메뉴 건너뛰기




Volumn 52, Issue 12, 2013, Pages 2089-2096

Unique proline-rich domain regulates the chaperone function of AIPL1

Author keywords

[No Author keywords available]

Indexed keywords

ARYL HYDROCARBON RECEPTOR; CHAPERONE ACTIVITY; CHAPERONE FUNCTIONS; FUNCTIONAL RELEVANCE; NEGATIVE REGULATORS; PROLINE-RICH DOMAINS; SEQUENCE IDENTITY; TETRATRICOPEPTIDE REPEAT DOMAINS;

EID: 84875644151     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi301648q     Document Type: Article
Times cited : (16)

References (60)
  • 1
    • 0024421221 scopus 로고
    • Hsp82 is an essential protein that is required in higher concentrations for growth of cells at higher temperatures
    • Borkovich, K. A., Farrelly, F. W., Finkelstein, D. B., Taulien, J., and Lindquist, S. (1989) hsp82 is an essential protein that is required in higher concentrations for growth of cells at higher temperatures Mol. Cell. Biol. 9, 3919-3930
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 3919-3930
    • Borkovich, K.A.1    Farrelly, F.W.2    Finkelstein, D.B.3    Taulien, J.4    Lindquist, S.5
  • 2
    • 43549102208 scopus 로고    scopus 로고
    • HSP90: The Rosetta stone for cellular protein dynamics?
    • Dezwaan, D. C. and Freeman, B. C. (2008) HSP90: the Rosetta stone for cellular protein dynamics? Cell Cycle 7, 1006-1012
    • (2008) Cell Cycle , vol.7 , pp. 1006-1012
    • Dezwaan, D.C.1    Freeman, B.C.2
  • 3
    • 77953916528 scopus 로고    scopus 로고
    • HSP90 at the hub of protein homeostasis: Emerging mechanistic insights
    • Taipale, M., Jarosz, D. F., and Lindquist, S. (2010) HSP90 at the hub of protein homeostasis: emerging mechanistic insights Nat. Rev. Mol. Cell Biol. 11, 515-528
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 515-528
    • Taipale, M.1    Jarosz, D.F.2    Lindquist, S.3
  • 4
    • 0035939668 scopus 로고    scopus 로고
    • Hsp90: A specialized but essential protein-folding tool
    • Young, J. C., Moarefi, I., and Hartl, F. U. (2001) Hsp90: a specialized but essential protein-folding tool J. Cell Biol. 154, 267-273
    • (2001) J. Cell Biol. , vol.154 , pp. 267-273
    • Young, J.C.1    Moarefi, I.2    Hartl, F.U.3
  • 5
    • 77955506092 scopus 로고    scopus 로고
    • Gymnastics of molecular chaperones
    • Mayer, M. P. (2010) Gymnastics of molecular chaperones Molecular cell 39, 321-331
    • (2010) Molecular Cell , vol.39 , pp. 321-331
    • Mayer, M.P.1
  • 6
    • 0031873752 scopus 로고    scopus 로고
    • The 90-kDa molecular chaperone family: Structure, function, and clinical applications. A comprehensive review
    • Csermely, P., Schnaider, T., Soti, C., Prohaszka, Z., and Nardai, G. (1998) The 90-kDa molecular chaperone family: structure, function, and clinical applications. A comprehensive review Pharmacol.Ther. 79, 129-168
    • (1998) Pharmacol.Ther. , vol.79 , pp. 129-168
    • Csermely, P.1    Schnaider, T.2    Soti, C.3    Prohaszka, Z.4    Nardai, G.5
  • 7
    • 0036810352 scopus 로고    scopus 로고
    • Heat-shock protein 90, a chaperone for folding and regulation
    • Picard, D. (2002) Heat-shock protein 90, a chaperone for folding and regulation Cell. Mol. Life Sci. 59, 1640-1648
    • (2002) Cell. Mol. Life Sci. , vol.59 , pp. 1640-1648
