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Volumn 3, Issue 10, 2007, Pages 619-629

Prolyl cis-trans isomerization as a molecular timer

Author keywords

[No Author keywords available]

Indexed keywords

CYCLOPHILIN; FK 506 BINDING PROTEIN; PEPTIDYLPROLYL ISOMERASE; PEPTIDYLPROLYL ISOMERASE PIN1;

EID: 34548660854     PISSN: 15524450     EISSN: 15524469     Source Type: Journal    
DOI: 10.1038/nchembio.2007.35     Document Type: Review
Times cited : (547)

References (137)
  • 1
    • 0031438929 scopus 로고    scopus 로고
    • Sequence-specific and phosphorylation-dependent proline isomerization: A potential mitotic regulatory mechanism
    • Yaffe, M.B. et al. Sequence-specific and phosphorylation-dependent proline isomerization: a potential mitotic regulatory mechanism. Science 278, 1957-1960 (1997).
    • (1997) Science , vol.278 , pp. 1957-1960
    • Yaffe, M.B.1
  • 2
    • 0032741457 scopus 로고    scopus 로고
    • Phosphorylation-dependent prolyl isomerization: A novel signaling regulatory mechanism
    • Zhou, X.Z., Lu, P.J., Wulf, G. & Lu, K.P. Phosphorylation-dependent prolyl isomerization: a novel signaling regulatory mechanism. Cell. Mol. Life Sci. 56, 788-806 (1999).
    • (1999) Cell. Mol. Life Sci , vol.56 , pp. 788-806
    • Zhou, X.Z.1    Lu, P.J.2    Wulf, G.3    Lu, K.P.4
  • 3
    • 1242292029 scopus 로고    scopus 로고
    • Regulation of peptide bond cis/transisomerization by enzyme catalysis and its implication in physiological processes
    • Fischer, G. & Aumuller, T. Regulation of peptide bond cis/transisomerization by enzyme catalysis and its implication in physiological processes. Rev. Physiol. Biochem. Pharmacol. 148, 105-150 (2003).
    • (2003) Rev. Physiol. Biochem. Pharmacol , vol.148 , pp. 105-150
    • Fischer, G.1    Aumuller, T.2
  • 4
    • 0042026692 scopus 로고    scopus 로고
    • Native state proline isomerization: An intrinsic molecular switch
    • Andreotti, A.H. Native state proline isomerization: an intrinsic molecular switch. Biochemistry 42, 9515-9524 (2003).
    • (2003) Biochemistry , vol.42 , pp. 9515-9524
    • Andreotti, A.H.1
  • 5
    • 18344387559 scopus 로고    scopus 로고
    • Phosphorylation-specific prolyl isomerization: Is there an underlying theme?
    • Wulf, G., Finn, G., Suizu, F. & Lu, K.P. Phosphorylation-specific prolyl isomerization: is there an underlying theme? Nat. Cell Biol. 7, 435-441 (2005).
    • (2005) Nat. Cell Biol , vol.7 , pp. 435-441
    • Wulf, G.1    Finn, G.2    Suizu, F.3    Lu, K.P.4
  • 6
    • 33847010532 scopus 로고    scopus 로고
    • Prolyl cis-trans isomerization as a molecular timer in Crk signaling
    • Nicholson, L.K. & Lu, K.P. Prolyl cis-trans isomerization as a molecular timer in Crk signaling. Mol. Cell 25, 483-485 (2007).
    • (2007) Mol. Cell , vol.25 , pp. 483-485
    • Nicholson, L.K.1    Lu, K.P.2
  • 7
    • 85029172829 scopus 로고    scopus 로고
    • The prolyl isomerase Pin1: A pivotal new twist in phosphorylation signalling and human disease
    • in the press
    • Lu, K.P. & Zhou, X.Z. The prolyl isomerase Pin1: a pivotal new twist in phosphorylation signalling and human disease. Nat. Rev. Mol. Cell Biol. (in the press).
    • Nat. Rev. Mol. Cell Biol
    • Lu, K.P.1    Zhou, X.Z.2
  • 8
    • 0024472603 scopus 로고
    • A receptor for the immunosuppressant FK506 is a cis-trans peptidyl-prolyl isomerase
    • Harding, M.W., Galat, A., Uehling, D.E. & Schreiber, S.L. A receptor for the immunosuppressant FK506 is a cis-trans peptidyl-prolyl isomerase. Nature 341, 758-760 (1989).
    • (1989) Nature , vol.341 , pp. 758-760
    • Harding, M.W.1    Galat, A.2    Uehling, D.E.3    Schreiber, S.L.4
  • 9
    • 0024959449 scopus 로고
    • Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins
    • Fischer, G., Wittmann-Liebold, B., Lang, K., Kiefhaber, T. & Schmid, F.X. Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins. Nature 337, 476-478 (1989).
    • (1989) Nature , vol.337 , pp. 476-478
    • Fischer, G.1    Wittmann-Liebold, B.2    Lang, K.3    Kiefhaber, T.4    Schmid, F.X.5
  • 10
    • 0024959451 scopus 로고
    • Peptidyl-prolyl cis-trans isomerase is the cyclosporin A-binding protein cyclophilin
    • Takahashi, N., Hayano, T. & Suzuki, M. Peptidyl-prolyl cis-trans isomerase is the cyclosporin A-binding protein cyclophilin. Nature 337, 473-475 (1989).
    • (1989) Nature , vol.337 , pp. 473-475
    • Takahashi, N.1    Hayano, T.2    Suzuki, M.3
  • 11
    • 0024442393 scopus 로고
    • A cytosolic binding protein for the immunosuppressant FK506 has peptidyl-prolyl isomerase activity but is distinct from cyclophilin
    • Siekierka, J.J., Hung, S.H., Poe, M., Lin, C.S. & Sigal, N.H. A cytosolic binding protein for the immunosuppressant FK506 has peptidyl-prolyl isomerase activity but is distinct from cyclophilin. Nature 341, 755-757 (1989).
    • (1989) Nature , vol.341 , pp. 755-757
    • Siekierka, J.J.1    Hung, S.H.2    Poe, M.3    Lin, C.S.4    Sigal, N.H.5
  • 12
    • 0025893168 scopus 로고
    • Calcineurin is a common target of cyclophilin-cyclosporin A and FKBP-FK506 complexes
    • Liu, J. et al. Calcineurin is a common target of cyclophilin-cyclosporin A and FKBP-FK506 complexes. Cell 66, 807-815 (1991).
    • (1991) Cell , vol.66 , pp. 807-815
    • Liu, J.1
  • 13
    • 0025776523 scopus 로고
    • Targets for cell cycle arrest by the immunosuppressant rapamycin in yeast
    • Heitman, J., Movva, N.R. & Hall, M.N. Targets for cell cycle arrest by the immunosuppressant rapamycin in yeast. Science 253, 905-909 (1991).
    • (1991) Science , vol.253 , pp. 905-909
    • Heitman, J.1    Movva, N.R.2    Hall, M.N.3
  • 14
    • 0026575932 scopus 로고
    • The mechanism of action of cyclosporin A and FK506
    • Schreiber, S.L. & Crabtree, G.R. The mechanism of action of cyclosporin A and FK506. Immunol. Today 13, 136-142 (1992).
    • (1992) Immunol. Today , vol.13 , pp. 136-142
    • Schreiber, S.L.1    Crabtree, G.R.2
  • 15
    • 0026857926 scopus 로고
    • Proline isomerases at the crossroads of protein folding, signal transduction, and immunosuppression
    • Heitman, J., Movva, N.R. & Hall, M.N. Proline isomerases at the crossroads of protein folding, signal transduction, and immunosuppression. New Biol. 4, 448-460 (1992).
    • (1992) New Biol , vol.4 , pp. 448-460
    • Heitman, J.1    Movva, N.R.2    Hall, M.N.3
  • 16
    • 0032559238 scopus 로고    scopus 로고
    • Prolyl isomerase and nuclear function
    • Hunter, T. Prolyl isomerase and nuclear function. Cell 92, 141-143 (1998).
