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Volumn 289, Issue 8, 2014, Pages 4600-4625

Differential loss of prolyl isomerase or chaperone activity of ran-binding protein 2 (Ranbp2) unveils distinct physiological roles of its cyclophilin domain in proteostasis

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE ACTIVITY; MECHANISTIC LINK; NONOVERLAPPING; PHYSIOLOGICAL ACTIVITY; PHYSIOLOGICAL ROLES; PHYSIOLOGICAL SUBSTRATE; PROLYL ISOMERASE; UBIQUITIN-PROTEASOME SYSTEM;

EID: 84896700727     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.538215     Document Type: Article
Times cited : (16)

References (136)
  • 1
    • 0016711868 scopus 로고
    • Consideration of the possibility that the slow step in protein denaturation reactions is due to cis-trans isomerism of proline residues
    • Brandts, J. F., Halvorson, H. R., and Brennan, M. (1975) Consideration of the possibility that the slow step in protein denaturation reactions is due to cis-trans isomerism of proline residues. Biochemistry 14, 4953-4963
    • (1975) Biochemistry , vol.14 , pp. 4953-4963
    • Brandts, J.F.1    Halvorson, H.R.2    Brennan, M.3
  • 2
    • 0018556595 scopus 로고
    • Role of proline isomerization in folding of ribonuclease A at low temperatures
    • Cook, K. H., Schmid, F. X., and Baldwin, R. L. (1979) Role of proline isomerization in folding of ribonuclease A at low temperatures. Proc. Natl. Acad. Sci. U.S.A. 76, 6157-6161
    • (1979) Proc. Natl. Acad. Sci. U.S.A. , vol.76 , pp. 6157-6161
    • Cook, K.H.1    Schmid, F.X.2    Baldwin, R.L.3
  • 4
    • 0021668676 scopus 로고
    • Determination of enzymatic catalysis for the cis-trans-isomerization of peptide binding in prolinecontaining peptides
    • Fischer, G., Bang, H., and Mech, C. (1984) Determination of enzymatic catalysis for the cis-trans-isomerization of peptide binding in prolinecontaining peptides. Biomed. Biochim. Acta 43, 1101-1111
    • (1984) Biomed. Biochim. Acta , vol.43 , pp. 1101-1111
    • Fischer, G.1    Bang, H.2    Mech, C.3
  • 5
    • 0024959449 scopus 로고
    • Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins
    • Fischer, G., Wittmann-Liebold, B., Lang, K., Kiefhaber, T., and Schmid, F. X. (1989) Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins. Nature 337, 476-478
    • (1989) Nature , vol.337 , pp. 476-478
    • Fischer, G.1    Wittmann-Liebold, B.2    Lang, K.3    Kiefhaber, T.4    Schmid, F.X.5
  • 6
    • 0024959451 scopus 로고
    • Peptidyl-prolyl cistrans isomerase is the cyclosporin A-binding protein cyclophilin
    • Takahashi, N., Hayano, T., and Suzuki, M. (1989) Peptidyl-prolyl cistrans isomerase is the cyclosporin A-binding protein cyclophilin. Nature 337, 473-475
    • (1989) Nature , vol.337 , pp. 473-475
    • Takahashi, N.1    Hayano, T.2    Suzuki, M.3
  • 7
    • 84874506843 scopus 로고    scopus 로고
    • Peptide bond cis/trans isomerases: A biocatalysis perspective of conformational dynamics in proteins
    • Schiene-Fischer, C., Aumüller, T., and Fischer, G. (2013) Peptide bond cis/trans isomerases: A biocatalysis perspective of conformational dynamics in proteins. Top. Curr. Chem. 328, 35-67
    • (2013) Top. Curr. Chem. , vol.328 , pp. 35-67
    • Schiene-Fischer, C.1    Aumüller, T.2    Fischer, G.3
  • 8
    • 0025831980 scopus 로고
    • Two cytoplasmic candidates for immunophilin action are revealed by affinity for a new cyclophilin: One in the presence and one in the absence of CsA
    • Friedman, J., and Weissman, I. (1991) Two cytoplasmic candidates for immunophilin action are revealed by affinity for a new cyclophilin: one in the presence and one in the absence of CsA. Cell 66, 799-806
    • (1991) Cell , vol.66 , pp. 799-806
    • Friedman, J.1    Weissman, I.2
  • 9
    • 0025893168 scopus 로고
    • Calcineurin is a common target of cyclophilincyclosporin A and FKBP-FK506 complexes
    • Liu, J., Farmer, J. D., Jr., Lane, W. S., Friedman, J., Weissman, I., and Schreiber, S. L. (1991) Calcineurin is a common target of cyclophilincyclosporin A and FKBP-FK506 complexes. Cell 66, 807-815
    • (1991) Cell , vol.66 , pp. 807-815
    • Liu, J.1    Farmer Jr., J.D.2    Lane, W.S.3    Friedman, J.4    Weissman, I.5    Schreiber, S.L.6
  • 10
    • 0026643141 scopus 로고
    • Identification of calcineurin as a key signalling enzyme in T-lymphocyte activation
    • Clipstone, N. A., and Crabtree, G. R. (1992) Identification of calcineurin as a key signalling enzyme in T-lymphocyte activation. Nature 357, 695-697
    • (1992) Nature , vol.357 , pp. 695-697
    • Clipstone, N.A.1    Crabtree, G.R.2
  • 11
    • 0025871394 scopus 로고
    • Nuclear association of a T-cell transcription factor blocked by FK-506 and cyclosporin A
    • Flanagan, W. M., Corthésy, B., Bram, R. J., and Crabtree, G. R. (1991) Nuclear association of a T-cell transcription factor blocked by FK-506 and cyclosporin A. Nature 352, 803-807
    • (1991) Nature , vol.352 , pp. 803-807
    • Flanagan, W.M.1    Corthésy, B.2    Bram, R.J.3    Crabtree, G.R.4
  • 12
    • 18644384463 scopus 로고    scopus 로고
    • Cyclophilin A-deficient mice are resistant to immunosuppression by cyclosporine
    • Colgan, J., Asmal, M., Yu, B., and Luban, J. (2005) Cyclophilin A-deficient mice are resistant to immunosuppression by cyclosporine. J. Immunol. 174, 6030-6038
    • (2005) J. Immunol. , vol.174 , pp. 6030-6038
    • Colgan, J.1    Asmal, M.2    Yu, B.3    Luban, J.4
  • 13
    • 0037133154 scopus 로고    scopus 로고