    • Picard, D.1
  • 8
    • 0030925683 scopus 로고    scopus 로고
    • Steroid receptor interactions with heat shock protein and immunophilin chaperones
    • Pratt, W. B. and Toft, D. O. (1997) Steroid receptor interactions with heat shock protein and immunophilin chaperones Endocr.Rev. 18, 306-360
    • (1997) Endocr.Rev. , vol.18 , pp. 306-360
    • Pratt, W.B.1    Toft, D.O.2
  • 10
    • 84857042271 scopus 로고    scopus 로고
    • The Hsp90 chaperone machinery: Conformational dynamics and regulation by co-chaperones
    • Li, J., Soroka, J., and Buchner, J. (2012) The Hsp90 chaperone machinery: Conformational dynamics and regulation by co-chaperones Biochim. Biophys. Acta 1823, 624-635
    • (2012) Biochim. Biophys. Acta , vol.1823 , pp. 624-635
    • Li, J.1    Soroka, J.2    Buchner, J.3
  • 11
    • 36849030809 scopus 로고    scopus 로고
    • FK506-binding protein 52 phosphorylation: A potential mechanism for regulating steroid hormone receptor activity
    • Cox, M. B., Riggs, D. L., Hessling, M., Schumacher, F., Buchner, J., and Smith, D. F. (2007) FK506-binding protein 52 phosphorylation: a potential mechanism for regulating steroid hormone receptor activity Mol. Endocrinol. 21, 2956-2967
    • (2007) Mol. Endocrinol. , vol.21 , pp. 2956-2967
    • Cox, M.B.1    Riggs, D.L.2    Hessling, M.3    Schumacher, F.4    Buchner, J.5    Smith, D.F.6
  • 12
    • 0028266874 scopus 로고
    • Characterization of a novel 23-kilodalton protein of unactive progesterone receptor complexes
    • Johnson, J. L., Beito, T. G., Krco, C. J., and Toft, D. O. (1994) Characterization of a novel 23-kilodalton protein of unactive progesterone receptor complexes Mol. Cell. Biol. 14, 1956-1963
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 1956-1963
    • Johnson, J.L.1    Beito, T.G.2    Krco, C.J.3    Toft, D.O.4
  • 13
    • 0027170713 scopus 로고
    • P59 (FK506 binding protein 59) interaction with heat shock proteins is highly conserved and may involve proteins other than steroid receptors
    • Tai, P. K., Chang, H., Albers, M. W., Schreiber, S. L., Toft, D. O., and Faber, L. E. (1993) P59 (FK506 binding protein 59) interaction with heat shock proteins is highly conserved and may involve proteins other than steroid receptors Biochemistry 32, 8842-8847
    • (1993) Biochemistry , vol.32 , pp. 8842-8847
    • Tai, P.K.1    Chang, H.2    Albers, M.W.3    Schreiber, S.L.4    Toft, D.O.5    Faber, L.E.6
  • 14
    • 0032541163 scopus 로고    scopus 로고
    • Specific binding of tetratricopeptide repeat proteins to the C-terminal 12-kDa domain of hsp90
    • Young, J. C., Obermann, W. M., and Hartl, F. U. (1998) Specific binding of tetratricopeptide repeat proteins to the C-terminal 12-kDa domain of hsp90 J. Biol. Chem. 273, 18007-18010
    • (1998) J. Biol. Chem. , vol.273 , pp. 18007-18010
    • Young, J.C.1    Obermann, W.M.2    Hartl, F.U.3
  • 15
    • 0034646511 scopus 로고    scopus 로고
    • Structure of TPR domain-peptide complexes: Critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine
    • Scheufler, C., Brinker, A., Bourenkov, G., Pegoraro, S., Moroder, L., Bartunik, H., Hartl, F. U., and Moarefi, I. (2000) Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine Cell 101, 199-210