    • (1998) Cell , vol.92 , pp. 141-143
    • Hunter, T.1
  • 17
    • 0030692139 scopus 로고    scopus 로고
    • All cyclophilins and FKBPs are dispensible for viability in Saccharomyces cerevisiae
    • Dolinski, K., Muir, S., Cardenas, M. & Heitman, J. All cyclophilins and FKBPs are dispensible for viability in Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA 94, 13093-13098 (1997).
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 13093-13098
    • Dolinski, K.1    Muir, S.2    Cardenas, M.3    Heitman, J.4
  • 18
    • 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. & Zuker, C.S. The ninaA gene required for visual transduction in Drosophila encodes a homologue of cyclosporin A-binding protein. Nature 338, 67-70 (1989).
    • (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
  • 19
    • 0027971782 scopus 로고
    • Functional association of cyclophilin A with HIV-1 virions
    • Thali, M. et al. Functional association of cyclophilin A with HIV-1 virions. Nature 372, 363-365 (1994).
    • (1994) Nature , vol.372 , pp. 363-365
    • Thali, M.1
  • 20
    • 0026710278 scopus 로고
    • Association of a 59-kilodalton immunophilin with the glucocorticoid receptor complex
    • Tai, P.K., Albers, M.W., Chang, H., Faber, L.E. & Schreiber, S.L. Association of a 59-kilodalton immunophilin with the glucocorticoid receptor complex. Science 256, 1315-1318 (1992).
    • (1992) Science , vol.256 , pp. 1315-1318
    • Tai, P.K.1    Albers, M.W.2    Chang, H.3    Faber, L.E.4    Schreiber, S.L.5
  • 21
    • 0028358901 scopus 로고
    • Stabilization of calcium release channel (ryanodine receptor) function by FK506-binding protein
    • Brillantes, A.B. et al. Stabilization of calcium release channel (ryanodine receptor) function by FK506-binding protein. Cell 77, 513-523 (1994).
    • (1994) Cell , vol.77 , pp. 513-523
    • Brillantes, A.B.1
  • 22
    • 0030576525 scopus 로고    scopus 로고
    • The immunophilin FKBP12 functions as a common inhibitor of the TGF beta family type I receptors
    • Wang, T. et al. The immunophilin FKBP12 functions as a common inhibitor of the TGF beta family type I receptors. Cell 86, 435-444 (1996).
    • (1996) Cell , vol.86 , pp. 435-444
    • Wang, T.1
  • 23
    • 0029916122 scopus 로고    scopus 로고
    • A human peptidyl-prolyl isomerase essential for regulation of mitosis
    • Lu, K.P., Hanes, S.D. & Hunter, T. A human peptidyl-prolyl isomerase essential for regulation of mitosis. Nature 380, 544-547 (1996).
    • (1996) Nature , vol.380 , pp. 544-547
    • Lu, K.P.1    Hanes, S.D.2    Hunter, T.3
  • 24
    • 0008233581 scopus 로고    scopus 로고
    • Structural and functional analysis of the mitotic peptidyl-prolyl isomerase Pin1 suggests that substrate recognition is phosphorylation dependent
    • Ranganathan, R., Lu, K.P., Hunter, T. & Noel, J.P. Structural and functional analysis of the mitotic peptidyl-prolyl isomerase Pin1 suggests that substrate recognition is phosphorylation dependent. Cell 89, 875-886 (1997).
    • (1997) Cell , vol.89 , pp. 875-886
    • Ranganathan, R.1    Lu, K.P.2    Hunter, T.3    Noel, J.P.4
  • 25
    • 0040017910 scopus 로고    scopus 로고
    • A function of WW domains as phosphoserineor phosphothreonine-binding modules
    • Lu, P.J., Zhou, X.Z., Shen, M. & Lu, K.P. A function of WW domains as phosphoserineor phosphothreonine-binding modules. Science 283, 1325-1328 (1999).
    • (1999) Science , vol.283 , pp. 1325-1328
    • Lu, P.J.1    Zhou, X.Z.2    Shen, M.3    Lu, K.P.4
  • 26
    • 1842763560 scopus 로고    scopus 로고
    • Pinning down cell signaling, cancer and Alzheimer's disease
    • Lu, K.P. Pinning down cell signaling, cancer and Alzheimer's disease. Trends Biochem. Sci. 29, 200-209 (2004).
    • (2004) Trends Biochem. Sci , vol.29 , pp. 200-209
    • Lu, K.P.1
  • 27
    • 33748029809 scopus 로고    scopus 로고
    • Pin1 in Alzheimer's disease
    • Butterfield, D.A. et al. Pin1 in Alzheimer's disease. J. Neurochem. 98, 1697-1706 (2006).
    • (2006) J. Neurochem , vol.98 , pp. 1697-1706
    • Butterfield, D.A.1
  • 28
    • 33645733774 scopus 로고    scopus 로고
    • Protein twists and turns in Alzheimer disease
    • Maudsley, S. & Mattson, M.P. Protein twists and turns in Alzheimer disease. Nat. Med. 12, 392-393 (2006).
    • (2006) Nat. Med , vol.12 , pp. 392-393
    • Maudsley, S.1    Mattson, M.P.2
  • 29
    • 34247490735 scopus 로고    scopus 로고
    • Pin1, the cell cycle and cancer
    • Yeh, E.S. & Means, A.R. Pin1, the cell cycle and cancer. Nat. Rev. Cancer 7, 381-388 (2007).
    • (2007) Nat. Rev. Cancer , vol.7 , pp. 381-388
    • Yeh, E.S.1    Means, A.R.2
  • 30
    • 22144435913 scopus 로고    scopus 로고
    • Prolyl isomerization as a molecular timer in phage infection
    • Eckert, B., Martin, A., Balbach, J. & Schmid, F.X. Prolyl isomerization as a molecular timer in phage infection. Nat. Struct. Mol. Biol. 12, 619-623 (2005).
    • (2005) Nat. Struct. Mol. Biol , vol.12 , pp. 619-623
    • Eckert, B.1    Martin, A.2    Balbach, J.3    Schmid, F.X.4
  • 31
    • 27744608733 scopus 로고    scopus 로고
    • Cis-trans isomerization at a proline opens the pore of a neurotransmitter-gated ion channel
    • Lummis, S.C. et al. Cis-trans isomerization at a proline opens the pore of a neurotransmitter-gated ion channel. Nature 438, 248-252 (2005).
    • (2005) Nature , vol.438 , pp. 248-252
    • Lummis, S.C.1
  • 32
    • 33748163064 scopus 로고    scopus 로고
    • Proline isomerization of histone H3 regulates lysine methylation and gene expression
    • Nelson, C.J., Santos-Rosa, H. & Kouzarides, T. Proline isomerization of histone H3 regulates lysine methylation and gene expression. Cell 126, 905-916 (2006).
    • (2006) Cell , vol.126 , pp. 905-916
    • Nelson, C.J.1    Santos-Rosa, H.2    Kouzarides, T.3
  • 33
    • 33846688095 scopus 로고    scopus 로고
    • Proline cis-trans isomerization controls autoinhibition of a signaling protein
    • Sarkar, P., Reichman, C., Saleh, T., Birge, R.B. & Kalodimos, C.G. Proline cis-trans isomerization controls autoinhibition of a signaling protein. Mol. Cell 25, 413-426 (2007).
    • (2007) Mol. Cell , vol.25 , pp. 413-426
    • Sarkar, P.1    Reichman, C.2    Saleh, T.3    Birge, R.B.4    Kalodimos, C.G.5
  • 34
    • 0025299887 scopus 로고
    • Occurrence and role of cis peptide bonds in protein structures
    • Stewart, D.E., Sarkar, A. & Wampler, J.E. Occurrence and role of cis peptide bonds in protein structures. J. Mol. Biol. 214, 253-260 (1990).
    • (1990) J. Mol. Biol , vol.214 , pp. 253-260
    • Stewart, D.E.1    Sarkar, A.2    Wampler, J.E.3
  • 35
    • 0033584887 scopus 로고    scopus 로고
    • Cis peptide bonds in proteins: Residues involved, their conformations, interactions and locations
    • Pal, D. & Chakrabarti, P. Cis peptide bonds in proteins: residues involved, their conformations, interactions and locations. J. Mol. Biol. 294, 271-288 (1999).