    • Regulation of the tyrosine kinase Itk by the peptidyl-prolyl isomerase cyclophilin A
    • Brazin, K. N., Mallis, R. J., Fulton, D. B., and Andreotti, A. H. (2002) Regulation of the tyrosine kinase Itk by the peptidyl-prolyl isomerase cyclophilin A. Proc. Natl. Acad. Sci. U.S.A. 99, 1899-1904
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 1899-1904
    • Brazin, K.N.1    Mallis, R.J.2    Fulton, D.B.3    Andreotti, A.H.4
  • 14
    • 4143074548 scopus 로고    scopus 로고
    • Cyclophilin A regulates TCR signal strength in CD4 T cells via a proline-directed conformational switch in Itk
    • Colgan, J., Asmal, M., Neagu, M., Yu, B., Schneidkraut, J., Lee, Y., Sokolskaja, E., Andreotti, A., and Luban, J. (2004) Cyclophilin A regulates TCR signal strength in CD4 T cells via a proline-directed conformational switch in Itk. Immunity 21, 189-201
    • (2004) Immunity , vol.21 , pp. 189-201
    • Colgan, J.1    Asmal, M.2    Neagu, M.3    Yu, B.4    Schneidkraut, J.5    Lee, Y.6    Sokolskaja, E.7    Andreotti, A.8    Luban, J.9
  • 15
    • 1242292029 scopus 로고    scopus 로고
    • Regulation of peptide bond cis/trans isomerization by enzyme catalysis and its implication in physiological processes
    • Fischer, G., and Aumüller, T. (2003) Regulation of peptide bond cis/trans isomerization by enzyme catalysis and its implication in physiological processes. Rev. Physiol. Biochem. Pharmacol. 148, 105-150
    • (2003) Rev. Physiol. Biochem. Pharmacol. , vol.148 , pp. 105-150
    • Fischer, G.1    Aumüller, T.2
  • 16
    • 0042026692 scopus 로고    scopus 로고
    • Native state proline isomerization: An intrinsic molecular switch
    • Andreotti, A. H. (2003) Native state proline isomerization: an intrinsic molecular switch. Biochemistry 42, 9515-9524
    • (2003) Biochemistry , vol.42 , pp. 9515-9524
    • Andreotti, A.H.1
  • 17
    • 0029859847 scopus 로고    scopus 로고
    • Cyclophilin-related protein RanBP2 acts as chaperone for red/green opsin
    • Ferreira, P. A., Nakayama, T. A., Pak, W. L., and Travis, G. H. (1996) Cyclophilin-related protein RanBP2 acts as chaperone for red/green opsin. Nature 383, 637-640
    • (1996) Nature , vol.383 , pp. 637-640
    • Ferreira, P.A.1    Nakayama, T.A.2    Pak, W.L.3    Travis, G.H.4
  • 18
    • 0031026269 scopus 로고    scopus 로고
    • Interconversion of red opsin isoforms by the cyclophilin-related chaperone protein Ranbinding protein 2
    • Ferreira, P. A., Nakayama, T. A., and Travis, G. H. (1997) Interconversion of red opsin isoforms by the cyclophilin-related chaperone protein Ranbinding protein 2. Proc. Natl. Acad. Sci. U.S.A. 94, 1556-1561
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 1556-1561
    • Ferreira, P.A.1    Nakayama, T.A.2    Travis, G.H.3
  • 19
    • 0031615108 scopus 로고    scopus 로고
    • Point mutations in v-Myb disrupt a cyclophilin-catalyzed negative regulatory mechanism
    • Leverson, J. D., and Ness, S. A. (1998) Point mutations in v-Myb disrupt a cyclophilin-catalyzed negative regulatory mechanism. Mol. Cell 1, 203-211
    • (1998) Mol. Cell , vol.1 , pp. 203-211
    • Leverson, J.D.1    Ness, S.A.2
  • 20
    • 0030925593 scopus 로고    scopus 로고
    • Peptidylprolyl cis-trans isomerase activity of cyclophilin A in functional homo-oligomeric receptor expression
    • Helekar, S. A., and Patrick, J. (1997) Peptidylprolyl cis-trans isomerase activity of cyclophilin A in functional homo-oligomeric receptor expression. Proc. Natl. Acad. Sci. U.S.A. 94, 5432-5437
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 5432-5437
    • Helekar, S.A.1    Patrick, J.2
  • 24
    • 0026499641 scopus 로고
    • Isomerase and chaperone activity of prolyl isomerase in the folding of carbonic anhydrase
    • Freskgard, P. O., Bergenhem, N., Jonsson, B. H., Svensson, M., and Carlsson, U. (1992) Isomerase and chaperone activity of prolyl isomerase in the folding of carbonic anhydrase. Science 258, 466-468
    • (1992) Science , vol.258 , pp. 466-468
    • Freskgard, P.O.1    Bergenhem, N.2    Jonsson, B.H.3    Svensson, M.4    Carlsson, U.5
  • 25
    • 76749168158 scopus 로고    scopus 로고
    • Chaperone activity of Cyp18 through hydrophobic condensation that enables rescue of transient misfolded molten globule intermediates
    • Moparthi, S. B., Fristedt, R., Mishra, R., Almstedt, K., Karlsson, M., Hammarström, P., and Carlsson, U. (2010) Chaperone activity of Cyp18 through hydrophobic condensation that enables rescue of transient misfolded molten globule intermediates. Biochemistry 49, 1137-1145
    • (2010) Biochemistry , vol.49 , pp. 1137-1145
    • Moparthi, S.B.1    Fristedt, R.2    Mishra, R.3    Almstedt, K.4    Karlsson, M.5    Hammarström, P.6    Carlsson, U.7
  • 26
    • 0028143610 scopus 로고
    • The cyclophilin homolog NinaA functions as a chaperone, forming a stable complex in vivo with its protein target rhodopsin
    • Baker, E. K., Colley, N. J., and Zuker, C. S. (1994) The cyclophilin homolog NinaA functions as a chaperone, forming a stable complex in vivo with its protein target rhodopsin. EMBO J. 13, 4886-4895
    • (1994) EMBO J. , vol.13 , pp. 4886-4895
    • Baker, E.K.1    Colley, N.J.2    Zuker, C.S.3
  • 27
    • 0025995535 scopus 로고
    • The cyclophilin homolog ninaA is required in the secretory pathway
    • Colley, N. J., Baker, E. K., Stamnes, M. A., and Zuker, C. S. (1991) The cyclophilin homolog ninaA is required in the secretory pathway. Cell 67, 255-263
    • (1991) Cell , vol.67 , pp. 255-263