    • (2000) Cell , vol.101 , pp. 199-210
    • Scheufler, C.1    Brinker, A.2    Bourenkov, G.3    Pegoraro, S.4    Moroder, L.5    Bartunik, H.6    Hartl, F.U.7    Moarefi, I.8
  • 16
    • 0032567434 scopus 로고    scopus 로고
    • Hop as an adaptor in the heat shock protein 70 (Hsp70) and hsp90 chaperone machinery
    • Chen, S. and Smith, D. F. (1998) Hop as an adaptor in the heat shock protein 70 (Hsp70) and hsp90 chaperone machinery J. Biol. Chem. 273, 35194-35200
    • (1998) J. Biol. Chem. , vol.273 , pp. 35194-35200
    • Chen, S.1    Smith, D.F.2
  • 17
    • 0031846768 scopus 로고    scopus 로고
    • Differential interactions of p23 and the TPR-containing proteins Hop, Cyp40, FKBP52 and FKBP51 with Hsp90 mutants
    • Chen, S., Sullivan, W. P., Toft, D. O., and Smith, D. F. (1998) Differential interactions of p23 and the TPR-containing proteins Hop, Cyp40, FKBP52 and FKBP51 with Hsp90 mutants Cell Stress.Chaperones. 3, 118-129
    • (1998) Cell Stress.Chaperones. , vol.3 , pp. 118-129
    • Chen, S.1    Sullivan, W.P.2    Toft, D.O.3    Smith, D.F.4
  • 19
    • 84875225582 scopus 로고    scopus 로고
    • Integration of the accelerator Aha1 in the Hsp90 co-chaperone cycle
    • 10.1038/nsnb.2502
    • Li, J., Richter, K., Reinstein, J., and Buchner, J. (2013) Integration of the accelerator Aha1 in the Hsp90 co-chaperone cycle Nat. Struct. Mol. Biol. 10.1038/nsnb.2502
    • (2013) Nat. Struct. Mol. Biol.
    • Li, J.1    Richter, K.2    Reinstein, J.3    Buchner, J.4
  • 21
    • 0027256152 scopus 로고
    • Evidence that the hormone binding domain of steroid receptors confers hormonal control on chimeric proteins by determining their hormone-regulated binding to heat-shock protein 90
    • Scherrer, L. C., Picard, D., Massa, E., Harmon, J. M., Simons, S. S., Jr., Yamamoto, K. R., and Pratt, W. B. (1993) Evidence that the hormone binding domain of steroid receptors confers hormonal control on chimeric proteins by determining their hormone-regulated binding to heat-shock protein 90 Biochemistry 32, 5381-5386
    • (1993) Biochemistry , vol.32 , pp. 5381-5386
    • Scherrer, L.C.1    Picard, D.2    Massa, E.3    Harmon, J.M.4    Simons Jr., S.S.5    Yamamoto, K.R.6    Pratt, W.B.7
  • 22
    • 0026543821 scopus 로고
    • Assembly of progesterone receptor with heat shock proteins and receptor activation are ATP mediated events
    • Smith, D. F., Stensgard, B. A., Welch, W. J., and Toft, D. O. (1992) Assembly of progesterone receptor with heat shock proteins and receptor activation are ATP mediated events J. Biol. Chem. 267, 1350-1356
    • (1992) J. Biol. Chem. , vol.267 , pp. 1350-1356
    • Smith, D.F.1    Stensgard, B.A.2    Welch, W.J.3    Toft, D.O.4
  • 23
    • 0031882767 scopus 로고    scopus 로고
    • Hepatitis B virus X-associated protein 2 is a subunit of the unliganded aryl hydrocarbon receptor core complex and exhibits transcriptional enhancer activity
    • Meyer, B. K., Pray-Grant, M. G., Vanden Heuvel, J. P., and Perdew, G. H. (1998) Hepatitis B virus X-associated protein 2 is a subunit of the unliganded aryl hydrocarbon receptor core complex and exhibits transcriptional enhancer activity Mol. Cell. Biol. 18, 978-988