    • (1999) J. Mol. Biol , vol.294 , pp. 271-288
    • Pal, D.1    Chakrabarti, P.2
  • 36
    • 15844415630 scopus 로고    scopus 로고
    • COPS-cis/trans peptide bond conformation prediction of amino acids on the basis of secondary structure information
    • Pahlke, D., Leitner, D., Wiedemann, U. & Labudde, D. COPS-cis/trans peptide bond conformation prediction of amino acids on the basis of secondary structure information. Bioinformatics 21, 685-686 (2005).
    • (2005) Bioinformatics , vol.21 , pp. 685-686
    • Pahlke, D.1    Leitner, D.2    Wiedemann, U.3    Labudde, D.4
  • 37
    • 19744375512 scopus 로고    scopus 로고
    • Statistically significant dependence of the Xaa-Pro peptide bond conformation on secondary structure and amino acid sequence
    • Pahlke, D., Freund, C., Leitner, D. & Labudde, D. Statistically significant dependence of the Xaa-Pro peptide bond conformation on secondary structure and amino acid sequence. BMC Struct. Biol. 5, 8 (2005).
    • (2005) BMC Struct. Biol , vol.5 , pp. 8
    • Pahlke, D.1    Freund, C.2    Leitner, D.3    Labudde, D.4
  • 38
    • 0025858482 scopus 로고
    • Structure of human cyclophilin and its binding site for cyclosporin A determined by X-ray crystallography and NMR spectroscopy
    • Kallen, J. et al. Structure of human cyclophilin and its binding site for cyclosporin A determined by X-ray crystallography and NMR spectroscopy. Nature 353, 276-279 (1991).
    • (1991) Nature , vol.353 , pp. 276-279
    • Kallen, J.1
  • 39
    • 0025826967 scopus 로고
    • Atomic structure of FKBP-FK506, an immunophilin-immunosuppressant complex
    • Van Duyne, G.D., Standaert, R.F., Karplus, P.A., Schreiber, S.L. & Clardy, J. Atomic structure of FKBP-FK506, an immunophilin-immunosuppressant complex. Science 252, 839-842 (1991).
    • (1991) Science , vol.252 , pp. 839-842
    • Van Duyne, G.D.1    Standaert, R.F.2    Karplus, P.A.3    Schreiber, S.L.4    Clardy, J.5
  • 40
    • 33746408988 scopus 로고    scopus 로고
    • Crystal structure of the PP2A phosphatase activator: Implications for its PP2A-specific PPIase activity
    • Leulliot, N. et al. Crystal structure of the PP2A phosphatase activator: implications for its PP2A-specific PPIase activity. Mol. Cell 23, 413-424 (2006).
    • (2006) Mol. Cell , vol.23 , pp. 413-424
    • Leulliot, N.1
  • 43
    • 33751099086 scopus 로고    scopus 로고
    • Catalytic mechanism of cyclophilin as observed in molecular dynamics simulations: Pathway prediction and reconciliation of X-ray crystallographic and NMR solution data
    • Trzesniak, D. & van Gunsteren, W.F. Catalytic mechanism of cyclophilin as observed in molecular dynamics simulations: pathway prediction and reconciliation of X-ray crystallographic and NMR solution data. Protein Sci. 15, 2544-2551 (2006).
    • (2006) Protein Sci , vol.15 , pp. 2544-2551
    • Trzesniak, D.1    van Gunsteren, W.F.2
  • 44
    • 33947144085 scopus 로고    scopus 로고
    • Structure and dynamics of Pin1 during catalysis by NMR
    • Labeikovsky, W., Eisenmesser, E.Z., Bosco, D.A. & Kern, D. Structure and dynamics of Pin1 during catalysis by NMR. J. Mol. Biol. 367, 1370-1381 (2007).
    • (2007) J. Mol. Biol , vol.367 , pp. 1370-1381
    • Labeikovsky, W.1    Eisenmesser, E.Z.2    Bosco, D.A.3    Kern, D.4
  • 45
    • 28444439801 scopus 로고    scopus 로고
    • Insights into the catalytic mechanism of peptidyl prolyl cis/trans isomerases
    • Fanghanel, J. & Fischer, G. Insights into the catalytic mechanism of peptidyl prolyl cis/trans isomerases. Front. Biosci. 9, 3453-3478 (2004).
    • (2004) Front. Biosci , vol.9 , pp. 3453-3478
    • Fanghanel, J.1    Fischer, G.2
  • 47
    • 0342322902 scopus 로고    scopus 로고
    • Evidence that the substrate backbone conformation is critical to phosphorylation by p42 MAP kinase
    • Weiwad, M., Kullertz, G., Schutkowski, M. & Fischer, G. Evidence that the substrate backbone conformation is critical to phosphorylation by p42 MAP kinase. FEBS Lett. 478, 39-42 (2000).
    • (2000) FEBS Lett , vol.478 , pp. 39-42
    • Weiwad, M.1    Kullertz, G.2    Schutkowski, M.3    Fischer, G.4
  • 48
    • 0033224309 scopus 로고    scopus 로고
    • The structural basis for specificity of substrate and recruitment peptides for cyclin-dependent kinases
    • Brown, N.R., Noble, M.E., Endicott, J.A. & Johnson, L.N. The structural basis for specificity of substrate and recruitment peptides for cyclin-dependent kinases. Nat. Cell Biol. 1, 438-443 (1999).
    • (1999) Nat. Cell Biol , vol.1 , pp. 438-443
    • Brown, N.R.1    Noble, M.E.2    Endicott, J.A.3    Johnson, L.N.4
  • 49
    • 0033638180 scopus 로고    scopus 로고
    • Pin1-dependent prolyl isomerization regulates dephosphorylation of Cdc25C and tau proteins
    • Zhou, X.Z. et al. Pin1-dependent prolyl isomerization regulates dephosphorylation of Cdc25C and tau proteins. Mol. Cell 6, 873-883 (2000).
    • (2000) Mol. Cell , vol.6 , pp. 873-883
    • Zhou, X.Z.1
  • 50
    • 0037169479 scopus 로고    scopus 로고
    • Critical role of WW domain phosphorylation in regulating its phosphoserine-binding activity and the Pin1 function
    • Lu, P.J., Zhou, X.Z., Liou, Y.C., Noel, J.P. & Lu, K.P. Critical role of WW domain phosphorylation in regulating its phosphoserine-binding activity and the Pin1 function. J. Biol. Chem. 277, 2381-2384 (2002).
    • (2002) J. Biol. Chem , vol.277 , pp. 2381-2384
    • Lu, P.J.1    Zhou, X.Z.2    Liou, Y.C.3    Noel, J.P.4    Lu, K.P.5
  • 51
    • 0038342514 scopus 로고    scopus 로고
    • Peptide binding induces large scale changes in inter-domain mobility in human Pin1
    • Jacobs, D.M. et al. Peptide binding induces large scale changes in inter-domain mobility in human Pin1. J. Biol. Chem. 278, 26174-26182 (2003).
    • (2003) J. Biol. Chem , vol.278 , pp. 26174-26182
    • Jacobs, D.M.1
  • 52
    • 22544455987 scopus 로고    scopus 로고
    • Regulation of Pin1 peptidyl-prolyl cis/trans isomerase activity by its WW binding module on a multi-phosphorylated peptide of Tau protein
    • Smet, C., Wieruszeski, J.M., Buee, L., Landrieu, I. & Lippens, G. Regulation of Pin1 peptidyl-prolyl cis/trans isomerase activity by its WW binding module on a multi-phosphorylated peptide of Tau protein. FEBS Lett. 579, 4159-4164 (2005).
