protein knockout mediated by anti-GFP nanobody. Nat. Struct. Mol. Biol. 19, 117-121
    • (2012) Nat. Struct. Mol. Biol. , vol.19 , pp. 117-121
    • Caussinus, E.1    Kanca, O.2    Affolter, M.3
  • 29
    • 84907481722 scopus 로고    scopus 로고
    • Site-specific chemoenzymatic labeling of aerolysin enables the identification of new aerolysin receptors
    • Wuethrich, I., Peeters, J. G., Blom, A. E., Theile, C. S., Li, Z., Spooner, E., Ploegh, H. L., and Guimaraes, C. P. (2014) Site-specific chemoenzymatic labeling of aerolysin enables the identification of new aerolysin receptors. PLoS ONE 9, e109883
    • (2014) PLoS ONE , vol.9 , pp. e109883
    • Wuethrich, I.1    Peeters, J.G.2    Blom, A.E.3    Theile, C.S.4    Li, Z.5    Spooner, E.6    Ploegh, H.L.7    Guimaraes, C.P.8
  • 30
  • 31
    • 84872871265 scopus 로고    scopus 로고
    • Sortase-mediated modification of αDEC205 affords optimization of antigen presentation and immunization against a set of viral epitopes
    • Swee, L. K., Guimaraes, C. P., Sehrawat, S., Spooner, E., Barrasa, M. I., and Ploegh, H. L. (2013) Sortase-mediated modification of αDEC205 affords optimization of antigen presentation and immunization against a set of viral epitopes. Proc. Natl. Acad. Sci. U.S.A. 110, 1428-1433
    • (2013) Proc. Natl. Acad. Sci. U.S.A. , vol.110 , pp. 1428-1433
    • Swee, L.K.1    Guimaraes, C.P.2    Sehrawat, S.3    Spooner, E.4    Barrasa, M.I.5    Ploegh, H.L.6
  • 37
    • 0036420965 scopus 로고    scopus 로고
    • Molecular recognition in anti-body-antigen complexes
    • Sundberg, E. J., and Mariuzza, R. A. (2002) Molecular recognition in anti-body-antigen complexes. Adv. Protein Chem. 61, 119-160
    • (2002) Adv. Protein Chem. , vol.61 , pp. 119-160
    • Sundberg, E.J.1    Mariuzza, R.A.2
  • 38
    • 84861683835 scopus 로고    scopus 로고
    • Increased zymogen activity of thrombin-activatable fibrinolysis inhibitor prolongs clot lysis
    • Mishra, N., Buelens, K., Theyskens, S., Compernolle, G., Gils, A., and Declerck, P. J. (2012) Increased zymogen activity of thrombin-activatable fibrinolysis inhibitor prolongs clot lysis. J. Thromb. Haemost. 10, 1091-1099
    • (2012) J. Thromb. Haemost. , vol.10 , pp. 1091-1099
    • Mishra, N.1    Buelens, K.2    Theyskens, S.3    Compernolle, G.4    Gils, A.5    Declerck, P.J.6
  • 39
    • 84914127487 scopus 로고    scopus 로고
    • Crystal structure of the human, FIC-domain containing protein HYPE and implications for its functions
    • Bunney, T. D., Cole, A. R., Broncel, M., Esposito, D., Tate, E. W., and Katan, M. (2014) Crystal structure of the human, FIC-domain containing protein HYPE and implications for its functions. Structure 1016./j.str.2014.10.007
    • (2014) Structure
    • Bunney, T.D.1    Cole, A.R.2    Broncel, M.3    Esposito, D.4    Tate, E.W.5    Katan, M.6
  • 40
    • 84924135708 scopus 로고    scopus 로고
    • A novel link between Fic (filamentation induced by cAMP)-mediated adenylylation/AMPylation and the unfolded protein response
    • Sanyal, A., Chen, A. J., Nakayasu, E. S., Lazar, C. S., Zbornik, E. A., Worby, C. A., Koller, A., and Mattoo, S. (2015) A novel link between Fic (filamentation induced by cAMP)-mediated adenylylation/AMPylation and the unfolded protein response. J. Biol. Chem. 10.1074/jbc.M114.618348
    • (2015) J. Biol. Chem.
    • Sanyal, A.1    Chen, A.J.2    Nakayasu, E.S.3    Lazar, C.S.4    Zbornik, E.A.5    Worby, C.A.6    Koller, A.7    Mattoo, S.8
  • 41
    • 81855220924 scopus 로고    scopus 로고
    • Synthesis, transport and incorporation into the nuclear envelope of A-type lamins and inner nuclear membrane proteins
    • González, J. M., and Andrés, V. (2011) Synthesis, transport and incorporation into the nuclear envelope of A-type lamins and inner nuclear membrane proteins. Biochem. Soc. Trans. 39, 1758-1763
    • (2011) Biochem. Soc. Trans. , vol.39 , pp. 1758-1763
    • González, J.M.1    Andrés, V.2
  • 43
    • 0018800811 scopus 로고
    • ADP-ribosylation of rat liver nucleosomal core histones
    • Burzio, L. O., Riquelme, P. T., and Koide, S. S. (1979) ADP-ribosylation of rat liver nucleosomal core histones. J. Biol. Chem. 254, 3029-3037
    • (1979) J. Biol. Chem. , vol.254 , pp. 3029-3037
    • Burzio, L.O.1    Riquelme, P.T.2    Koide, S.S.3
  • 44
    • 0024670391 scopus 로고
    • DNA strand breaks alter histone ADP-ribosylation
    • Boulikas, T. (1989) DNA strand breaks alter histone ADP-ribosylation. Proc. Natl. Acad. Sci. U.S.A. 86, 3499-3503
    • (1989) Proc. Natl. Acad. Sci. U.S.A. , vol.86 , pp. 3499-3503
    • Boulikas, T.1
  • 45
    • 38649118240 scopus 로고    scopus 로고
    • Chk1 is a histone H3 threonine 11 kinase that regulates DNA damage-induced transcriptional repression
    • Shimada, M., Niida, H., Zineldeen, D. H., Tagami, H., Tanaka, M., Saito, H., and Nakanishi, M. (2008) Chk1 is a histone H3 threonine 11 kinase that regulates DNA damage-induced transcriptional repression. Cell 132, 221-232
    • (2008) Cell , vol.132 , pp. 221-232
    • Shimada, M.1    Niida, H.2    Zineldeen, D.H.3    Tagami, H.4    Tanaka, M.5    Saito, H.6    Nakanishi, M.7
  • 46
    • 84865337735 scopus 로고    scopus 로고
    • Examining histone posttranslational modification patterns by high-resolution mass spectrometry
    • Lin, S., and Garcia, B. A. (2012) Examining histone posttranslational modification patterns by high-resolution mass spectrometry. Methods Enzymol. 512, 3-28
    • (2012) Methods Enzymol. , vol.512 , pp. 3-28
    • Lin, S.1    Garcia, B.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.