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Volumn 13, Issue 7, 2007, Pages 475-480

Multimer formation by FKBP-12: Roles for cysteine 23 and phenylalanine 36

Author keywords

cis trans peptidylprolyl isomerase; Dimer; Disulfide bonds; FKBP 12; IP3 receptor; Ryanodine receptor; TGF receptor

Indexed keywords

AMINO ACID; CYSTEINE 23; DIMER; FK 506 BINDING PROTEIN; FK 506 BINDING PROTEIN 12; INOSITOL 1,4,5 TRISPHOSPHATE RECEPTOR; PEPTIDYLPROLYL ISOMERASE; PHENYLALANINE 36; RAPAMYCIN; RYANODINE; RYANODINE RECEPTOR; TACROLIMUS; TRANSFORMING GROWTH FACTOR BETA; UNCLASSIFIED DRUG;

EID: 34447581208     PISSN: 10752617     EISSN: 10991387     Source Type: Journal    
DOI: 10.1002/psc.871     Document Type: Article
Times cited : (4)

References (26)
  • 1
    • 0025635897 scopus 로고
    • The cytosolic-binding protein for the immunosuppressant FK-506 is both a ubiquitous and highly conserved peptidyl-prolyl cis-trans isomerase
    • Siekierka JJ, Wiederrecht G, Greulich H, Boulton D, Hung SHY, Cryan J, Hodges PJ, Sigal NH. The cytosolic-binding protein for the immunosuppressant FK-506 is both a ubiquitous and highly conserved peptidyl-prolyl cis-trans isomerase. J. Biol. Chem. 1990; 265: 21011-21015.
    • (1990) J. Biol. Chem , vol.265 , pp. 21011-21015
    • Siekierka, J.J.1    Wiederrecht, G.2    Greulich, H.3    Boulton, D.4    Hung, S.H.Y.5    Cryan, J.6    Hodges, P.J.7    Sigal, N.H.8
  • 2
    • 0029867394 scopus 로고    scopus 로고
    • Structure-function relationships in the FK506-binding protein (FKBP) family of peptidylprolyl cis-trans isomerases
    • Kay JE. Structure-function relationships in the FK506-binding protein (FKBP) family of peptidylprolyl cis-trans isomerases. Biochem. J. 1996; 314: 361-385.
    • (1996) Biochem. J , vol.314 , pp. 361-385
    • Kay, J.E.1
  • 3
    • 0025893168 scopus 로고
    • Calcineurin is a common target of cyclophilin-cyclosporin A and FKBP-FK506 complexes
    • Liu J, Farmer JD Jr, Lane WS, Friedman J, Weissman I, Schreiber SL. Calcineurin is a common target of cyclophilin-cyclosporin A and FKBP-FK506 complexes. Cell 1991; 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
  • 4
    • 0026503434 scopus 로고
    • Calcineurin phosphatase activity in T lymphocytes is inhibited by FK 506 and cyclosporin A
    • Fruman DA, Klee CB, Bierer BE, Burakoff SJ. Calcineurin phosphatase activity in T lymphocytes is inhibited by FK 506 and cyclosporin A. Proc. Natl. Acad. Sci. U.S.A. 1992; 89: 3686-3690.
    • (1992) Proc. Natl. Acad. Sci. U.S.A , vol.89 , pp. 3686-3690
    • Fruman, D.A.1    Klee, C.B.2    Bierer, B.E.3    Burakoff, S.J.4
  • 6
    • 15844391440 scopus 로고    scopus 로고
    • Mechanism of action of the immunosuppressant rapamycin
    • Dumont FJ, Su Q. Mechanism of action of the immunosuppressant rapamycin. Life Sci. 1996; 58: 373-395.
    • (1996) Life Sci , vol.58 , pp. 373-395
    • Dumont, F.J.1    Su, Q.2
  • 7
    • 0025302066 scopus 로고
    • Inhibition of FKBP rotamase activity by immunosuppressant FK506: Twisted amide surrogate
    • Rosen MF, Standaert RF, Galat A, Nakatsuka M, Schreiber SL. Inhibition of FKBP rotamase activity by immunosuppressant FK506: twisted amide surrogate. Science 1990; 248: 863-866.
    • (1990) Science , vol.248 , pp. 863-866
    • Rosen, M.F.1    Standaert, R.F.2    Galat, A.3    Nakatsuka, M.4    Schreiber, S.L.5
  • 10
  • 11
    • 0030784252 scopus 로고    scopus 로고
    • FKBP12 binds to the inositol 1,4,5-triphosphate receptor at leucine-proline (1400-1401) and anchors calcineurin to this FK506-like domain
    • Cameron AM, Nucifora FC, Fung ET, Livingston DJ, Aldape RA, Ross CA, Snyder SH. FKBP12 binds to the inositol 1,4,5-triphosphate receptor at leucine-proline (1400-1401) and anchors calcineurin to this FK506-like domain. J. Biol. Chem. 1997; 272: 27582-27588.