    • (2005) FEBS Lett , vol.579 , pp. 4159-4164
    • Smet, C.1    Wieruszeski, J.M.2    Buee, L.3    Landrieu, I.4    Lippens, G.5
  • 53
    • 33847656165 scopus 로고    scopus 로고
    • Substrate recognition reduces side-chain flexibility for conserved hydrophobic residues in human Pin1
    • Namanja, A.T. et al. Substrate recognition reduces side-chain flexibility for conserved hydrophobic residues in human Pin1. Structure 15, 313-327 (2007).
    • (2007) Structure , vol.15 , pp. 313-327
    • Namanja, A.T.1
  • 54
    • 34247180580 scopus 로고    scopus 로고
    • Sequence-specific dynamics modulate recognition specificity in WW domains
    • Peng, T., Zintsmaster, J.S., Namanja, A.T. & Peng, J.W. Sequence-specific dynamics modulate recognition specificity in WW domains. Nat. Struct. Mol. Biol. 14, 325-331 (2007).
    • (2007) Nat. Struct. Mol. Biol , vol.14 , pp. 325-331
    • Peng, T.1    Zintsmaster, J.S.2    Namanja, A.T.3    Peng, J.W.4
  • 55
    • 0036901957 scopus 로고    scopus 로고
    • Cyclin dependent kinases and cell cycle control (Nobel lecture)
    • Nurse, P. Cyclin dependent kinases and cell cycle control (Nobel lecture). ChemBioChem 3, 596-603 (2002).
    • (2002) ChemBioChem , vol.3 , pp. 596-603
    • Nurse, P.1
  • 56
    • 0242300176 scopus 로고    scopus 로고
    • Targets of the cyclin-dependent kinase Cdk1
    • Ubersax, J.A. et al. Targets of the cyclin-dependent kinase Cdk1. Nature 425, 859-864 (2003).
    • (2003) Nature , vol.425 , pp. 859-864
    • Ubersax, J.A.1
  • 57
    • 0034050649 scopus 로고    scopus 로고
    • Requirement of the prolyl isomerase Pin1 for the replication checkpoint
    • Winkler, K.E., Swenson, K.I., Kornbluth, S. & Means, A.R. Requirement of the prolyl isomerase Pin1 for the replication checkpoint. Science 287, 1644-1647 (2000).
    • (2000) Science , vol.287 , pp. 1644-1647
    • Winkler, K.E.1    Swenson, K.I.2    Kornbluth, S.3    Means, A.R.4
  • 58
    • 0035947078 scopus 로고    scopus 로고
    • Pin1 acts catalytically to promote a conformational change in Cdc25
    • Stukenberg, P.T. & Kirschner, M.W. Pin1 acts catalytically to promote a conformational change in Cdc25. Mol. Cell 7, 1071-1083 (2001).
    • (2001) Mol. Cell , vol.7 , pp. 1071-1083
    • Stukenberg, P.T.1    Kirschner, M.W.2
  • 59
    • 0032031634 scopus 로고    scopus 로고
    • The essential mitotic peptidylprolyl isomerase Pin1 binds and regulates mitosis-specific phosphoproteins
    • Shen, M., Stukenberg, P.T., Kirschner, M.W. & Lu, K.P. The essential mitotic peptidylprolyl isomerase Pin1 binds and regulates mitosis-specific phosphoproteins. Genes Dev. 12, 706-720 (1998).
    • (1998) Genes Dev , vol.12 , pp. 706-720
    • Shen, M.1    Stukenberg, P.T.2    Kirschner, M.W.3    Lu, K.P.4
  • 60
    • 0032473350 scopus 로고    scopus 로고
    • The mitotic peptidyl-prolyl isomerase, Pin1, interacts with Cdc25 and Plx1
    • Crenshaw, D.G., Yang, J., Means, A.R. & Kornbluth, S. The mitotic peptidyl-prolyl isomerase, Pin1, interacts with Cdc25 and Plx1. EMBO J. 17, 1315-1327 (1998).
    • (1998) EMBO J , vol.17 , pp. 1315-1327
    • Crenshaw, D.G.1    Yang, J.2    Means, A.R.3    Kornbluth, S.4
  • 61
    • 34247282654 scopus 로고    scopus 로고
    • Mechanism for inactivation of the mitotic inhibitory kinase Wee1 at M phase
    • Okamoto, K. & Sagata, N. Mechanism for inactivation of the mitotic inhibitory kinase Wee1 at M phase. Proc. Natl. Acad. Sci. USA 104, 3753-3758 (2007).
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 3753-3758
    • Okamoto, K.1    Sagata, N.2
  • 62
    • 33846002376 scopus 로고    scopus 로고
    • Pin1 stabilizes Emi1 during G2 phase by preventing its association with SCF(betatrcp)
    • 91-98
    • Bernis, C. et al. Pin1 stabilizes Emi1 during G2 phase by preventing its association with SCF(betatrcp). EMBO Rep. 8, 91-98 (2007).
    • (2007) EMBO Rep , vol.8
    • Bernis, C.1
  • 63
    • 34247196176 scopus 로고    scopus 로고
    • The prolyl isomerase Pin1 functions in mitotic chromosome condensation
    • Xu, Y.X. & Manley, J.L. The prolyl isomerase Pin1 functions in mitotic chromosome condensation. Mol. Cell 26, 287-300 (2007).
    • (2007) Mol. Cell , vol.26 , pp. 287-300
    • Xu, Y.X.1    Manley, J.L.2
  • 64
    • 0035796405 scopus 로고    scopus 로고
    • Pin1 is overexpressed in breast cancer and potentiates the transcriptional activity of phosphorylated c-Jun towards the cyclin D1 gene
    • Wulf, G.M. et al. Pin1 is overexpressed in breast cancer and potentiates the transcriptional activity of phosphorylated c-Jun towards the cyclin D1 gene. EMBO J. 20, 3459-3472 (2001).
    • (2001) EMBO J , vol.20 , pp. 3459-3472
    • Wulf, G.M.1
  • 65
    • 0034840950 scopus 로고    scopus 로고
    • Pin1 regulates turnover and subcellular localization of beta-catenin by inhibiting its interaction with APC
    • Ryo, A., Nakamura, N., Wulf, G., Liou, Y.C. & Lu, K.P. Pin1 regulates turnover and subcellular localization of beta-catenin by inhibiting its interaction with APC. Nat. Cell Biol. 3, 793-801 (2001).
    • (2001) Nat. Cell Biol , vol.3 , pp. 793-801
    • Ryo, A.1    Nakamura, N.2    Wulf, G.3    Liou, Y.C.4    Lu, K.P.5
  • 66
    • 0347955360 scopus 로고    scopus 로고
    • Regulation of NF-kappaB signaling by Pin1-dependent prolyl isomerization and ubiquitin-mediated proteolysis of p65/RelA
    • Ryo, A. et al. Regulation of NF-kappaB signaling by Pin1-dependent prolyl isomerization and ubiquitin-mediated proteolysis of p65/RelA. Mol. Cell 12, 1413-1426 (2003).
    • (2003) Mol. Cell , vol.12 , pp. 1413-1426
    • Ryo, A.1
  • 67
    • 0037022355 scopus 로고    scopus 로고
    • Loss of Pin1 function in the mouse causes phenotypes resembling cyclin D1-null phenotypes
    • Liou, Y.C. et al. Loss of Pin1 function in the mouse causes phenotypes resembling cyclin D1-null phenotypes. Proc. Natl. Acad. Sci. USA 99, 1335-1340 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 1335-1340
    • Liou, Y.C.1
  • 68
    • 2342526543 scopus 로고    scopus 로고
    • A signalling pathway controlling c-Myc degradation that impacts oncogenic transformation of human cells
    • Yeh, E. et al. A signalling pathway controlling c-Myc degradation that impacts oncogenic transformation of human cells. Nat. Cell Biol. 6, 308-318 (2004).
    • (2004) Nat. Cell Biol , vol.6 , pp. 308-318
    • Yeh, E.1
  • 69
    • 33745508920 scopus 로고    scopus 로고
    • Ubiquitylation of cyclin E requires the sequential function of SCF complexes containing distinct hCdc4 isoforms
    • van Drogen, F. et al. Ubiquitylation of cyclin E requires the sequential function of SCF complexes containing distinct hCdc4 isoforms. Mol. Cell 23, 37-48 (2006).
