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Volumn 227, Issue 12, 2012, Pages 3768-3777

Protein sequences involved in the mitochondrial import of the 3,5,3′-L-triiodothyronine receptor p43

Author keywords

[No Author keywords available]

Indexed keywords

COLECALCIFEROL; CYTOSOL RECEPTOR; ESTROGEN; GLUCOCORTICOID; LIOTHYRONINE; PROTEIN P43; TYLOXAPOL;

EID: 84865408112     PISSN: 00219541     EISSN: 10974652     Source Type: Journal    
DOI: 10.1002/jcp.24085     Document Type: Article
Times cited : (12)

References (49)
  • 1
    • 0030692798 scopus 로고    scopus 로고
    • Chicken thyroid hormone receptor alpha requires the N-terminal amino acids for exclusive nuclear localization
    • Andersson ML, Vennström B. 1997. Chicken thyroid hormone receptor alpha requires the N-terminal amino acids for exclusive nuclear localization. FEBS Lett 416: 291-296.
    • (1997) FEBS Lett , vol.416 , pp. 291-296
    • Andersson, M.L.1    Vennström, B.2
  • 2
    • 0030272378 scopus 로고    scopus 로고
    • Role of Tim23 as voltage sensor and presequence receptor in protein import into mitochondria
    • Bauer MF, Sirrenberg C, Neupert W, Brunner M. 1996. Role of Tim23 as voltage sensor and presequence receptor in protein import into mitochondria. Cell 87: 33-41.
    • (1996) Cell , vol.87 , pp. 33-41
    • Bauer, M.F.1    Sirrenberg, C.2    Neupert, W.3    Brunner, M.4
  • 3
    • 0023791461 scopus 로고
    • c-ErbA encodes multiple proteins in chicken erythroid cells
    • Bigler J, Eisenman RN. 1988. c-ErbA encodes multiple proteins in chicken erythroid cells. Mol Cell Biol 8: 4155-4161.
    • (1988) Mol Cell Biol , vol.8 , pp. 4155-4161
    • Bigler, J.1    Eisenman, R.N.2
  • 4
    • 0026665611 scopus 로고
    • Thyroid hormone receptor transcriptional activity is potentially autoregulated by truncated forms of the receptor
    • Bigler J, Hokanson W, Eisenman RN. 1992. Thyroid hormone receptor transcriptional activity is potentially autoregulated by truncated forms of the receptor. Mol Cell Biol 12: 2406-2417.
    • (1992) Mol Cell Biol , vol.12 , pp. 2406-2417
    • Bigler, J.1    Hokanson, W.2    Eisenman, R.N.3
  • 5
    • 0037160054 scopus 로고    scopus 로고
    • Import of yeast mitochondrial transcription factor (Mtf1p) via a nonconventional pathway
    • Biswas TK, Getz GS. 2002. Import of yeast mitochondrial transcription factor (Mtf1p) via a nonconventional pathway. J Biol Chem 277: 45704-45714.
    • (2002) J Biol Chem , vol.277 , pp. 45704-45714
    • Biswas, T.K.1    Getz, G.S.2
  • 7
    • 84865439205 scopus 로고    scopus 로고
    • Transcription factors and muscle differentiation.
    • Giordano A, Galderisi U, editors. New York, Dordrecht, Heidelberg, London: Springer Science+Business Media.
    • Cabello G, Casas F, Wrutniak-Cabello C. 2010. Transcription factors and muscle differentiation. In: Giordano A, Galderisi U, editors. Cell cycle regulation and differentiation in cardiovascular and neural systems. New York, Dordrecht, Heidelberg, London: Springer Science+Business Media. pp 35-68.
    • (2010) Cell cycle regulation and differentiation in cardiovascular and neural systems , pp. 35-68
    • Cabello, G.1    Casas, F.2    Wrutniak-Cabello, C.3
  • 11
    • 49649115956 scopus 로고    scopus 로고
    • Mechanisms of hormone carcinogenesis: Evolution of views, role of mitochondria