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 978-988
    • Meyer, B.K.1    Pray-Grant, M.G.2    Vanden Heuvel, J.P.3    Perdew, G.H.4
  • 24
    • 0033551511 scopus 로고    scopus 로고
    • Characterization of the AhR-hsp90-XAP2 core complex and the role of the immunophilin-related protein XAP2 in AhR stabilization
    • Meyer, B. K. and Perdew, G. H. (1999) Characterization of the AhR-hsp90-XAP2 core complex and the role of the immunophilin-related protein XAP2 in AhR stabilization Biochemistry 38, 8907-8917
    • (1999) Biochemistry , vol.38 , pp. 8907-8917
    • Meyer, B.K.1    Perdew, G.H.2
  • 25
    • 0033669662 scopus 로고    scopus 로고
    • Aryl hydrocarbon (Ah) receptor levels are selectively modulated by hsp90-associated immunophilin homolog XAP2
    • Meyer, B. K., Petrulis, J. R., and Perdew, G. H. (2000) Aryl hydrocarbon (Ah) receptor levels are selectively modulated by hsp90-associated immunophilin homolog XAP2 Cell Stress Chaperones 5, 243-254
    • (2000) Cell Stress Chaperones , vol.5 , pp. 243-254
    • Meyer, B.K.1    Petrulis, J.R.2    Perdew, G.H.3
  • 26
    • 80053446776 scopus 로고    scopus 로고
    • The immunophilin-like protein XAP2 is a negative regulator of estrogen signaling through interaction with estrogen receptor alpha
    • Cai, W., Kramarova, T. V., Berg, P., Korbonits, M., and Pongratz, I. (2011) The immunophilin-like protein XAP2 is a negative regulator of estrogen signaling through interaction with estrogen receptor alpha PloS One 6, e25201
    • (2011) PloS One , vol.6 , pp. 25201
    • Cai, W.1    Kramarova, T.V.2    Berg, P.3    Korbonits, M.4    Pongratz, I.5
  • 31
    • 0032230312 scopus 로고    scopus 로고
    • Analysis of FKBP51/FKBP52 chimeras and mutants for Hsp90 binding and association with progesterone receptor complexes
    • Barent, R. L., Nair, S. C., Carr, D. C., Ruan, Y., Rimerman, R. A., Fulton, J., Zhang, Y., and Smith, D. F. (1998) Analysis of FKBP51/FKBP52 chimeras and mutants for Hsp90 binding and association with progesterone receptor complexes Mol. Endocrinol. 12, 342-354
    • (1998) Mol. Endocrinol. , vol.12 , pp. 342-354
    • Barent, R.L.1    Nair, S.C.2    Carr, D.C.3    Ruan, Y.4    Rimerman, R.A.5    Fulton, J.6    Zhang, Y.7    Smith, D.F.8
  • 33
    • 0033952307 scopus 로고    scopus 로고
    • Enzymes that catalyse the restructuring of proteins
    • Schiene, C. and Fischer, G. (2000) Enzymes that catalyse the restructuring of proteins Curr. Opin. Struct. Biol. 10, 40-45
    • (2000) Curr. Opin. Struct. Biol. , vol.10 , pp. 40-45
    • Schiene, C.1    Fischer, G.2
  • 34
    • 4644359356 scopus 로고    scopus 로고
    • Purification, characterisation and intracellular localisation of aryl hydrocarbon interacting protein-like 1 (AIPL1) and effects of mutations associated with inherited retinal dystrophies
    • Gallon, V. A., Wilkie, S. E., Deery, E. C., Newbold, R. J., Sohocki, M. M., Bhattacharya, S. S., Hunt, D. M., and Warren, M. J. (2004) Purification, characterisation and intracellular localisation of aryl hydrocarbon interacting protein-like 1 (AIPL1) and effects of mutations associated with inherited retinal dystrophies Biochim. Biophys. Acta 1690, 141-149