    • (2006) Mol. Cell , vol.23 , pp. 37-48
    • van Drogen, F.1
  • 70
    • 0033619755 scopus 로고    scopus 로고
    • Mice lacking Pin1 develop normally, but are defective in entering cell cycle from G(0) arrest
    • Fujimori, F., Takahashi, K., Uchida, C. & Uchida, T. Mice lacking Pin1 develop normally, but are defective in entering cell cycle from G(0) arrest. Biochem. Biophys. Res. Commun. 265, 658-663 (1999).
    • (1999) Biochem. Biophys. Res. Commun , vol.265 , pp. 658-663
    • Fujimori, F.1    Takahashi, K.2    Uchida, C.3    Uchida, T.4
  • 71
    • 32044460171 scopus 로고    scopus 로고
    • Pin1 regulates centrosome duplication and its overexpression induces centrosome amplification, chromosome instability and oncogenesis
    • Suizu, F., Ryo, A., Wulf, G., Lim, J. & Lu, K.P. Pin1 regulates centrosome duplication and its overexpression induces centrosome amplification, chromosome instability and oncogenesis. Mol. Cell. Biol. 26, 1463-1479 (2006).
    • (2006) Mol. Cell. Biol , vol.26 , pp. 1463-1479
    • Suizu, F.1    Ryo, A.2    Wulf, G.3    Lim, J.4    Lu, K.P.5
  • 72
    • 0036315162 scopus 로고    scopus 로고
    • Pin1 is an E2F target gene essential for the Neu/Ras-induced transformation of mammary epithelial cells
    • Ryo, A. et al. Pin1 is an E2F target gene essential for the Neu/Ras-induced transformation of mammary epithelial cells. Mol. Cell. Biol. 22, 5281-5295 (2002).
    • (2002) Mol. Cell. Biol , vol.22 , pp. 5281-5295
    • Ryo, A.1
  • 73
    • 0035956972 scopus 로고    scopus 로고
    • FKBP12, the 12-kDa FK506-binding protein, is a physiologic regulator of the cell cycle
    • Aghdasi, B. et al. FKBP12, the 12-kDa FK506-binding protein, is a physiologic regulator of the cell cycle. Proc. Natl. Acad. Sci. USA 98, 2425-2430 (2001).
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 2425-2430
    • Aghdasi, B.1
  • 74
    • 19944430124 scopus 로고    scopus 로고
    • Regulation of Raf-1 by direct feedback phosphorylation
    • Dougherty, M.K. et al. Regulation of Raf-1 by direct feedback phosphorylation. Mol. Cell 17, 215-224 (2005).
    • (2005) Mol. Cell , vol.17 , pp. 215-224
    • Dougherty, M.K.1
  • 75
    • 27444440554 scopus 로고    scopus 로고
    • Regulation of the transcriptional activity of c-Fos by ERK. A novel role for the prolyl isomerase Pin1
    • Monje, P., Hernandez-Losa, J., Lyons, R.J., Castellone, M.D. & Gutkind, J.S. Regulation of the transcriptional activity of c-Fos by ERK. A novel role for the prolyl isomerase Pin1. J. Biol. Chem. 280, 35081-35084 (2005).
    • (2005) J. Biol. Chem , vol.280 , pp. 35081-35084
    • Monje, P.1    Hernandez-Losa, J.2    Lyons, R.J.3    Castellone, M.D.4    Gutkind, J.S.5
  • 76
    • 4444309643 scopus 로고    scopus 로고
    • Modeling breast cancer in vivo and ex vivo reveals an essential role of Pin1 in tumorigenesis
    • Wulf, G., Garg, P., Liou, Y.C., Iglehart, D. & Lu, K.P. Modeling breast cancer in vivo and ex vivo reveals an essential role of Pin1 in tumorigenesis. EMBO J. 23, 3397-3407 (2004).
    • (2004) EMBO J , vol.23 , pp. 3397-3407
    • Wulf, G.1    Garg, P.2    Liou, Y.C.3    Iglehart, D.4    Lu, K.P.5
  • 77
    • 0037205007 scopus 로고    scopus 로고
    • The promise and perils of Wnt signaling through beta-catenin
    • Moon, R.T., Bowerman, B., Boutros, M. & Perrimon, N. The promise and perils of Wnt signaling through beta-catenin. Science 296, 1644-1646 (2002).
    • (2002) Science , vol.296 , pp. 1644-1646
    • Moon, R.T.1    Bowerman, B.2    Boutros, M.3    Perrimon, N.4
  • 78
    • 2942588392 scopus 로고    scopus 로고
    • Pin1 overexpression and beta-catenin gene mutations are distinct oncogenic events in human hepatocellular carcinoma
    • Pang, R. et al. Pin1 overexpression and beta-catenin gene mutations are distinct oncogenic events in human hepatocellular carcinoma. Oncogene 23, 4182-4186 (2004).
    • (2004) Oncogene , vol.23 , pp. 4182-4186
    • Pang, R.1
  • 79
    • 31344433667 scopus 로고    scopus 로고
    • Activation of beta-catenin signaling in prostate cancer by peptidylprolyl isomerase Pin1-mediated abrogation of the androgen receptor-beta-catenin interaction
    • Chen, S.Y. et al. Activation of beta-catenin signaling in prostate cancer by peptidylprolyl isomerase Pin1-mediated abrogation of the androgen receptor-beta-catenin interaction. Mol. Cell. Biol. 26, 929-939 (2006).
    • (2006) Mol. Cell. Biol , vol.26 , pp. 929-939
    • Chen, S.Y.1
  • 80
    • 0036895828 scopus 로고    scopus 로고
    • Structural characterization of a proline-driven conformational switch within the Itk SH2 domain
    • Mallis, R.J., Brazin, K.N., Fulton, D.B. & Andreotti, A.H. Structural characterization of a proline-driven conformational switch within the Itk SH2 domain. Nat. Struct. Biol. 9, 900-905 (2002).
    • (2002) Nat. Struct. Biol , vol.9 , pp. 900-905
    • Mallis, R.J.1    Brazin, K.N.2    Fulton, D.B.3    Andreotti, A.H.4
  • 81
    • 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. & Andreotti, A.H. Regulation of the tyrosine kinase Itk by the peptidyl-prolyl isomerase cyclophilin A. Proc. Natl. Acad. Sci. USA 99, 1899-1904 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 1899-1904
    • Brazin, K.N.1    Mallis, R.J.2    Fulton, D.B.3    Andreotti, A.H.4
  • 82
    • 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. et al. Cyclophilin A regulates TCR signal strength in CD4+ T cells via a proline-directed conformational switch in Itk. Immunity 21, 189-201 (2004).
    • (2004) Immunity , vol.21 , pp. 189-201
    • Colgan, J.1
  • 83
    • 33344472738 scopus 로고    scopus 로고
    • Molecular details of Itk activation by prolyl isomerization and phospholigand binding: The NMR structure of the Itk SH2 domain bound to a phosphopeptide
    • Pletneva, E.V., Sundd, M., Fulton, D.B. & Andreotti, A.H. Molecular details of Itk activation by prolyl isomerization and phospholigand binding: the NMR structure of the Itk SH2 domain bound to a phosphopeptide. J. Mol. Biol. 357, 550-561 (2006).
    • (2006) J. Mol. Biol , vol.357 , pp. 550-561
    • Pletneva, E.V.1    Sundd, M.2    Fulton, D.B.3    Andreotti, A.H.4
  • 84
    • 18644384688 scopus 로고    scopus 로고
    • The prolyl isomerase Pin1 is a regulator of p53 in genotoxic response
    • Zheng, H. et al. The prolyl isomerase Pin1 is a regulator of p53 in genotoxic response. Nature 419, 849-853 (2002).
    • (2002) Nature , vol.419 , pp. 849-853
    • Zheng, H.1
  • 85
    • 18644384283 scopus 로고    scopus 로고
    • The prolyl isomerase Pin1 reveals a mechanism to control p53 functions after genotoxic insults
    • Zacchi, P. et al. The prolyl isomerase Pin1 reveals a mechanism to control p53 functions after genotoxic insults. Nature 419, 853-857 (2002).