    • Chen JQ, Brown TR, Yager JD. 2008. Mechanisms of hormone carcinogenesis: Evolution of views, role of mitochondria. Adv Exp Med Biol 630: 1-18.
    • (2008) Adv Exp Med Biol , vol.630 , pp. 1-18
    • Chen, J.Q.1    Brown, T.R.2    Yager, J.D.3
  • 12
    • 0016378181 scopus 로고
    • Subcellular fractionation of rat liver
    • Fleischer S, Kervina M. 1974. Subcellular fractionation of rat liver. Methods Enzymol 31: 6-41.
    • (1974) Methods Enzymol , vol.31 , pp. 6-41
    • Fleischer, S.1    Kervina, M.2
  • 14
    • 0033305499 scopus 로고    scopus 로고
    • Orphan nuclear receptors: From gene to function
    • Giguère V. 1999. Orphan nuclear receptors: From gene to function. Endocr Rev 20: 689-725.
    • (1999) Endocr Rev , vol.20 , pp. 689-725
    • Giguère, V.1
  • 17
    • 0023803436 scopus 로고
    • Effect of mitochondrial protein synthesis inhibitors on erythroid differentiation of mouse erythroleukemia (Friend) cells
    • Kaneko T, Watanabe T, Oishi M. 1988. Effect of mitochondrial protein synthesis inhibitors on erythroid differentiation of mouse erythroleukemia (Friend) cells. Mol Cell Biol 8: 3311-3315.
    • (1988) Mol Cell Biol , vol.8 , pp. 3311-3315
    • Kaneko, T.1    Watanabe, T.2    Oishi, M.3
  • 18
    • 0029833868 scopus 로고    scopus 로고
    • Protein import into mammamian mitochondria: Characterization of the intermediates along the import pathway of the precursor into the matrix
    • Komiya T, Mihara K. 1996. Protein import into mammamian mitochondria: Characterization of the intermediates along the import pathway of the precursor into the matrix. J Biol Chem 271: 22105-22110.
    • (1996) J Biol Chem , vol.271 , pp. 22105-22110
    • Komiya, T.1    Mihara, K.2
  • 21
    • 0018706325 scopus 로고
    • Studies of the effect of Chloramphenicol, ethidium bromide and camptothecin on the reproduction of Rous sarcoma virus in infected chick embryo cells
    • Leblond-Larouche L, Morais R, Zollinger M. 1979. Studies of the effect of Chloramphenicol, ethidium bromide and camptothecin on the reproduction of Rous sarcoma virus in infected chick embryo cells. J Gen Virol 44: 323-331.
    • (1979) J Gen Virol , vol.44 , pp. 323-331
    • Leblond-Larouche, L.1    Morais, R.2    Zollinger, M.3
  • 22
    • 0019987178 scopus 로고
    • Role of mitochondrial membrane potential in the regulation of murine erythroleukemia cell differentiation
    • Levenson R, Macara IG, Smith RL, Cantley L, Housman D. 1982. Role of mitochondrial membrane potential in the regulation of murine erythroleukemia cell differentiation. Cell 28: 855-863.
    • (1982) Cell , vol.28 , pp. 855-863
    • Levenson, R.1    Macara, I.G.2    Smith, R.L.3    Cantley, L.4    Housman, D.5
  • 23
    • 0025953614 scopus 로고
    • Role of an energized inner membrane in mitochondrial protein import. Delta psi drives the movement of presequences
    • Martin J, Mahlke K, Pfanner M. 1991. Role of an energized inner membrane in mitochondrial protein import. Delta psi drives the movement of presequences. J Biol Chem 266: 18051-18057.
    • (1991) J Biol Chem , vol.266 , pp. 18051-18057
    • Martin, J.1    Mahlke, K.2    Pfanner, M.3
  • 24
    • 27844535385 scopus 로고    scopus 로고
    • Protein import into mitochondria
    • Mokranjac D, Neupert W. 2005. Protein import into mitochondria. Biochem Soc Trans 33: 1019-1023.
    • (2005) Biochem Soc Trans , vol.33 , pp. 1019-1023
    • Mokranjac, D.1    Neupert, W.2