    • Colley, N.J.1    Baker, E.K.2    Stamnes, M.A.3    Zuker, C.S.4
  • 28
    • 0025907054 scopus 로고
    • The cyclophilin homolog ninaA is a tissue-specific integral membrane protein required for the proper synthesis of a subset of Drosophila rhodopsins
    • Stamnes, M. A., Shieh, B. H., Chuman, L., Harris, G. L., and Zuker, C. S. (1991) The cyclophilin homolog ninaA is a tissue-specific integral membrane protein required for the proper synthesis of a subset of Drosophila rhodopsins. Cell 65, 219-227
    • (1991) Cell , vol.65 , pp. 219-227
    • Stamnes, M.A.1    Shieh, B.H.2    Chuman, L.3    Harris, G.L.4    Zuker, C.S.5
  • 29
    • 0037040541 scopus 로고    scopus 로고
    • Molecular chaperones in the cytosol: From nascent chain to folded protein
    • Hartl, F. U., and Hayer-Hartl, M. (2002) Molecular chaperones in the cytosol: from nascent chain to folded protein. Science 295, 1852-1858
    • (2002) Science , vol.295 , pp. 1852-1858
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 30
    • 0024959573 scopus 로고
    • The ninaA gene required for visual transduction in Drosophila encodes a homologue of cyclosporin A-binding protein
    • Shieh, B. H., Stamnes, M. A., Seavello, S., Harris, G. L., and Zuker, C. S. (1989) The ninaA gene required for visual transduction in Drosophila encodes a homologue of cyclosporin A-binding protein. Nature 338, 67-70
    • (1989) Nature , vol.338 , pp. 67-70
    • Shieh, B.H.1    Stamnes, M.A.2    Seavello, S.3    Harris, G.L.4    Zuker, C.S.5
  • 33
    • 0032755251 scopus 로고    scopus 로고
    • Manipulating the amyloid aggregation pathway with chemical chaperones
    • Yang, D. S., Yip, C. M., Huang, T. H., Chakrabartty, A., and Fraser, P. E. (1999) Manipulating the amyloid aggregation pathway with chemical chaperones. J. Biol. Chem. 274, 32970-32974
    • (1999) J. Biol. Chem. , vol.274 , pp. 32970-32974
    • Yang, D.S.1    Yip, C.M.2    Huang, T.H.3    Chakrabartty, A.4    Fraser, P.E.5
  • 34
    • 0038529723 scopus 로고    scopus 로고
    • Pharmacological chaperone-mediated in vivo folding and stabilization of the P23H-opsin mutant associated with autosomal dominant retinitis pigmentosa
    • Noorwez, S. M., Kuksa, V., Imanishi, Y., Zhu, L., Filipek, S., Palczewski, K., and Kaushal, S. (2003) Pharmacological chaperone-mediated in vivo folding and stabilization of the P23H-opsin mutant associated with autosomal dominant retinitis pigmentosa. J. Biol. Chem. 278, 14442-14450
    • (2003) J. Biol. Chem. , vol.278 , pp. 14442-14450
    • Noorwez, S.M.1    Kuksa, V.2    Imanishi, Y.3    Zhu, L.4    Filipek, S.5    Palczewski, K.6    Kaushal, S.7
  • 35
    • 77958543957 scopus 로고    scopus 로고
    • Cyclosporine A-sensitive, cyclophilin B-dependent endoplasmic reticulum-associated degradation
    • Bernasconi, R., Soldà, T., Galli, C., Pertel, T., Luban, J., and Molinari, M. (2010) Cyclosporine A-sensitive, cyclophilin B-dependent endoplasmic reticulum-associated degradation. PLoS One 5, e13008
    • (2010) PLoS One , vol.5
    • Bernasconi, R.1    Soldà, T.2    Galli, C.3    Pertel, T.4    Luban, J.5    Molinari, M.6
  • 37
    • 84863863992 scopus 로고    scopus 로고
    • From Drosophila to humans: Reflections on the roles of the prolyl isomerases and chaperones, cyclophilins, in cell function and disease
    • Ferreira, P. A., and Orry, A. (2012) From Drosophila to humans: reflections on the roles of the prolyl isomerases and chaperones, cyclophilins, in cell function and disease. J. Neurogenet. 26, 132-143
    • (2012) J. Neurogenet. , vol.26 , pp. 132-143
    • Ferreira, P.A.1    Orry, A.2
  • 38
    • 84862691109 scopus 로고    scopus 로고
    • Mutation in cyclophilin B that causes hyperelastosis cutis in American Quarter Horse does not affect peptidylprolyl cis-trans isomerase activity but shows altered cyclophilin B-protein interactions and affects collagen folding
    • Ishikawa, Y., Vranka, J. A., Boudko, S. P., Pokidysheva, E., Mizuno, K., Zientek, K., Keene, D. R., Rashmir-Raven, A. M., Nagata, K., Winand, N. J., and Bächinger, H. P. (2012) Mutation in cyclophilin B that causes hyperelastosis cutis in American Quarter Horse does not affect peptidylprolyl cis-trans isomerase activity but shows altered cyclophilin B-protein interactions and affects collagen folding. J. Biol. Chem. 287, 22253-22265
    • (2012) J. Biol. Chem. , vol.287 , pp. 22253-22265
    • Ishikawa, Y.1    Vranka, J.A.2    Boudko, S.P.3    Pokidysheva, E.4    Mizuno, K.5    Zientek, K.6    Keene, D.R.7    Rashmir-Raven, A.M.8    Nagata, K.9    Winand, N.J.10    Bächinger, H.P.11
  • 41
    • 78649731916 scopus 로고    scopus 로고
    • Cyclophilin B interacts with sodiumpotassium ATPase and is required for pump activity in proximal tubule cells of the kidney
    • Suñé, G., Sarró, E., Puigmulé, M., López-Hellín, J., Zufferey, M., Pertel, T., Luban, J., and Meseguer, A. (2010) Cyclophilin B interacts with sodiumpotassium ATPase and is required for pump activity in proximal tubule cells of the kidney. PLoS One 5, e13930
    • (2010) PLoS One , vol.5
    • Suñé, G.1    Sarró, E.2    Puigmulé, M.3    López-Hellín, J.4    Zufferey, M.5    Pertel, T.6    Luban, J.7    Meseguer, A.8
  • 42
    • 0030692139 scopus 로고    scopus 로고
    • All cyclophilins and FK506 binding proteins are, individually and collectively, dispensable for viability in Saccharomyces cerevisiae