    • (2002) Nature , vol.419 , pp. 853-857
    • Zacchi, P.1
  • 86
    • 0037073713 scopus 로고    scopus 로고
    • Role of Pin1 in the regulation of p53 stability and p21 transactivation, and cell cycle checkpoints in response to DNA damage
    • Wulf, G.M., Liou, Y.C., Ryo, A., Lee, S.W. & Lu, K.P. Role of Pin1 in the regulation of p53 stability and p21 transactivation, and cell cycle checkpoints in response to DNA damage. J. Biol. Chem. 277, 47976-47979 (2002).
    • (2002) J. Biol. Chem , vol.277 , pp. 47976-47979
    • Wulf, G.M.1    Liou, Y.C.2    Ryo, A.3    Lee, S.W.4    Lu, K.P.5
  • 87
    • 2942547565 scopus 로고    scopus 로고
    • Pin1 links the activities of c-Abl and p300 in regulating p73 function
    • Mantovani, F. et al. Pin1 links the activities of c-Abl and p300 in regulating p73 function. Mol. Cell 14, 625-636 (2004).
    • (2004) Mol. Cell , vol.14 , pp. 625-636
    • Mantovani, F.1
  • 88
    • 0033885803 scopus 로고    scopus 로고
    • Structural basis for phosphoserine-proline recognition by group IV WW domains
    • Verdecia, M.A., Bowman, M.E., Lu, K.P., Hunter, T. & Noel, J.P. Structural basis for phosphoserine-proline recognition by group IV WW domains. Nat. Struct. Biol. 7, 639-643 (2000).
    • (2000) Nat. Struct. Biol , vol.7 , pp. 639-643
    • Verdecia, M.A.1    Bowman, M.E.2    Lu, K.P.3    Hunter, T.4    Noel, J.P.5
  • 89
    • 0034679626 scopus 로고    scopus 로고
    • The Ess1 prolyl isomerase is linked to chromatin remodeling complexes and the general transcription machinery
    • Wu, X. et al. The Ess1 prolyl isomerase is linked to chromatin remodeling complexes and the general transcription machinery. EMBO J. 19, 3727-3738 (2000).
    • (2000) EMBO J , vol.19 , pp. 3727-3738
    • Wu, X.1
  • 90
    • 0037181170 scopus 로고    scopus 로고
    • Pin1 enhances the dephosphorylation of the C-terminal domain of the RNA polymerase II by Fcp1
    • Kops, O., Zhou, X.Z. & Lu, K.P. Pin1 enhances the dephosphorylation of the C-terminal domain of the RNA polymerase II by Fcp1. FEBS Lett. 513, 305-311 (2002).
    • (2002) FEBS Lett , vol.513 , pp. 305-311
    • Kops, O.1    Zhou, X.Z.2    Lu, K.P.3
  • 91
    • 0344011538 scopus 로고    scopus 로고
    • Pin1 modulates the structure and function of human RNA polymerase II
    • Xu, Y.X., Hirose, Y., Zhou, X.Z., Lu, K.P. & Manley, J.L. Pin1 modulates the structure and function of human RNA polymerase II. Genes Dev. 17, 2765-2776 (2003).
    • (2003) Genes Dev , vol.17 , pp. 2765-2776
    • Xu, Y.X.1    Hirose, Y.2    Zhou, X.Z.3    Lu, K.P.4    Manley, J.L.5
  • 92
    • 0031615108 scopus 로고    scopus 로고
    • Point mutations in v-Myb disrupt a cyclophilin-catalyzed negative regulatory mechanism
    • Leverson, J.D. & Ness, S.A. Point mutations in v-Myb disrupt a cyclophilin-catalyzed negative regulatory mechanism. Mol. Cell 1, 203-211 (1998).
    • (1998) Mol. Cell , vol.1 , pp. 203-211
    • Leverson, J.D.1    Ness, S.A.2
  • 93
    • 30044436160 scopus 로고    scopus 로고
    • The peptidyl-prolyl isomerase Pin1 regulates the stability of granulocyte-macrophage colony-stimulating factor mRNA in activated eosinophils
    • Shen, Z.J., Esnault, S. & Malter, J.S. The peptidyl-prolyl isomerase Pin1 regulates the stability of granulocyte-macrophage colony-stimulating factor mRNA in activated eosinophils. Nat. Immunol. 6, 1280-1287 (2005).
    • (2005) Nat. Immunol , vol.6 , pp. 1280-1287
    • Shen, Z.J.1    Esnault, S.2    Malter, J.S.3
  • 94
    • 33744499683 scopus 로고    scopus 로고
    • Negative regulation of interferon-regulatory factor 3-dependent innate antiviral response by the prolyl isomerase Pin1
    • Saitoh, T. et al. Negative regulation of interferon-regulatory factor 3-dependent innate antiviral response by the prolyl isomerase Pin1. Nat. Immunol. 7, 598-605 (2006).
    • (2006) Nat. Immunol , vol.7 , pp. 598-605
    • Saitoh, T.1
  • 95
    • 34548693416 scopus 로고    scopus 로고
    • Pin1 modulates the type 1 immune response
    • Esnault, S. et al. Pin1 modulates the type 1 immune response. PLoS ONE 2, e226 (2007).
    • (2007) PLoS ONE , vol.2
    • Esnault, S.1
  • 96
    • 33745830461 scopus 로고    scopus 로고
    • Regulation of Bruton's tyrosine kinase (Btk) by the peptidyl-prolyl isomerase Pin1
    • Yu, L. et al. Regulation of Bruton's tyrosine kinase (Btk) by the peptidyl-prolyl isomerase Pin1. J. Biol. Chem. 281, 18201-18207 (2006).
    • (2006) J. Biol. Chem , vol.281 , pp. 18201-18207
    • Yu, L.1
  • 97
    • 22244476202 scopus 로고    scopus 로고
    • Role of cyclophilin B in activation of interferon regulatory factor-3
    • Obata, Y. et al. Role of cyclophilin B in activation of interferon regulatory factor-3. J. Biol. Chem. 280, 18355-18360 (2005).
    • (2005) J. Biol. Chem , vol.280 , pp. 18355-18360
    • Obata, Y.1
  • 98
    • 0032142911 scopus 로고    scopus 로고
    • Immunophilins in the nervous system
    • Snyder, S.H., Lai, M.M. & Burnett, P.E. Immunophilins in the nervous system. Neuron 21, 283-294 (1998).
    • (1998) Neuron , vol.21 , pp. 283-294
    • Snyder, S.H.1    Lai, M.M.2    Burnett, P.E.3
  • 99
    • 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. & Zuker, C.S. 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).
    • (1994) EMBO J , vol.13 , pp. 4886-4895
    • Baker, E.K.1    Colley, N.J.2    Zuker, C.S.3
  • 100
    • 0037149508 scopus 로고    scopus 로고
    • Oestrogen protects FKBP12.6 null mice from cardiac hypertrophy
    • Xin, H.B. et al. Oestrogen protects FKBP12.6 null mice from cardiac hypertrophy. Nature 416, 334-338 (2002).
    • (2002) Nature , vol.416 , pp. 334-338
    • Xin, H.B.1
  • 101
    • 0037708928 scopus 로고    scopus 로고
    • FKBP12.6 deficiency and defective calcium release channel (ryanodine receptor) function linked to exercise-induced sudden cardiac death
    • Wehrens, X.H. et al. FKBP12.6 deficiency and defective calcium release channel (ryanodine receptor) function linked to exercise-induced sudden cardiac death. Cell 113, 829-840 (2003).
    • (2003) Cell , vol.113 , pp. 829-840
    • Wehrens, X.H.1
  • 102
    • 0033057483 scopus 로고    scopus 로고
    • The role of immunophilins in mutant superoxide dismutase-1linked familial amyotrophic lateral sclerosis
    • Lee, J.P. et al. The role of immunophilins in mutant superoxide dismutase-1linked familial amyotrophic lateral sclerosis. Proc. Natl. Acad. Sci. USA 96, 3251-3256 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 3251-3256
    • Lee, J.P.1
  • 103
    • 0031594542 scopus 로고    scopus 로고
    • Neural actions of immunophilin ligands
    • Snyder, S.H. et al. Neural actions of immunophilin ligands. Trends Pharmacol. Sci. 19, 21-26 (1998).