  • 25
    • 0018862049 scopus 로고
    • Chick embryo cells rendered respiration-deficient by chloramphenicol and ethidium bromide are auxotrophic for pyrimidines
    • Morais R, Gregoire L, Jeanotte L, Gravel D. 1980. Chick embryo cells rendered respiration-deficient by chloramphenicol and ethidium bromide are auxotrophic for pyrimidines. Biochem Biophys Res Comm 94: 71-77.
    • (1980) Biochem Biophys Res Comm , vol.94 , pp. 71-77
    • Morais, R.1    Gregoire, L.2    Jeanotte, L.3    Gravel, D.4
  • 26
    • 0024322179 scopus 로고
    • Thyroid hormone and not growth hormone is the principle regulator of mammalian mitochondrial biogenesis
    • Mutvei A, Husman B, Andersson G, Nelson BD. 1989. Thyroid hormone and not growth hormone is the principle regulator of mammalian mitochondrial biogenesis. Acta Endocrinol (Copenh) 121: 223-228.
    • (1989) Acta Endocrinol (Copenh) , vol.121 , pp. 223-228
    • Mutvei, A.1    Husman, B.2    Andersson, G.3    Nelson, B.D.4
  • 27
    • 0030969942 scopus 로고    scopus 로고
    • Protein import into mitochondria
    • Neupert W. 1997. Protein import into mitochondria. Annu Rev Biochem 66: 863-917.
    • (1997) Annu Rev Biochem , vol.66 , pp. 863-917
    • Neupert, W.1
  • 28
    • 0037459081 scopus 로고    scopus 로고
    • Mitochondria: Releasing power for life and unleashing the machineries of death
    • Newmeyer DD, Ferguson-Miller S. 2003. Mitochondria: Releasing power for life and unleashing the machineries of death. Cell 112: 481-490.
    • (2003) Cell , vol.112 , pp. 481-490
    • Newmeyer, D.D.1    Ferguson-Miller, S.2
  • 29
    • 0035344460 scopus 로고    scopus 로고
    • Versatility of the mitochondrial protein import machinery
    • Pfanner N, Geissler A. 2001. Versatility of the mitochondrial protein import machinery. Nat Rev Mol Cell Biol 2: 339-349.
    • (2001) Nat Rev Mol Cell Biol , vol.2 , pp. 339-349
    • Pfanner, N.1    Geissler, A.2
  • 30
    • 80051792747 scopus 로고    scopus 로고
    • Glucocorticoids induce mitochondrial gene transcription i, HepG2 cells:role of the mitochondrial glucocorticoid receptor
    • Psarra AM, Sekeris CE. 2011. Glucocorticoids induce mitochondrial gene transcription i, HepG2 cells:role of the mitochondrial glucocorticoid receptor. Biochem Biophys Acta 1813: 1814-1821.
    • (2011) Biochem Biophys Acta , vol.1813 , pp. 1814-1821
    • Psarra, A.M.1    Sekeris, C.E.2
  • 31
    • 0034723175 scopus 로고    scopus 로고
    • Mitochondrial activity is involved in the regulation of myoblast differentiation through myogenin expression and myogenic factors activity
    • Rochard P, Rodier A, Casas F, Cassar-Malek I, Marchal-Victorion S, Daury L, Wrutniak C, Cabello G. 2000. Mitochondrial activity is involved in the regulation of myoblast differentiation through myogenin expression and myogenic factors activity. J Biol Chem 275: 2733-2744.
    • (2000) J Biol Chem , vol.275 , pp. 2733-2744
    • Rochard, P.1    Rodier, A.2    Casas, F.3    Cassar-Malek, I.4    Marchal-Victorion, S.5    Daury, L.6    Wrutniak, C.7    Cabello, G.8
  • 32
    • 0029013884 scopus 로고
    • Import of transcription factor MTF1 into the yeast mitochondria takes place through an unusual pathway
    • Sanyal A, Getz GS. 1995. Import of transcription factor MTF1 into the yeast mitochondria takes place through an unusual pathway. J Biol Chem 270: 11970-11976.