    • Dolinski, K., Muir, S., Cardenas, M., and Heitman, J. (1997) All cyclophilins and FK506 binding proteins are, individually and collectively, dispensable for viability in Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. U.S.A. 94, 13093-13098
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 13093-13098
    • Dolinski, K.1    Muir, S.2    Cardenas, M.3    Heitman, J.4
  • 44
    • 0029949799 scopus 로고    scopus 로고
    • Cyclophilin A is required for an early step in the life cycle of human immunodeficiency virus type 1 before the initiation of reverse transcription
    • Braaten, D., Franke, E. K., and Luban, J. (1996) Cyclophilin A is required for an early step in the life cycle of human immunodeficiency virus type 1 before the initiation of reverse transcription. J. Virol. 70, 3551-3560
    • (1996) J. Virol. , vol.70 , pp. 3551-3560
    • Braaten, D.1    Franke, E.K.2    Luban, J.3
  • 45
    • 0027207885 scopus 로고
    • Human immunodeficiency virus type 1 Gag protein binds to cyclophilins A and B
    • Luban, J., Bossolt, K. L., Franke, E. K., Kalpana, G. V., and Goff, S. P. (1993) Human immunodeficiency virus type 1 Gag protein binds to cyclophilins A and B. Cell 73, 1067-1078
    • (1993) Cell , vol.73 , pp. 1067-1078
    • Luban, J.1    Bossolt, K.L.2    Franke, E.K.3    Kalpana, G.V.4    Goff, S.P.5
  • 48
    • 78650776859 scopus 로고    scopus 로고
    • Perturbation of host nuclear membrane component RanBP2 impairs the nuclear import of human immunodeficiency virus 1 preintegration complex (DNA)
    • Zhang, R., Mehla, R., and Chauhan, A. (2010) Perturbation of host nuclear membrane component RanBP2 impairs the nuclear import of human immunodeficiency virus 1 preintegration complex (DNA). PLoS One 5, e15620
    • (2010) PLoS One , vol.5
    • Zhang, R.1    Mehla, R.2    Chauhan, A.3
  • 52
    • 84867772865 scopus 로고    scopus 로고
    • Cyclophilin involvement in the replication of hepatitis C virus and other viruses
    • Baugh, J., and Gallay, P. (2012) Cyclophilin involvement in the replication of hepatitis C virus and other viruses. Biol. Chem. 393, 579-587
    • (2012) Biol. Chem. , vol.393 , pp. 579-587
    • Baugh, J.1    Gallay, P.2
  • 53
    • 77951051950 scopus 로고    scopus 로고
    • Cyclophilin A-independent recruitment of NS5A and NS5B into hepatitis C virus replication complexes
    • Chatterji, U., Bobardt, M. D., Lim, P., and Gallay, P. A. (2010) Cyclophilin A-independent recruitment of NS5A and NS5B into hepatitis C virus replication complexes. J. Gen. Virol. 91, 1189-1193
    • (2010) J. Gen. Virol. , vol.91 , pp. 1189-1193
    • Chatterji, U.1    Bobardt, M.D.2    Lim, P.3    Gallay, P.A.4
  • 55
    • 77957357258 scopus 로고    scopus 로고
    • Molecular aspects of cyclophilins mediating therapeutic actions of their ligands
    • Galat, A., and Bua, J. (2010) Molecular aspects of cyclophilins mediating therapeutic actions of their ligands. Cell. Mol. Life Sci. 67, 3467-3488
    • (2010) Cell. Mol. Life Sci. , vol.67 , pp. 3467-3488
    • Galat, A.1    Bua, J.2
  • 58
    • 0029112610 scopus 로고
    • Retina-specifically expressed novel subtypes of bovine cyclophilin
    • Ferreira, P. A., Hom, J. T., and Pak, W. L. (1995) Retina-specifically expressed novel subtypes of bovine cyclophilin. J. Biol. Chem. 270, 23179-23188
    • (1995) J. Biol. Chem. , vol.270 , pp. 23179-23188
    • Ferreira, P.A.1    Hom, J.T.2    Pak, W.L.3
  • 59
    • 0029070074 scopus 로고
    • Nup358, a cytoplasmically exposed nucleoporin with peptide repeats, Ran-GTP binding sites, zinc fingers, a cyclophilin A homologous domain, and a leucine-rich region
    • Wu, J., Matunis, M. J., Kraemer, D., Blobel, G., and Coutavas, E. (1995) Nup358, a cytoplasmically exposed nucleoporin with peptide repeats, Ran-GTP binding sites, zinc fingers, a cyclophilin A homologous domain, and a leucine-rich region. J. Biol. Chem. 270, 14209-14213
    • (1995) J. Biol. Chem. , vol.270 , pp. 14209-14213
    • Wu, J.1    Matunis, M.J.2    Kraemer, D.3    Blobel, G.4    Coutavas, E.5
  • 62
    • 0030696935 scopus 로고    scopus 로고
    • RanGTP targets p97 to RanBP2, a filamentous protein localized at the cytoplasmic periphery of the nuclear pore complex
    • Delphin, C., Guan, T., Melchior, F., and Gerace, L. (1997) RanGTP targets p97 to RanBP2, a filamentous protein localized at the cytoplasmic periphery of the nuclear pore complex. Mol. Biol. Cell 8, 2379-2390
    • (1997) Mol. Biol. Cell , vol.8 , pp. 2379-2390
    • Delphin, C.1    Guan, T.2    Melchior, F.3    Gerace, L.4
  • 63
    • 0033601233 scopus 로고    scopus 로고
    • The zinc finger cluster domain of RanBP2 is a specific docking site for the nuclear export factor, exportin-1
    • Singh, B. B., Patel, H. H., Roepman, R., Schick, D., and Ferreira, P. A. (1999) The zinc finger cluster domain of RanBP2 is a specific docking site for the nuclear export factor, exportin-1. J. Biol. Chem. 274, 37370-37378
    • (1999) J. Biol. Chem. , vol.274 , pp. 37370-37378
    • Singh, B.B.1    Patel, H.H.2    Roepman, R.3    Schick, D.4    Ferreira, P.A.5
  • 64
    • 66849125858 scopus 로고    scopus 로고
    • The nuclear pore component Nup358 promotes transportin-dependent nuclear import
    • Hutten, S., Wälde, S., Spillner, C., Hauber, J., and Kehlenbach, R. H. (2009) The nuclear pore component Nup358 promotes transportin-dependent nuclear import. J. Cell Sci. 122, 1100-1110
    • (2009) J. Cell Sci. , vol.122 , pp. 1100-1110
    • Hutten, S.1    Wälde, S.2    Spillner, C.3    Hauber, J.4    Kehlenbach, R.H.5
  • 65
    • 79952161712 scopus 로고    scopus 로고