    • (1998) Trends Pharmacol. Sci , vol.19 , pp. 21-26
    • Snyder, S.H.1
  • 105
    • 0034327611 scopus 로고    scopus 로고
    • Hinges, swivels and switches: The role of prolines in signalling via transmembrane alpha-helices
    • Sansom, M.S. & Weinstein, H. Hinges, swivels and switches: the role of prolines in signalling via transmembrane alpha-helices. Trends Pharmacol. Sci. 21, 445-451 (2000).
    • (2000) Trends Pharmacol. Sci , vol.21 , pp. 445-451
    • Sansom, M.S.1    Weinstein, H.2
  • 106
    • 0037322816 scopus 로고    scopus 로고
    • Proline-directed phosphorylation and isomerization in mitotic regulation and in Alzheimer's disease
    • Lu, K.P., Liou, Y.C. & Vincent, I. Proline-directed phosphorylation and isomerization in mitotic regulation and in Alzheimer's disease. Bioessays 25, 174-181 (2003).
    • (2003) Bioessays , vol.25 , pp. 174-181
    • Lu, K.P.1    Liou, Y.C.2    Vincent, I.3
  • 107
    • 33947289969 scopus 로고    scopus 로고
    • Cell division in the CNS: Protective response or lethal event in post-mitotic neurons?
    • Yang, Y. & Herrup, K. Cell division in the CNS: protective response or lethal event in post-mitotic neurons? Biochim. Biophys. Acta 1772, 457-466 (2007).
    • (2007) Biochim. Biophys. Acta , vol.1772 , pp. 457-466
    • Yang, Y.1    Herrup, K.2
  • 108
    • 0028295848 scopus 로고
    • Cell cycle-dependent regulation of the phosphorylation and metabolism of the Alzheimer amyloid precursor protein
    • Suzuki, T. et al. Cell cycle-dependent regulation of the phosphorylation and metabolism of the Alzheimer amyloid precursor protein. EMBO J. 13, 1114-1122 (1994).
    • (1994) EMBO J , vol.13 , pp. 1114-1122
    • Suzuki, T.1
  • 109
    • 0142123260 scopus 로고    scopus 로고
    • APP processing is regulated by cytoplasmic phosphorylation
    • Lee, M.S. et al. APP processing is regulated by cytoplasmic phosphorylation. J. Cell Biol. 163, 83-95 (2003).
    • (2003) J. Cell Biol , vol.163 , pp. 83-95
    • Lee, M.S.1
  • 110
    • 0033600242 scopus 로고    scopus 로고
    • The prolyl isomerase Pin1 restores the function of Alzheimer-associated phosphorylated tau protein
    • Lu, P.J., Wulf, G., Zhou, X.Z., Davies, P. & Lu, K.P. The prolyl isomerase Pin1 restores the function of Alzheimer-associated phosphorylated tau protein. Nature 399, 784-788 (1999).
    • (1999) Nature , vol.399 , pp. 784-788
    • Lu, P.J.1    Wulf, G.2    Zhou, X.Z.3    Davies, P.4    Lu, K.P.5
  • 111
    • 5144224351 scopus 로고    scopus 로고
    • Shortfalls in the peptidyl-prolyl cis-trans isomerase protein Pin1 in neurons are associated with frontotemporal dementias
    • Thorpe, J.R. et al. Shortfalls in the peptidyl-prolyl cis-trans isomerase protein Pin1 in neurons are associated with frontotemporal dementias. Neurobiol. Dis. 17, 237-249 (2004).
    • (2004) Neurobiol. Dis , vol.17 , pp. 237-249
    • Thorpe, J.R.1
  • 112
    • 33745095542 scopus 로고    scopus 로고
    • Pin1 allows for differential Tau dephosphorylation in neuronal cells
    • Hamdane, M. et al. Pin1 allows for differential Tau dephosphorylation in neuronal cells. Mol. Cell. Neurosci. 32, 155-160 (2006).
    • (2006) Mol. Cell. Neurosci , vol.32 , pp. 155-160
    • Hamdane, M.1
  • 113
    • 33646511135 scopus 로고    scopus 로고
    • Oxidative modification and down-regulation of Pin1 in Alzheimer's disease hippocampus: A redox proteomics analysis
    • Sultana, R. et al. Oxidative modification and down-regulation of Pin1 in Alzheimer's disease hippocampus: a redox proteomics analysis. Neurobiol. Aging 27, 918-925 (2006).
    • (2006) Neurobiol. Aging , vol.27 , pp. 918-925
    • Sultana, R.1
  • 114
    • 33751327516 scopus 로고    scopus 로고
    • Pin1 promoter polymorphisms are associated with Alzheimer's disease
    • Segat, L. et al. Pin1 promoter polymorphisms are associated with Alzheimer's disease. Neurobiol. Aging 28, 69-74 (2007).
    • (2007) Neurobiol. Aging , vol.28 , pp. 69-74
    • Segat, L.1
  • 115
    • 34247867974 scopus 로고    scopus 로고
    • Nowotny, P. et al. Association studies between common variants in prolyl isomerase Pin1 and the risk for late-onset Alzheimer's disease. Neurosci. Lett. 419, 15-17 (2007).
    • Nowotny, P. et al. Association studies between common variants in prolyl isomerase Pin1 and the risk for late-onset Alzheimer's disease. Neurosci. Lett. 419, 15-17 (2007).
  • 116
    • 0043069764 scopus 로고    scopus 로고
    • Role of the prolyl isomerase Pin1 in protecting against age-dependent neurodegeneration
    • Liou, Y.-C. et al. Role of the prolyl isomerase Pin1 in protecting against age-dependent neurodegeneration. Nature 424, 556-561 (2003).
    • (2003) Nature , vol.424 , pp. 556-561
    • Liou, Y.-C.1
  • 117
    • 0035970301 scopus 로고    scopus 로고
    • Phosphorylation-induced structural changes in the amyloid precursor protein cytoplasmic tail detected by NMR
    • Ramelot, T.A. & Nicholson, L.K. Phosphorylation-induced structural changes in the amyloid precursor protein cytoplasmic tail detected by NMR. J. Mol. Biol. 307, 871-884 (2001).
    • (2001) J. Mol. Biol , vol.307 , pp. 871-884
    • Ramelot, T.A.1    Nicholson, L.K.2
  • 118
    • 33645300736 scopus 로고    scopus 로고
    • The prolyl isomerase Pin1 regulates amyloid precursor protein processing and amyloid-beta production
    • Pastorino, L. et al. The prolyl isomerase Pin1 regulates amyloid precursor protein processing and amyloid-beta production. Nature 440, 528-534 (2006).
    • (2006) Nature , vol.440 , pp. 528-534
    • Pastorino, L.1
  • 119
    • 24644444767 scopus 로고    scopus 로고
    • Pin1 promotes production of Alzheimer's amyloid beta from beta-cleaved amyloid precursor protein
    • Akiyama, H., Shin, R.W., Uchida, C., Kitamoto, T. & Uchida, T. Pin1 promotes production of Alzheimer's amyloid beta from beta-cleaved amyloid precursor protein. Biochem. Biophys. Res. Commun. 336, 521-529 (2005).
    • (2005) Biochem. Biophys. Res. Commun , vol.336 , pp. 521-529
    • Akiyama, H.1    Shin, R.W.2    Uchida, C.3    Kitamoto, T.4    Uchida, T.5
  • 120
    • 0036303818 scopus 로고    scopus 로고
    • Genetically engineered mouse models of neurodegenerative diseases
    • Wong, P.C., Cai, H., Borchelt, D.R. & Price, D.L. Genetically engineered mouse models of neurodegenerative diseases. Nat. Neurosci. 5, 633-639 (2002).