    • (1995) J Biol Chem , vol.270 , pp. 11970-11976
    • Sanyal, A.1    Getz, G.S.2
  • 33
    • 0029979607 scopus 로고    scopus 로고
    • Common principles of protein translocation across membranes
    • Schatz G, Dobberstein B. 1996. Common principles of protein translocation across membranes. Science 271: 1519-1526.
    • (1996) Science , vol.271 , pp. 1519-1526
    • Schatz, G.1    Dobberstein, B.2
  • 37
    • 77649262473 scopus 로고    scopus 로고
    • Mitochondrial localization of vitamin D receptor in human platelets and differentiated megakaryocytes
    • Silvagno F, De Vivo E, Attanasio A, Gallo V, Mazzucco G, Pescarmona G. 2010. Mitochondrial localization of vitamin D receptor in human platelets and differentiated megakaryocytes. PloS One 5: e8670.
    • (2010) PloS One , vol.5
    • Silvagno, F.1    De Vivo, E.2    Attanasio, A.3    Gallo, V.4    Mazzucco, G.5    Pescarmona, G.6
  • 38
    • 47849092592 scopus 로고    scopus 로고
    • Estrogen actions on mitochondria:physiological and pathological implications
    • Simpkins JW, Yang SH, Sarkar SN, Pearce V. 2008. Estrogen actions on mitochondria:physiological and pathological implications. Mol Cell Endocrinol 290: 51-59.
    • (2008) Mol Cell Endocrinol , vol.290 , pp. 51-59
    • Simpkins, J.W.1    Yang, S.H.2    Sarkar, S.N.3    Pearce, V.4
  • 39
    • 0025080475 scopus 로고
    • L-lactate oxidation by skeletal muscle mitochondria
    • Szczesna-Kaczmarek A. 1990. L-lactate oxidation by skeletal muscle mitochondria. Intl J Biochem 22: 617-620.
    • (1990) Intl J Biochem , vol.22 , pp. 617-620
    • Szczesna-Kaczmarek, A.1
  • 41
    • 0026799250 scopus 로고
    • Relationship between culture conditions and the dependency on mitochondrial function of mammalian cell proliferation
    • Van den Bogert C, Spelbrink JN, Dekker HL. 1992. Relationship between culture conditions and the dependency on mitochondrial function of mammalian cell proliferation. J Cell Physiol 152: 632-638.
    • (1992) J Cell Physiol , vol.152 , pp. 632-638
    • Van den Bogert, C.1    Spelbrink, J.N.2    Dekker, H.L.3
  • 42
    • 0024542834 scopus 로고
    • Domain structure of mitochondrial and chloroplast targeting peptides
    • Von Heijne G, Steppun J, Hermann RG. 1989. Domain structure of mitochondrial and chloroplast targeting peptides. Eur J Biochem 180: 535-545.
    • (1989) Eur J Biochem , vol.180 , pp. 535-545
    • Von Heijne, G.1    Steppun, J.2    Hermann, R.G.3
  • 47
    • 33947413972 scopus 로고    scopus 로고
    • Mitochondrial estrogen receptors. New insights into specific functions
    • Yager JD, Chen JQ. 2007. Mitochondrial estrogen receptors. New insights into specific functions. Trends Endocrinol Metab 18: 89-91.
    • (2007) Trends Endocrinol Metab , vol.18 , pp. 89-91
    • Yager, J.D.1    Chen, J.Q.2
  • 49
    • 18144405281 scopus 로고    scopus 로고
    • Nuclear and mitochondrial localization signals overlap within bovine herpesvirus 1 tegument protein VP22
    • Zhu J, Qiu Z, Wiese C, Ishii Y, Friedrichsen J, Rajashekara G, Splitter GA. 2005. Nuclear and mitochondrial localization signals overlap within bovine herpesvirus 1 tegument protein VP22. J Biol Chem 280: 16038-16044.
    • (2005) J Biol Chem , vol.280 , pp. 16038-16044
    • Zhu, J.1    Qiu, Z.2    Wiese, C.3    Ishii, Y.4    Friedrichsen, J.5    Rajashekara, G.6    Splitter, G.A.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.