    • Insights into the function of the CRM1 cofactor RanBP3 from the structure of its Ran-binding domain
    • Langer, K., Dian, C., Rybin, V., Müller, C. W., and Petosa, C. (2011) Insights into the function of the CRM1 cofactor RanBP3 from the structure of its Ran-binding domain. PLoS One 6, e17011
    • (2011) PLoS One , vol.6
    • Langer, K.1    Dian, C.2    Rybin, V.3    Müller, C.W.4    Petosa, C.5
  • 69
    • 84879679091 scopus 로고    scopus 로고
    • Distinct and atypical intrinsic and extrinsic cell death pathways between photoreceptor cell types upon specific ablation of Ranbp2 in cone photoreceptors
    • Cho, K. I., Haque, M., Wang, J., Yu, M., Hao, Y., Qiu, S., Pillai, I. C., Peachey, N. S., and Ferreira, P. A. (2013) Distinct and atypical intrinsic and extrinsic cell death pathways between photoreceptor cell types upon specific ablation of Ranbp2 in cone photoreceptors. PLoS Genet. 9, e1003555
    • (2013) PLoS Genet. , vol.9
    • Cho, K.I.1    Haque, M.2    Wang, J.3    Yu, M.4    Hao, Y.5    Qiu, S.6    Pillai, I.C.7    Peachey, N.S.8    Ferreira, P.A.9
  • 71
    • 84964603387 scopus 로고    scopus 로고
    • Structural and functional plasticity of subcellular tethering, targeting and processing of RPGRIP1 by RPGR isoforms
    • Patil, H., Guruju, M. R., Cho, K. I., Yi, H., Orry, A., Kim, H., and Ferreira, P. A. (2012) Structural and functional plasticity of subcellular tethering, targeting and processing of RPGRIP1 by RPGR isoforms. Biol. Open 1, 140-160
    • (2012) Biol. Open , vol.1 , pp. 140-160
    • Patil, H.1    Guruju, M.R.2    Cho, K.I.3    Yi, H.4    Orry, A.5    Kim, H.6    Ferreira, P.A.7
  • 72
    • 0034093244 scopus 로고    scopus 로고
    • Characterization of RanBP2-associated molecular components in neuroretina
    • Ferreira, P. A. (2000) Characterization of RanBP2-associated molecular components in neuroretina. Methods Enzymol. 315, 455-468
    • (2000) Methods Enzymol. , vol.315 , pp. 455-468
    • Ferreira, P.A.1
  • 73
    • 0025868143 scopus 로고
    • Determination of kinetic constants for peptidylprolyl cis-trans isomerases by an improved spectrophotometric assay
    • Kofron, J. L., Kuzmic, P., Kishore, V., Colón-Bonilla, E., and Rich, D. H. (1991) Determination of kinetic constants for peptidylprolyl cis-trans isomerases by an improved spectrophotometric assay. Biochemistry 30, 6127-6134
    • (1991) Biochemistry , vol.30 , pp. 6127-6134
    • Kofron, J.L.1    Kuzmic, P.2    Kishore, V.3    Colón-Bonilla, E.4    Rich, D.H.5
  • 75
    • 0036707864 scopus 로고    scopus 로고
    • Identification of RanBP2-and kinesin-mediated transport pathways with restricted neuronal and subcellular localization
    • Mavlyutov, T. A., Cai, Y., and Ferreira, P. A. (2002) Identification of RanBP2-and kinesin-mediated transport pathways with restricted neuronal and subcellular localization. Traffic 3, 630-640
    • (2002) Traffic , vol.3 , pp. 630-640
    • Mavlyutov, T.A.1    Cai, Y.2    Ferreira, P.A.3
  • 76
    • 27644518292 scopus 로고    scopus 로고
    • Monitoring activity and inhibition of 26S proteasomes with fluorogenic peptide substrates
    • Kisselev, A. F., and Goldberg, A. L. (2005) Monitoring activity and inhibition of 26S proteasomes with fluorogenic peptide substrates. Methods Enzymol. 398, 364-378
    • (2005) Methods Enzymol. , vol.398 , pp. 364-378
    • Kisselev, A.F.1    Goldberg, A.L.2
  • 77
    • 84862803353 scopus 로고    scopus 로고
    • Age-related changes in visual function in cystathionine-synthase mutant mice, a model of hyperhomocysteinemia
    • Yu, M., Sturgill-Short, G., Ganapathy, P., Tawfik, A., Peachey, N. S., and Smith, S. B. (2012) Age-related changes in visual function in cystathionine-synthase mutant mice, a model of hyperhomocysteinemia. Exp. Eye Res. 96, 124-131
    • (2012) Exp. Eye Res. , vol.96 , pp. 124-131
    • Yu, M.1    Sturgill-Short, G.2    Ganapathy, P.3    Tawfik, A.4    Peachey, N.S.5    Smith, S.B.6
  • 78
    • 0027071803 scopus 로고
    • Active site mutants of human cyclophilin A separate peptidyl-prolyl isomerase activity from cyclosporin A binding and calcineurin inhibition
    • Zydowsky, L. D., Etzkorn, F. A., Chang, H. Y., Ferguson, S. B., Stolz, L. A., Ho, S. I., and Walsh, C. T. (1992) Active site mutants of human cyclophilin A separate peptidyl-prolyl isomerase activity from cyclosporin A binding and calcineurin inhibition. Protein Sci. 1, 1092-1099
    • (1992) Protein Sci. , vol.1 , pp. 1092-1099
    • Zydowsky, L.D.1    Etzkorn, F.A.2    Chang, H.Y.3    Ferguson, S.B.4    Stolz, L.A.5    Ho, S.I.6    Walsh, C.T.7
  • 79
    • 33750456519 scopus 로고    scopus 로고
    • Global, in vivo, and site-specific phosphorylation dynamics in signaling networks
    • Olsen, J. V., Blagoev, B., Gnad, F., Macek, B., Kumar, C., Mortensen, P., and Mann, M. (2006) Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell 127, 635-648
    • (2006) Cell , vol.127 , pp. 635-648
    • Olsen, J.V.1    Blagoev, B.2    Gnad, F.3    Macek, B.4    Kumar, C.5    Mortensen, P.6    Mann, M.7
  • 80
    • 0034996105 scopus 로고    scopus 로고
    • Genomic organization, expression, and localization of murine Ran-binding protein 2 (RanBP2) gene
    • Fauser, S., Aslanukov, A., Roepman, R., and Ferreira, P. A. (2001) Genomic organization, expression, and localization of murine Ran-binding protein 2 (RanBP2) gene. Mamm. Genome 12, 406-415
    • (2001) Mamm. Genome , vol.12 , pp. 406-415
    • Fauser, S.1    Aslanukov, A.2    Roepman, R.3    Ferreira, P.A.4