    • (2002) Nat. Neurosci , vol.5 , pp. 633-639
    • Wong, P.C.1    Cai, H.2    Borchelt, D.R.3    Price, D.L.4
  • 121
    • 0344688272 scopus 로고    scopus 로고
    • Tau phosphorylation, tangles, and neurodegeneration: The chicken or the egg
    • Geschwind, D.H. Tau phosphorylation, tangles, and neurodegeneration: the chicken or the egg. Neuron 40, 457-460 (2003).
    • (2003) Neuron , vol.40 , pp. 457-460
    • Geschwind, D.H.1
  • 122
    • 34247204919 scopus 로고    scopus 로고
    • Post-phosphorylation prolyl isomerisation of gephyrin represents a mechanism to modulate glycine receptors function
    • Zita, M.M. et al. Post-phosphorylation prolyl isomerisation of gephyrin represents a mechanism to modulate glycine receptors function. EMBO J. 26, 1761-1771 (2007).
    • (2007) EMBO J , vol.26 , pp. 1761-1771
    • Zita, M.M.1
  • 123
    • 34548671392 scopus 로고    scopus 로고
    • Activation of JNK3 after injury induces cytochrome C release by facilitating Pin1-dependent degradation of Mcl-1
    • Li, Q.M. et al. Activation of JNK3 after injury induces cytochrome C release by facilitating Pin1-dependent degradation of Mcl-1. J. Neurosci. 27, 8395-8404 (2007).
    • (2007) J. Neurosci , vol.27 , pp. 8395-8404
    • Li, Q.M.1
  • 124
    • 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. & Luban, J. 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).
    • (1996) J. Virol , vol.70 , pp. 3551-3560
    • Braaten, D.1    Franke, E.K.2    Luban, J.3
  • 125
    • 0141796317 scopus 로고    scopus 로고
    • Cyclophilin A modulates the sensitivity of HIV-1 to host restriction factors
    • Towers, G.J. et al. Cyclophilin A modulates the sensitivity of HIV-1 to host restriction factors. Nat. Med. 9, 1138-1143 (2003).
    • (2003) Nat. Med , vol.9 , pp. 1138-1143
    • Towers, G.J.1
  • 126
    • 0037427448 scopus 로고    scopus 로고
    • Evolutionary stabilization of the gene-3-protein of phage fd reveals the principles that govern the thermodynamic stability of two-domain proteins
    • Martin, A. & Schmid, F.X. Evolutionary stabilization of the gene-3-protein of phage fd reveals the principles that govern the thermodynamic stability of two-domain proteins. J. Mol. Biol. 328, 863-875 (2003).
    • (2003) J. Mol. Biol , vol.328 , pp. 863-875
    • Martin, A.1    Schmid, F.X.2
  • 127
    • 0002543237 scopus 로고
    • Fundamental dimensions of polypeptide chains
    • Corey, R.B. & Pauling, L. Fundamental dimensions of polypeptide chains. Proc. R. Soc. Lond. B 141, 10-20 (1953).
    • (1953) Proc. R. Soc. Lond. B , vol.141 , pp. 10-20
    • Corey, R.B.1    Pauling, L.2
  • 128
    • 0035126518 scopus 로고    scopus 로고
    • Linus Pauling and the planar peptide bond
    • Edison, A.S. Linus Pauling and the planar peptide bond. Nat. Struct. Biol. 8, 201-202 (2001).
    • (2001) Nat. Struct. Biol , vol.8 , pp. 201-202
    • Edison, A.S.1
  • 129
    • 84985715908 scopus 로고
    • NMR studies of the rates of proline cis-trans isomerization in oligopeptides
    • Christoph, C. & Wuthrich, K. NMR studies of the rates of proline cis-trans isomerization in oligopeptides. Biopolymers 20, 2623-2633 (1981).
    • (1981) Biopolymers , vol.20 , pp. 2623-2633
    • Christoph, C.1    Wuthrich, K.2
  • 130
    • 0025868143 scopus 로고
    • Determination of kinetic constants for peptidyl prolyl cis-trans isomerases by an improved spectrophotometric assay
    • Kofron, J.L., Kuzmic, P., Kishore, V., Colon-Bonilla, E. & Rich, D.H. Determination of kinetic constants for peptidyl prolyl cis-trans isomerases by an improved spectrophotometric assay. Biochemistry 30, 6127-6134 (1991).
    • (1991) Biochemistry , vol.30 , pp. 6127-6134
    • Kofron, J.L.1    Kuzmic, P.2    Kishore, V.3    Colon-Bonilla, E.4    Rich, D.H.5
  • 131
    • 0026649497 scopus 로고
    • PPIase catalysis by human FK506-binding protein proceeds through a conformational twist mechanism
    • Park, S.T., Aldape, R.A., Futer, O., DeCenzo, M.T. & Livingston, D.J. PPIase catalysis by human FK506-binding protein proceeds through a conformational twist mechanism. J. Biol. Chem. 267, 3316-3324 (1992).
    • (1992) J. Biol. Chem , vol.267 , pp. 3316-3324
    • Park, S.T.1    Aldape, R.A.2    Futer, O.3    DeCenzo, M.T.4    Livingston, D.J.5
  • 132
    • 0000535768 scopus 로고
    • Solvent effects on the energetics of prolyl peptide bond isomerization
    • Eberhardt, E.S., Loh, S.N., Hinck, A.P. & Raines, R.T. Solvent effects on the energetics of prolyl peptide bond isomerization. J. Am. Chem. Soc. 114, 5437-5439 (1992).
    • (1992) J. Am. Chem. Soc , vol.114 , pp. 5437-5439
    • Eberhardt, E.S.1    Loh, S.N.2    Hinck, A.P.3    Raines, R.T.4
  • 133
    • 0017773191 scopus 로고
    • Theoretical studies of environmental effects on protein conformation. 1. Flexibility of the peptide bond
    • Scheiner, S. & Kern, C.W. Theoretical studies of environmental effects on protein conformation. 1. Flexibility of the peptide bond. J. Am. Chem. Soc. 99, 7042-7050 (1977).
    • (1977) J. Am. Chem. Soc , vol.99 , pp. 7042-7050
    • Scheiner, S.1    Kern, C.W.2
  • 134
    • 0031194998 scopus 로고    scopus 로고
    • FKBP-like catalysis of peptidyl-prolyl bond isomerization by micelles and membranes
    • Kramer, M.L. & Fischer, G. FKBP-like catalysis of peptidyl-prolyl bond isomerization by micelles and membranes. Biopolymers 42, 49-60 (1997).
    • (1997) Biopolymers , vol.42 , pp. 49-60
    • Kramer, M.L.1    Fischer, G.2
  • 135
    • 0032560498 scopus 로고    scopus 로고
    • Antibody catalysis of peptidyl-prolyl cis-trans isomerization in the folding of RNase T1
    • Ma, L., Hsieh-Wilson, L.C. & Schultz, P.G. Antibody catalysis of peptidyl-prolyl cis-trans isomerization in the folding of RNase T1. Proc. Natl. Acad. Sci. USA 95, 7251-7256 (1998).
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 7251-7256
    • Ma, L.1    Hsieh-Wilson, L.C.2    Schultz, P.G.3
  • 136
    • 0029999156 scopus 로고    scopus 로고
    • Catalytic antibodies with peptidyl-prolyl cis-trans isomerase activity
    • Yli-Kauhaluoma, J.T. et al. Catalytic antibodies with peptidyl-prolyl cis-trans isomerase activity. J. Am. Chem. Soc. 118, 5496-5497 (1996).
    • (1996) J. Am. Chem. Soc , vol.118 , pp. 5496-5497
    • Yli-Kauhaluoma, J.T.1
  • 137
    • 0027742843 scopus 로고
    • A mechanism for rotamase catalysis by the FK506 binding protein (FKBP)
    • Fischer, S., Michnick, S. & Karplus, M. A mechanism for rotamase catalysis by the FK506 binding protein (FKBP). Biochemistry 32, 13830-13837 (1993).
    • (1993) Biochemistry , vol.32 , pp. 13830-13837
    • Fischer, S.1    Michnick, S.2    Karplus, M.3


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