    • (2004) Biochim. Biophys. Acta , vol.1690 , pp. 141-149
    • Gallon, V.A.1    Wilkie, S.E.2    Deery, E.C.3    Newbold, R.J.4    Sohocki, M.M.5    Bhattacharya, S.S.6    Hunt, D.M.7    Warren, M.J.8
  • 35
    • 0034680878 scopus 로고    scopus 로고
    • Binding of aryl hydrocarbon receptor (AhR) to AhR-interacting protein. The role of hsp90
    • Bell, D. R. and Poland, A. (2000) Binding of aryl hydrocarbon receptor (AhR) to AhR-interacting protein. The role of hsp90 J. Biol. Chem. 275, 36407-36414
    • (2000) J. Biol. Chem. , vol.275 , pp. 36407-36414
    • Bell, D.R.1    Poland, A.2
  • 36
    • 70350491197 scopus 로고    scopus 로고
    • A library of fluorescent peptides for exploring the substrate specificities of prolyl isomerases
    • Zoldak, G., Aumuller, T., Lucke, C., Hritz, J., Oostenbrink, C., Fischer, G., and Schmid, F. X. (2009) A library of fluorescent peptides for exploring the substrate specificities of prolyl isomerases Biochemistry 48, 10423-10436
    • (2009) Biochemistry , vol.48 , pp. 10423-10436
    • Zoldak, G.1    Aumuller, T.2    Lucke, C.3    Hritz, J.4    Oostenbrink, C.5    Fischer, G.6    Schmid, F.X.7
  • 37
    • 0028940309 scopus 로고
    • Transient interaction of Hsp90 with early unfolding intermediates of citrate synthase. Implications for heat shock in vivo
    • Jakob, U., Lilie, H., Meyer, I., and Buchner, J. (1995) Transient interaction of Hsp90 with early unfolding intermediates of citrate synthase. Implications for heat shock in vivo J. Biol. Chem. 270, 7288-7294
    • (1995) J. Biol. Chem. , vol.270 , pp. 7288-7294
    • Jakob, U.1    Lilie, H.2    Meyer, I.3    Buchner, J.4
  • 39
    • 0034968549 scopus 로고    scopus 로고
    • Comparative analysis of aryl-hydrocarbon receptor interacting protein-like 1 (Aipl1), a gene associated with inherited retinal disease in humans
    • Sohocki, M. M., Sullivan, L. S., Tirpak, D. L., and Daiger, S. P. (2001) Comparative analysis of aryl-hydrocarbon receptor interacting protein-like 1 (Aipl1), a gene associated with inherited retinal disease in humans Mamm. Genome 12, 566-568
    • (2001) Mamm. Genome , vol.12 , pp. 566-568
    • Sohocki, M.M.1    Sullivan, L.S.2    Tirpak, D.L.3    Daiger, S.P.4
  • 40
    • 77955551442 scopus 로고    scopus 로고
    • Charge-rich regions modulate the anti-aggregation activity of Hsp90
    • Wayne, N. and Bolon, D. N. (2010) Charge-rich regions modulate the anti-aggregation activity of Hsp90 J. Mol. Biol. 401, 931-939
    • (2010) J. Mol. Biol. , vol.401 , pp. 931-939
    • Wayne, N.1    Bolon, D.N.2
  • 41
    • 0034968225 scopus 로고    scopus 로고
    • Functional analysis of the Hsp90-associated human peptidyl prolyl cis/trans isomerases FKBP51, FKBP52 and Cyp40
    • Pirkl, F. and Buchner, J. (2001) Functional analysis of the Hsp90-associated human peptidyl prolyl cis/trans isomerases FKBP51, FKBP52 and Cyp40 Mol. Biol. 308, 795-806
    • (2001) Mol. Biol. , vol.308 , pp. 795-806
    • Pirkl, F.1    Buchner, J.2
  • 42
    • 0025728258 scopus 로고
    • Solution structure of the major binding protein for the immunosuppressant FK506
    • Moore, J. M., Peattie, D. A., Fitzgibbon, M. J., and Thomson, J. A. (1991) Solution structure of the major binding protein for the immunosuppressant FK506 Nature 351, 248-250