  • 81
    • 0035487293 scopus 로고    scopus 로고
    • Recombineering: A powerful new tool for mouse functional genomics
    • Copeland, N. G., Jenkins, N. A., and Court, D. L. (2001) Recombineering: a powerful new tool for mouse functional genomics. Nat. Rev. Genet. 2, 769-779
    • (2001) Nat. Rev. Genet. , vol.2 , pp. 769-779
    • Copeland, N.G.1    Jenkins, N.A.2    Court, D.L.3
  • 82
    • 0037076393 scopus 로고    scopus 로고
    • The intranuclear prolactin/ cyclophilin B complex as a transcriptional inducer
    • Rycyzyn, M. A., and Clevenger, C. V. (2002) The intranuclear prolactin/ cyclophilin B complex as a transcriptional inducer. Proc. Natl. Acad. Sci. U.S.A. 99, 6790-6795
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 6790-6795
    • Rycyzyn, M.A.1    Clevenger, C.V.2
  • 84
    • 58249095006 scopus 로고    scopus 로고
    • Haploinsufficiency of RanBP2 is neuroprotective against light-elicited and age-dependent degeneration of photoreceptor neurons
    • Cho, K. I., Yi, H., Yeh, A., Tserentsoodol, N., Cuadrado, L., Searle, K., Hao, Y., and Ferreira, P. A. (2009) Haploinsufficiency of RanBP2 is neuroprotective against light-elicited and age-dependent degeneration of photoreceptor neurons. Cell Death Differ. 16, 287-297
    • (2009) Cell Death Differ. , vol.16 , pp. 287-297
    • Cho, K.I.1    Yi, H.2    Yeh, A.3    Tserentsoodol, N.4    Cuadrado, L.5    Searle, K.6    Hao, Y.7    Ferreira, P.A.8
  • 85
    • 67249123818 scopus 로고    scopus 로고
    • Depleting Rac1 in mouse rod photoreceptors protects them from photo-oxidative stress without affecting their structure or function
    • Haruta, M., Bush, R. A., Kjellstrom, S., Vijayasarathy, C., Zeng, Y., Le, Y. Z., and Sieving, P. A. (2009) Depleting Rac1 in mouse rod photoreceptors protects them from photo-oxidative stress without affecting their structure or function. Proc. Natl. Acad. Sci. U.S.A. 106, 9397-9402
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 9397-9402
    • Haruta, M.1    Bush, R.A.2    Kjellstrom, S.3    Vijayasarathy, C.4    Zeng, Y.5    Le, Y.Z.6    Sieving, P.A.7
  • 87
    • 0032544588 scopus 로고    scopus 로고
    • The cyclophilin-like domain mediates the association of Ran-binding protein 2 with subunits of the 19 S regulatory complex of the proteasome
    • Ferreira, P. A., Yunfei, C., Schick, D., and Roepman, R. (1998) The cyclophilin-like domain mediates the association of Ran-binding protein 2 with subunits of the 19 S regulatory complex of the proteasome. J. Biol. Chem. 273, 24676-24682
    • (1998) J. Biol. Chem. , vol.273 , pp. 24676-24682
    • Ferreira, P.A.1    Yunfei, C.2    Schick, D.3    Roepman, R.4
  • 88
    • 36849028012 scopus 로고    scopus 로고
    • The cyclophilin-like domain of Ran-binding protein-2 modulates selectively the activity of the ubiquitin-proteasome system and protein biogenesis
    • Yi, H., Friedman, J. L., and Ferreira, P. A. (2007) The cyclophilin-like domain of Ran-binding protein-2 modulates selectively the activity of the ubiquitin-proteasome system and protein biogenesis. J. Biol. Chem. 282, 34770-34778
    • (2007) J. Biol. Chem. , vol.282 , pp. 34770-34778
    • Yi, H.1    Friedman, J.L.2    Ferreira, P.A.3
  • 89
    • 77956553887 scopus 로고    scopus 로고
    • Neuroprotection resulting from insufficiency of RANBP2 is associated with the modulation of protein and lipid homeostasis of functionally diverse but linked pathways in response to oxidative stress
    • Cho, K. I., Yi, H., Tserentsoodol, N., Searle, K., and Ferreira, P. A. (2010) Neuroprotection resulting from insufficiency of RANBP2 is associated with the modulation of protein and lipid homeostasis of functionally diverse but linked pathways in response to oxidative stress. Dis Model. Mech. 3, 595-604
    • (2010) Dis Model. Mech. , vol.3 , pp. 595-604
    • Cho, K.I.1    Yi, H.2    Tserentsoodol, N.3    Searle, K.4    Ferreira, P.A.5
  • 92
    • 50849143144 scopus 로고    scopus 로고
    • HDAC-class II specific inhibition involves HDAC proteasome-dependent degradation mediated by RANBP2
    • Scognamiglio, A., Nebbioso, A., Manzo, F., Valente, S., Mai, A., and Altucci, L. (2008) HDAC-class II specific inhibition involves HDAC proteasome-dependent degradation mediated by RANBP2. Biochim. Biophys. Acta 1783, 2030-2038
    • (2008) Biochim. Biophys. Acta , vol.1783 , pp. 2030-2038
    • Scognamiglio, A.1    Nebbioso, A.2    Manzo, F.3    Valente, S.4    Mai, A.5    Altucci, L.6
  • 93
    • 58149389397 scopus 로고    scopus 로고
    • HDAC4 regulates neuronal survival in normal and diseased retinas
    • Chen, B., and Cepko, C. L. (2009) HDAC4 regulates neuronal survival in normal and diseased retinas. Science 323, 256-259
    • (2009) Science , vol.323 , pp. 256-259
    • Chen, B.1    Cepko, C.L.2
  • 95
    • 84860692938 scopus 로고    scopus 로고
    • Nuclear accumulation of HDAC4 in ATM deficiency promotes neurodegeneration in ataxia telangiectasia
    • Li, J., Chen, J., Ricupero, C. L., Hart, R. P., Schwartz, M. S., Kusnecov, A., and Herrup, K. (2012) Nuclear accumulation of HDAC4 in ATM deficiency promotes neurodegeneration in ataxia telangiectasia. Nat. Med. 18, 783-790
    • (2012) Nat. Med. , vol.18 , pp. 783-790
    • Li, J.1    Chen, J.2    Ricupero, C.L.3    Hart, R.P.4    Schwartz, M.S.5    Kusnecov, A.6    Herrup, K.7
  • 99
    • 84856977664 scopus 로고    scopus 로고
    • The ubiquitin proteasome system in neurodegenerative diseases: Culprit, accomplice or victim?