    • (1997) J. Biol. Chem , vol.272 , pp. 27582-27588
    • Cameron, A.M.1    Nucifora, F.C.2    Fung, E.T.3    Livingston, D.J.4    Aldape, R.A.5    Ross, C.A.6    Snyder, S.H.7
  • 14
    • 0028836746 scopus 로고
    • Characterization of an exchange reaction between soluble FKBP-12 and the FKBP-ryanodine receptor complex. Modulation by FKBP mutants deficient in peptidyl-prolyl isomerase activity
    • Timerman AP, Wiederrecht G, Marcy A, Fleischer S. Characterization of an exchange reaction between soluble FKBP-12 and the FKBP-ryanodine receptor complex. Modulation by FKBP mutants deficient in peptidyl-prolyl isomerase activity. J. Biol. Chem. 1995; 270: 2451-2459.
    • (1995) J. Biol. Chem , vol.270 , pp. 2451-2459
    • Timerman, A.P.1    Wiederrecht, G.2    Marcy, A.3    Fleischer, S.4
  • 15
    • 0025061678 scopus 로고
    • Molecular cloning and overexpression of the human FK506-binding protein FKBP
    • Standaert RF, Galat A, Verdine GL, Schreiber SL. Molecular cloning and overexpression of the human FK506-binding protein FKBP. Nature 1990; 346: 671-674.
    • (1990) Nature , vol.346 , pp. 671-674
    • Standaert, R.F.1    Galat, A.2    Verdine, G.L.3    Schreiber, S.L.4
  • 16
    • 0023820854 scopus 로고
    • 2+ release by skeletal muscle sarcoplasmic reticulum: Differing sensitivity to inhalational anesthetics
    • 2+ release by skeletal muscle sarcoplasmic reticulum: differing sensitivity to inhalational anesthetics. Anesthesiology 1988; 69: 571-577.
    • (1988) Anesthesiology , vol.69 , pp. 571-577
    • Nelson, T.E.1    Sweo, T.2
  • 21
    • 0028074989 scopus 로고
    • A homodimer represents an active species of the peptidyl-prolyl cis/ trans isomerase FKBP25mem from Legionella pneumophila
    • Schmidt B, Rahfeld J, Schierhorn A, Ludwig B, Hacker J, Fischer G. A homodimer represents an active species of the peptidyl-prolyl cis/ trans isomerase FKBP25mem from Legionella pneumophila. FEBS Lett. 1994; 352: 185-190.
    • (1994) FEBS Lett , vol.352 , pp. 185-190
    • Schmidt, B.1    Rahfeld, J.2    Schierhorn, A.3    Ludwig, B.4    Hacker, J.5    Fischer, G.6
  • 22
    • 0022409022 scopus 로고
    • Electron spin resonance studies of intact mammalian skeletal muscle
    • Jackson MJ, Edwards RHT, Symons MCR. Electron spin resonance studies of intact mammalian skeletal muscle. Biochim. Biophys. Acta 1985; 847: 185-190.
    • (1985) Biochim. Biophys. Acta , vol.847 , pp. 185-190
    • Jackson, M.J.1    Edwards, R.H.T.2    Symons, M.C.R.3
  • 25
    • 33846003833 scopus 로고    scopus 로고
    • Identification of cysteines involved in S-nitrosylation, S-glutathionylation, and oxidation to disulfides in ryanodine receptor type 1
    • Aracena-Parks P, Goonasekera SA, Gilman CP, Dirksen RT, Hidalgo C, Hamilton SL. Identification of cysteines involved in S-nitrosylation, S-glutathionylation, and oxidation to disulfides in ryanodine receptor type 1. J. Biol. Chem. 2006; 281: 40354-40368.
    • (2006) J. Biol. Chem , vol.281 , pp. 40354-40368
    • Aracena-Parks, P.1    Goonasekera, S.A.2    Gilman, C.P.3    Dirksen, R.T.4    Hidalgo, C.5    Hamilton, S.L.6
  • 26
    • 34147092002 scopus 로고    scopus 로고
    • Redox sensitivity of the ryanodine receptor interaction with FK506-binding protein
    • Zissimopoulos S, Docrat N, Lai FA. Redox sensitivity of the ryanodine receptor interaction with FK506-binding protein. J. Biol. Chem. 2007; 282: 6976-6983.
    • (2007) J. Biol. Chem , vol.282 , pp. 6976-6983
    • Zissimopoulos, S.1    Docrat, N.2    Lai, F.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.