    • (1991) Nature , vol.351 , pp. 248-250
    • Moore, J.M.1    Peattie, D.A.2    Fitzgibbon, M.J.3    Thomson, J.A.4
  • 43
    • 0029852803 scopus 로고    scopus 로고
    • Chaperone function of Hsp90-associated proteins
    • Bose, S., Weikl, T., Bugl, H., and Buchner, J. (1996) Chaperone function of Hsp90-associated proteins Science 274, 1715-1717
    • (1996) Science , vol.274 , pp. 1715-1717
    • Bose, S.1    Weikl, T.2    Bugl, H.3    Buchner, J.4
  • 45
    • 77955326627 scopus 로고    scopus 로고
    • AIP gene and familial isolated pituitary adenomas
    • Ozfirat, Z. and Korbonits, M. (2010) AIP gene and familial isolated pituitary adenomas Mol. Cell. Endocrinol. 326, 71-79
    • (2010) Mol. Cell. Endocrinol. , vol.326 , pp. 71-79
    • Ozfirat, Z.1    Korbonits, M.2
  • 47
    • 33747385427 scopus 로고    scopus 로고
    • Biochemical function of the LCA linked protein, aryl hydrocarbon receptor interacting protein like-1 (AIPL1). Role of AIPL1 in retina
    • Schwartz, M. L., Hurley, J. B., and Ramamurthy, V. (2006) Biochemical function of the LCA linked protein, aryl hydrocarbon receptor interacting protein like-1 (AIPL1). Role of AIPL1 in retina Adv. Expt. Med. Biol. 572, 89-94
    • (2006) Adv. Expt. Med. Biol. , vol.572 , pp. 89-94
    • Schwartz, M.L.1    Hurley, J.B.2    Ramamurthy, V.3
  • 48
    • 28444439801 scopus 로고    scopus 로고
    • Insights into the catalytic mechanism of peptidyl prolyl cis/trans isomerases
    • Fanghanel, J. and Fischer, G. (2004) Insights into the catalytic mechanism of peptidyl prolyl cis/trans isomerases Frontiers Biosci: J. Virtual Lib. 9, 3453-3478
    • (2004) Frontiers Biosci: J. Virtual Lib. , vol.9 , pp. 3453-3478
    • Fanghanel, J.1    Fischer, G.2
  • 49
    • 84875640709 scopus 로고    scopus 로고
    • The FKBP-type Domain of the Human Aryl-hydrocarbon Receptor-interacting Protein (AIP) Reveals an Unusual Hsp90 Interaction
    • 10.1021/bi301649m
    • Linnert, M., Lin, Y.-J., Manns, A., Haupt, K., Paschke, A.-K., Fischer, G., Weiwad, M., and Lucke, C. (2013) The FKBP-type Domain of the Human Aryl-hydrocarbon Receptor-interacting Protein (AIP) Reveals an Unusual Hsp90 Interaction Biochemstry 10.1021/bi301649m
    • (2013) Biochemstry
    • Linnert, M.1    Lin, Y.-J.2    Manns, A.3    Haupt, K.4    Paschke, A.-K.5    Fischer, G.6    Weiwad, M.7    Lucke, C.8
  • 50
    • 0033490140 scopus 로고    scopus 로고
    • Expression of the estrogen receptor-associated immunophilins, cyclophilin 40 and FKBP52, in breast cancer
    • Ward, B. K., Mark, P. J., Ingram, D. M., Minchin, R. F., and Ratajczak, T. (1999) Expression of the estrogen receptor-associated immunophilins, cyclophilin 40 and FKBP52, in breast cancer Breast Cancer Res. Treatment 58, 267-280
    • (1999) Breast Cancer Res. Treatment , vol.58 , pp. 267-280
    • Ward, B.K.1    Mark, P.J.2    Ingram, D.M.3    Minchin, R.F.4    Ratajczak, T.5
  • 51
    • 37549067731 scopus 로고    scopus 로고
    • Noncatalytic role of the FKBP52 peptidyl-prolyl isomerase domain in the regulation of steroid hormone signaling