    • Dennissen, F. J., Kholod, N., and van Leeuwen, F. W. (2012) The ubiquitin proteasome system in neurodegenerative diseases: culprit, accomplice or victim? Prog. Neurobiol. 96, 190-207
    • (2012) Prog. Neurobiol. , vol.96 , pp. 190-207
    • Dennissen, F.J.1    Kholod, N.2    Van Leeuwen, F.W.3
  • 101
    • 79959906646 scopus 로고    scopus 로고
    • Balancing act: Deubiquitinating enzymes in the nervous system
    • Todi, S. V., and Paulson, H. L. (2011) Balancing act: deubiquitinating enzymes in the nervous system. Trends Neurosci. 34, 370-382
    • (2011) Trends Neurosci. , vol.34 , pp. 370-382
    • Todi, S.V.1    Paulson, H.L.2
  • 102
    • 62649104153 scopus 로고    scopus 로고
    • K63-specific deubiquitination by two JAMM/ MPN complexes: BRISC-associated Brcc36 and proteasomal Poh1
    • Cooper, E. M., Cutcliffe, C., Kristiansen, T. Z., Pandey, A., Pickart, C. M., and Cohen, R. E. (2009) K63-specific deubiquitination by two JAMM/ MPN complexes: BRISC-associated Brcc36 and proteasomal Poh1. EMBO J. 28, 621-631
    • (2009) EMBO J. , vol.28 , pp. 621-631
    • Cooper, E.M.1    Cutcliffe, C.2    Kristiansen, T.Z.3    Pandey, A.4    Pickart, C.M.5    Cohen, R.E.6
  • 103
    • 79953778442 scopus 로고    scopus 로고
    • Characterization of selective ubiquitin and ubiquitin-like protease inhibitors using a fluorescencebased multiplex assay format
    • Tian, X., Isamiddinova, N. S., Peroutka, R. J., Goldenberg, S. J., Mattern, M. R., Nicholson, B., and Leach, C. (2011) Characterization of selective ubiquitin and ubiquitin-like protease inhibitors using a fluorescencebased multiplex assay format. Assay Drug Dev. Technol. 9, 165-173
    • (2011) Assay Drug Dev. Technol. , vol.9 , pp. 165-173
    • Tian, X.1    Isamiddinova, N.S.2    Peroutka, R.J.3    Goldenberg, S.J.4    Mattern, M.R.5    Nicholson, B.6    Leach, C.7
  • 106
    • 84857935771 scopus 로고    scopus 로고
    • The structure of the 26S proteasome subunit Rpn2 reveals its PC repeat domain as a closed toroid of two concentric helical rings
    • He, J., Kulkarni, K., da Fonseca, P. C., Krutauz, D., Glickman, M. H., Barford, D., and Morris, E. P. (2012) The structure of the 26S proteasome subunit Rpn2 reveals its PC repeat domain as a closed toroid of two concentric helical rings. Structure 20, 513-521
    • (2012) Structure , vol.20 , pp. 513-521
    • He, J.1    Kulkarni, K.2    Da Fonseca, P.C.3    Krutauz, D.4    Glickman, M.H.5    Barford, D.6    Morris, E.P.7
  • 107
    • 0031899462 scopus 로고    scopus 로고
    • Alteration of early components of the visual evoked potential in amyotrophic lateral sclerosis
    • Münte, T. F., Tröger, M. C., Nusser, I., Wieringa, B. M., Johannes, S., Matzke, M., and Dengler, R. (1998) Alteration of early components of the visual evoked potential in amyotrophic lateral sclerosis. J. Neurol. 245, 206-210
    • (1998) J. Neurol. , vol.245 , pp. 206-210
    • Münte, T.F.1    Tröger, M.C.2    Nusser, I.3    Wieringa, B.M.4    Johannes, S.5    Matzke, M.6    Dengler, R.7
  • 108
    • 77949883029 scopus 로고    scopus 로고
    • Electrophysiological and histologic assessment of retinal ganglion cell fate in a mouse model for OPA1-associated autosomal dominant optic atrophy
    • Heiduschka, P., Schnichels, S., Fuhrmann, N., Hofmeister, S., Schraermeyer, U., Wissinger, B., and Alavi, M. V. (2010) Electrophysiological and histologic assessment of retinal ganglion cell fate in a mouse model for OPA1-associated autosomal dominant optic atrophy. Invest. Ophthalmol. Vis. Sci. 51, 1424-1431
    • (2010) Invest. Ophthalmol. Vis. Sci. , vol.51 , pp. 1424-1431
    • Heiduschka, P.1    Schnichels, S.2    Fuhrmann, N.3    Hofmeister, S.4    Schraermeyer, U.5    Wissinger, B.6    Alavi, M.V.7
  • 110
    • 0017263248 scopus 로고
    • Delayed visual perception and delayed visual evoked potentials in the spinal form of multiple sclerosis and in retrobulbar neuritis
    • Regan, D., Milner, B. A., and Heron, J. R. (1976) Delayed visual perception and delayed visual evoked potentials in the spinal form of multiple sclerosis and in retrobulbar neuritis. Brain 99, 43-66
    • (1976) Brain , vol.99 , pp. 43-66
    • Regan, D.1    Milner, B.A.2    Heron, J.R.3
  • 111
    • 38049125795 scopus 로고    scopus 로고
    • Cyclophilin A is required for CXCR4-mediated nuclear export of heterogeneous nuclear ribonucleoprotein A2, activation and nuclear translocation of ERK1/2, and chemotactic cell migration
    • Pan, H., Luo, C., Li, R., Qiao, A., Zhang, L., Mines, M., Nyanda, A. M., Zhang, J., and Fan, G. H. (2008) Cyclophilin A is required for CXCR4-mediated nuclear export of heterogeneous nuclear ribonucleoprotein A2, activation and nuclear translocation of ERK1/2, and chemotactic cell migration. J. Biol. Chem. 283, 623-637
    • (2008) J. Biol. Chem. , vol.283 , pp. 623-637
    • Pan, H.1    Luo, C.2    Li, R.3    Qiao, A.4    Zhang, L.5    Mines, M.6    Nyanda, A.M.7    Zhang, J.8    Fan, G.H.9
  • 112
    • 0028357909 scopus 로고
    • Cyclosporin A inhibits growth of autocrine tumour cell lines by destabilizing interleukin-3 mRNA
    • Nair, A. P., Hahn, S., Banholzer, R., Hirsch, H. H., and Moroni, C. (1994) Cyclosporin A inhibits growth of autocrine tumour cell lines by destabilizing interleukin-3 mRNA. Nature 369, 239-242
    • (1994) Nature , vol.369 , pp. 239-242
    • Nair, A.P.1    Hahn, S.2    Banholzer, R.3    Hirsch, H.H.4    Moroni, C.5
  • 114
    • 84862780073 scopus 로고    scopus 로고
    • A size-exclusion permeability barrier and nucleoporins characterize a ciliary pore complex that regulates transport into cilia
    • Kee, H. L., Dishinger, J. F., Blasius, T. L., Liu, C. J., Margolis, B., and Verhey, K. J. (2012) A size-exclusion permeability barrier and nucleoporins characterize a ciliary pore complex that regulates transport into cilia. Nat. Cell Biol. 14, 431-437
    • (2012) Nat. Cell Biol. , vol.14 , pp. 431-437
    • Kee, H.L.1    Dishinger, J.F.2    Blasius, T.L.3    Liu, C.J.4    Margolis, B.5    Verhey, K.J.6
  • 117
    • 0028937195 scopus 로고
    • Co-activation of RanGTPase and inhibition of GTP dissociation by Ran-GTP binding protein RanBP1
    • Bischoff, F. R., Krebber, H., Smirnova, E., Dong, W., and Ponstingl, H. (1995) Co-activation of RanGTPase and inhibition of GTP dissociation by Ran-GTP binding protein RanBP1. EMBO J. 14, 705-715
    • (1995) EMBO J. , vol.14 , pp. 705-715
    • Bischoff, F.R.1    Krebber, H.2    Smirnova, E.3    Dong, W.4    Ponstingl, H.5
  • 118
    • 0033522118 scopus 로고    scopus 로고
    • Structure of a Ran-binding domain complexed with Ran bound to a GTP analogue: Implications for nuclear transport
    • Vetter, I. R., Nowak, C., Nishimoto, T., Kuhlmann, J., and Wittinghofer, A. (1999) Structure of a Ran-binding domain complexed with Ran bound to a GTP analogue: implications for nuclear transport. Nature 398, 39-46
    • (1999) Nature , vol.398 , pp. 39-46
    • Vetter, I.R.1    Nowak, C.2    Nishimoto, T.3    Kuhlmann, J.4    Wittinghofer, A.5
  • 119
    • 0034718525 scopus 로고    scopus 로고
    • Different structural and kinetic requirements for the interaction of Ran with the Ran-binding domains from RanBP2 and importin
    • Villa Braslavsky, C. I., Nowak, C., Görlich, D., Wittinghofer, A., and Kuhlmann, J. (2000) Different structural and kinetic requirements for the interaction of Ran with the Ran-binding domains from RanBP2 and importin-. Biochemistry 39, 11629-11639
    • (2000) Biochemistry , vol.39 , pp. 11629-11639
    • Villa Braslavsky, C.I.1    Nowak, C.2    Görlich, D.3    Wittinghofer, A.4    Kuhlmann, J.5
  • 120
    • 0030856315 scopus 로고    scopus 로고
    • The asymmetric distribution of the constituents of the Ran system is essential for transport into and out of the nucleus
    • Izaurralde, E., Kutay, U., von Kobbe, C., Mattaj, I. W., and Görlich, D. (1997) The asymmetric distribution of the constituents of the Ran system is essential for transport into and out of the nucleus. EMBO J. 16, 6535-6547
    • (1997) EMBO J. , vol.16 , pp. 6535-6547
    • Izaurralde, E.1    Kutay, U.2    Von Kobbe, C.3    Mattaj, I.W.4    Görlich, D.5
  • 121
    • 0042131538 scopus 로고    scopus 로고
    • RPGRIP1s with distinct neuronal localization and biochemical properties associate selectively with RanBP2 in amacrine neurons
    • Castagnet, P., Mavlyutov, T., Cai, Y., Zhong, F., and Ferreira, P. (2003) RPGRIP1s with distinct neuronal localization and biochemical properties associate selectively with RanBP2 in amacrine neurons. Hum. Mol. Genet. 12, 1847-1863
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 1847-1863
    • Castagnet, P.1    Mavlyutov, T.2    Cai, Y.3    Zhong, F.4    Ferreira, P.5
  • 122
    • 84864880444 scopus 로고    scopus 로고
    • Selective loss of RPGRIP1-dependent ciliary targeting of NPHP4, RPGR and SDCCAG8 underlies the degeneration of photoreceptor neurons
    • Patil, H., Tserentsoodol, N., Saha, A., Hao, Y., Webb, M., and Ferreira, P. A. (2012) Selective loss of RPGRIP1-dependent ciliary targeting of NPHP4, RPGR and SDCCAG8 underlies the degeneration of photoreceptor neurons. Cell Death Dis. 3, e355
    • (2012) Cell Death Dis. , vol.3
    • Patil, H.1    Tserentsoodol, N.2    Saha, A.3    Hao, Y.4    Webb, M.5    Ferreira, P.A.6
  • 124
    • 84865803029 scopus 로고    scopus 로고
    • The oncogene eIF4E reprograms the nuclear pore complex to promote mRNA export and oncogenic transformation
    • Culjkovic-Kraljacic, B., Baguet, A., Volpon, L., Amri, A., and Borden, K. L. (2012) The oncogene eIF4E reprograms the nuclear pore complex to promote mRNA export and oncogenic transformation. Cell Reports 2, 207-215
    • (2012) Cell Reports , vol.2 , pp. 207-215
    • Culjkovic-Kraljacic, B.1    Baguet, A.2    Volpon, L.3    Amri, A.4    Borden, K.L.5
  • 125
    • 0026013566 scopus 로고
    • Human cyclophilin B: A second cyclophilin gene encodes a peptidyl-prolyl isomerase with a signal sequence
    • Price, E. R., Zydowsky, L. D., Jin, M. J., Baker, C. H., McKeon, F. D., and Walsh, C. T. (1991) Human cyclophilin B: a second cyclophilin gene encodes a peptidyl-prolyl isomerase with a signal sequence. Proc. Natl. Acad. Sci. U.S.A. 88, 1903-1907
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 1903-1907
    • Price, E.R.1    Zydowsky, L.D.2    Jin, M.J.3    Baker, C.H.4    McKeon, F.D.5    Walsh, C.T.6
  • 127
    • 17644413069 scopus 로고    scopus 로고
    • Vanishingly low levels of Ess1 prolyl-isomerase activity are sufficient for growth in Saccharomyces cerevisiae
    • Gemmill, T. R., Wu, X., and Hanes, S. D. (2005) Vanishingly low levels of Ess1 prolyl-isomerase activity are sufficient for growth in Saccharomyces cerevisiae. J. Biol. Chem. 280, 15510-15517
    • (2005) J. Biol. Chem. , vol.280 , pp. 15510-15517
    • Gemmill, T.R.1    Wu, X.2    Hanes, S.D.3
  • 130
    • 61449129071 scopus 로고    scopus 로고
    • Ubiquitin dimers control the hydrolase activity of UCH-L3
    • Setsuie, R., Sakurai, M., Sakaguchi, Y., and Wada, K. (2009) Ubiquitin dimers control the hydrolase activity of UCH-L3. Neurochem. Int. 54, 314-321
    • (2009) Neurochem. Int. , vol.54 , pp. 314-321
    • Setsuie, R.1    Sakurai, M.2    Sakaguchi, Y.3    Wada, K.4
  • 134
    • 84877773337 scopus 로고    scopus 로고
    • Kinesin-1 and mitochondrial motility control by discrimination of structurally equivalent but distinct subdomains in Ran-GTP-binding domains of Ran-binding protein 2
    • Patil, H., Cho, K. I., Lee, J., Yang, Y., Orry, A., and Ferreira, P. A. (2013) Kinesin-1 and mitochondrial motility control by discrimination of structurally equivalent but distinct subdomains in Ran-GTP-binding domains of Ran-binding protein 2. Open Biol. 3, 120183
    • (2013) Open Biol. , vol.3 , pp. 120183
    • Patil, H.1    Cho, K.I.2    Lee, J.3    Yang, Y.4    Orry, A.5    Ferreira, P.A.6
  • 135
    • 71449103005 scopus 로고    scopus 로고
    • Hidden alternative structures of proline isomerase essential for catalysis
    • Fraser, J. S., Clarkson, M. W., Degnan, S. C., Erion, R., Kern, D., and Alber, T. (2009) Hidden alternative structures of proline isomerase essential for catalysis. Nature 462, 669-673
    • (2009) Nature , vol.462 , pp. 669-673
    • Fraser, J.S.1    Clarkson, M.W.2    Degnan, S.C.3    Erion, R.4    Kern, D.5    Alber, T.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.