    • Riggs, D. L., Cox, M. B., Tardif, H. L., Hessling, M., Buchner, J., and Smith, D. F. (2007) Noncatalytic role of the FKBP52 peptidyl-prolyl isomerase domain in the regulation of steroid hormone signaling Mol. Cell. Biol. 27, 8658-8669
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 8658-8669
    • Riggs, D.L.1    Cox, M.B.2    Tardif, H.L.3    Hessling, M.4    Buchner, J.5    Smith, D.F.6
  • 52
    • 78650983812 scopus 로고    scopus 로고
    • Mixed Hsp90-cochaperone complexes are important for the progression of the reaction cycle
    • Li, J., Richter, K., and Buchner, J. (2011) Mixed Hsp90-cochaperone complexes are important for the progression of the reaction cycle Nature Struct. Mol. Biol. 18, 61-66
    • (2011) Nature Struct. Mol. Biol. , vol.18 , pp. 61-66
    • Li, J.1    Richter, K.2    Buchner, J.3
  • 53
    • 0029852712 scopus 로고    scopus 로고
    • Molecular chaperone machines: Chaperone activities of the cyclophilin Cyp-40 and the steroid aporeceptor-associated protein p23
    • Freeman, B. C., Toft, D. O., and Morimoto, R. I. (1996) Molecular chaperone machines: chaperone activities of the cyclophilin Cyp-40 and the steroid aporeceptor-associated protein p23 Science 274, 1718-1720
    • (1996) Science , vol.274 , pp. 1718-1720
    • Freeman, B.C.1    Toft, D.O.2    Morimoto, R.I.3
  • 54
    • 0035813134 scopus 로고    scopus 로고
    • Localization of the chaperone domain of FKBP52
    • Pirkl, F., Fischer, E., Modrow, S., and Buchner, J. (2001) Localization of the chaperone domain of FKBP52 J. Biol. Chem. 276, 37034-37041
    • (2001) J. Biol. Chem. , vol.276 , pp. 37034-37041
    • Pirkl, F.1    Fischer, E.2    Modrow, S.3    Buchner, J.4
  • 58
    • 0035824559 scopus 로고    scopus 로고
    • Targeting of NEDD8 and its conjugates for proteasomal degradation by NUB1
    • Kamitani, T., Kito, K., Fukuda-Kamitani, T., and Yeh, E. T. (2001) Targeting of NEDD8 and its conjugates for proteasomal degradation by NUB1 J. Biol. Chem. 276, 46655-46660
    • (2001) J. Biol. Chem. , vol.276 , pp. 46655-46660
    • Kamitani, T.1    Kito, K.2    Fukuda-Kamitani, T.3    Yeh, E.T.4
  • 59
    • 9144244348 scopus 로고    scopus 로고
    • The Leber congenital amaurosis protein AIPL1 modulates the nuclear translocation of NUB1 and suppresses inclusion formation by NUB1 fragments
    • van der Spuy, J. and Cheetham, M. E. (2004) The Leber congenital amaurosis protein AIPL1 modulates the nuclear translocation of NUB1 and suppresses inclusion formation by NUB1 fragments J. Biol. Chem. 279, 48038-48047
    • (2004) J. Biol. Chem. , vol.279 , pp. 48038-48047
    • Van Der Spuy, J.1    Cheetham, M.E.2
  • 60
    • 71449097363 scopus 로고    scopus 로고
    • AIPL1, a protein associated with childhood blindness, interacts with alpha-subunit of rod phosphodiesterase (PDE6) and is essential for its proper assembly
    • Kolandaivelu, S., Huang, J., Hurley, J. B., and Ramamurthy, V. (2009) AIPL1, a protein associated with childhood blindness, interacts with alpha-subunit of rod phosphodiesterase (PDE6) and is essential for its proper assembly J. Biol. Chem. 284, 30853-30861
    • (2009) J. Biol. Chem. , vol.284 , pp. 30853-30861
    • Kolandaivelu, S.1    Huang, J.2    Hurley, J.B.3    Ramamurthy, V.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.